ID BAIP2_HUMAN Reviewed; 552 AA. AC Q9UQB8; O43858; Q53HB1; Q86WC1; Q8N5C0; Q96CR7; Q9UBR3; Q9UQ43; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 204. DE RecName: Full=Brain-specific angiogenesis inhibitor 1-associated protein 2; DE Short=BAI-associated protein 2; DE Short=BAI1-associated protein 2; DE Short=Protein BAP2; DE AltName: Full=Fas ligand-associated factor 3; DE Short=FLAF3; DE AltName: Full=Insulin receptor substrate p53/p58; DE Short=IRS-58; DE Short=IRSp53/58; DE AltName: Full=Insulin receptor substrate protein of 53 kDa; DE Short=IRSp53; DE Short=Insulin receptor substrate p53; GN Name=BAIAP2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), INTERACTION WITH ADGRB1, RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC TISSUE=Fetal brain; RX PubMed=10343108; DOI=10.1159/000015219; RA Oda K., Shiratsuchi T., Nishimori H., Inazawa J., Yoshikawa H., RA Taketani Y., Nakamura Y., Tokino T.; RT "Identification of BAIAP2 (BAI-associated protein 2), a novel human RT homologue of hamster IRSp53, whose SH3 domain interacts with the RT cytoplasmic domain of BAI1."; RL Cytogenet. Cell Genet. 84:75-82(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4), PHOSPHORYLATION AT TYROSINE RP RESIDUES, SUBCELLULAR LOCATION, INTERACTION WITH ATN1, AND TISSUE RP SPECIFICITY. RC TISSUE=Fetal brain; RX PubMed=10332026; DOI=10.1093/hmg/8.6.947; RA Okamura-Oho Y., Miyashita T., Ohmi K., Yamada M.; RT "Dentatorubral-pallidoluysian atrophy protein interacts through a proline- RT rich region near polyglutamine with the SH3 domain of an insulin receptor RT tyrosine kinase substrate."; RL Hum. Mol. Genet. 8:947-957(1999). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2; 4 AND 5). RX PubMed=12884081; DOI=10.1007/s10038-003-0047-x; RA Miyahara A., Okumura-Oho Y., Miyashita T., Hoshika A., Yamada M.; RT "Genomic structure and alternative splicing of the insulin receptor RT tyrosine kinase substrate of 53-kDa protein."; RL J. Hum. Genet. 48:410-414(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6). RC TISSUE=Brain; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 6). RC TISSUE=Brain, and Duodenum; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-328. RC TISSUE=Placenta; RA Hachiya T., Kobayasi A., Touji S., Tamai K.; RT "A Fas-ligand associated factor 3, FLAF3, potentiates Fas-ligand RT stability."; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [7] RP FUNCTION, AND INTERACTION WITH RAC1; CDC42; WASF1 AND WASF2. RX PubMed=11130076; DOI=10.1038/35047107; RA Miki H., Yamaguchi H., Suetsugu S., Takenawa T.; RT "IRSp53 is an essential intermediate between Rac and WAVE in the regulation RT of membrane ruffling."; RL Nature 408:732-735(2000). RN [8] RP FUNCTION, INTERACTION WITH CDC42 AND ENAH, AND MUTAGENESIS OF PHE-427 AND RP PRO-428. RX PubMed=11696321; DOI=10.1016/s0960-9822(01)00506-1; RA Krugmann S., Jordens I., Gevaert K., Driessens M., Vandekerckhove J., RA Hall A.; RT "Cdc42 induces filopodia by promoting the formation of an IRSp53:Mena RT complex."; RL Curr. Biol. 11:1645-1655(2001). RN [9] RP INTERACTION WITH CDC42, MUTAGENESIS OF ILE-267, AND TISSUE SPECIFICITY. RX PubMed=11157984; DOI=10.1083/jcb.152.3.579; RA Govind S., Kozma R., Monfries C., Lim L., Ahmed S.; RT "Cdc42Hs facilitates cytoskeletal reorganization and neurite outgrowth by RT localizing the 58-kD insulin receptor substrate to filamentous actin."; RL J. Cell Biol. 152:579-594(2001). RN [10] RP INTERACTION WITH SHANK1; SHANK2; SHANK3 AND CDC42, AND SUBCELLULAR RP LOCATION. RX PubMed=12504591; DOI=10.1006/mcne.2002.1201; RA Soltau M., Richter D., Kreienkamp H.-J.; RT "The insulin receptor substrate IRSp53 links postsynaptic shank1 to the RT small G-protein cdc42."; RL Mol. Cell. Neurosci. 21:575-583(2002). RN [11] RP INTERACTION WITH EPS8, AND SUBCELLULAR LOCATION. RX PubMed=15289329; DOI=10.1158/0008-5472.can-04-0327; RA Funato Y., Terabayashi T., Suenaga N., Seiki M., Takenawa T., Miki H.; RT "IRSp53/Eps8 complex is important for positive regulation of Rac and cancer RT cell motility/invasiveness."; RL Cancer Res. 64:5237-5244(2004). RN [12] RP DOMAIN, AND FUNCTION. RX PubMed=14752106; DOI=10.1074/jbc.m309408200; RA Yamagishi A., Masuda M., Ohki T., Onishi H., Mochizuki N.; RT "A novel actin bundling/filopodium-forming domain conserved in insulin RT receptor tyrosine kinase substrate p53 and missing in metastasis protein."; RL J. Biol. Chem. 279:14929-14936(2004). RN [13] RP FUNCTION, INTERACTION WITH EPS8, AND MUTAGENESIS OF TRP-413. RX PubMed=17115031; DOI=10.1038/ncb1502; RA Disanza A., Mantoani S., Hertzog M., Gerboth S., Frittoli E., Steffen A., RA Berhoerster K., Kreienkamp H.J., Milanesi F., Di Fiore P.P., Ciliberto A., RA Stradal T.E., Scita G.; RT "Regulation of cell shape by Cdc42 is mediated by the synergic actin- RT bundling activity of the Eps8-IRSp53 complex."; RL Nat. Cell Biol. 8:1337-1347(2006). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-296; SER-323; SER-325; RP SER-346 AND SER-366, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [16] RP INTERACTION WITH E.COLI EFFECTOR PROTEIN ESPF(U) AND WITH E.COLI INTIMIN RP RECEPTOR TIR. RX PubMed=19286134; DOI=10.1016/j.chom.2009.02.003; RA Weiss S.M., Ladwein M., Schmidt D., Ehinger J., Lommel S., Stading K., RA Beutling U., Disanza A., Frank R., Jansch L., Scita G., Gunzer F., RA Rottner K., Stradal T.E.; RT "IRSp53 links the enterohemorrhagic E. coli effectors Tir and EspFU for RT actin pedestal formation."; RL Cell Host Microbe 5:244-258(2009). RN [17] RP FUNCTION, INTERACTION WITH E.COLI EFFECTOR PROTEIN ESPF(U), AND SUBCELLULAR RP LOCATION. RX PubMed=19366662; DOI=10.1073/pnas.0809131106; RA Vingadassalom D., Kazlauskas A., Skehan B., Cheng H.C., Magoun L., RA Robbins D., Rosen M.K., Saksela K., Leong J.M.; RT "Insulin receptor tyrosine kinase substrate links the E. coli O157:H7 actin RT assembly effectors Tir and EspF(U) during pedestal formation."; RL Proc. Natl. Acad. Sci. U.S.A. 106:6754-6759(2009). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-340, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-454, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261; SER-325; SER-336; RP THR-340; THR-360; SER-366 AND SER-384, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [23] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-250, AND MUTAGENESIS OF LYS-142; RP LYS-143; LYS-146 AND LYS-147. RX PubMed=15635447; DOI=10.1038/sj.emboj.7600535; RA Millard T.H., Bompard G., Heung M.Y., Dafforn T.R., Scott D.J., RA Machesky L.M., Fuetterer K.; RT "Structural basis of filopodia formation induced by the IRSp53/MIM homology RT domain of human IRSp53."; RL EMBO J. 24:240-250(2005). RN [24] RP X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS) OF 1-228. RG RIKEN structural genomics initiative (RSGI); RT "Crystal structure of RCB domain of IRSP53."; RL Submitted (JUN-2005) to the PDB data bank. CC -!- FUNCTION: Adapter protein that links membrane-bound small G-proteins to CC cytoplasmic effector proteins. Necessary for CDC42-mediated CC reorganization of the actin cytoskeleton and for RAC1-mediated membrane CC ruffling. Involved in the regulation of the actin cytoskeleton by WASF CC family members and the Arp2/3 complex. Plays a role in neurite growth. CC Acts syngeristically with ENAH to promote filipodia formation. Plays a CC role in the reorganization of the actin cytoskeleton in response to CC bacterial infection. Participates in actin bundling when associated CC with EPS8, promoting filopodial protrusions. CC {ECO:0000269|PubMed:11130076, ECO:0000269|PubMed:11696321, CC ECO:0000269|PubMed:14752106, ECO:0000269|PubMed:17115031, CC ECO:0000269|PubMed:19366662}. CC -!- SUBUNIT: Homodimer. Interacts with CDC42 and RAC1 that have been CC activated by GTP binding. Interacts with ATN1, ADGRB1, EPS8, SHANK1, CC SHANK2, SHANK3, WASF1 and WASF2. Interacts with ENAH after recruitment CC of CDC42. Interacts with TIAM1 and DIAPH1 (By similarity). Interacts CC (via SH3 domain) with E.coli effector protein EspF(U) (via PXXP CC motifs). Interacts with E.coli intimin receptor Tir. {ECO:0000250, CC ECO:0000269|PubMed:10332026, ECO:0000269|PubMed:10343108, CC ECO:0000269|PubMed:11130076, ECO:0000269|PubMed:11157984, CC ECO:0000269|PubMed:11696321, ECO:0000269|PubMed:12504591, CC ECO:0000269|PubMed:15289329, ECO:0000269|PubMed:17115031, CC ECO:0000269|PubMed:19286134, ECO:0000269|PubMed:19366662}. CC -!- INTERACTION: CC Q9UQB8; Q9UQB8: BAIAP2; NbExp=5; IntAct=EBI-525456, EBI-525456; CC Q9UQB8; Q9UFG5: C19orf25; NbExp=3; IntAct=EBI-525456, EBI-741214; CC Q9UQB8; P60953: CDC42; NbExp=2; IntAct=EBI-525456, EBI-81752; CC Q9UQB8; P60953-2: CDC42; NbExp=2; IntAct=EBI-525456, EBI-287394; CC Q9UQB8; P00533: EGFR; NbExp=4; IntAct=EBI-525456, EBI-297353; CC Q9UQB8; Q12929: EPS8; NbExp=10; IntAct=EBI-525456, EBI-375576; CC Q9UQB8; Q14678: KANK1; NbExp=6; IntAct=EBI-525456, EBI-2556221; CC Q9UQB8; Q9NZQ3: NCKIPSD; NbExp=2; IntAct=EBI-525456, EBI-745080; CC Q9UQB8; Q9NZ81: PRR13; NbExp=3; IntAct=EBI-525456, EBI-740924; CC Q9UQB8; P63000: RAC1; NbExp=4; IntAct=EBI-525456, EBI-413628; CC Q9UQB8; Q15427: SF3B4; NbExp=3; IntAct=EBI-525456, EBI-348469; CC Q9UQB8; P31947: SFN; NbExp=4; IntAct=EBI-525456, EBI-476295; CC Q9UQB8; Q13625-3: TP53BP2; NbExp=3; IntAct=EBI-525456, EBI-10175039; CC Q9UQB8; P62258: YWHAE; NbExp=5; IntAct=EBI-525456, EBI-356498; CC Q9UQB8; P63104: YWHAZ; NbExp=5; IntAct=EBI-525456, EBI-347088; CC Q9UQB8; Q8CFN2: Cdc42; Xeno; NbExp=2; IntAct=EBI-525456, EBI-7023929; CC Q9UQB8; Q03173: Enah; Xeno; NbExp=3; IntAct=EBI-525456, EBI-6083294; CC Q9UQB8; Q08509: Eps8; Xeno; NbExp=8; IntAct=EBI-525456, EBI-375596; CC Q9UQB8; Q7DB77: tir; Xeno; NbExp=3; IntAct=EBI-525456, EBI-6480811; CC Q9UQB8-3; Q86V38: ATN1; NbExp=3; IntAct=EBI-9091996, EBI-11954292; CC Q9UQB8-3; P42858: HTT; NbExp=18; IntAct=EBI-9091996, EBI-466029; CC Q9UQB8-3; Q92876: KLK6; NbExp=3; IntAct=EBI-9091996, EBI-2432309; CC Q9UQB8-3; Q7Z412: PEX26; NbExp=3; IntAct=EBI-9091996, EBI-752057; CC Q9UQB8-3; D3DTS7: PMP22; NbExp=3; IntAct=EBI-9091996, EBI-25882629; CC Q9UQB8-3; Q8IUH5: ZDHHC17; NbExp=3; IntAct=EBI-9091996, EBI-524753; CC Q9UQB8-4; Q9UQB8-4: BAIAP2; NbExp=4; IntAct=EBI-6174091, EBI-6174091; CC Q9UQB8-4; P60953: CDC42; NbExp=4; IntAct=EBI-6174091, EBI-81752; CC Q9UQB8-4; P60953-2: CDC42; NbExp=5; IntAct=EBI-6174091, EBI-287394; CC Q9UQB8-4; Q12929: EPS8; NbExp=4; IntAct=EBI-6174091, EBI-375576; CC Q9UQB8-4; Q14678-2: KANK1; NbExp=4; IntAct=EBI-6174091, EBI-6173812; CC Q9UQB8-4; P50552: VASP; NbExp=6; IntAct=EBI-6174091, EBI-748201; CC Q9UQB8-4; Q9Y6W5: WASF2; NbExp=5; IntAct=EBI-6174091, EBI-4290615; CC Q9UQB8-4; B7UM99: tir; Xeno; NbExp=3; IntAct=EBI-6174091, EBI-2504426; CC Q9UQB8-4; Q7DB77: tir; Xeno; NbExp=5; IntAct=EBI-6174091, EBI-6480811; CC Q9UQB8-6; Q86V38: ATN1; NbExp=3; IntAct=EBI-9092016, EBI-11954292; CC Q9UQB8-6; P54253: ATXN1; NbExp=6; IntAct=EBI-9092016, EBI-930964; CC Q9UQB8-6; Q9UHR4: BAIAP2L1; NbExp=3; IntAct=EBI-9092016, EBI-2483278; CC Q9UQB8-6; P28329-3: CHAT; NbExp=3; IntAct=EBI-9092016, EBI-25837549; CC Q9UQB8-6; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-9092016, EBI-3866319; CC Q9UQB8-6; P02489: CRYAA; NbExp=3; IntAct=EBI-9092016, EBI-6875961; CC Q9UQB8-6; P50570-2: DNM2; NbExp=3; IntAct=EBI-9092016, EBI-10968534; CC Q9UQB8-6; P22607: FGFR3; NbExp=3; IntAct=EBI-9092016, EBI-348399; CC Q9UQB8-6; Q8TB36: GDAP1; NbExp=3; IntAct=EBI-9092016, EBI-11110431; CC Q9UQB8-6; P14136: GFAP; NbExp=3; IntAct=EBI-9092016, EBI-744302; CC Q9UQB8-6; P13378: HOXD8; NbExp=3; IntAct=EBI-9092016, EBI-7098661; CC Q9UQB8-6; P42858: HTT; NbExp=18; IntAct=EBI-9092016, EBI-466029; CC Q9UQB8-6; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-9092016, EBI-1055254; CC Q9UQB8-6; O60333-2: KIF1B; NbExp=3; IntAct=EBI-9092016, EBI-10975473; CC Q9UQB8-6; Q92876: KLK6; NbExp=3; IntAct=EBI-9092016, EBI-2432309; CC Q9UQB8-6; Q15428: SF3A2; NbExp=3; IntAct=EBI-9092016, EBI-2462271; CC Q9UQB8-6; Q9UPX8-4: SHANK2; NbExp=3; IntAct=EBI-9092016, EBI-11959011; CC Q9UQB8-6; Q99593: TBX5; NbExp=3; IntAct=EBI-9092016, EBI-297043; CC Q9UQB8-6; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-9092016, EBI-11952721; CC Q9UQB8-6; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-9092016, EBI-741480; CC Q9UQB8-6; O76024: WFS1; NbExp=3; IntAct=EBI-9092016, EBI-720609; CC Q9UQB8-6; Q8IUH5: ZDHHC17; NbExp=2; IntAct=EBI-9092016, EBI-524753; CC Q9UQB8-6; Q9Y649; NbExp=3; IntAct=EBI-9092016, EBI-25900580; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. CC Cell projection, filopodium. Cell projection, ruffle. Cytoplasm, CC cytoskeleton. Note=Detected throughout the cytoplasm in the absence of CC specific binding partners. Detected in filopodia and close to membrane CC ruffles. Recruited to actin pedestals that are formed upon infection by CC bacteria at bacterial attachment sites. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; Synonyms=IRSp53(L); CC IsoId=Q9UQB8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UQB8-2; Sequence=VSP_015506; CC Name=3; CC IsoId=Q9UQB8-3; Sequence=VSP_015505; CC Name=4; Synonyms=BAIAP2-alpha; CC IsoId=Q9UQB8-4; Sequence=VSP_015503; CC Name=5; Synonyms=BAIAP2-beta; CC IsoId=Q9UQB8-5; Sequence=VSP_015504; CC Name=6; CC IsoId=Q9UQB8-6; Sequence=VSP_015502, VSP_015503; CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 4 are expressed almost CC exclusively in brain. Isoform 4 is barely detectable in placenta, CC prostate and testis. A short isoform is ubiquitous, with the highest CC expression in liver, prostate, testis and placenta. CC {ECO:0000269|PubMed:10332026, ECO:0000269|PubMed:10343108, CC ECO:0000269|PubMed:11157984}. CC -!- DOMAIN: The IMD domain forms a coiled coil. The isolated domain can CC induce actin bundling and filopodia formation. In the absence of G- CC proteins intramolecular interaction between the IMD and the SH3 domain CC gives rise to an auto-inhibited state of the protein. Interaction of CC the IMD with RAC1 or CDC42 leads to activation. CC {ECO:0000269|PubMed:14752106}. CC -!- DOMAIN: The SH3 domain interacts with ATN1, ADGRB1, WASF1, WASF2, CC SHANK1, DIAPH1 and ENAH. {ECO:0000269|PubMed:14752106}. CC -!- PTM: Phosphorylated on tyrosine residues by INSR in response to insulin CC treatment. {ECO:0000269|PubMed:10332026}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-59 is the initiator. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB015019; BAA36586.1; -; mRNA. DR EMBL; AB015020; BAA36587.1; -; mRNA. DR EMBL; AB017119; BAA74773.1; -; mRNA. DR EMBL; AB017120; BAA74774.1; -; mRNA. DR EMBL; AB104726; BAC57945.1; -; Genomic_DNA. DR EMBL; AB104726; BAC57946.1; -; Genomic_DNA. DR EMBL; AB104726; BAC57947.1; -; Genomic_DNA. DR EMBL; AB104726; BAC57948.1; -; Genomic_DNA. DR EMBL; AK222670; BAD96390.1; -; mRNA. DR EMBL; BC014020; AAH14020.1; -; mRNA. DR EMBL; BC032559; AAH32559.1; -; mRNA. DR EMBL; U70669; AAB93497.1; -; mRNA. DR CCDS; CCDS11775.1; -. [Q9UQB8-1] DR CCDS; CCDS11776.1; -. [Q9UQB8-5] DR CCDS; CCDS11777.1; -. [Q9UQB8-4] DR CCDS; CCDS45806.1; -. [Q9UQB8-2] DR RefSeq; NP_001138360.1; NM_001144888.1. [Q9UQB8-2] DR RefSeq; NP_006331.1; NM_006340.2. [Q9UQB8-5] DR RefSeq; NP_059344.1; NM_017450.2. [Q9UQB8-4] DR RefSeq; NP_059345.1; NM_017451.2. [Q9UQB8-1] DR RefSeq; XP_005257005.1; XM_005256948.3. DR PDB; 1WDZ; X-ray; 2.63 A; A/B=1-228. DR PDB; 1Y2O; X-ray; 2.20 A; A/B=1-250. DR PDB; 2YKT; X-ray; 2.11 A; A=1-250. DR PDB; 3RNJ; X-ray; 1.50 A; A=375-436. DR PDB; 4JS0; X-ray; 1.90 A; B=260-291. DR PDB; 6BCR; X-ray; 1.99 A; C/D/G/H=333-346. DR PDB; 6BCY; X-ray; 2.30 A; C/D/G/H=354-366. DR PDB; 6BD1; X-ray; 2.35 A; C/D/G/H=360-373. DR PDB; 6BD2; X-ray; 2.90 A; C=335-372. DR PDB; 6BQT; X-ray; 2.80 A; C/F/I/L=335-366. DR PDB; 6ZEG; X-ray; 1.09 A; A/B=448-464. DR PDB; 6ZEI; X-ray; 1.39 A; A/B=448-464. DR PDBsum; 1WDZ; -. DR PDBsum; 1Y2O; -. DR PDBsum; 2YKT; -. DR PDBsum; 3RNJ; -. DR PDBsum; 4JS0; -. DR PDBsum; 6BCR; -. DR PDBsum; 6BCY; -. DR PDBsum; 6BD1; -. DR PDBsum; 6BD2; -. DR PDBsum; 6BQT; -. DR PDBsum; 6ZEG; -. DR PDBsum; 6ZEI; -. DR AlphaFoldDB; Q9UQB8; -. DR SMR; Q9UQB8; -. DR BioGRID; 115721; 188. DR DIP; DIP-29272N; -. DR IntAct; Q9UQB8; 116. DR MINT; Q9UQB8; -. DR STRING; 9606.ENSP00000316338; -. DR GlyGen; Q9UQB8; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9UQB8; -. DR PhosphoSitePlus; Q9UQB8; -. DR SwissPalm; Q9UQB8; -. DR BioMuta; BAIAP2; -. DR DMDM; 73917636; -. DR EPD; Q9UQB8; -. DR jPOST; Q9UQB8; -. DR MassIVE; Q9UQB8; -. DR MaxQB; Q9UQB8; -. DR PaxDb; 9606-ENSP00000316338; -. DR PeptideAtlas; Q9UQB8; -. DR ProteomicsDB; 85532; -. [Q9UQB8-1] DR ProteomicsDB; 85533; -. [Q9UQB8-2] DR ProteomicsDB; 85534; -. [Q9UQB8-3] DR ProteomicsDB; 85535; -. [Q9UQB8-4] DR ProteomicsDB; 85536; -. [Q9UQB8-5] DR ProteomicsDB; 85537; -. [Q9UQB8-6] DR Pumba; Q9UQB8; -. DR ABCD; Q9UQB8; 11 sequenced antibodies. DR Antibodypedia; 19790; 605 antibodies from 38 providers. DR DNASU; 10458; -. DR Ensembl; ENST00000321280.11; ENSP00000315685.7; ENSG00000175866.16. [Q9UQB8-4] DR Ensembl; ENST00000321300.10; ENSP00000316338.6; ENSG00000175866.16. [Q9UQB8-1] DR Ensembl; ENST00000428708.7; ENSP00000401022.2; ENSG00000175866.16. [Q9UQB8-2] DR Ensembl; ENST00000435091.7; ENSP00000413069.3; ENSG00000175866.16. [Q9UQB8-5] DR Ensembl; ENST00000575712.5; ENSP00000458964.1; ENSG00000175866.16. [Q9UQB8-3] DR GeneID; 10458; -. DR KEGG; hsa:10458; -. DR MANE-Select; ENST00000428708.7; ENSP00000401022.2; NM_001144888.2; NP_001138360.1. [Q9UQB8-2] DR UCSC; uc002jyz.5; human. [Q9UQB8-1] DR AGR; HGNC:947; -. DR CTD; 10458; -. DR DisGeNET; 10458; -. DR GeneCards; BAIAP2; -. DR HGNC; HGNC:947; BAIAP2. DR HPA; ENSG00000175866; Low tissue specificity. DR MIM; 605475; gene. DR neXtProt; NX_Q9UQB8; -. DR OpenTargets; ENSG00000175866; -. DR PharmGKB; PA25251; -. DR VEuPathDB; HostDB:ENSG00000175866; -. DR eggNOG; ENOG502QUM6; Eukaryota. DR GeneTree; ENSGT00940000153560; -. DR HOGENOM; CLU_025877_0_1_1; -. DR InParanoid; Q9UQB8; -. DR OMA; KNSYATX; -. DR OrthoDB; 3059844at2759; -. DR PhylomeDB; Q9UQB8; -. DR TreeFam; TF325648; -. DR PathwayCommons; Q9UQB8; -. DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation. DR Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway. DR Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs. DR Reactome; R-HSA-9013148; CDC42 GTPase cycle. DR Reactome; R-HSA-9013149; RAC1 GTPase cycle. DR Reactome; R-HSA-9013423; RAC3 GTPase cycle. DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis. DR SignaLink; Q9UQB8; -. DR SIGNOR; Q9UQB8; -. DR BioGRID-ORCS; 10458; 24 hits in 1168 CRISPR screens. DR ChiTaRS; BAIAP2; human. DR EvolutionaryTrace; Q9UQB8; -. DR GeneWiki; BAIAP2; -. DR GenomeRNAi; 10458; -. DR Pharos; Q9UQB8; Tbio. DR PRO; PR:Q9UQB8; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q9UQB8; Protein. DR Bgee; ENSG00000175866; Expressed in Brodmann (1909) area 10 and 172 other cell types or tissues. DR ExpressionAtlas; Q9UQB8; baseline and differential. DR GO; GO:0005912; C:adherens junction; HDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0043198; C:dendritic shaft; IEA:Ensembl. DR GO; GO:0061846; C:dendritic spine cytoplasm; IEA:Ensembl. DR GO; GO:0060076; C:excitatory synapse; IEA:Ensembl. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl. DR GO; GO:0005874; C:microtubule; IEA:Ensembl. DR GO; GO:0061845; C:neuron projection branch point; IEA:Ensembl. DR GO; GO:0044306; C:neuron projection terminus; IEA:Ensembl. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0099524; C:postsynaptic cytosol; IEA:Ensembl. DR GO; GO:0099092; C:postsynaptic density, intracellular component; IEA:Ensembl. DR GO; GO:0099523; C:presynaptic cytosol; IEA:Ensembl. DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell. DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl. DR GO; GO:0030141; C:secretory granule; IEA:Ensembl. DR GO; GO:0097060; C:synaptic membrane; IEA:Ensembl. DR GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; HDA:BHF-UCL. DR GO; GO:0008093; F:cytoskeletal anchor activity; TAS:ProtInc. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl. DR GO; GO:0070064; F:proline-rich region binding; IDA:UniProtKB. DR GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl. DR GO; GO:0001221; F:transcription coregulator binding; IEA:Ensembl. DR GO; GO:0051764; P:actin crosslink formation; ISS:UniProtKB. DR GO; GO:0051017; P:actin filament bundle assembly; ISS:UniProtKB. DR GO; GO:0007409; P:axonogenesis; TAS:ProtInc. DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl. DR GO; GO:1905232; P:cellular response to L-glutamate; IEA:Ensembl. DR GO; GO:0016358; P:dendrite development; IEA:Ensembl. DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:ProtInc. DR GO; GO:0007009; P:plasma membrane organization; IEA:InterPro. DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IBA:GO_Central. DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IEA:Ensembl. DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IEA:Ensembl. DR GO; GO:0035418; P:protein localization to synapse; IEA:Ensembl. DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB. DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB. DR GO; GO:1905274; P:regulation of modification of postsynaptic actin cytoskeleton; IEA:Ensembl. DR GO; GO:0048167; P:regulation of synaptic plasticity; IEA:Ensembl. DR CDD; cd07646; I-BAR_IMD_IRSp53; 1. DR CDD; cd11915; SH3_Irsp53; 1. DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR027267; AH/BAR_dom_sf. DR InterPro; IPR013606; I-BAR_dom. DR InterPro; IPR027681; IRSp53/IRTKS/Pinkbar. DR InterPro; IPR030128; IRSp53_I-BAR_dom. DR InterPro; IPR035594; Irsp53_SH3. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR PANTHER; PTHR14206; BRAIN-SPECIFIC ANGIOGENESIS INHIBITOR 1-ASSOCIATED PROTEIN 2; 1. DR PANTHER; PTHR14206:SF3; BRAIN-SPECIFIC ANGIOGENESIS INHIBITOR 1-ASSOCIATED PROTEIN 2; 1. DR Pfam; PF08397; IMD; 1. DR Pfam; PF07653; SH3_2; 1. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF103657; BAR/IMD domain-like; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS51338; IMD; 1. DR PROSITE; PS50002; SH3; 1. DR UCD-2DPAGE; Q9UQB8; -. DR Genevisible; Q9UQB8; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell projection; Coiled coil; KW Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein; Reference proteome; KW SH3 domain. FT CHAIN 1..552 FT /note="Brain-specific angiogenesis inhibitor 1-associated FT protein 2" FT /id="PRO_0000064816" FT DOMAIN 1..250 FT /note="IMD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00668" FT DOMAIN 374..437 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT REGION 295..369 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 447..466 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 525..552 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 132..153 FT /evidence="ECO:0000255" FT COMPBIAS 322..367 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 261 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 296 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 323 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 325 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 336 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 340 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 346 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 360 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 366 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 384 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 395 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BKX1" FT MOD_RES 454 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT VAR_SEQ 356 FT /note="T -> TA (in isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4" FT /id="VSP_015502" FT VAR_SEQ 512..552 FT /note="RNPFAHVQLKPTVTNDRCDLSAQGPEGREHGDGSARTLAGR -> SGSGTLV FT STV (in isoform 4 and isoform 6)" FT /evidence="ECO:0000303|PubMed:10332026, FT ECO:0000303|PubMed:10343108, ECO:0000303|PubMed:15489334, FT ECO:0000303|Ref.4" FT /id="VSP_015503" FT VAR_SEQ 512..552 FT /note="RNPFAHVQLKPTVTNDRCDLSAQGPEGREHGDGSARTLAGR -> SADVEVA FT RF (in isoform 5)" FT /evidence="ECO:0000303|PubMed:10343108" FT /id="VSP_015504" FT VAR_SEQ 513..552 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_015505" FT VAR_SEQ 529..552 FT /note="CDLSAQGPEGREHGDGSARTLAGR -> SAPLLS (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_015506" FT VARIANT 519 FT /note="Q -> R (in dbSNP:rs4969391)" FT /id="VAR_050686" FT MUTAGEN 142 FT /note="K->E: Abolishes actin-bundling and filopodia FT formation; when associated with E-143; E-146 and E147." FT /evidence="ECO:0000269|PubMed:15635447" FT MUTAGEN 143 FT /note="K->E: Abolishes actin-bundling and filopodia FT formation; when associated with E-142; E-146 and E147." FT /evidence="ECO:0000269|PubMed:15635447" FT MUTAGEN 146 FT /note="K->E: Abolishes actin-bundling and filopodia FT formation; when associated with E-142; E-143 and E147." FT /evidence="ECO:0000269|PubMed:15635447" FT MUTAGEN 147 FT /note="K->E: Abolishes actin-bundling and filopodia FT formation; when associated with E-142; E-143 and E146." FT /evidence="ECO:0000269|PubMed:15635447" FT MUTAGEN 267 FT /note="I->N: Loss of interaction with CDC42. Loss of FT stimulation of neurite growth." FT /evidence="ECO:0000269|PubMed:11157984" FT MUTAGEN 413 FT /note="W->G: Impairs the SH3 domain and abolishes the FT interaction with EPS8." FT /evidence="ECO:0000269|PubMed:17115031" FT MUTAGEN 427 FT /note="F->A: Loss of interaction with ENAH and no induction FT of filopodia; when associated with A-428." FT /evidence="ECO:0000269|PubMed:11696321" FT MUTAGEN 428 FT /note="P->A: Loss of interaction with ENAH and no induction FT of filopodia; when associated with A-427." FT /evidence="ECO:0000269|PubMed:11696321" FT CONFLICT 84 FT /note="R -> W (in Ref. 4; BAD96390)" FT /evidence="ECO:0000305" FT CONFLICT 415 FT /note="Y -> H (in Ref. 4; BAD96390)" FT /evidence="ECO:0000305" FT CONFLICT 473 FT /note="A -> T (in Ref. 4; BAD96390)" FT /evidence="ECO:0000305" FT HELIX 5..22 FT /evidence="ECO:0007829|PDB:2YKT" FT HELIX 24..64 FT /evidence="ECO:0007829|PDB:2YKT" FT STRAND 66..68 FT /evidence="ECO:0007829|PDB:2YKT" FT HELIX 70..98 FT /evidence="ECO:0007829|PDB:2YKT" FT TURN 99..101 FT /evidence="ECO:0007829|PDB:2YKT" FT HELIX 102..146 FT /evidence="ECO:0007829|PDB:2YKT" FT HELIX 150..152 FT /evidence="ECO:0007829|PDB:1WDZ" FT TURN 154..157 FT /evidence="ECO:0007829|PDB:1Y2O" FT HELIX 159..228 FT /evidence="ECO:0007829|PDB:2YKT" FT HELIX 238..246 FT /evidence="ECO:0007829|PDB:1Y2O" FT HELIX 281..286 FT /evidence="ECO:0007829|PDB:4JS0" FT STRAND 378..383 FT /evidence="ECO:0007829|PDB:3RNJ" FT STRAND 401..404 FT /evidence="ECO:0007829|PDB:3RNJ" FT STRAND 406..408 FT /evidence="ECO:0007829|PDB:3RNJ" FT STRAND 413..418 FT /evidence="ECO:0007829|PDB:3RNJ" FT TURN 419..421 FT /evidence="ECO:0007829|PDB:3RNJ" FT STRAND 424..428 FT /evidence="ECO:0007829|PDB:3RNJ" FT HELIX 429..431 FT /evidence="ECO:0007829|PDB:3RNJ" FT STRAND 432..434 FT /evidence="ECO:0007829|PDB:3RNJ" FT TURN 458..460 FT /evidence="ECO:0007829|PDB:6ZEI" SQ SEQUENCE 552 AA; 60868 MW; 3B9EDC6405DCC99D CRC64; MSLSRSEEMH RLTENVYKTI MEQFNPSLRN FIAMGKNYEK ALAGVTYAAK GYFDALVKMG ELASESQGSK ELGDVLFQMA EVHRQIQNQL EEMLKSFHNE LLTQLEQKVE LDSRYLSAAL KKYQTEQRSK GDALDKCQAE LKKLRKKSQG SKNPQKYSDK ELQYIDAISN KQGELENYVS DGYKTALTEE RRRFCFLVEK QCAVAKNSAA YHSKGKELLA QKLPLWQQAC ADPSKIPERA VQLMQQVASN GATLPSALSA SKSNLVISDP IPGAKPLPVP PELAPFVGRM SAQESTPIMN GVTGPDGEDY SPWADRKAAQ PKSLSPPQSQ SKLSDSYSNT LPVRKSVTPK NSYATTENKT LPRSSSMAAG LERNGRMRVK AIFSHAAGDN STLLSFKEGD LITLLVPEAR DGWHYGESEK TKMRGWFPFS YTRVLDSDGS DRLHMSLQQG KSSSTGNLLD KDDLAIPPPD YGAASRAFPA QTASGFKQRP YSVAVPAFSQ GLDDYGARSM SRNPFAHVQL KPTVTNDRCD LSAQGPEGRE HGDGSARTLA GR //