Linked Life Data

Q9UQB8

Source:http://identifiers.org/uniprot/Q9UQB8

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
biopax3:comment
FUNCTION: Adapter protein that links membrane-bound small G- proteins to cytoplasmic effector proteins. Necessary for CDC42- mediated reorganization of the actin cytoskeleton and for RAC1- mediated membrane ruffling. Involved in the regulation of the actin cytoskeleton by WASF family members and the Arp2/3 complex. Plays a role in neurite growth. Acts syngeristically with ENAH to promote filipodia formation. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection. SUBUNIT: Homodimer. Interacts with CDC42 and RAC1 that have been activated by GTP binding. Interacts with ATN1, BAI1, EPS8, SHANK1, SHANK2, SHANK3, WASF1 and WASF2. Interacts with ENAH after recruitment of CDC42. Interacts with TIAM1 and DIAPH1 (By similarity). Interacts (via SH3 domain) with E.coli effector protein EspF(U) (via PXXP motifs). Interacts with E.coli intimin receptor Tir. SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Cell projection, filopodium. Cell projection, ruffle. Cytoplasm, cytoskeleton. Note=Detected throughout the cytoplasm in the absence of specific binding partners. Detected in filopodia and close to membrane ruffles. Recruited to actin pedestals that are formed upon infection by bacteria at bacterial attachment sites. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=6; Name=1; Synonyms=IRSp53(L); IsoId=Q9UQB8-1; Sequence=Displayed; Name=2; IsoId=Q9UQB8-2; Sequence=VSP_015506; Name=3; IsoId=Q9UQB8-3; Sequence=VSP_015505; Name=4; Synonyms=BAIAP2-alpha; IsoId=Q9UQB8-4; Sequence=VSP_015503; Name=5; Synonyms=BAIAP2-beta; IsoId=Q9UQB8-5; Sequence=VSP_015504; Name=6; IsoId=Q9UQB8-6; Sequence=VSP_015502, VSP_015503; TISSUE SPECIFICITY: Isoform 1 and isoform 4 are expressed almost exclusively in brain. Isoform 4 is barely detectable in placenta, prostate and testis. A short isoform is ubiquitous, with the highest expression in liver, prostate, testis and placenta. DOMAIN: The IMD domain forms a coiled coil. The isolated domain can induce actin bundling and filopodia formation. In the absence of G-proteins intramolecular interaction between the IMD and the SH3 domain gives rise to an auto-inhibited state of the protein. Interaction of the IMD with RAC1 or CDC42 leads to activation. DOMAIN: The SH3 domain interacts with ATN1, BAI1, WASF1, WASF2, SHANK1, DIAPH1 and ENAH. PTM: Phosphorylated on tyrosine residues by INSR in response to insulin treatment. SIMILARITY: Contains 1 IMD (IRSp53/MIM homology) domain. SIMILARITY: Contains 1 SH3 domain. CAUTION: It is uncertain whether Met-1 or Met-59 is the initiator. GENE SYNONYMS:BAIAP2. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License., SEQUENCE 552 AA; 60868 MW; 3B9EDC6405DCC99D CRC64;
biopax3:xref
biopax3:displayName
BAIP2_HUMAN
biopax3:name
BAI-associated protein 2, BAI1-associated protein 2, BAIAP2, FLAF3, Fas ligand-associated factor 3, IRS-58, IRSp53, IRSp53/58, Insulin receptor substrate p53, Insulin receptor substrate p53/p58, Insulin receptor substrate protein of 53 kDa, Protein BAP2
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biopax3:organism
biopax3:sequence
MSLSRSEEMHRLTENVYKTIMEQFNPSLRNFIAMGKNYEKALAGVTYAAKGYFDALVKMGELASESQGSKELGDVLFQMAEVHRQIQNQLEEMLKSFHNELLTQLEQKVELDSRYLSAALKKYQTEQRSKGDALDKCQAELKKLRKKSQGSKNPQKYSDKELQYIDAISNKQGELENYVSDGYKTALTEERRRFCFLVEKQCAVAKNSAAYHSKGKELLAQKLPLWQQACADPSKIPERAVQLMQQVASNGATLPSALSASKSNLVISDPIPGAKPLPVPPELAPFVGRMSAQESTPIMNGVTGPDGEDYSPWADRKAAQPKSLSPPQSQSKLSDSYSNTLPVRKSVTPKNSYATTENKTLPRSSSMAAGLERNGRMRVKAIFSHAAGDNSTLLSFKEGDLITLLVPEARDGWHYGESEKTKMRGWFPFSYTRVLDSDGSDRLHMSLQQGKSSSTGNLLDKDDLAIPPPDYGAASRAFPAQTASGFKQRPYSVAVPAFSQGLDDYGARSMSRNPFAHVQLKPTVTNDRCDLSAQGPEGREHGDGSARTLAGR
biopax3:standardName
Brain-specific angiogenesis inhibitor 1-associated protein 2