BAIP2_HUMAN
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 03-AUG-2022, entry version 195.
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=3; 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; Q13625-3: TP53BP2; NbExp=3; IntAct=EBI-525456, EBI-10175039;
CC Q9UQB8; P63104: YWHAZ; NbExp=3; 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}.
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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. [Q9UQB8-6]
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; 144.
DR DIP; DIP-29272N; -.
DR IntAct; Q9UQB8; 100.
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 BioMuta; BAIAP2; -.
DR DMDM; 73917636; -.
DR UCD-2DPAGE; Q9UQB8; -.
DR EPD; Q9UQB8; -.
DR jPOST; Q9UQB8; -.
DR MassIVE; Q9UQB8; -.
DR MaxQB; Q9UQB8; -.
DR PaxDb; Q9UQB8; -.
DR PeptideAtlas; Q9UQB8; -.
DR PRIDE; 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 ABCD; Q9UQB8; 11 sequenced antibodies.
DR Antibodypedia; 19790; 561 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 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; EYAVHSH; -.
DR OrthoDB; 457637at2759; -.
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; 22 hits in 1089 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 170 other tissues.
DR ExpressionAtlas; Q9UQB8; baseline and differential.
DR Genevisible; Q9UQB8; HS.
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:UniProtKB.
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:0005794; C:Golgi apparatus; 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:0005791; C:rough endoplasmic reticulum; 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:0008022; F:protein C-terminus binding; TAS:ProtInc.
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:0007420; P:brain development; IEA:Ensembl.
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:0099564; P:modification of synaptic structure, modulating synaptic transmission; IEA:Ensembl.
DR GO; GO:0007009; P:plasma membrane organization; IEA:InterPro.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IBA:GO_Central.
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 GO; GO:0009617; P:response to bacterium; IMP:UniProtKB.
DR CDD; cd11915; SH3_Irsp53; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR013606; I-BAR_dom.
DR InterPro; IPR030128; IRSp53.
DR InterPro; IPR027681; IRSp53/IRTKS/Pinkbar.
DR InterPro; IPR035594; Irsp53_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR14206; PTHR14206; 1.
DR PANTHER; PTHR14206:SF3; PTHR14206:SF3; 1.
DR Pfam; PF08397; IMD; 1.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51338; IMD; 1.
DR PROSITE; PS50002; SH3; 1.
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
