Comment on the data in the container class. This property should be used instead of the OWL documentation elements (rdfs:comment) for instances because information in COMMENT is data to be exchanged, whereas the rdfs:comment field is used for metadata about the structure of the BioPAX ontology.
Source:http://www.biopax.org/release/biopax-level2.owl#COMMENT
| Subject | Object |
|---|---|
| cpath:CPATH-16 |
FUNCTION: Appears to play multiple roles in cell cycle progression, cytokinesis and apoptosis. The p110 isoforms have been suggested to be involved in pre-mRNA splicing, potentially by phosphorylating the splicing protein SFRS7. The p58 isoform may act as a negative regulator of normal cell cycle progression. CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. COFACTOR: Magnesium. ENZYME REGULATION: Phosphorylation at Thr-436 or Tyr-437 inactivates the enzyme, while phosphorylation at Thr-583 activates it (By similarity). SUBUNIT: The cleaved p110 isoform, p110C, binds to the serine/threonine kinase PAK1. The p58 isoform but not the p110 isoform or p110C interacts with CCND3. The p110 isoforms are found in large molecular weight complexes containing CCNL1 and SFRS7. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. ALTERNATIVE PRODUCTS: Event=Alternative splicing, Alternative initiation; Named isoforms=8; Comment=Additional isoforms seem to exist; Name=SV6; Synonyms=p110; IsoId=Q9UQ88-1; Sequence=Displayed; Name=SV1; Synonyms=Pbeta21, Beta 2-1; IsoId=Q9UQ88-2; Sequence=VSP_008286, VSP_008288; Note=Ref.1 (AAA19594) sequence is in conflict in positions: 109:C->R, 112:H->R; Name=SV2; Synonyms=Pbeta22; IsoId=Q9UQ88-3; Sequence=VSP_008287, VSP_008288; Note=Ref.1 (AAA19595) sequence is in conflict in position: 158:F->V; Name=SV3; IsoId=Q9UQ88-4; Sequence=VSP_008288; Name=SV7; Synonyms=SV8; IsoId=Q9UQ88-5; Sequence=VSP_008283, VSP_008289; Name=SV12; IsoId=Q9UQ88-8; Sequence=VSP_008284, VSP_008292; Name=SV13; IsoId=Q9UQ88-9; Sequence=VSP_008281, VSP_008287, VSP_008288, VSP_008290, VSP_008291; Name=4; Synonyms=Beta 1, p58; IsoId=Q9UQ88-10; Sequence=VSP_018836; Note=Produced by alternative initiation at Met-345 of isoform SV6; TISSUE SPECIFICITY: Expressed ubiquitously. Some evidence of isoform-specific tissue distribution. INDUCTION: The p58 isoform is specifically induced in G2/M phase of the cell cycle. PTM: During apoptosis, induced by Fas or tumor necrosis factor, specific CKD11 p110 isoforms are cleaved by caspases to produce a protein (p110C) that contains the C-terminal kinase domain of the CDK11 proteins. MISCELLANEOUS: Duplicated gene. CDK11A and CDK11B encode almost identical protein kinases of 110 kDa that contain at their C- termini the open reading frame of a smaller 58 kDa isoform which is expressed following IRES-mediated alternative initiation of translation. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. SIMILARITY: Contains 1 protein kinase domain. CAUTION: Many references talk about 'p110 isoforms' but it is not yet known if this refers to CDK11A and/or CDK11B or one/some of the isoforms of each. SEQUENCE CAUTION: Sequence=AAC95297.1; Type=Erroneous gene model prediction; Sequence=AAC95298.1; Type=Erroneous gene model prediction; Sequence=AAC95299.1; Type=Erroneous gene model prediction; Sequence=AAC95300.1; Type=Erroneous gene model prediction; Sequence=AAC95302.1; Type=Erroneous gene model prediction; Sequence=AAC95303.1; Type=Erroneous gene model prediction; GENE SYNONYMS: CDC2L2 CDC2L3 PITSLREB. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-18 |
FUNCTION: Inhibits the Wnt/Wingless pathway by binding to beta- catenin and inhibiting beta-catenin-mediated transcriptional activation through competition with TCF/LEF transcription factors. Has also been shown to play a role in regulating the intracellular trafficking of polycystin-2/PKD2 and possibly of other intracellular proteins. Promotes adipocyte and cardiomyocyte differentiation. SUBUNIT: Homodimer. Interacts with polycystin-2/PKD2 and GM130. Interacts with the C-terminal region of beta-catenin. SUBCELLULAR LOCATION: Nucleus speckle. Golgi apparatus, trans- Golgi network. Note=Nuclear, in a punctate manner. Also found in the trans-Golgi. TISSUE SPECIFICITY: Widely expressed. Expressed at higher levels in heart, skeletal muscle, kidney and placenta. Also found in brain, lung, liver and testis. Significantly down-regulated in thyroid and metastatic uterine tumors. MISCELLANEOUS: 'Chibby' is Japanese for 'small'; the gene was so named for the RNAi phenotype seen in flies. SIMILARITY: Belongs to the chibby family. GENE SYNONYMS: ARB1 C22orf2 CBY PGEA1. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-22 |
FUNCTION: Regulatory component of the cyclin D2-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Component of the ternary complex, cyclin D2/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex (By similarity). SUBUNIT: Interacts with either CDK4 or CDK6 protein kinase to form a serine/threonine kinase holoenzyme complex. The cyclin subunit imparts substrate specificity to the complex. Component of the ternary complex cyclin D/CDK4/CDKN1B required for nuclear translocation and modulation of CDK4-mediated kinase activity. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Membrane. Note=Cyclin D- CDK4 complexes accumulate at the nuclear membrane and are then translocated into the nucleus through interaction with KIP/CIP family members (By similarity). SIMILARITY: Belongs to the cyclin family. Cyclin D subfamily. SIMILARITY: Contains 1 cyclin N-terminal domain. WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/ccnd2/"; COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-28 |
SIMILARITY: Belongs to the UPF0704 family. SEQUENCE CAUTION: Sequence=BAC04234.1; Type=Miscellaneous discrepancy; Note=Intron retention; COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-30 |
FUNCTION: Cadherins are calcium dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. TISSUE SPECIFICITY: Mainly expressed in brain. Found in certain nerve cell lines, such as retinoblasts, glioma cells and neuroblasts. SIMILARITY: Contains 5 cadherin domains. SEQUENCE CAUTION: Sequence=AAA35628.1; Type=Erroneous initiation; COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-42 |
FUNCTION: Important for the epidermal barrier integrity. SUBCELLULAR LOCATION: Secreted. Note=Found in corneodesmosomes, the intercellular structures that are involved in desquamation. TISSUE SPECIFICITY: Exclusively expressed in skin. POLYMORPHISM: Genetic variation in CDSN may be associated with susceptibility to psoriasis [MIM:177900]. Various CDSN alleles are known including alleles 1.11, 1.21, 1.31, 1.32, 1.41, 1.42, 1.43, 1.51, 1.52, 2.11, 2.21, 2.22 and 2.23. DISEASE: Defects in CDSN are a cause of hypotrichosis simplex of the scalp (HTSS) [MIM:146520]; also known as hypotrichosis Spanish type. HTSS is an autosomal dominant form of isolated alopecia. Affected individuals have normal hair in early childhood but experience progressive loss of scalp hair beginning in the middle of the first decade and almost complete baldness by the third decade. DISEASE: Defects in CDSN are the cause of peeling skin syndrome type B (BPSS) [MIM:270300]; also known as peeling skin syndrome or deciduous skin or keratolysis exfoliativa congenita. BPSS is a genodermatosis characterized by the continuous shedding of the outer layers of the epidermis, associated with pruritus and atopy. It is an ichthyosiform erythroderma characterized by lifelong patchy peeling of the entire skin with onset at birth or shortly thereafter. Several patients have been reported with high IgE levels. SEQUENCE CAUTION: Sequence=AAA21321.1; Type=Frameshift; Positions=501; Sequence=BAB63316.1; Type=Erroneous initiation; Note=Translation N-terminally extended; Sequence=BAC54948.1; Type=Erroneous initiation; Note=Translation N-terminally extended; COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-50 |
FUNCTION: Essential for the control of the cell cycle at the G1/S (start) and the G2/M (mitosis) transitions. SUBUNIT: Interacts with the CDK1 and CDK2 protein kinases to form a serine/threonine kinase holoenzyme complex. The cyclin subunit imparts substrate specificity to the complex. When associated with CDK2 (but not with CDK1), interacts with SCAPER. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Cytoplasmic when associated with SCAPER. DEVELOPMENTAL STAGE: Accumulates steadily during G2 and is abruptly destroyed at mitosis. PTM: Polyubiquitinated via 'Lys-11'-linked ubiquitin by the anaphase-promoting complex (APC/C), leading to its degradation by the proteasome. Deubiquitinated and stabilized by USP37 enables entry into S phase (By similarity). SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily. WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/ccna2/"; GENE SYNONYMS: CCN1 CCNA. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
FUNCTION: Essential for the control of the cell cycle at the G1/S (start) and the G2/M (mitosis) transitions. SUBUNIT: Interacts with the CDK1 and CDK2 protein kinases to form a serine/threonine kinase holoenzyme complex. The cyclin subunit imparts substrate specificity to the complex. When associated with CDK2 (but not with CDK1), interacts with SCAPER. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Cytoplasmic when associated with SCAPER. DEVELOPMENTAL STAGE: Accumulates steadily during G2 and is abruptly destroyed at mitosis. PTM: Polyubiquitinated via 'Lys-11'-linked ubiquitin by the anaphase-promoting complex (APC/C), leading to its degradation by the proteasome. Deubiquitinated and stabilized by USP37 enables entry into S phase (By similarity). SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily. WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/ccna2/"; GENE SYNONYMS: CCN1 CCNA. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-58 |
FUNCTION: Probable role in assembly and expression of the TCR complex as well as signal transduction upon antigen triggering. SUBUNIT: The TCR/CD3 complex of T-lymphocytes consists of either a TCR alpha/beta or TCR gamma/delta heterodimer coexpressed at the cell surface with the invariant subunits of CD3 labeled gamma, delta, epsilon, zeta, and eta. CD3-zeta forms either homodimers or heterodimers with CD3-eta. Interacts with SLA and SLA2. Interacts with DOCK2 and TRAT1. Interacts with HIV-1; this interaction up- regulates the expression of the Fas ligand (FASLG) at the cell surface. Interacts with HIV-2 Nef protein; this interaction induces down-regulation of cell surface TCR/CD3 complexes. Interacts with SHB. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=3; Name=1; Synonyms=CD-3-zeta; IsoId=P20963-1; Sequence=Displayed; Name=2; Synonyms=CD-3-eta; IsoId=P20963-2; Sequence=Not described; Name=3; IsoId=P20963-3; Sequence=VSP_036459; DOMAIN: The ITAM domains mediate interaction with SHB. PTM: Phosphorylated on Tyr residues after T-cell receptor triggering (By similarity). DISEASE: Defects in CD247 are the cause of immunodeficiency due to defect in CD3-zeta (CD3ZID) [MIM:610163]. An immunological deficiency characterized by T-cells impaired immune response to alloantigens, tetanus toxoid and mitogens. SIMILARITY: Belongs to the CD3Z/FCER1G family. SIMILARITY: Contains 3 ITAM domains. WEB RESOURCE: Name=CD247base; Note=CD247 mutation db; URL="http://bioinf.uta.fi/CD247base/"; WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/cd3z/"; GENE SYNONYMS: CD3Z T3Z TCRZ. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-60 |
FUNCTION: Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond- specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N. CATALYTIC ACTIVITY: Similar to cathepsin L, but with much less activity on Z-Phe-Arg-|-NHMec, and more activity on the Z-Val-Val- Arg-|-Xaa compound. SUBUNIT: Monomer. SUBCELLULAR LOCATION: Lysosome. SIMILARITY: Belongs to the peptidase C1 family. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-62 |
SEQUENCE CAUTION: Sequence=BAB14642.1; Type=Erroneous initiation; Note=Translation N-terminally extended; COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-64 |
ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q49AR2-1; Sequence=Displayed; Name=2; IsoId=Q49AR2-2; Sequence=VSP_028183; Note=No experimental confirmation available; Name=3; IsoId=Q49AR2-3; Sequence=VSP_028182, VSP_028184; Note=No experimental confirmation available; SIMILARITY: Belongs to the UPF0489 family. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-66 |
FUNCTION: DNA-binding component of the FA core complex involved in DNA damage repair and genome maintenance. Required for optimal chromatin association of the FA core complex. Required for efficient damage-induced monoubiquitination and focus formation of FANCD2. Stabilizes FAAD24, FANCM and STRA13/CENPX in the FA core complex. Plays a role in DNA interstrand cross-linking (ICL) repair and in recorery of replication forks stalled by topoisomerase I-DNA cleavage intermediates induced by camptothecin. As a component of the APITD1/CENPS complex, is also essential for the stable assembly of the outer kinetchore. Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. SUBUNIT: Component of a discrete APITD1/CENPS complex composed of at least APITD1/CENPS and STRA13/CENPX. Belongs to the multisubunit FA complex composed of APITD1/CENPS, FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL/PHF9, FANCM, FAAP24 and STRA13/CENPX. Component of the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and APITD1/CENPS. The CENPA-CAD complex interacts with the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and MLF1IP/CENPU. Interacts with APITD1/CENPS, FANCM and FAAP24. Binds DNA. SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere. Note=Localizes exclusively in the centromeres. The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q8N2Z9-1; Sequence=Displayed; Name=2; IsoId=Q8N2Z9-2; Sequence=VSP_020434; Note=No experimental confirmation available; Name=3; IsoId=Q8N2Z9-3; Sequence=VSP_020432, VSP_020433; Note=No experimental confirmation available; TISSUE SPECIFICITY: Ubiquitously expressed. SIMILARITY: Belongs to the TAF9 family. GENE SYNONYMS: CENPS FAAP16 MHF1. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-80 |
FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1- like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Involved in sexual development, acting as activator of NR5A1 expression. SUBUNIT: Component of a PRC1-like complex. SUBCELLULAR LOCATION: Nucleus. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q14781-1; Sequence=Displayed; Name=2; IsoId=Q14781-2; Sequence=VSP_015816, VSP_015817; Note=No experimental confirmation available; DISEASE: Defects in CBX2 are the cause of 46,XY sex reversal type 5 (SRXY5) [MIM:613080]. It is a disorder of sex development. Affected individuals have a 46,XY karyotype but present as phenotypically normal females. MISCELLANEOUS: The human orthologuous proteins of Drosphila Polycomb group protein Pc, CBX2, CBX4, CBX6, CBX7 and CBX8, show distinct nulear localizations, contribute differently to transcriptional repression, and appear to be part of distinct PRC1-like protein complexes. The hPRC-H complex purification reported by PubMed:12167701 probably presents a mixture of different complexes. SIMILARITY: Contains 1 A.T hook DNA-binding domain. SIMILARITY: Contains 1 chromo domain. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-86 |
FUNCTION: Identifies cytotoxic/suppressor T-cells that interact with MHC class I bearing targets. CD8 is thought to play a role in the process of T-cell mediated killing. CD8 alpha chains binds to class I MHC molecules alpha-3 domains. SUBUNIT: In general heterodimer of an alpha and a beta chain linked by two disulfide bonds. Can also form homodimers. Shown to be expressed as heterodimer on thymocytes and as homodimer on peripheral blood T-lymphocytes. Interacts with the MHC class I HLA-A/B2M dimer. Interacts with LCK in a zinc-dependent manner. SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I membrane protein. SUBCELLULAR LOCATION: Isoform 2: Secreted. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; Synonyms=membrane, mCD8alpha; IsoId=P01732-1; Sequence=Displayed; Name=2; Synonyms=secreted, sCD8alpha; IsoId=P01732-2; Sequence=VSP_012653; PTM: All of the five most carboxyl-terminal cysteines form inter- chain disulfide bonds in dimers and higher multimers, while the four N-terminal cysteines do not (By similarity). DISEASE: Defects in CD8A are a cause of familial CD8 deficiency (CD8 deficiency) [MIM:608957]. Familial CD8 deficiency is a novel autosomal recessive immunologic defect characterized by absence of CD8+ cells, leading to recurrent bacterial infections. SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like) domain. WEB RESOURCE: Name=CD8Abase; Note=CD8A mutation db; URL="http://bioinf.uta.fi/CD8Abase/"; WEB RESOURCE: Name=Wikipedia; Note=CD8 entry; URL="http://en.wikipedia.org/wiki/CD8"; GENE SYNONYMS: MAL. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-88 |
FUNCTION: May act as a receptor in regulating T-cell proliferation. CD5 interacts with CD72/LYB-2. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Contains 3 SRCR domains. GENE SYNONYMS: LEU1. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-98 |
FUNCTION: Involved in platelet activation and aggregation. Regulates paranodal junction formation. Involved in cell adhesion, cell motility and tumor metastasis. Required for sperm-egg fusion. SUBUNIT: Forms both disulfide-linked homodimers and higher homooligomers as well as heterooligomers with other members of the tetraspanin family. Associates with CR2/CD21 and with PTGFRN/CD9P1. Interacts directly with IGSF8. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed by a variety of hematopoietic and epithelial cells. PTM: Protein exists in three forms with molecular masses between 22 and 27 kDa, and is known to carry covalently linked fatty acids. SIMILARITY: Belongs to the tetraspanin (TM4SF) family. WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/cd9/"; GENE SYNONYMS: MIC3 TSPAN29. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-100 |
SEQUENCE CAUTION: Sequence=AAI11467.1; Type=Erroneous initiation; COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-104 |
FUNCTION: Required for initiation of chromosomal DNA replication. SUBUNIT: Associated with ORC2. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. TISSUE SPECIFICITY: Widely expressed, highest levels are found in adult testis and thymus and in fetal liver. DEVELOPMENTAL STAGE: Transcript peaks at G1-S transition, but total protein remains constant throughout the cell cycle. Expressed in multiple tissues during embryogenesis, including neural crest-derived structures. SIMILARITY: Belongs to the CDC45 family. WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/cdc45l/"; GENE SYNONYMS: CDC45L CDC45L2. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-110 |
FUNCTION: Believed to be a non-apoptotic caspase which is involved in epidermal differentiation. Seems to play a role in keratinocyte differentiation and cornification. Probably regulates maturation of the epidermis by proteolytically processing filaggrin (By similarity). SUBUNIT: Complex of unprocessed caspase-14 and processed 19 kDa (p19) and 10 kDa (p10) subunits. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. TISSUE SPECIFICITY: Expressed in keratinocytes of adult skin suprabasal layers (from spinous layers to the stratum granulosum and stratum corneum) (at protein level). Expressed in keratinocytes of hair shaft and sebaceous glands (at protein level). In psoriatic skin only expressed at very low levels. INDUCTION: In undifferentiated keratinocytes under postconfluency growth conditions (in vitro). SIMILARITY: Belongs to the peptidase C14A family. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-122 |
ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q8N4S0-1; Sequence=Displayed; Name=2; IsoId=Q8N4S0-2; Sequence=VSP_035403, VSP_035404; PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. SEQUENCE CAUTION: Sequence=BAB15683.1; Type=Frameshift; Positions=527; COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-124 |
FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Plays an important role in the correct PLK1 localization to the mitotic kinetochores. A scaffold protein responsible for the initial recruitment and maintenance of the kinetochore PLK1 population until its degradation. Involved in transcriptional repression. SUBUNIT: Component of the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and MLF1IP/CENPU. The CENPA-NAC complex interacts with the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. Interacts with the N-terminal domain of Kaposi's sarcoma- associated herpesvirus latent nuclear antigen (LNA). Interacts with MLF1. Interacts with PLK1. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Chromosome, centromere, kinetochore. Note=Localizes in the kinetochore domain of centromeres. Colocalizes with PLK1 at the interzone between the inner and the outer kinetochore plates. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q71F23-1; Sequence=Displayed; Name=2; IsoId=Q71F23-2; Sequence=VSP_020030; TISSUE SPECIFICITY: Expressed at high levels in the testis, fetal liver, thymus, bone marrow and at lower levels in the lymph nodes, placenta, colon and spleen. Present in all cell lines examined, including B-cells, T-cells, epithelial cells and fibroblast cells. Expressed at high levels in glioblastoma cell lines. PTM: Phosphorylated by PLK1 at Thr-78, creating a self-tethering site that specifically interacts with the polo-box domain of PLK1. GENE SYNONYMS: CENPU ICEN24 KLIP1 PBIP1. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-130 |
FUNCTION: Seems to be involved in transcriptional silencing in heterochromatin-like complexes. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. May contribute to the association of the heterochromatin with the inner nuclear membrane through its interaction with lamin B receptor (LBR). Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins. SUBUNIT: Binds directly to CHAF1A. Interacts with histone H3 methylated at 'Lys-9'. Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, L3MBTL2 and YAF2. Interacts with LBR, INCENP, TRIM28/TIF1B, SUV420H1, SUV420H2 and SP100. Interacts with TIF1A (By similarity). Interacts with MIS12 and DSN1. Can interact directly with CBX5 via the chromoshadow domain. Interacts with POGZ. SUBCELLULAR LOCATION: Nucleus (Potential). Note=Associates with euchromatin and is largely excluded from constitutive heterochromatin. May be associated with microtubules and mitotic poles during mitosis (Potential). PTM: Phosphorylated by PIM1. Phosphorylated during interphase and possibly hyper-phosphorylated during mitosis. SIMILARITY: Contains 2 chromo domains. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-132 |
FUNCTION: Regulator of sister chromatid cohesion in mitosis stabilizing cohesin complex association with chromatin. May antagonize the action of WAPAL which stimulates cohesin dissociation from chromatin. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. Required for efficient DNA double-stranded break repair. SUBUNIT: Interacts with the APC/C complex (By similarity). Interacts with the chromatin-bound cohesin complex; the interaction is indirect, occurs after DNA replication and requires acetylation of the cohesin component SMC3. Interacts (via the FGF motif) with PDS5A and PDS5B; the interaction is direct and prevents the interaction of PDS5A with WAPAL. SUBCELLULAR LOCATION: Nucleus. Chromosome. Cytoplasm. Note=Associates with nuclear chromatin from S phase until metaphase and is released in the cytoplasm upon nuclear envelope breakdown. DOMAIN: The KEN box is required for the association with the APC/C complex (By similarity). PTM: Phosphorylated. Phosphorylation, as cells enter mitosis, disrupts the interaction with PDS5A and relieves the inhibition of WAPAL by CDCA5. PTM: Ubiquitinated by the APC/C complex in G1, leading to its degradation (Probable). MISCELLANEOUS: Named sororin after the Latin word 'soror', which means 'sister', because of its critical role in sister chromatid cohesion. SIMILARITY: Belongs to the sororin family. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-134 |
FUNCTION: Acetylates histones, giving a specific tag for transcriptional activation. Also acetylates non-histone proteins, like NCOA3 coactivator. Binds specifically to phosphorylated CREB and enhances its transcriptional activity toward cAMP-responsive genes. Acts as a coactivator of ALX1 in the presence of EP300. CATALYTIC ACTIVITY: Acetyl-CoA + [histone] = CoA + acetyl- [histone]. SUBUNIT: Found in a complex containing NCOA2; NCOA3; IKKA; IKKB and IKBKG. Probably part of a complex with HIF1A and EP300. Interacts with phosphorylated CREB1. Interacts with the C-terminal region of CITED4. The TAZ-type 1 domain interacts with HIF1A. Interacts with MAF, SRCAP, CARM1, ELF3, MLLT7/FOXO4, N4BP2, NCOA1, NCOA3, NCOA6, PCAF, PELP1, PML, SMAD1, SMAD2, SMAD3, SPIB and TRERF1. Interacts with HTLV-1 Tax and p30II. Interacts with HIV-1 Tat. Interacts with KLF1; the interaction results in acetylation of KLF1 and enhancement of its transcriptional activity. Interacts with ZCCHC12 (By similarity). Interacts with DAXX; the interaction is dependent on CBP sumoylation and results in suppression of the transcriptional activiy via recruitment of HDAC2 to DAAX (By similarity). Interacts with MTDH. Interacts with NFATC4. Interacts with MAFG; the interaction acetylates MAFG in the basic region and stimulates NFE2 transcriptional activity through increasing its DNA-binding activity. Interacts with IRF2; the interaction acetylates IRF2 and regulates its activity on the H4 promoter. Interacts (via N-terminus) with SS18L1/CREST (via C-terminus). Interacts with MECOM. Interacts with CITED1 (via C-terminus). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Recruited to nuclear bodies by SS18L1/CREST. In the presence of ALX1 relocalizes from the cytoplasm to the nucleus. DOMAIN: The KIX domain mediates binding to HIV-1 Tat. PTM: Methylation of the KIX domain by CARM1 blocks association with CREB. This results in the blockade of CREB signaling, and in activation of apoptotic response (By similarity). PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. PTM: Sumoylation negatively regulates transcriptional activity via the recruitment of DAAX (By similarity). DISEASE: Note=Chromosomal aberrations involving CREBBP may be a cause of acute myeloid leukemias. Translocation t(8;16)(p11;p13) with MYST3/MOZ; translocation t(11;16)(q23;p13.3) with MLL/HRX; translocation t(10;16)(q22;p13) with MYST4/MORF. MYST3-CREBBP may induce leukemia by inhibiting RUNX1-mediated transcription. DISEASE: Defects in CREBBP are a cause of Rubinstein-Taybi syndrome type 1 (RSTS1) [MIM:180849]. RSTS1 is an autosomal dominant disorder characterized by craniofacial abnormalities, broad thumbs, broad big toes, mental retardation and a propensity for development of malignancies. SIMILARITY: Contains 1 bromo domain. SIMILARITY: Contains 1 KIX domain. SIMILARITY: Contains 2 TAZ-type zinc fingers. SIMILARITY: Contains 1 ZZ-type zinc finger. WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/CBPID42.html"; WEB RESOURCE: Name=GeneReviews; URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/CREBBP"; WEB RESOURCE: Name=Wikipedia; Note=P300/CBP entry; URL="http://en.wikipedia.org/wiki/P300/CBP"; GENE SYNONYMS: CBP. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
FUNCTION: Acetylates histones, giving a specific tag for transcriptional activation. Also acetylates non-histone proteins, like NCOA3 coactivator. Binds specifically to phosphorylated CREB and enhances its transcriptional activity toward cAMP-responsive genes. Acts as a coactivator of ALX1 in the presence of EP300. CATALYTIC ACTIVITY: Acetyl-CoA + [histone] = CoA + acetyl- [histone]. SUBUNIT: Found in a complex containing NCOA2; NCOA3; IKKA; IKKB and IKBKG. Probably part of a complex with HIF1A and EP300. Interacts with phosphorylated CREB1. Interacts with the C-terminal region of CITED4. The TAZ-type 1 domain interacts with HIF1A. Interacts with MAF, SRCAP, CARM1, ELF3, MLLT7/FOXO4, N4BP2, NCOA1, NCOA3, NCOA6, PCAF, PELP1, PML, SMAD1, SMAD2, SMAD3, SPIB and TRERF1. Interacts with HTLV-1 Tax and p30II. Interacts with HIV-1 Tat. Interacts with KLF1; the interaction results in acetylation of KLF1 and enhancement of its transcriptional activity. Interacts with ZCCHC12 (By similarity). Interacts with DAXX; the interaction is dependent on CBP sumoylation and results in suppression of the transcriptional activiy via recruitment of HDAC2 to DAAX (By similarity). Interacts with MTDH. Interacts with NFATC4. Interacts with MAFG; the interaction acetylates MAFG in the basic region and stimulates NFE2 transcriptional activity through increasing its DNA-binding activity. Interacts with IRF2; the interaction acetylates IRF2 and regulates its activity on the H4 promoter. Interacts (via N-terminus) with SS18L1/CREST (via C-terminus). Interacts with MECOM. Interacts with CITED1 (via C-terminus). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Recruited to nuclear bodies by SS18L1/CREST. In the presence of ALX1 relocalizes from the cytoplasm to the nucleus. DOMAIN: The KIX domain mediates binding to HIV-1 Tat. PTM: Methylation of the KIX domain by CARM1 blocks association with CREB. This results in the blockade of CREB signaling, and in activation of apoptotic response (By similarity). PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. PTM: Sumoylation negatively regulates transcriptional activity via the recruitment of DAAX (By similarity). DISEASE: Note=Chromosomal aberrations involving CREBBP may be a cause of acute myeloid leukemias. Translocation t(8;16)(p11;p13) with MYST3/MOZ; translocation t(11;16)(q23;p13.3) with MLL/HRX; translocation t(10;16)(q22;p13) with MYST4/MORF. MYST3-CREBBP may induce leukemia by inhibiting RUNX1-mediated transcription. DISEASE: Defects in CREBBP are a cause of Rubinstein-Taybi syndrome type 1 (RSTS1) [MIM:180849]. RSTS1 is an autosomal dominant disorder characterized by craniofacial abnormalities, broad thumbs, broad big toes, mental retardation and a propensity for development of malignancies. SIMILARITY: Contains 1 bromo domain. SIMILARITY: Contains 1 KIX domain. SIMILARITY: Contains 2 TAZ-type zinc fingers. SIMILARITY: Contains 1 ZZ-type zinc finger. WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/CBPID42.html"; WEB RESOURCE: Name=GeneReviews; URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/CREBBP"; WEB RESOURCE: Name=Wikipedia; Note=P300/CBP entry; URL="http://en.wikipedia.org/wiki/P300/CBP"; GENE SYNONYMS: CBP. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
FUNCTION: Acetylates histones, giving a specific tag for transcriptional activation. Also acetylates non-histone proteins, like NCOA3 coactivator. Binds specifically to phosphorylated CREB and enhances its transcriptional activity toward cAMP-responsive genes. Acts as a coactivator of ALX1 in the presence of EP300. CATALYTIC ACTIVITY: Acetyl-CoA + [histone] = CoA + acetyl- [histone]. SUBUNIT: Found in a complex containing NCOA2; NCOA3; IKKA; IKKB and IKBKG. Probably part of a complex with HIF1A and EP300. Interacts with phosphorylated CREB1. Interacts with the C-terminal region of CITED4. The TAZ-type 1 domain interacts with HIF1A. Interacts with MAF, SRCAP, CARM1, ELF3, MLLT7/FOXO4, N4BP2, NCOA1, NCOA3, NCOA6, PCAF, PELP1, PML, SMAD1, SMAD2, SMAD3, SPIB and TRERF1. Interacts with HTLV-1 Tax and p30II. Interacts with HIV-1 Tat. Interacts with KLF1; the interaction results in acetylation of KLF1 and enhancement of its transcriptional activity. Interacts with ZCCHC12 (By similarity). Interacts with DAXX; the interaction is dependent on CBP sumoylation and results in suppression of the transcriptional activiy via recruitment of HDAC2 to DAAX (By similarity). Interacts with MTDH. Interacts with NFATC4. Interacts with MAFG; the interaction acetylates MAFG in the basic region and stimulates NFE2 transcriptional activity through increasing its DNA-binding activity. Interacts with IRF2; the interaction acetylates IRF2 and regulates its activity on the H4 promoter. Interacts (via N-terminus) with SS18L1/CREST (via C-terminus). Interacts with MECOM. Interacts with CITED1 (via C-terminus). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Recruited to nuclear bodies by SS18L1/CREST. In the presence of ALX1 relocalizes from the cytoplasm to the nucleus. DOMAIN: The KIX domain mediates binding to HIV-1 Tat. PTM: Methylation of the KIX domain by CARM1 blocks association with CREB. This results in the blockade of CREB signaling, and in activation of apoptotic response (By similarity). PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. PTM: Sumoylation negatively regulates transcriptional activity via the recruitment of DAAX (By similarity). DISEASE: Note=Chromosomal aberrations involving CREBBP may be a cause of acute myeloid leukemias. Translocation t(8;16)(p11;p13) with MYST3/MOZ; translocation t(11;16)(q23;p13.3) with MLL/HRX; translocation t(10;16)(q22;p13) with MYST4/MORF. MYST3-CREBBP may induce leukemia by inhibiting RUNX1-mediated transcription. DISEASE: Defects in CREBBP are a cause of Rubinstein-Taybi syndrome type 1 (RSTS1) [MIM:180849]. RSTS1 is an autosomal dominant disorder characterized by craniofacial abnormalities, broad thumbs, broad big toes, mental retardation and a propensity for development of malignancies. SIMILARITY: Contains 1 bromo domain. SIMILARITY: Contains 1 KIX domain. SIMILARITY: Contains 2 TAZ-type zinc fingers. SIMILARITY: Contains 1 ZZ-type zinc finger. WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/CBPID42.html"; WEB RESOURCE: Name=GeneReviews; URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/CREBBP"; WEB RESOURCE: Name=Wikipedia; Note=P300/CBP entry; URL="http://en.wikipedia.org/wiki/P300/CBP"; GENE SYNONYMS: CBP. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-136 |
SUBCELLULAR LOCATION: Lysosome membrane. SIMILARITY: Belongs to the CCZ1 family. GENE SYNONYMS: C7orf28A. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-148 |
SEQUENCE CAUTION: Sequence=BAB71418.1; Type=Erroneous initiation; COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-150 |
FUNCTION: Important role in the capacity of milk to transport calcium phosphate. FUNCTION: Casoxin D acts as opioid antagonist and has vasorelaxing activity mediated by bradykinin B1 receptors. SUBUNIT: Heteromultimers of alpha-s1 casein and kappa-casein; disulfide-linked. SUBCELLULAR LOCATION: Secreted. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=P47710-1; Sequence=Displayed; Name=2; IsoId=P47710-2; Sequence=VSP_000795; Name=3; IsoId=P47710-3; Sequence=VSP_000796; TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk. PTM: Not glycosylated. MISCELLANEOUS: In milk, the alpha s1- and beta-caseins precipitate in presence of calcium (so-called calcium-sensitive caseins). Kappa-casein prevents the precipitation of the other caseins by calcium through the formation of large stable colloidal particles termed micelles. SIMILARITY: Belongs to the alpha-casein family. WEB RESOURCE: Name=Protein Spotlight; Note=Of buttons, digestion and glue - Issue 16 of November 2001; URL="http://web.expasy.org/spotlight/back_issues/sptlt016.shtml"; GENE SYNONYMS: CASA CSN1. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-156 |
FUNCTION: Regulator of EGFR mediated signal transduction. SUBUNIT: Interacts with a restricted range of SH3 domain proteins. SUBCELLULAR LOCATION: Nucleus (Potential). ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=Long; IsoId=Q9ULV8-1; Sequence=Displayed; Name=Short; IsoId=Q9ULV8-2; Sequence=VSP_005732; TISSUE SPECIFICITY: Ubiquitous. DOMAIN: The N-terminus is composed of the phosphotyrosine binding (PTB) domain, a short linker region and the RING-type zinc finger. The PTB domain, which is also called TKB (tyrosine kinase binding) domain, is composed of three different subdomains: a four-helix bundle (4H), a calcium-binding EF hand and a divergent SH2 domain. DOMAIN: The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme (By similarity). PTM: Phosphorylated on tyrosines by EGFR. MISCELLANEOUS: This protein has one functional calcium-binding site (By similarity). SIMILARITY: Contains 1 Cbl-PTB (Cbl-type phosphotyrosine-binding) domain. SIMILARITY: Contains 1 RING-type zinc finger. WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/CBLcID194.html"; GENE SYNONYMS: CBL3 RNF57. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
FUNCTION: Regulator of EGFR mediated signal transduction. SUBUNIT: Interacts with a restricted range of SH3 domain proteins. SUBCELLULAR LOCATION: Nucleus (Potential). ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=Long; IsoId=Q9ULV8-1; Sequence=Displayed; Name=Short; IsoId=Q9ULV8-2; Sequence=VSP_005732; TISSUE SPECIFICITY: Ubiquitous. DOMAIN: The N-terminus is composed of the phosphotyrosine binding (PTB) domain, a short linker region and the RING-type zinc finger. The PTB domain, which is also called TKB (tyrosine kinase binding) domain, is composed of three different subdomains: a four-helix bundle (4H), a calcium-binding EF hand and a divergent SH2 domain. DOMAIN: The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme (By similarity). PTM: Phosphorylated on tyrosines by EGFR. MISCELLANEOUS: This protein has one functional calcium-binding site (By similarity). SIMILARITY: Contains 1 Cbl-PTB (Cbl-type phosphotyrosine-binding) domain. SIMILARITY: Contains 1 RING-type zinc finger. WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/CBLcID194.html"; GENE SYNONYMS: CBL3 RNF57. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-172 |
FUNCTION: This protein may be involved in the regulation of B-cell activation and proliferation. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Expressed on B-cells. PTM: Phosphorylated. Might be functionally regulated by protein kinase(s). DISEASE: Defects in MS4A1 are the cause of immunodeficiency common variable type 5 (CVID5) [MIM:613495]; also called antibody deficiency due to CD20 defect. CVID5 is a primary immunodeficiency characterized by antibody deficiency, hypogammaglobulinemia, recurrent bacterial infections and an inability to mount an antibody response to antigen. The defect results from a failure of B-cell differentiation and impaired secretion of immunoglobulins; the numbers of circulating B cells is usually in the normal range, but can be low. PHARMACEUTICAL: Monoclonal antibodies (mAb) against CD20 are used to treat B-cell non-Hodgkin lymphoma (NHL). These antibodies include Rituximab (Mabthera), Britumomab (Zevalin) and Tositumomab (Bexxar). CD20 engaged by mAb can generate transmembrane signals capable of directly controlling cell growth and triggering cell death in certain tumors. Alternatively, mAb can mediate complement-dependent cytotoxicity. SIMILARITY: Belongs to the MS4A family. CAUTION: Epitope 1, mapped in PubMed:16785532, is predicted to be buried in the membrane. Its accessibility to the extracellular space, and thus to antibody recognition, is not explained. WEB RESOURCE: Name=Wikipedia; Note=CD20 entry; URL="http://en.wikipedia.org/wiki/CD20"; GENE SYNONYMS: CD20. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-174 |
FUNCTION: May cooperate with MD-1 and TLR4 to mediate the innate immune response to bacterial lipopolysaccharide (LPS) in B-cells. Leads to NF-kappa-B activation. Also involved in the life/death decision of B-cells (By similarity). SUBUNIT: Binds to MD-1. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. TISSUE SPECIFICITY: Expressed mainly on mature peripherical B cells. Detected in spleen, lymph node and appendix. Not detected in pre-B and -T cells. SIMILARITY: Belongs to the Toll-like receptor family. SIMILARITY: Contains 19 LRR (leucine-rich) repeats. SIMILARITY: Contains 1 LRRCT domain. GENE SYNONYMS: LY64 RP105. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-176 |
FUNCTION: May be similar to that of authentic calmodulin and may actually compete with calmodulin by binding, with different affinities, to cellular substrates. TISSUE SPECIFICITY: Expressed in normal mammary, prostate, cervical, and epidermal tissues. It is greatly reduced or undetectable in transformed cells. INDUCTION: By TGFB1. MISCELLANEOUS: Binds four calcium ions. SIMILARITY: Belongs to the calmodulin family. SIMILARITY: Contains 4 EF-hand domains. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-182 |
CAUTION: It is uncertain whether Met-1 or Met-18 is the initiator. SEQUENCE CAUTION: Sequence=BAD96381.1; Type=Erroneous initiation; COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-190 |
FUNCTION: C/EBP are DNA-binding proteins that recognize two different motifs: the CCAAT homology common to many promoters and the enhanced core homology common to many enhancers. SUBUNIT: Binds DNA as a dimer and can form stable heterodimers with C/EBP delta. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Strongest expression occurs in promyelocyte and late-myeloblast-like cell lines. PTM: Phosphorylated. SIMILARITY: Belongs to the bZIP family. C/EBP subfamily. SIMILARITY: Contains 1 bZIP domain. SEQUENCE CAUTION: Sequence=AAC51130.1; Type=Frameshift; Positions=4; WEB RESOURCE: Name=CEBPEbase; Note=CEBPE mutation db; URL="http://bioinf.uta.fi/CEBPEbase/"; COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-192 |
FUNCTION: Factor D cleaves factor B when the latter is complexed with factor C3b, activating the C3bbb complex, which then becomes the C3 convertase of the alternate pathway. Its function is homologous to that of C1s in the classical pathway. CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Lys bond in complement factor B when in complex with complement subcomponent C3b or with cobra venom factor. SUBCELLULAR LOCATION: Secreted. DISEASE: Defects in CFD are the cause of complement factor D deficiency (CFD deficiency) [MIM:134350]. CFD deficiency predisposes to invasive meningococcal disease. SIMILARITY: Belongs to the peptidase S1 family. SIMILARITY: Contains 1 peptidase S1 domain. SEQUENCE CAUTION: Sequence=AAA35527.1; Type=Erroneous initiation; WEB RESOURCE: Name=CFDbase; Note=CFD mutation db; URL="http://bioinf.uta.fi/CFDbase/"; GENE SYNONYMS: DF PFD. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-196 |
SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton (Probable). Note=May be a cytoskeletal protein. TISSUE SPECIFICITY: Ubiquitously expressed. DOMAIN: The protein has mostly an alpha helical conformation similar to myosin heavy-chain tail that might adopt a coiled-coil conformation. DISEASE: Defects in CCDC6 are a cause of thyroid papillary carcinoma (TPC) [MIM:188550]. TPC is a common tumor of the thyroid that typically arises as an irregular, solid or cystic mass from otherwise normal thyroid tissue. Papillary carcinomas are malignant neoplasm characterized by the formation of numerous, irregular, finger-like projections of fibrous stroma that is covered with a surface layer of neoplastic epithelial cells. Note=A chromosomal aberration involving CCDC6 is found in thyroid papillary carcinomas. Inversion inv(10)(q11.2;q21) generates the RET/CCDC6 (PTC1) oncogene. SEQUENCE CAUTION: Sequence=AAC60637.1; Type=Frameshift; Positions=456; WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/H4ID280.html"; GENE SYNONYMS: D10S170 TST1. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-200 |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, centrosome. Cytoplasm, cytoskeleton, spindle pole. PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. GENE SYNONYMS: CCDC45 CEP45. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-204 |
FUNCTION: Required for normal spindle assembly. Plays a role in DNA damage response: following DNA double strand breaks (DSBs), it is delocalized from centrosomes, leading to inactivate spindle assembly and delay mitotic progression (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, centrosome. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=Q96MT8-1; Sequence=Displayed; Name=2; IsoId=Q96MT8-2; Sequence=VSP_012252; Name=3; IsoId=Q96MT8-3; Sequence=VSP_012251, VSP_012252; Name=4; IsoId=Q96MT8-4; Sequence=VSP_012251, VSP_012253, VSP_012254; SIMILARITY: Belongs to the CEP63 family. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-206 |
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (Potential). ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9NWD8-1; Sequence=Displayed; Name=2; IsoId=Q9NWD8-2; Sequence=VSP_026736, VSP_026737; Note=No experimental confirmation available; SIMILARITY: Belongs to the UPF0458 family. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-210 |
FUNCTION: Factor B which is part of the alternate pathway of the complement system is cleaved by factor D into 2 fragments: Ba and Bb. Bb, a serine protease, then combines with complement factor 3b to generate the C3 or C5 convertase. It has also been implicated in proliferation and differentiation of preactivated B- lymphocytes, rapid spreading of peripheral blood monocytes, stimulation of lymphocyte blastogenesis and lysis of erythrocytes. Ba inhibits the proliferation of preactivated B-lymphocytes. CATALYTIC ACTIVITY: Cleavage of Arg-|-Ser bond in complement component C3 alpha-chain to yield C3a and C3b, and Arg-|-Xaa bond in complement component C5 alpha-chain to yield C5a and C5b. SUBUNIT: Monomer. SUBCELLULAR LOCATION: Secreted. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P00751-1; Sequence=Displayed; Name=2; IsoId=P00751-2; Sequence=VSP_005380, VSP_005381; POLYMORPHISM: Two major variants, F and S, and 2 minor variants, as well as at least 14 very rare variants, have been identified. The variants His-9 and Gln-32 are associated with a reduced risk of age-related macular degeneration (ARMD) [MIM:603075]. ARMD is a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. DISEASE: Defects in CFB are a cause of susceptibility to hemolytic uremic syndrome atypical type 4 (AHUS4) [MIM:612924]. An atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease. Note=Susceptibility to the development of atypical hemolytic uremic syndrome can be conferred by mutations in various components of or regulatory factors in the complement cascade system. Other genes may play a role in modifying the phenotype. SIMILARITY: Belongs to the peptidase S1 family. SIMILARITY: Contains 1 peptidase S1 domain. SIMILARITY: Contains 3 Sushi (CCP/SCR) domains. SIMILARITY: Contains 1 VWFA domain. WEB RESOURCE: Name=GeneReviews; URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/CFB"; WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/bf/"; GENE SYNONYMS: BF BFD. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-212 |
FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. SUBUNIT: Heterodimer of an alpha and a beta subunit. Interacts with S100A (By similarity). Component of the WASH complex, composed of F-actin-capping protein subunit alpha (CAPZA1, CAPZA2 or CAPZA3), F-actin-capping protein subunit beta (CAPZB), WASH (WASH1, WASH2P, WASH3P, WASH4P, WASH5P or WASH6P), FAM21 (FAM21A, FAM21B or FAM21C), KIAA1033, KIAA0196 and CCDC53. Interacts with S100B. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity). SIMILARITY: Belongs to the F-actin-capping protein alpha subunit family. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-214 |
ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q8IYX3-1; Sequence=Displayed; Name=2; IsoId=Q8IYX3-2; Sequence=VSP_021175; Note=No experimental confirmation available; COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-222 |
FUNCTION: Identifies cytotoxic/suppressor T-cells that interact with MHC class I bearing targets. CD8 is thought to play a role in the process of T-cell mediated killing. SUBUNIT: In general heterodimer of an alpha and a beta chain linked by two disulfide bonds. SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I membrane protein (Probable). SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Single-pass type I membrane protein (Probable). SUBCELLULAR LOCATION: Isoform 3: Secreted (Probable). SUBCELLULAR LOCATION: Isoform 4: Cell membrane; Single-pass type I membrane protein (Probable). SUBCELLULAR LOCATION: Isoform 5: Cell membrane; Single-pass type I membrane protein (Probable). SUBCELLULAR LOCATION: Isoform 6: Secreted (Probable). SUBCELLULAR LOCATION: Isoform 7: Secreted (Probable). SUBCELLULAR LOCATION: Isoform 8: Secreted (Probable). ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=8; Name=1; Synonyms=M-1, Mbeta1; IsoId=P10966-1; Sequence=Displayed; Name=2; Synonyms=M-3, Mbeta2; IsoId=P10966-2; Sequence=VSP_002490; Name=3; Synonyms=S-1, Sbeta3; IsoId=P10966-3; Sequence=VSP_002492, VSP_002493; Name=4; Synonyms=M-2; IsoId=P10966-4; Sequence=VSP_002491; Name=5; Synonyms=Mbeta3; IsoId=P10966-6; Sequence=VSP_002493; Note=Ref.6 (AAI00915) sequence is in conflict in position: 213:I->V; Name=6; Synonyms=Sbeta1; IsoId=P10966-7; Sequence=VSP_002492; Name=7; Synonyms=Sbeta4; IsoId=P10966-8; Sequence=VSP_039654; Name=8; Synonyms=Sbeta5; IsoId=P10966-9; Sequence=VSP_039655; TISSUE SPECIFICITY: Isoform 1, isoform 3, isoform 5, isoform 6, isoform 7 and isoform 8 are expressed in both thymus and peripheral CD8+ T-cells. Expression of isoform 1 is higher in thymus CD8+ T-cells than in peripheral CD8+ T-cells. Expression of isoform 6 is higher in peripheral CD8+ T-cells than in thymus CD8+ T-cells. PTM: Phosphorylated as a consequence of T-cell activation (Potential). SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like) domain. SEQUENCE CAUTION: Sequence=AAD13877.1; Type=Erroneous gene model prediction; WEB RESOURCE: Name=Wikipedia; Note=CD8 entry; URL="http://en.wikipedia.org/wiki/CD8"; GENE SYNONYMS: CD8B1. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-230 |
FUNCTION: May be involved in gametogenesis (By similarity). ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q8TC57-1; Sequence=Displayed; Name=2; IsoId=Q8TC57-2; Sequence=VSP_035293, VSP_035294; Note=No experimental confirmation available; Name=3; IsoId=Q8TC57-3; Sequence=VSP_035291, VSP_035292; Note=No experimental confirmation available; COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-234 |
FUNCTION: Plays a fundamental role in microtubule-organizing center structure and function. SUBUNIT: Monomer (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, centrosome. Note=Centrosome of interphase and mitotic cells. SIMILARITY: Belongs to the centrin family. SIMILARITY: Contains 4 EF-hand domains. GENE SYNONYMS: CEN3. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-238 |
FUNCTION: Complex that is thought to mediate chromatin assembly in DNA replication and DNA repair. Assembles histone octamers onto replicating DNA in vitro. CAF-1 performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer. The CCR4-NOT complex functions as general transcription regulation complex. SUBUNIT: Subunit of the CAF-1 complex that contains RBBP4, CHAF1B and CHAF1A. CHAF1A binds directly to CHAF1B. Only minor amounts of RBBP4 are complexed with CHAF1A and CHAF1B in G1 phase. In G2 and S phase also monomeric CHAF1B is detected. Subunit of the CCR4-NOT core complex that contains CHAF1A, CHAF1B, CNOT1, CNOT2, CNOT3, CNOT4, CNOT6 and CNOT8. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=DNA replication foci. Cytoplasmic in M phase. DEVELOPMENTAL STAGE: Active complex is found in G1, S and G2 phases. PTM: Differentially phosphorylated during cell cycle. During mitosis the p60 subunit of inactive CAF-1 is hyperphosphorylated and displaced into the cytosol. Progressivly dephosphorylated from G1 to S and G2 phase. Phosphorylated p60 is recruited to chromatin undergoing DNA repair after UV irradiation in G1, S or G2 phases. SIMILARITY: Belongs to the WD repeat HIR1 family. SIMILARITY: Contains 7 WD repeats. GENE SYNONYMS: CAF1A CAF1P60 MPHOSPH7 MPP7. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-250 |
FUNCTION: Monokine with inflammatory and chemokinetic properties. Binds to CCR5. One of the major HIV-suppressive factors produced by CD8+ T-cells. Recombinant MIP-1-beta induces a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV). The processed form MIP-1-beta(3-69) retains the abilities to induce down-modulation of surface expression of the chemokine receptor CCR5 and to inhibit the CCR5- mediated entry of HIV-1 in T-cells. MIP-1-beta(3-69) is also a ligand for CCR1 and CCR2 isoform B. SUBUNIT: Homodimer and heterodimer of MIP-1-alpha(4-69) and MIP-1- beta(3-69). SUBCELLULAR LOCATION: Secreted. INDUCTION: By mitogens. PTM: N-terminal processed form MIP-1-beta(3-69) is produced by proteolytic cleavage after secretion from peripheral blood lymphocytes. SIMILARITY: Belongs to the intercrine beta (chemokine CC) family. CAUTION: Was originally (PubMed:9521068) thought to be a ligand for CCR8. WEB RESOURCE: Name=Wikipedia; Note=Macrophage inflammatory protein entry; URL="http://en.wikipedia.org/wiki/Macrophage_Inflammatory_Protein"; GENE SYNONYMS: LAG1 MIP1B SCYA4. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-252 |
FUNCTION: Able to inhibit growth in several cell lines (By similarity). SIMILARITY: Contains 1 RING-type zinc finger. GENE SYNONYMS: CGR19 RNF197. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-266 |
FUNCTION: Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis. CATALYTIC ACTIVITY: Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides. SUBUNIT: Dimer of a heavy chain and a light chain cross-linked by a disulfide bond. Interacts with SRPX2. SUBCELLULAR LOCATION: Lysosome. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. SIMILARITY: Belongs to the peptidase C1 family. WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/CTSBID40202ch8p23.html"; GENE SYNONYMS: CPSB. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-268 |
FUNCTION: Chemotactic factor for T-lymphocytes but not monocytes or granulocytes. May play a role in T-cell development in thymus and in trafficking and activation of mature T-cells. Binds to CCR4. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Expressed at high levels in thymus and at low levels in the lung, colon and small intestine. INDUCTION: By phytohemagglutinin (PHA) in the peripheral blood mononuclear cells and by cytokines in monocytes. SIMILARITY: Belongs to the intercrine beta (chemokine CC) family. CAUTION: Was originally (PubMed:9521068) thought to be a ligand for CCR8. WEB RESOURCE: Name=Wikipedia; Note=CCL17 entry; URL="http://en.wikipedia.org/wiki/CCL17"; GENE SYNONYMS: SCYA17 TARC. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-270 |
CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=Q15131-1; Sequence=Displayed; Name=2; IsoId=Q15131-2; Sequence=VSP_021642; Note=No experimental confirmation available; Name=3; IsoId=Q15131-3; Sequence=VSP_021642, VSP_021643; Name=4; IsoId=Q15131-4; Sequence=VSP_021642, VSP_021644; SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. SIMILARITY: Contains 1 protein kinase domain. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-276 |
FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. CATALYTIC ACTIVITY: Broad endopeptidase specificity. COFACTOR: Binds 3 calcium ions. ENZYME REGULATION: Activated by micromolar concentrations of calcium and inhibited by calpastatin. SUBUNIT: Forms a heterodimer with a small (regulatory) subunit (CAPNS1). SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane (By similarity). Note=Translocates to the plasma membrane upon Ca(2+) binding (By similarity). TISSUE SPECIFICITY: Ubiquitous. SIMILARITY: Belongs to the peptidase C2 family. SIMILARITY: Contains 1 calpain catalytic domain. SIMILARITY: Contains 4 EF-hand domains. WEB RESOURCE: Name=CaBP; Note=Calpain; URL="http://structbio.vanderbilt.edu/cabp_database/general/prot_pages/calpain.html"; WEB RESOURCE: Name=Calpains homepage; URL="http://ag.arizona.edu/calpains/"; WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/capn1/"; GENE SYNONYMS: CANPL1. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. CATALYTIC ACTIVITY: Broad endopeptidase specificity. COFACTOR: Binds 3 calcium ions. ENZYME REGULATION: Activated by micromolar concentrations of calcium and inhibited by calpastatin. SUBUNIT: Forms a heterodimer with a small (regulatory) subunit (CAPNS1). SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane (By similarity). Note=Translocates to the plasma membrane upon Ca(2+) binding (By similarity). TISSUE SPECIFICITY: Ubiquitous. SIMILARITY: Belongs to the peptidase C2 family. SIMILARITY: Contains 1 calpain catalytic domain. SIMILARITY: Contains 4 EF-hand domains. WEB RESOURCE: Name=CaBP; Note=Calpain; URL="http://structbio.vanderbilt.edu/cabp_database/general/prot_pages/calpain.html"; WEB RESOURCE: Name=Calpains homepage; URL="http://ag.arizona.edu/calpains/"; WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/capn1/"; GENE SYNONYMS: CANPL1. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-278 |
FUNCTION: Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Expressed in bone marrow and testis and neutrophils. PTM: The N-terminus is blocked. SIMILARITY: Belongs to the cathelicidin family. CAUTION: PubMed:11238224 sequence was incorrectly assigned to originate from M.mulatta. GENE SYNONYMS: CAP18 FALL39. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-284 |
FUNCTION: Mediates B-cell B-cell interactions. May be involved in the localization of B-cells in lymphoid tissues. Binds sialylated glycoproteins; one of which is CD45. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site can be masked by cis interactions with sialic acids on the same cell surface. Upon ligand induced tyrosine phosphorylation in the immune response seems to be involved in regulation of B-cell antigen receptor signaling. Plays a role in positive regulation through interaction with Src family tyrosine kinases and may also act as an inhibitory receptor by recruiting cytoplasmic phosphatases via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules. SUBUNIT: Predominantly monomer of isoform CD22-beta. Also found as heterodimer of isoform CD22-beta and a shorter isoform. Interacts with PTPN6/SHP-1, LYN, SYK, PIK3R1/PIK3R2 and PLCG1 upon phosphorylation. Interacts with GRB2, INPP5D and SHC1 upon phosphorylation (By similarity). May form a complex with INPP5D/SHIP, GRB2 and SHC1. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Comment=Additional isoforms seem to exist; Name=CD22-beta; IsoId=P20273-1; Sequence=Displayed; Name=CD22-alpha; IsoId=P20273-2; Sequence=VSP_002531; TISSUE SPECIFICITY: B-lymphocytes. DOMAIN: Contains 4 copies of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2- containing phosphatases. PTM: Phosphorylation of Tyr-762, Tyr-807 and Tyr-822 are involved in binding to SYK, GRB2 and SYK, respectively. Phosphorylation of Tyr-842 is involved in binding to SYK, PLCG2 and PIK3R1/PIK3R2. PTM: Phosphorylated on tyrosine residues by LYN (By similarity). SIMILARITY: Belongs to the immunoglobulin superfamily. SIGLEC (sialic acid binding Ig-like lectin) family. SIMILARITY: Contains 6 Ig-like C2-type (immunoglobulin-like) domains. SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like) domain. SEQUENCE CAUTION: Sequence=CAA36988.1; Type=Frameshift; Positions=806; WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding; Note=Siglec-2 [3 Fc Domains]; URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Itlect_00001"; WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding; Note=Siglec-2; URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Itlect_269"; GENE SYNONYMS: SIGLEC2. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-288 |
FUNCTION: Involved in the transport of chloride ions. May regulate bicarbonate secretion and salvage in epithelial cells by regulating the SLC4A7 transporter. CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. SUBUNIT: Interacts with SHANK2 (By similarity). Interacts with SLC9A3R1, MYO6 and GOPC. Interacts with SLC4A7 through SLC9A3R1. Found in a complex with MYO5B and RAB11A. SUBCELLULAR LOCATION: Early endosome membrane; Multi-pass membrane protein. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=P13569-1; Sequence=Displayed; Name=2; IsoId=P13569-2; Sequence=VSP_022123; Note=Exon skipping favored by a high number of TG repeats and a low number of T repeats at the intron-exon boundary. Causes congenital bilateral absence of the vas deferens (CBAVD); Name=3; IsoId=P13569-3; Sequence=VSP_022124, VSP_022125; Note=Alternative acceptor site favored by mutation in an exonic splicing enhancer (ESE). Causes cystic fibrosis (CF); TISSUE SPECIFICITY: Found on the surface of the epithelial cells that line the lungs and other organs. DOMAIN: The PDZ-binding motif mediates interactions with GOPC and with the SLC4A7, SLC9A3R1/EBP50 complex. PTM: Phosphorylated; activates the channel. It is not clear whether PKC phosphorylation itself activates the channel or permits activation by phosphorylation at PKA sites. PTM: Ubiquitinated, leading to its degradation in the lysosome. Deubiquitination by USP10 in early endosomes, enhances its endocytic recycling. DISEASE: Defects in CFTR are the cause of cystic fibrosis (CF) [MIM:219700]; also known as mucoviscidosis. CF is the most common genetic disease in the Caucasian population, with a prevalence of about 1 in 2'000 live births. Inheritance is autosomal recessive. CF is a common generalized disorder of exocrine gland function which impairs clearance of secretions in a variety of organs. It is characterized by the triad of chronic bronchopulmonary disease (with recurrent respiratory infections), pancreatic insufficiency (which leads to malabsorption and growth retardation) and elevated sweat electrolytes. DISEASE: Defects in CFTR are the cause of congenital bilateral absence of the vas deferens (CBAVD) [MIM:277180]. CBAVD is an important cause of sterility in men and could represent an incomplete form of cystic fibrosis, as the majority of men suffering from cystic fibrosis lack the vas deferens. SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family. CFTR transporter (TC 3.A.1.202) subfamily. SIMILARITY: Contains 2 ABC transmembrane type-1 domains. SIMILARITY: Contains 2 ABC transporter domains. WEB RESOURCE: Name=CFTR; Note=Cystic fibrosis mutation db; URL="http://www.genet.sickkids.on.ca/cftr/app"; WEB RESOURCE: Name=GeneReviews; URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/CFTR"; WEB RESOURCE: Name=Wikipedia; Note=CFTR entry; URL="http://en.wikipedia.org/wiki/Cystic_fibrosis_transmembrane_conductance_regulator"; GENE SYNONYMS: ABCC7. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-300 |
FUNCTION: Plays a role in mitotic exit and cytokinesis. Not required for microtubule nucleation. Recruits PDCD6IP and TSG101 to midbody during cytokinesis. SUBUNIT: Homodimer. Interacts (phosphorylated on Ser-425 and Ser- 428) with PLK1. Interacts with AKAP9; the interaction occurs in interphase and is lost upon mitotic entry. Interacts with PCNT; the interaction occurs in interphase and is lost upon mitotic entry. Interacts with PDCD6IP; the interaction is direct; CEP55 binds PDCD6IP in a 2:1 stoechiometry; PDCD6IP competes with TSG101 for the same binding site. Interacts with TSG101; TSG101 competes with PDCD6IP for the same binding site; interaction is required for cytokinesis but not for viral budding. Interacts with FAM125A, VPS37B, VPS37C and VPS28. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, centrosome, centriole. Cytoplasm, cytoskeleton, centrosome. Cleavage furrow. Midbody. Note=Present at the centrosomes at interphase. A small portion is associated preferentially with the mother centriole, whereas the majority localizes to the pericentriolar material. During mitosis, loss of affinity for the centrosome at the onset of prophase and diffusion throughout the cell. This dissociation from the centrosome is phosphorylation-dependent. May remain localized at the centrosome during mitosis in certain cell types. Appears at the cleavage furrow in late anaphase and in the midbody in cytokinesis. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q53EZ4-1; Sequence=Displayed; Name=2; IsoId=Q53EZ4-2; Sequence=VSP_014750, VSP_014751; Note=No experimental confirmation available; TISSUE SPECIFICITY: Widely expressed, mostly in proliferative tissues. Highly expressed in testis. Intermediate levels in adult and fetal thymus, as well as in various cancer cell lines. Low levels in different parts of the digestive tract, bone marrow, lymph nodes, placenta, fetal heart and fetal spleen. Hardly detected in brain. PTM: There is a hierachy of phosphorylation, where both Ser-425 and Ser-428 are phosphorylated at the onset of mitosis, prior to Ser-436. Phosphorylation at Ser-425 and Ser-428 is required for dissociation from the centrosome at the G2/M boundary. Phosphorylation at the 3 sites, Ser-425, Ser-428 and Ser-436, is required for protein function at the final stages of cell division to complete cytokinesis successfully. SEQUENCE CAUTION: Sequence=BAA91670.1; Type=Erroneous initiation; Note=Translation N-terminally extended; GENE SYNONYMS: C10orf3 URCC6. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-302 |
FUNCTION: Has low NADPH-dependent oxidoreductase activity towards 4-benzoylpyridine and menadione (in vitro). CATALYTIC ACTIVITY: R-CHOH-R' + NADP(+) = R-CO-R' + NADPH. BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=25 uM for menadione (PubMed:15537833); KM=43 uM for menadione (PubMed:18493841); KM=90 uM for NADPH (PubMed:15537833); KM=38 uM for NADPH (PubMed:18493841); pH dependence: Optimum pH is 5.5-7; SUBCELLULAR LOCATION: Cytoplasm. TISSUE SPECIFICITY: Detected in ovary, pancreas, intestine, colon, kidney, brain, thymus, lung, heart, liver, spleen, leukocyte, prostate and testis. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family. WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/cbr3/"; COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-308 |
ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=5; Name=1; IsoId=Q8N5R6-1; Sequence=Displayed; Name=2; IsoId=Q8N5R6-2; Sequence=VSP_028757, VSP_028758; Name=4; IsoId=Q8N5R6-4; Sequence=VSP_028755, VSP_028756, VSP_028759; Name=5; IsoId=Q8N5R6-5; Sequence=VSP_028755, VSP_028756, VSP_028757, VSP_028759; Name=6; IsoId=Q8N5R6-6; Sequence=VSP_040258, VSP_040259; SIMILARITY: Contains 1 C2 domain. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-316 |
FUNCTION: Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. CATALYTIC ACTIVITY: 4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O. COFACTOR: Binds 6 copper ions per monomer. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. DISEASE: Defects in CP are the cause of aceruloplasminemia (ACERULOP) [MIM:604290]. It is an autosomal recessive disorder of iron metabolism characterized by iron accumulation in the brain as well as visceral organs. Clinical features consist of the triad of retinal degeneration, diabetes mellitus and neurological disturbances. DISEASE: Note=Ceruloplasmin levels are decreased in Wilson disease, in which copper cannot be incorporated into ceruloplasmin in liver because of defects in the copper-transporting ATPase 2. SIMILARITY: Belongs to the multicopper oxidase family. SIMILARITY: Contains 3 F5/8 type A domains. SIMILARITY: Contains 6 plastocyanin-like domains. WEB RESOURCE: Name=GeneReviews; URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/CP"; WEB RESOURCE: Name=Wikipedia; Note=Ceruloplasmin entry; URL="http://en.wikipedia.org/wiki/Ceruloplasmin"; COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-324 |
FUNCTION: Inhibits hemopoiesis and stimulates chemotaxis. Chemotactic in vitro for thymocytes and activated T-cells, but not for B-cells, macrophages, or neutrophils. Shows preferential activity towards naive T-cells. May play a role in mediating homing of lymphocytes to secondary lymphoid organs. SUBUNIT: Binds to CCR7. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Highly expressed in high endothelial venules of lymph nodes, spleen and appendix. Intermediate levels found in small intestine, thyroid gland and trachea. Low level expression in thymus, bone marrow, liver, and pancreas. Also found in tonsil, fetal heart and fetal spleen. SIMILARITY: Belongs to the intercrine beta (chemokine CC) family. WEB RESOURCE: Name=Wikipedia; Note=CCL21 entry; URL="http://en.wikipedia.org/wiki/CCL21"; GENE SYNONYMS: SCYA21. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-326 |
FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Required for chromosome congression and efficiently align the chromosomes on a metaphase plate. SUBUNIT: Self-associates. Component of the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and MLF1IP/CENPU. The CENPA-NAC complex interacts with the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. Interacts directly with CENPK. Interacts with KIF2C and NDC80. Interacts with TRIM36 (By similarity). SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore. Note=Associates with active centromere-kinetochore complexes throughout the cell cycle. Colocalizes with inner kinetochore plate proteins CENPA and CENPC1 during both interphase and metaphase. SIMILARITY: Belongs to the centromere protein H family. GENE SYNONYMS: ICEN35. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-328 |
FUNCTION: Capable of inducing cell cycle arrest in G1 and G2 phases. Acts as a tumor suppressor. Binds to MDM2 and blocks its nucleocytoplasmic shuttling by sequestering it in the nucleolus. This inhibits the oncogenic action of MDM2 by blocking MDM2- induced degradation of p53 and enhancing p53-dependent transactivation and apoptosis. Also induces G2 arrest and apoptosis in a p53-independent manner by preventing the activation of cyclin B1/CDC2 complexes. Binds to BCL6 and down-regulates BCL6-induced transcriptional repression. Binds to E2F1 and MYC and blocks their transcriptional activator activity but has no effect on MYC transcriptional repression. Binds to TOP1/TOPOI and stimulates its activity. This complex binds to rRNA gene promoters and may play a role in rRNA transcription and/or maturation. Interacts with NPM1/B23 and promotes its polyubiquitination and degradation, thus inhibiting rRNA processing. Interacts with COMMD1 and promotes its 'Lys63'-linked polyubiquitination. Interacts with UBE2I/UBC9 and enhances sumoylation of a number of its binding partners including MDM2 and E2F1. Binds to HUWE1 and represses its ubiquitin ligase activity. May play a role in controlling cell proliferation and apoptosis during mammary gland development. SUBUNIT: Does not interact with cyclins, CDK1, CDK2, CDK4, CDK5 or CDK6. Binds to BCL6, E2F1, HUWE1, MDM2, MYC, NPM1/B23, TOP1/TOPOI and UBE2I/UBC9. Interacts with TBRG1 and COMMD1. Interacts with CDKN2AIP and E4F1. SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=4; Comment=Isoform 1 and isoform 4 arise due to the use of two alternative first exons joined to a common exon 2 at the same acceptor site but in different reading frames, resulting in two completely different isoforms; Name=4; Synonyms=p14ARF, p19ARF, ARF; IsoId=Q8N726-1; Sequence=Displayed; Name=1; Synonyms=p16INK4a; IsoId=P42771-1; Sequence=External; Name=2; IsoId=P42771-2; Sequence=External; Name=3; Synonyms=p12; IsoId=P42771-3; Sequence=External; SEQUENCE CAUTION: Sequence=AAA82236.1; Type=Erroneous initiation; Note=Translation N-terminally extended; Sequence=AAC60649.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/cdkn2a/"; GENE SYNONYMS: CDKN2 MLM. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-332 |
FUNCTION: May have a regulatory bifunctional role. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein (By similarity). SIMILARITY: Belongs to the CAP family. SIMILARITY: Contains 1 C-CAP/cofactor C-like domain. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-338 |
FUNCTION: Antigen-presenting protein that binds self and non-self glycolipids and presents them to T-cell receptors on natural killer T-cells. SUBUNIT: Heterodimer with B2M (beta-2-microglobulin). Interacts with MHC II. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Endosome membrane. Lysosome membrane. Note=Subject to intracellular trafficking between the cell membrane, endosomes and lysosomes. TISSUE SPECIFICITY: Expressed on cortical thymocytes, on certain T-cell leukemias, and in various other tissues. MISCELLANEOUS: During protein synthesis and maturation, CD1 family members bind endogenous lipids that are replaced by lipid or glycolipid antigens when the proteins are internalized and pass through endosomes, before trafficking back to the cell surface (By similarity). SIMILARITY: Contains 1 Ig-like (immunoglobulin-like) domain. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-346 |
FUNCTION: Activates ATF4-mediated transcription. Involved in ciliogenesis (By similarity). Required for the correct localization of ciliary and phototransduction proteins in retinal photoreceptor cells; may play a role in ciliary transport processes. SUBUNIT: Interacts with ATF4 via its N-terminal region. Part of selected centrosomal and microtubule-associated protein complexes. Interacts with CC2D2A. Interacts with IQCB1. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, centrosome. Nucleus. Cell projection, cilium. Note=Connecting cilium of photoreceptor cells, base of cilium in kidney intramedullary collecting duct cells. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O15078-1; Sequence=Displayed; Name=2; IsoId=O15078-2; Sequence=VSP_021027; Note=No experimental confirmation available; TISSUE SPECIFICITY: Ubiquitous. Expressed strongly in placenta and weakly in brain. DISEASE: Defects in CEP290 are a cause of Joubert syndrome type 5 (JBTS5) [MIM:610188]. Joubert syndrome is an autosomal recessive disease characterized by cerebellar vermis hypoplasia with prominent superior cerebellar peduncles (the 'molar tooth sign' on axial magnetic resonance imaging), psychomotor delay, hypotonia, ataxia, oculomotor apraxia and neonatal breathing abnormalities. JBTS5 shares the neurologic and neuroradiologic features of Joubert syndrome together with severe retinal dystrophy and/or progressive renal failure characterized by nephronophthisis. DISEASE: Defects in CEP290 are a cause of Senior-Loken syndrome type 6 (SLSN6) [MIM:610189]. Senior-Loken syndrome is also known as juvenile nephronophthisis with Leber amaurosis. It is an autosomal recessive renal-retinal disorder, characterized by progressive wasting of the filtering unit of the kidney, with or without medullary cystic renal disease, and progressive eye disease. DISEASE: Defects in CEP290 are the cause of Leber congenital amaurosis type 10 (LCA10) [MIM:611755]. LCA designates a clinically and genetically heterogeneous group of childhood retinal degenerations, generally inherited in an autosomal recessive manner. Affected infants have little or no retinal photoreceptor function as tested by electroretinography. LCA represents the most common genetic cause of congenital visual impairment in infants and children. DISEASE: Defects in CEP290 are the cause of Meckel syndrome type 4 (MKS4) [MIM:611134]. MKS4 is an autosomal recessive disorder characterized by a combination of renal cysts and variably associated features including developmental anomalies of the central nervous system (typically encephalocele), hepatic ductal dysplasia and cysts, and polydactyly. DISEASE: Note=Antibodies against CEP290 are present in sera from patients with cutaneous T-cell lymphomas, but not in the healthy control population. DISEASE: Defects in CEP290 are the cause of Bardet-Biedl syndrome type 14 (BBS14) [MIM:209900]. A syndrome characterized by usually severe pigmentary retinopathy, early-onset obesity, polydactyly, hypogenitalism, renal malformation and mental retardation. Secondary features include diabetes mellitus, hypertension and congenital heart disease. Inheritance is autosomal recessive, but three mutated alleles (two at one locus, and a third at a second locus) may be required for disease manifestation in some cases (triallelic inheritance). SEQUENCE CAUTION: Sequence=AAG34904.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence; Sequence=AK023677; Type=Frameshift; Positions=556; Sequence=BAA20828.2; Type=Erroneous initiation; Sequence=BAB15196.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence; WEB RESOURCE: Name=GeneReviews; URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/CEP290"; WEB RESOURCE: Name=CEP290 Mutation Database; URL="http://medgen.ugent.be/cep290base/index.php"; GENE SYNONYMS: BBS14 KIAA0373 NPHP6. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-348 |
FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. PATHWAY: Protein modification; protein ubiquitination. SUBUNIT: The APC/C is composed of at least 12 subunits. Interacts with PPP5C and CDC20. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, centrosome. Cytoplasm, cytoskeleton, spindle. Note=Colocalizes with CDC27 to the centrosome at all stages of the cell cycle and to the mitotic spindle. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q13042-1; Sequence=Displayed; Name=2; IsoId=Q13042-2; Sequence=VSP_008427; Note=No experimental confirmation available; Name=3; IsoId=Q13042-3; Sequence=VSP_008427, VSP_008428; PTM: Phosphorylated. Phosphorylation on Ser-560 occurs specifically during mitosis. SIMILARITY: Belongs to the APC6/CDC16 family. SIMILARITY: Contains 7 TPR repeats. WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/cdc16/"; GENE SYNONYMS: ANAPC6. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. PATHWAY: Protein modification; protein ubiquitination. SUBUNIT: The APC/C is composed of at least 12 subunits. Interacts with PPP5C and CDC20. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, centrosome. Cytoplasm, cytoskeleton, spindle. Note=Colocalizes with CDC27 to the centrosome at all stages of the cell cycle and to the mitotic spindle. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q13042-1; Sequence=Displayed; Name=2; IsoId=Q13042-2; Sequence=VSP_008427; Note=No experimental confirmation available; Name=3; IsoId=Q13042-3; Sequence=VSP_008427, VSP_008428; PTM: Phosphorylated. Phosphorylation on Ser-560 occurs specifically during mitosis. SIMILARITY: Belongs to the APC6/CDC16 family. SIMILARITY: Contains 7 TPR repeats. WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/cdc16/"; GENE SYNONYMS: ANAPC6. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-350 |
FUNCTION: Modulate other receptor-ligand interactions to enhance leukocyte activation. SUBUNIT: Interacts with CD48. Following phosphorylation, it is able to recruit PTPN11/SHP-2 and SH2D1A/SAP. Binding of SH2D1A/SAP to CD244 prevents its association with PTPN11/SHP-2. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein (Potential). ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=4; Name=1; Synonyms=H2B4-B; IsoId=Q9BZW8-1; Sequence=Displayed; Note=No experimental confirmation available; Name=2; Synonyms=H2B4-A; IsoId=Q9BZW8-2; Sequence=VSP_010397; Name=3; Synonyms=H2B4; IsoId=Q9BZW8-3; Sequence=VSP_010397, VSP_010399, VSP_010400; Note=No experimental confirmation available; Name=4; Synonyms=H2B4b; IsoId=Q9BZW8-4; Sequence=VSP_010398; Note=No experimental confirmation available; TISSUE SPECIFICITY: Expressed in spleen, PBL, followed by lung, liver, testis and small intestine. Expressed not only in NK cells, but also on monocytes and basophils. SIMILARITY: Contains 2 Ig-like (immunoglobulin-like) domains. GENE SYNONYMS: 2B4. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-352 |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, centrosome. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q5JTW2-1; Sequence=Displayed; Name=2; IsoId=Q5JTW2-2; Sequence=VSP_026321, VSP_026322, VSP_026323; Note=No experimental confirmation available; Name=3; IsoId=Q5JTW2-3; Sequence=VSP_026322; Note=Gene prediction based on EST data. No experimental confirmation available; SIMILARITY: Belongs to the CEP78 family. SEQUENCE CAUTION: Sequence=AAH91515.1; Type=Erroneous initiation; Note=Translation N-terminally extended; Sequence=AAH91515.1; Type=Miscellaneous discrepancy; Note=Probable intron retention; Sequence=CAI40238.1; Type=Erroneous gene model prediction; Sequence=CAI40239.1; Type=Erroneous gene model prediction; GENE SYNONYMS: C9orf81. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-354 |
FUNCTION: Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin-T1) complex, also called positive transcription elongation factor B (P-TEFb), which is proposed to facilitate the transition from abortive to productive elongation by phosphorylating the CTD (carboxy-terminal domain) of the large subunit of RNA polymerase II (RNA Pol II). In case of HIV or SIV infections, binds to the transactivation domain of the viral nuclear transcriptional activator, Tat, thereby increasing Tat's affinity for the transactivating response RNA element (TAR RNA). Serves as an essential cofactor for Tat, by promoting RNA Pol II activation, allowing transcription of viral genes. SUBUNIT: Cyclin-T1 is the predominant cyclin that associates with CDK9 to form a heterodimer called P-TEFb. P-TEFb forms a complex with AFF4/AF5Q31. Interacts with the transactivation region of HIV-1, HIV-2 and SIV Tat. Component of a complex which is at least composed of HTATSF1/Tat-SF1, P-TEFb complex, RNA pol II, SUPT5H, and NCL/nucleolin. Component of the 7SK snRNP complex at least composed of P-TEFb (composed of CDK9 and CCNT1/cyclin-T1), HEXIM1, HEXIM2, BCDIN3, SART3 proteins and 7SK and U6 snRNAs. Interacts with MDFIC. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Ubiquitously expressed. MISCELLANEOUS: Interaction between Tat and cyclin-T1 requires zinc. SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-360 |
SIMILARITY: Belongs to the CDR2 family. SEQUENCE CAUTION: Sequence=AAA51961.1; Type=Frameshift; Positions=379, 384, 393; Sequence=AAB20813.1; Type=Erroneous initiation; Sequence=BAA02360.1; Type=Erroneous initiation; GENE SYNONYMS: PCD17. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-364 |
FUNCTION: May be the important intermediate by which p53/TP53 mediates its role as an inhibitor of cellular proliferation in response to DNA damage. Binds to and inhibits cyclin-dependent kinase activity, preventing phosphorylation of critical cyclin- dependent kinase substrates and blocking cell cycle progression. Functions in the nuclear localization and assembly of cyclin D- CDK4 complex and promotes its kinase activity towards RB1. At higher stoichiometric ratios, inhibits the kinase activity of the cyclin D-CDK4 complex. SUBUNIT: Interacts with MKRN1. Interacts with PSMA3. Interacts with PCNA. Component of the ternary complex, cyclin D-CDK4-CDKN1A. Interacts (via its N-terminal domain) with CDK4; the interaction promotes the assembly of the cyclin D-CDK4 complex, its nuclear translocation and promotes the cyclin D-dependent enzyme activity of CDK4. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. TISSUE SPECIFICITY: Expressed in all adult human tissues, with 5- fold lower levels observed in the brain. INDUCTION: By p53/TP53, mezerein (antileukemic compound) and IFNB1. DOMAIN: The PIP-box K+4 motif mediates both the interaction with PCNA and the recuitment of the DCX(DTL) complex: while the PIP-box interacts with PCNA, the presence of the K+4 submotif, recruits the DCX(DTL) complex, leading to its ubiquitination. DOMAIN: The C-terminal is required for nuclear localization of the cyclin D-CDK4 complex. PTM: Phosphorylation of Thr-145 by Akt or of Ser-146 by PKC impairs binding to PCNA. Phosphorylation at Ser-114 by GSK3-beta enhances ubiquitination by the DCX(DTL) complex. PTM: Ubiquitinated by MKRN1; leading to polyubiquitination and 26S proteasome-dependent degradation. Ubiquitinated by the DCX(DTL) complex, also named CRL4(CDT2) complex, leading to its degradation during S phase or following UV irradiation. Ubiquitination by the DCX(DTL) complex is essential to control replication licensing and is PCNA-dependent: interacts with PCNA via its PIP-box, while the presence of the containing the 'K+4' motif in the PIP box, recruit the DCX(DTL) complex, leading to its degradation. SIMILARITY: Belongs to the CDI family. SEQUENCE CAUTION: Sequence=AAB59559.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; Sequence=AAB59560.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/CDKN1AID139.html"; WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/cdkn1a/"; GENE SYNONYMS: CAP20 CDKN1 CIP1 MDA6 PIC1 SDI1 WAF1. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
FUNCTION: May be the important intermediate by which p53/TP53 mediates its role as an inhibitor of cellular proliferation in response to DNA damage. Binds to and inhibits cyclin-dependent kinase activity, preventing phosphorylation of critical cyclin- dependent kinase substrates and blocking cell cycle progression. Functions in the nuclear localization and assembly of cyclin D- CDK4 complex and promotes its kinase activity towards RB1. At higher stoichiometric ratios, inhibits the kinase activity of the cyclin D-CDK4 complex. SUBUNIT: Interacts with MKRN1. Interacts with PSMA3. Interacts with PCNA. Component of the ternary complex, cyclin D-CDK4-CDKN1A. Interacts (via its N-terminal domain) with CDK4; the interaction promotes the assembly of the cyclin D-CDK4 complex, its nuclear translocation and promotes the cyclin D-dependent enzyme activity of CDK4. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. TISSUE SPECIFICITY: Expressed in all adult human tissues, with 5- fold lower levels observed in the brain. INDUCTION: By p53/TP53, mezerein (antileukemic compound) and IFNB1. DOMAIN: The PIP-box K+4 motif mediates both the interaction with PCNA and the recuitment of the DCX(DTL) complex: while the PIP-box interacts with PCNA, the presence of the K+4 submotif, recruits the DCX(DTL) complex, leading to its ubiquitination. DOMAIN: The C-terminal is required for nuclear localization of the cyclin D-CDK4 complex. PTM: Phosphorylation of Thr-145 by Akt or of Ser-146 by PKC impairs binding to PCNA. Phosphorylation at Ser-114 by GSK3-beta enhances ubiquitination by the DCX(DTL) complex. PTM: Ubiquitinated by MKRN1; leading to polyubiquitination and 26S proteasome-dependent degradation. Ubiquitinated by the DCX(DTL) complex, also named CRL4(CDT2) complex, leading to its degradation during S phase or following UV irradiation. Ubiquitination by the DCX(DTL) complex is essential to control replication licensing and is PCNA-dependent: interacts with PCNA via its PIP-box, while the presence of the containing the 'K+4' motif in the PIP box, recruit the DCX(DTL) complex, leading to its degradation. SIMILARITY: Belongs to the CDI family. SEQUENCE CAUTION: Sequence=AAB59559.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; Sequence=AAB59560.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/CDKN1AID139.html"; WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/cdkn1a/"; GENE SYNONYMS: CAP20 CDKN1 CIP1 MDA6 PIC1 SDI1 WAF1. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-366 |
FUNCTION: Directly regulates filament dynamics and has been implicated in a number of complex developmental and morphological processes, including mRNA localization and the establishment of cell polarity. SUBUNIT: Homodimer. Binds actin monomers. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein (By similarity). ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q01518-1; Sequence=Displayed; Name=2; IsoId=Q01518-2; Sequence=VSP_036038; SIMILARITY: Belongs to the CAP family. SIMILARITY: Contains 1 C-CAP/cofactor C-like domain. GENE SYNONYMS: CAP. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-374 |
FUNCTION: May be either a bona fide (dihydro)ceramide synthase or a modulator of its activity. When overexpressed in cells is involved in the production of sphingolipids containing mainly one fatty acid donor (N-linked stearoyl- (C18) ceramide) in a fumonisin B1-independent manner (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein (By similarity). SUBCELLULAR LOCATION: Isoform 1: Endoplasmic reticulum membrane; Multi-pass membrane protein (By similarity). Golgi apparatus membrane; Multi-pass membrane protein (By similarity). Note=Isoform 1 may recycle from the Golgi to the endoplasmic reticulum. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P27544-1; Sequence=Displayed; Name=2; IsoId=P27544-2; Sequence=VSP_003049; Note=No experimental confirmation available; MISCELLANEOUS: This protein is produced by a bicistronic gene which also produces the GDF1 protein from a non-overlapping reading frame. SIMILARITY: Contains 1 TLC (TRAM/LAG1/CLN8) domain. GENE SYNONYMS: LAG1 LASS1 UOG1. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-376 |
FUNCTION: Cadherins are calcium dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein (Potential). SIMILARITY: Contains 5 cadherin domains. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-384 |
FUNCTION: Appears to play multiple roles in cell cycle progression, cytokinesis and apoptosis. The p110 isoforms have been suggested to be involved in pre-mRNA splicing, potentially by phosphorylating the splicing protein SFRS7. The p58 isoform may act as a negative regulator of normal cell cycle progression. CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. COFACTOR: Magnesium. ENZYME REGULATION: Phosphorylation at Thr-448 or Tyr-449 inactivates the enzyme, while phosphorylation at Thr-595 activates it (By similarity). SUBUNIT: The cleaved p110 isoform, p110C, binds to the serine/threonine kinase PAK1 and RANBP9. p110C interacts with RNPS1. The p58 isoform but not the p110 isoforms or p110C interacts with CCND3. The p110 isoforms are found in large molecular weight complexes containing CCNL1 and SFRS7. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. ALTERNATIVE PRODUCTS: Event=Alternative splicing, Alternative initiation; Named isoforms=10; Name=SV9; Synonyms=p110; IsoId=P21127-1; Sequence=Displayed; Name=SV1; Synonyms=Alpha 2-1; IsoId=P21127-2; Sequence=VSP_008280; Name=2; Synonyms=Alpha 2-2; IsoId=P21127-3; Sequence=VSP_008278, VSP_008279, VSP_008280; Name=3; Synonyms=Alpha 1; IsoId=P21127-4; Sequence=VSP_008276; Name=SV4; IsoId=P21127-5; Sequence=VSP_008275; Name=SV5; IsoId=P21127-6; Sequence=VSP_008273, VSP_008277, VSP_008278, VSP_008280; Name=8; Synonyms=Alpha 2-3; IsoId=P21127-8; Sequence=VSP_008278, VSP_008280; Name=SV10; IsoId=P21127-9; Sequence=VSP_008273, VSP_008277, VSP_008280; Name=SV11; Synonyms=Alpha 2-4; IsoId=P21127-10; Sequence=VSP_008274, VSP_008280; Name=7; Synonyms=p58; IsoId=P21127-12; Sequence=VSP_018834; Note=Produced by alternative initiation at Met-357 of isoform SV9; TISSUE SPECIFICITY: Expressed ubiquitously. Some evidence of isoform-specific tissue distribution. INDUCTION: The p58 isoform is specifically induced in G2/M phase of the cell cycle. PTM: During apoptosis, induced by Fas or tumor necrosis factor, specific CKD11 p110 isoforms are cleaved by caspases to produce a protein (p110C) that contains the C-terminal kinase domain of the CDK11 proteins. PTM: p110C can be autophosphorylated. MISCELLANEOUS: Duplicated gene. CDK11A and CDK11B encode almost identical protein kinases of 110 kDa that contain at their C- termini the open reading frame of a smaller 58 kDa isoform which is expressed following IRES-mediated alternative initiation of translation. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. SIMILARITY: Contains 1 protein kinase domain. CAUTION: Many references talk about 'p110 isoforms' but it is not yet known if this refers to CDK11A and/or CDK11B or one/some of the isoforms of each. SEQUENCE CAUTION: Sequence=AAC83664.1; Type=Erroneous gene model prediction; Sequence=AAF36538.1; Type=Erroneous initiation; GENE SYNONYMS: CDC2L1 CDK11 PITSLREA PK58. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-392 |
FUNCTION: Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also phosphorylates SMAD3 in a cell-cycle-dependent manner and represses its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex. CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. ENZYME REGULATION: Both phosphorylation at Thr-172 and binding of a D-type cyclin are necessary for enzymatic activity. Full activation of the cyclin-D-CDK4 complex appears to require other factors such as recruitment of the substrate via a substrate recruitment motif, and/or formation of the CDKN1B ternary complex. Inhibited by INK4 family members. In resting cells, the non- tyrosine-phosphorylated form of CDKN1B prevents phosphorylation at Thr-172 and inactivation, while, in proliferating cells, tyrosine phosphorylation of CDKN1B allows phosphorylation of Thr-172 of CDK4 and subsequennt activation. SUBUNIT: Component of the D-CDK4 complex, composed of CDK4 and some D-type G1 cyclin (CCND1, CCND2 or CCND3). Interacts directly in the complex with CCND1, CCND2 or CCND3. Interacts with SEI1 and ZNF655. Forms a ternary complex, cyclin D-CDK4-CDKN1B, involved in modulating CDK4 enzymatic activity. Interacts directly with CDKN1B (phosphorylated on 'Tyr-88' and 'Tyr-89'); the interaction allows assembly of the cyclin D-CDK4 complex, Thr-172 phosphorylation, nuclear translocation and enhances the cyclin D-CDK4 complex activity. CDK4 activity is either inhibited or enhanced depending on stoichiometry of complex. The non-tyrosine-phosphorylated form of CDKN1B prevents T-loop phosphosphorylation of CDK4 producing inactive CDK4. Interacts (unphosphorylated form) with CDK2. Also forms ternary complexes with CDKN1A or CDKN2A. Interacts directly with CDKN1A (via its N-terminal); the interaction promotes the assembly of the cyclin D-CDK4 complex, its nuclear translocation and promotes the cyclin D-dependent enzyme activity of CDK4. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Membrane. Note=Cytoplasmic when non-complexed. Forms a cyclin D-CDK4 complex in the cytoplasm as cells progress through G(1) phase. The complex accumulates on the nuclear membrane and enters the nucleus on transition from G(1) to S phase. Also present in nucleoli and heterochromatin lumps. Colocalizes with RB1 after release into the nucleus. PTM: Phosphorylation at Thr-172 is required for enzymatic activity. Phosphorylated, in vitro, at this site by CCNH-CDK7, but, in vivo, appears to be phosphorylated by a proline-directed kinase. In the cyclin D-CDK4-CDKN1B complex, this phosphorylation and consequent CDK4 enzyme activity, is dependent on the tyrosine phosphorylation state of CDKN1B. Thus, in proliferating cells, CDK4 within the complex is phosphorylated on Thr-172 in the T- loop. In resting cells, phosphorylation on Thr-172 is prevented by the non-tyrosine-phosphorylated form of CDKN1B. DISEASE: Defects in CDK4 are a cause of susceptibility to cutaneous malignant melanoma type 3 (CMM3) [MIM:609048]. Malignant melanoma is a malignant neoplasm of melanocytes, arising de novo or from a pre-existing benign nevus, which occurs most often in the skin but also may involve other sites. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. SIMILARITY: Contains 1 protein kinase domain. WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/CDK4ID238ch12q14.html"; WEB RESOURCE: Name=GeneReviews; URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/CDK4"; WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/cdk4/"; COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
FUNCTION: Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also phosphorylates SMAD3 in a cell-cycle-dependent manner and represses its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex. CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. ENZYME REGULATION: Both phosphorylation at Thr-172 and binding of a D-type cyclin are necessary for enzymatic activity. Full activation of the cyclin-D-CDK4 complex appears to require other factors such as recruitment of the substrate via a substrate recruitment motif, and/or formation of the CDKN1B ternary complex. Inhibited by INK4 family members. In resting cells, the non- tyrosine-phosphorylated form of CDKN1B prevents phosphorylation at Thr-172 and inactivation, while, in proliferating cells, tyrosine phosphorylation of CDKN1B allows phosphorylation of Thr-172 of CDK4 and subsequennt activation. SUBUNIT: Component of the D-CDK4 complex, composed of CDK4 and some D-type G1 cyclin (CCND1, CCND2 or CCND3). Interacts directly in the complex with CCND1, CCND2 or CCND3. Interacts with SEI1 and ZNF655. Forms a ternary complex, cyclin D-CDK4-CDKN1B, involved in modulating CDK4 enzymatic activity. Interacts directly with CDKN1B (phosphorylated on 'Tyr-88' and 'Tyr-89'); the interaction allows assembly of the cyclin D-CDK4 complex, Thr-172 phosphorylation, nuclear translocation and enhances the cyclin D-CDK4 complex activity. CDK4 activity is either inhibited or enhanced depending on stoichiometry of complex. The non-tyrosine-phosphorylated form of CDKN1B prevents T-loop phosphosphorylation of CDK4 producing inactive CDK4. Interacts (unphosphorylated form) with CDK2. Also forms ternary complexes with CDKN1A or CDKN2A. Interacts directly with CDKN1A (via its N-terminal); the interaction promotes the assembly of the cyclin D-CDK4 complex, its nuclear translocation and promotes the cyclin D-dependent enzyme activity of CDK4. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Membrane. Note=Cytoplasmic when non-complexed. Forms a cyclin D-CDK4 complex in the cytoplasm as cells progress through G(1) phase. The complex accumulates on the nuclear membrane and enters the nucleus on transition from G(1) to S phase. Also present in nucleoli and heterochromatin lumps. Colocalizes with RB1 after release into the nucleus. PTM: Phosphorylation at Thr-172 is required for enzymatic activity. Phosphorylated, in vitro, at this site by CCNH-CDK7, but, in vivo, appears to be phosphorylated by a proline-directed kinase. In the cyclin D-CDK4-CDKN1B complex, this phosphorylation and consequent CDK4 enzyme activity, is dependent on the tyrosine phosphorylation state of CDKN1B. Thus, in proliferating cells, CDK4 within the complex is phosphorylated on Thr-172 in the T- loop. In resting cells, phosphorylation on Thr-172 is prevented by the non-tyrosine-phosphorylated form of CDKN1B. DISEASE: Defects in CDK4 are a cause of susceptibility to cutaneous malignant melanoma type 3 (CMM3) [MIM:609048]. Malignant melanoma is a malignant neoplasm of melanocytes, arising de novo or from a pre-existing benign nevus, which occurs most often in the skin but also may involve other sites. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. SIMILARITY: Contains 1 protein kinase domain. WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/CDK4ID238ch12q14.html"; WEB RESOURCE: Name=GeneReviews; URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/CDK4"; WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/cdk4/"; COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-394 |
FUNCTION: Plays a fundamental role in microtubule-organizing center structure and function. Required for centriole duplication and correct spindle formation. Has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CEP110. FUNCTION: Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with RAD23B appears to stabilize XPC. In vitro, stimulates DNA binding of the XPC:RAD23B dimer. FUNCTION: The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. SUBUNIT: Monomer. Homooligomer. Interacts with CEP110, SFI1. Component of the XPC complex composed of XPC, RAD23B and CETN2. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, centrosome, centriole. Nucleus (Probable). Note=Centrosome of S-phase, interphase and mitotic cells. MISCELLANEOUS: Binds two moles of calcium per mole of protein. SIMILARITY: Belongs to the centrin family. SIMILARITY: Contains 4 EF-hand domains. WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/cetn2/"; GENE SYNONYMS: CALT CEN2. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-396 |
FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. CENPC recruits DNA methylation and DNMT3B to both centromeric and pericentromeric satellite repeats and regulates the histone code in these regions. SUBUNIT: Oligomer. Component of the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and MLF1IP/CENPU. The CENPA-NAC complex interacts with the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. Binds to DAXX. Interacts directly with CENPA. SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore. Note=Localizes exclusively in the kinetochore domain of centromeres. DOMAIN: The MIF2 homology domain II targets centromeres and binds the alpha satellite DNA in vivo. The MIF2 homology domain III can induce CENPC dimerization/oligomerization. SIMILARITY: Belongs to the CENPC family. GENE SYNONYMS: CENPC ICEN7. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-402 |
FUNCTION: Component of heterochromatin that recognizes and binds histone H3 tails methylated at 'Lys-9' (H3K9me), leading to epigenetic repression. In contrast, it is excluded from chromatin when 'Tyr-41' of histone H3 is phosphorylated (H3Y41ph). Can interact with lamin-B receptor (LBR). This interaction can contribute to the association of the heterochromatin with the inner nuclear membrane. Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins. SUBUNIT: Interacts with SUV420H1 and SUV420H2 (By similarity). Interacts with HP1BP3 (By similarity). Interacts directly with ATRX, CHAF1A, LBR, NIPBL, SP100, STAM2 and TRIM28 via the chromoshadow domain. Can interact directly with CBX3 via the chromoshadow domain. Interacts with histone H3 methylated at 'Lys- 9'. Interacts with BAHD1, MIS12 and DSN1. Interacts with POGZ; POGZ and PXVXL motif-containing proteins such as INCENP and TRIM28 compete for interaction with CBX5. Interacts with INCENP and TRIM24. Interacts with JC virus agnoprotein; this interaction induces the dissociation of CBX5 from LBR, resulting in destabilization of the nuclear envelope. SUBCELLULAR LOCATION: Nucleus. Chromosome. Chromosome, centromere. Note=Component of centromeric and pericentromeric heterochromatin. Associates with chromosomes during mitosis. Associates specifically with chromatin during metaphase and anaphase. PTM: Phosphorylation of HP1 and LBR may be responsible for some of the alterations in chromatin organization and nuclear structure which occur at various times during the cell cycle (By similarity). Phosphorylated during interphase and possibly hyper- phosphorylated during mitosis. PTM: Ubiquitinated. SIMILARITY: Contains 2 chromo domains. GENE SYNONYMS: HP1A. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-406 |
SUBCELLULAR LOCATION: Mitochondrion (Potential). TISSUE SPECIFICITY: Expressed in nasopharyngeal epithelium and trachea but not in esophagus, stomach, large intestine, liver, cerebrum, heart, bladder, kidney, thymus, or lung. SEQUENCE CAUTION: Sequence=AAD55817.1; Type=Erroneous initiation; Note=Translation N-terminally extended; Sequence=AAD55817.1; Type=Frameshift; Positions=441; GENE SYNONYMS: NESG1. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-410 |
ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=Q96LX7-4; Sequence=Displayed; Note=No experimental confirmation available; Name=2; IsoId=Q96LX7-5; Sequence=VSP_039653; Note=No experimental confirmation available; Name=3; IsoId=Q96LX7-2; Sequence=VSP_039651; Note=May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay; Name=4; IsoId=Q96LX7-3; Sequence=VSP_039652; Note=No experimental confirmation available; SEQUENCE CAUTION: Sequence=BAB71539.1; Type=Miscellaneous discrepancy; Note=Incompletely spliced mRNA; COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-418 |
SIMILARITY: Belongs to the CCDC42 family. GENE SYNONYMS: CCDC42A. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-424 |
FUNCTION: Participates in signal transduction in hematopoietic cells. Adapter protein that functions as a negative regulator of many signaling pathways that start from receptors at the cell surface. Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Recognizes activated receptor tyrosine kinases, including PDGFA, EGF and CSF1, and terminates signaling. Essential for osteoclastic bone resorption. The Tyr-731 phosphorylated form induces the activation and recruitment of phosphatidylinositol 3- kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. PATHWAY: Protein modification; protein ubiquitination. SUBUNIT: Associates with NCK via its SH3 domain. The phosphorylated C-terminus interacts with CD2AP via its second SH3 domain. Binds to UBE2L3. Interacts with adapters SLA, SLA2 and with the phosphorylated C-terminus of SH2B2. Interacts with EGFR, SYK and ZAP70 via the highly conserved Cbl-N region. Also interacts with SORBS1 and INPPL1/SHIP2. Interacts with phosphorylated LAT2. May interact with CBLB (By similarity). SUBCELLULAR LOCATION: Cytoplasm. DOMAIN: The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme. DOMAIN: The N-terminus is composed of the phosphotyrosine binding (PTB) domain, a short linker region and the RING-type zinc finger. The PTB domain, which is also called TKB (tyrosine kinase binding) domain, is composed of three different subdomains: a four-helix bundle (4H), a calcium-binding EF hand and a divergent SH2 domain. PTM: Phosphorylated on tyrosine residues by EGFR, SYK, FYN and ZAP70 (By similarity). Phosphorylated on tyrosine residues by INSR. DISEASE: Defects in CBL are the cause of Noonan syndrome-like disorder with or without juvenile myelomonocytic leukemia (NSLL) [MIM:613563]. A syndrome characterized by a phenotype reminiscent of Noonan syndrome. Clinical features are highly variable, including facial dysmorphism, short neck, developmental delay, hyperextensible joints and thorax abnormalities with widely spaced nipples. The facial features consist of triangular face with hypertelorism, large low-set ears, ptosis, and flat nasal bridge. Some patients manifest cardiac defects. MISCELLANEOUS: This protein has one functional calcium-binding site. SIMILARITY: Contains 1 Cbl-PTB (Cbl-type phosphotyrosine-binding) domain. SIMILARITY: Contains 1 RING-type zinc finger. SIMILARITY: Contains 1 UBA domain. WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/CBLID171.html"; GENE SYNONYMS: CBL2 RNF55. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
FUNCTION: Participates in signal transduction in hematopoietic cells. Adapter protein that functions as a negative regulator of many signaling pathways that start from receptors at the cell surface. Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Recognizes activated receptor tyrosine kinases, including PDGFA, EGF and CSF1, and terminates signaling. Essential for osteoclastic bone resorption. The Tyr-731 phosphorylated form induces the activation and recruitment of phosphatidylinositol 3- kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. PATHWAY: Protein modification; protein ubiquitination. SUBUNIT: Associates with NCK via its SH3 domain. The phosphorylated C-terminus interacts with CD2AP via its second SH3 domain. Binds to UBE2L3. Interacts with adapters SLA, SLA2 and with the phosphorylated C-terminus of SH2B2. Interacts with EGFR, SYK and ZAP70 via the highly conserved Cbl-N region. Also interacts with SORBS1 and INPPL1/SHIP2. Interacts with phosphorylated LAT2. May interact with CBLB (By similarity). SUBCELLULAR LOCATION: Cytoplasm. DOMAIN: The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme. DOMAIN: The N-terminus is composed of the phosphotyrosine binding (PTB) domain, a short linker region and the RING-type zinc finger. The PTB domain, which is also called TKB (tyrosine kinase binding) domain, is composed of three different subdomains: a four-helix bundle (4H), a calcium-binding EF hand and a divergent SH2 domain. PTM: Phosphorylated on tyrosine residues by EGFR, SYK, FYN and ZAP70 (By similarity). Phosphorylated on tyrosine residues by INSR. DISEASE: Defects in CBL are the cause of Noonan syndrome-like disorder with or without juvenile myelomonocytic leukemia (NSLL) [MIM:613563]. A syndrome characterized by a phenotype reminiscent of Noonan syndrome. Clinical features are highly variable, including facial dysmorphism, short neck, developmental delay, hyperextensible joints and thorax abnormalities with widely spaced nipples. The facial features consist of triangular face with hypertelorism, large low-set ears, ptosis, and flat nasal bridge. Some patients manifest cardiac defects. MISCELLANEOUS: This protein has one functional calcium-binding site. SIMILARITY: Contains 1 Cbl-PTB (Cbl-type phosphotyrosine-binding) domain. SIMILARITY: Contains 1 RING-type zinc finger. SIMILARITY: Contains 1 UBA domain. WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/CBLID171.html"; GENE SYNONYMS: CBL2 RNF55. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-430 |
SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein (Potential). COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-85466 |
SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein (Potential). COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-85666 |
SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein (Potential). COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-86072 |
SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein (Potential). COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-97303 |
SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein (Potential). COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-109366 |
SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein (Potential). COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-110184 |
SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein (Potential). COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-110381 |
SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein (Potential). COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| cpath:CPATH-110972 |
SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein (Potential). COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|