Linked Life Data

CPATH-124851

Source:http://cbio.mskcc.org/cpath#CPATH-124851

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
http://www.biopax.org/relea...
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KH domain-containing, RNA-binding, signal transduction-associated protein 1, KH domain-containing, RNA-binding, signal transduction-associated protein 1
http://www.biopax.org/relea...
KHDR1_HUMAN, KHDR1_HUMAN
http://www.biopax.org/relea...
http://www.biopax.org/relea...
GAP-associated tyrosine phosphoprotein p62, GAP-associated tyrosine phosphoprotein p62, Sam68, Sam68, Src-associated in mitosis 68 kDa protein, Src-associated in mitosis 68 kDa protein, p21 Ras GTPase-activating protein-associated p62, p21 Ras GTPase-activating protein-associated p62, p68, p68
http://www.biopax.org/relea...
FUNCTION: Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain- containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. FUNCTION: Isoform 3, which is expressed in growth-arrested cells only, inhibits S phase. SUBUNIT: Self-associates to form homooligomers when bound to RNA, oligomerization appears to be limited when binding to proteins. Interacts with CBL, KHDRBS3, LCK, GRB2, JAK3, PIK3R1, PLCG1, PTPN6, RASA1, RBMY1A1 and STAT3. Interacts with PRMT1. Binds the WW domains of WBP4/FBP21, FNBP4/FBP30 and the SH3 domain of FYN through the Arg/Gly-rich-flanked Pro-rich regions (By similarity). Forms a complex with ILF2, ILF3, YLPM1, RBMX, NCOA5 and PPP1CA. SUBCELLULAR LOCATION: Nucleus. Membrane. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q07666-1; Sequence=Displayed; Name=2; IsoId=Q07666-2; Sequence=VSP_051719; Note=No experimental confirmation available; Name=3; Synonyms=DeltaKH; IsoId=Q07666-3; Sequence=VSP_051720; TISSUE SPECIFICITY: Ubiquitously expressed in all tissue examined. Isoform 1 is expressed at lower levels in brain, skeletal muscle, and liver whereas isoform 3 is intensified in skeletal muscle and in liver. DEVELOPMENTAL STAGE: Isoform 3 is only expressed in growth- arrested cells. DOMAIN: The KH domain is required for binding to RNA (By similarity). DOMAIN: The Pro-rich domains are flanked by Arg/Gly-rich motifs which can be asymmetric dimethylated on arginine residues to give the DMA/Gly-rich regions. Selective methylation on these motifs can modulate protein-protein interactions (By similarity). PTM: Tyrosine phosphorylated by several non-receptor tyrosine kinases, for example LCK, FYN and JAK3. Negatively correlates with ability to bind RNA but required for many interactions with proteins. PTM: Acetylated. Positively correlates with ability to bind RNA. PTM: Arginine methylation is required for nuclear localization. Also can affect interaction with other proteins. Inhibits interaction with Src-like SH3 domains, but not interaction with WW domains of WBP4/FBP21 AND FNBP4/FBP30. PTM: Arg-291, Arg-331 and Arg-346 are found to be also dimethylated, probably to asymmetric dimethylarginine. SIMILARITY: Belongs to the KHDRBS family. SIMILARITY: Contains 1 KH domain. SEQUENCE CAUTION: Sequence=AAH10132.1; Type=Miscellaneous discrepancy; Note=Intron retention; GENE SYNONYMS: SAM68. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License., FUNCTION: Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain- containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. FUNCTION: Isoform 3, which is expressed in growth-arrested cells only, inhibits S phase. SUBUNIT: Self-associates to form homooligomers when bound to RNA, oligomerization appears to be limited when binding to proteins. Interacts with CBL, KHDRBS3, LCK, GRB2, JAK3, PIK3R1, PLCG1, PTPN6, RASA1, RBMY1A1 and STAT3. Interacts with PRMT1. Binds the WW domains of WBP4/FBP21, FNBP4/FBP30 and the SH3 domain of FYN through the Arg/Gly-rich-flanked Pro-rich regions (By similarity). Forms a complex with ILF2, ILF3, YLPM1, RBMX, NCOA5 and PPP1CA. SUBCELLULAR LOCATION: Nucleus. Membrane. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q07666-1; Sequence=Displayed; Name=2; IsoId=Q07666-2; Sequence=VSP_051719; Note=No experimental confirmation available; Name=3; Synonyms=DeltaKH; IsoId=Q07666-3; Sequence=VSP_051720; TISSUE SPECIFICITY: Ubiquitously expressed in all tissue examined. Isoform 1 is expressed at lower levels in brain, skeletal muscle, and liver whereas isoform 3 is intensified in skeletal muscle and in liver. DEVELOPMENTAL STAGE: Isoform 3 is only expressed in growth- arrested cells. DOMAIN: The KH domain is required for binding to RNA (By similarity). DOMAIN: The Pro-rich domains are flanked by Arg/Gly-rich motifs which can be asymmetric dimethylated on arginine residues to give the DMA/Gly-rich regions. Selective methylation on these motifs can modulate protein-protein interactions (By similarity). PTM: Tyrosine phosphorylated by several non-receptor tyrosine kinases, for example LCK, FYN and JAK3. Negatively correlates with ability to bind RNA but required for many interactions with proteins. PTM: Acetylated. Positively correlates with ability to bind RNA. PTM: Arginine methylation is required for nuclear localization. Also can affect interaction with other proteins. Inhibits interaction with Src-like SH3 domains, but not interaction with WW domains of WBP4/FBP21 AND FNBP4/FBP30. PTM: Arg-291, Arg-331 and Arg-346 are found to be also dimethylated, probably to asymmetric dimethylarginine. SIMILARITY: Belongs to the KHDRBS family. SIMILARITY: Contains 1 KH domain. SEQUENCE CAUTION: Sequence=AAH10132.1; Type=Miscellaneous discrepancy; Note=Intron retention; GENE SYNONYMS: SAM68. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
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