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Brain-specific angiogenesis inhibitor 1-associated protein 2 (BAI-associated protein 2) (BAI1-associated protein 2) (Protein BAP2) (Fas ligand-associated factor 3) (FLAF3) (Insulin receptor substrate p53/p58) (IRS-58) (IRSp53/58) (Insulin receptor substrate protein of 53 kDa) (IRSp53) (Insulin receptor substrate p53)

 BAIP2_HUMAN             Reviewed;         552 AA.
Q9UQB8; O43858; Q53HB1; Q86WC1; Q8N5C0; Q96CR7; Q9UBR3; Q9UQ43;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
22-NOV-2017, entry version 164.
RecName: Full=Brain-specific angiogenesis inhibitor 1-associated protein 2;
Short=BAI-associated protein 2;
Short=BAI1-associated protein 2;
Short=Protein BAP2;
AltName: Full=Fas ligand-associated factor 3;
Short=FLAF3;
AltName: Full=Insulin receptor substrate p53/p58;
Short=IRS-58;
Short=IRSp53/58;
AltName: Full=Insulin receptor substrate protein of 53 kDa;
Short=IRSp53;
Short=Insulin receptor substrate p53;
Name=BAIAP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), INTERACTION WITH
ADGRB1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Fetal brain;
PubMed=10343108;
Oda K., Shiratsuchi T., Nishimori H., Inazawa J., Yoshikawa H.,
Taketani Y., Nakamura Y., Tokino T.;
"Identification of BAIAP2 (BAI-associated protein 2), a novel human
homologue of hamster IRSp53, whose SH3 domain interacts with the
cytoplasmic domain of BAI1.";
Cytogenet. Cell Genet. 84:75-82(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4), PHOSPHORYLATION AT
TYROSINE RESIDUES, SUBCELLULAR LOCATION, INTERACTION WITH ATN1, AND
TISSUE SPECIFICITY.
TISSUE=Fetal brain;
PubMed=10332026; DOI=10.1093/hmg/8.6.947;
Okamura-Oho Y., Miyashita T., Ohmi K., Yamada M.;
"Dentatorubral-pallidoluysian atrophy protein interacts through a
proline-rich region near polyglutamine with the SH3 domain of an
insulin receptor tyrosine kinase substrate.";
Hum. Mol. Genet. 8:947-957(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2; 4 AND 5).
PubMed=12884081; DOI=10.1007/s10038-003-0047-x;
Miyahara A., Okumura-Oho Y., Miyashita T., Hoshika A., Yamada M.;
"Genomic structure and alternative splicing of the insulin receptor
tyrosine kinase substrate of 53-kDa protein.";
J. Hum. Genet. 48:410-414(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
TISSUE=Brain;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 6).
TISSUE=Brain, and Duodenum;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-328.
TISSUE=Placenta;
Hachiya T., Kobayasi A., Touji S., Tamai K.;
"A Fas-ligand associated factor 3, FLAF3, potentiates Fas-ligand
stability.";
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
[7]
FUNCTION, AND INTERACTION WITH RAC1; CDC42; WASF1 AND WASF2.
PubMed=11130076; DOI=10.1038/35047107;
Miki H., Yamaguchi H., Suetsugu S., Takenawa T.;
"IRSp53 is an essential intermediate between Rac and WAVE in the
regulation of membrane ruffling.";
Nature 408:732-735(2000).
[8]
FUNCTION, INTERACTION WITH CDC42 AND ENAH, AND MUTAGENESIS OF PHE-427
AND PRO-428.
PubMed=11696321; DOI=10.1016/S0960-9822(01)00506-1;
Krugmann S., Jordens I., Gevaert K., Driessens M., Vandekerckhove J.,
Hall A.;
"Cdc42 induces filopodia by promoting the formation of an IRSp53:Mena
complex.";
Curr. Biol. 11:1645-1655(2001).
[9]
INTERACTION WITH CDC42, MUTAGENESIS OF ILE-267, AND TISSUE
SPECIFICITY.
PubMed=11157984; DOI=10.1083/jcb.152.3.579;
Govind S., Kozma R., Monfries C., Lim L., Ahmed S.;
"Cdc42Hs facilitates cytoskeletal reorganization and neurite outgrowth
by localizing the 58-kD insulin receptor substrate to filamentous
actin.";
J. Cell Biol. 152:579-594(2001).
[10]
INTERACTION WITH SHANK1; SHANK2; SHANK3 AND CDC42, AND SUBCELLULAR
LOCATION.
PubMed=12504591; DOI=10.1006/mcne.2002.1201;
Soltau M., Richter D., Kreienkamp H.-J.;
"The insulin receptor substrate IRSp53 links postsynaptic shank1 to
the small G-protein cdc42.";
Mol. Cell. Neurosci. 21:575-583(2002).
[11]
INTERACTION WITH EPS8, AND SUBCELLULAR LOCATION.
PubMed=15289329; DOI=10.1158/0008-5472.CAN-04-0327;
Funato Y., Terabayashi T., Suenaga N., Seiki M., Takenawa T., Miki H.;
"IRSp53/Eps8 complex is important for positive regulation of Rac and
cancer cell motility/invasiveness.";
Cancer Res. 64:5237-5244(2004).
[12]
DOMAIN, AND FUNCTION.
PubMed=14752106; DOI=10.1074/jbc.M309408200;
Yamagishi A., Masuda M., Ohki T., Onishi H., Mochizuki N.;
"A novel actin bundling/filopodium-forming domain conserved in insulin
receptor tyrosine kinase substrate p53 and missing in metastasis
protein.";
J. Biol. Chem. 279:14929-14936(2004).
[13]
FUNCTION, INTERACTION WITH EPS8, AND MUTAGENESIS OF TRP-413.
PubMed=17115031; DOI=10.1038/ncb1502;
Disanza A., Mantoani S., Hertzog M., Gerboth S., Frittoli E.,
Steffen A., Berhoerster K., Kreienkamp H.J., Milanesi F.,
Di Fiore P.P., Ciliberto A., Stradal T.E., Scita G.;
"Regulation of cell shape by Cdc42 is mediated by the synergic actin-
bundling activity of the Eps8-IRSp53 complex.";
Nat. Cell Biol. 8:1337-1347(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-296; SER-323; SER-325;
SER-346 AND SER-366, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[16]
INTERACTION WITH E.COLI EFFECTOR PROTEIN ESPF(U) AND WITH E.COLI
INTIMIN RECEPTOR TIR.
PubMed=19286134; DOI=10.1016/j.chom.2009.02.003;
Weiss S.M., Ladwein M., Schmidt D., Ehinger J., Lommel S., Stading K.,
Beutling U., Disanza A., Frank R., Jansch L., Scita G., Gunzer F.,
Rottner K., Stradal T.E.;
"IRSp53 links the enterohemorrhagic E. coli effectors Tir and EspFU
for actin pedestal formation.";
Cell Host Microbe 5:244-258(2009).
[17]
FUNCTION, INTERACTION WITH E.COLI EFFECTOR PROTEIN ESPF(U), AND
SUBCELLULAR LOCATION.
PubMed=19366662; DOI=10.1073/pnas.0809131106;
Vingadassalom D., Kazlauskas A., Skehan B., Cheng H.C., Magoun L.,
Robbins D., Rosen M.K., Saksela K., Leong J.M.;
"Insulin receptor tyrosine kinase substrate links the E. coli O157:H7
actin assembly effectors Tir and EspF(U) during pedestal formation.";
Proc. Natl. Acad. Sci. U.S.A. 106:6754-6759(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-340, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-454, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261; SER-325; SER-336;
THR-340; THR-360; SER-366 AND SER-384, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[23]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-250, AND MUTAGENESIS OF
LYS-142; LYS-143; LYS-146 AND LYS-147.
PubMed=15635447; DOI=10.1038/sj.emboj.7600535;
Millard T.H., Bompard G., Heung M.Y., Dafforn T.R., Scott D.J.,
Machesky L.M., Fuetterer K.;
"Structural basis of filopodia formation induced by the IRSp53/MIM
homology domain of human IRSp53.";
EMBO J. 24:240-250(2005).
[24]
X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS) OF 1-228.
RIKEN structural genomics initiative (RSGI);
"Crystal structure of RCB domain of IRSP53.";
Submitted (JUN-2005) to the PDB data bank.
-!- 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.
Participates in actin bundling when associated with EPS8,
promoting filopodial protrusions. {ECO:0000269|PubMed:11130076,
ECO:0000269|PubMed:11696321, ECO:0000269|PubMed:14752106,
ECO:0000269|PubMed:17115031, ECO:0000269|PubMed:19366662}.
-!- SUBUNIT: Homodimer. Interacts with CDC42 and RAC1 that have been
activated by GTP binding. Interacts with ATN1, ADGRB1, 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. {ECO:0000250, ECO:0000269|PubMed:10332026,
ECO:0000269|PubMed:10343108, ECO:0000269|PubMed:11130076,
ECO:0000269|PubMed:11157984, ECO:0000269|PubMed:11696321,
ECO:0000269|PubMed:12504591, ECO:0000269|PubMed:15289329,
ECO:0000269|PubMed:17115031, ECO:0000269|PubMed:19286134,
ECO:0000269|PubMed:19366662}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-525456, EBI-525456;
Q9UFG5:C19orf25; NbExp=3; IntAct=EBI-525456, EBI-741214;
P60953:CDC42; NbExp=4; IntAct=EBI-6174091, EBI-81752;
P60953-2:CDC42; NbExp=5; IntAct=EBI-6174091, EBI-287394;
Q8CFN2:Cdc42 (xeno); NbExp=2; IntAct=EBI-525456, EBI-7023929;
Q03173:Enah (xeno); NbExp=3; IntAct=EBI-525456, EBI-6083294;
Q12929:EPS8; NbExp=10; IntAct=EBI-525456, EBI-375576;
Q08509:Eps8 (xeno); NbExp=8; IntAct=EBI-525456, EBI-375596;
Q14678:KANK1; NbExp=6; IntAct=EBI-525456, EBI-2556221;
Q14678-2:KANK1; NbExp=4; IntAct=EBI-6174091, EBI-6173812;
Q9NZQ3:NCKIPSD; NbExp=2; IntAct=EBI-525456, EBI-745080;
Q9NZ81:PRR13; NbExp=3; IntAct=EBI-525456, EBI-740924;
P63000:RAC1; NbExp=4; IntAct=EBI-525456, EBI-413628;
Q15428:SF3A2; NbExp=4; IntAct=EBI-9092016, EBI-2462271;
Q15427:SF3B4; NbExp=3; IntAct=EBI-525456, EBI-348469;
Q99593:TBX5; NbExp=4; IntAct=EBI-9092016, EBI-297043;
B7UM99:tir (xeno); NbExp=3; IntAct=EBI-6174091, EBI-2504426;
Q7DB77:tir (xeno); NbExp=5; IntAct=EBI-6174091, EBI-6480811;
Q13625-3:TP53BP2; NbExp=3; IntAct=EBI-525456, EBI-10175039;
P50552:VASP; NbExp=6; IntAct=EBI-6174091, EBI-748201;
Q9Y6W5:WASF2; NbExp=5; IntAct=EBI-6174091, EBI-4290615;
Q8IUH5:ZDHHC17; NbExp=3; IntAct=EBI-9091996, EBI-524753;
-!- 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.
{ECO:0000269|PubMed:10332026, ECO:0000269|PubMed:10343108,
ECO:0000269|PubMed:11157984}.
-!- 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.
{ECO:0000269|PubMed:14752106}.
-!- DOMAIN: The SH3 domain interacts with ATN1, ADGRB1, WASF1, WASF2,
SHANK1, DIAPH1 and ENAH. {ECO:0000269|PubMed:14752106}.
-!- PTM: Phosphorylated on tyrosine residues by INSR in response to
insulin treatment. {ECO:0000269|PubMed:10332026}.
-!- CAUTION: It is uncertain whether Met-1 or Met-59 is the initiator.
{ECO:0000305}.
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EMBL; AB015019; BAA36586.1; -; mRNA.
EMBL; AB015020; BAA36587.1; -; mRNA.
EMBL; AB017119; BAA74773.1; -; mRNA.
EMBL; AB017120; BAA74774.1; -; mRNA.
EMBL; AB104726; BAC57945.1; -; Genomic_DNA.
EMBL; AB104726; BAC57946.1; -; Genomic_DNA.
EMBL; AB104726; BAC57947.1; -; Genomic_DNA.
EMBL; AB104726; BAC57948.1; -; Genomic_DNA.
EMBL; AK222670; BAD96390.1; -; mRNA.
EMBL; BC014020; AAH14020.1; -; mRNA.
EMBL; BC032559; AAH32559.1; -; mRNA.
EMBL; U70669; AAB93497.1; -; mRNA.
CCDS; CCDS11775.1; -. [Q9UQB8-1]
CCDS; CCDS11776.1; -. [Q9UQB8-5]
CCDS; CCDS11777.1; -. [Q9UQB8-4]
CCDS; CCDS45806.1; -. [Q9UQB8-2]
RefSeq; NP_001138360.1; NM_001144888.1. [Q9UQB8-2]
RefSeq; NP_006331.1; NM_006340.2. [Q9UQB8-5]
RefSeq; NP_059344.1; NM_017450.2. [Q9UQB8-4]
RefSeq; NP_059345.1; NM_017451.2. [Q9UQB8-1]
RefSeq; XP_005257005.1; XM_005256948.3. [Q9UQB8-6]
UniGene; Hs.128316; -.
PDB; 1WDZ; X-ray; 2.63 A; A/B=1-228.
PDB; 1Y2O; X-ray; 2.20 A; A/B=1-250.
PDB; 2YKT; X-ray; 2.11 A; A=1-250.
PDB; 3RNJ; X-ray; 1.50 A; A=375-436.
PDB; 4JS0; X-ray; 1.90 A; B=260-291.
PDBsum; 1WDZ; -.
PDBsum; 1Y2O; -.
PDBsum; 2YKT; -.
PDBsum; 3RNJ; -.
PDBsum; 4JS0; -.
ProteinModelPortal; Q9UQB8; -.
SMR; Q9UQB8; -.
BioGrid; 115721; 68.
DIP; DIP-29272N; -.
IntAct; Q9UQB8; 58.
MINT; MINT-92955; -.
STRING; 9606.ENSP00000316338; -.
iPTMnet; Q9UQB8; -.
PhosphoSitePlus; Q9UQB8; -.
BioMuta; BAIAP2; -.
DMDM; 73917636; -.
UCD-2DPAGE; Q9UQB8; -.
EPD; Q9UQB8; -.
PaxDb; Q9UQB8; -.
PeptideAtlas; Q9UQB8; -.
PRIDE; Q9UQB8; -.
DNASU; 10458; -.
Ensembl; ENST00000321280; ENSP00000315685; ENSG00000175866. [Q9UQB8-4]
Ensembl; ENST00000321300; ENSP00000316338; ENSG00000175866. [Q9UQB8-1]
Ensembl; ENST00000428708; ENSP00000401022; ENSG00000175866. [Q9UQB8-2]
Ensembl; ENST00000435091; ENSP00000413069; ENSG00000175866. [Q9UQB8-5]
Ensembl; ENST00000575712; ENSP00000458964; ENSG00000175866. [Q9UQB8-3]
GeneID; 10458; -.
KEGG; hsa:10458; -.
UCSC; uc002jyz.5; human. [Q9UQB8-1]
CTD; 10458; -.
DisGeNET; 10458; -.
EuPathDB; HostDB:ENSG00000175866.15; -.
GeneCards; BAIAP2; -.
HGNC; HGNC:947; BAIAP2.
HPA; HPA023310; -.
HPA; HPA027421; -.
MIM; 605475; gene.
neXtProt; NX_Q9UQB8; -.
OpenTargets; ENSG00000175866; -.
PharmGKB; PA25251; -.
eggNOG; ENOG410IKMM; Eukaryota.
eggNOG; ENOG41110CD; LUCA.
GeneTree; ENSGT00390000005995; -.
HOVERGEN; HBG054462; -.
InParanoid; Q9UQB8; -.
KO; K05627; -.
PhylomeDB; Q9UQB8; -.
TreeFam; TF325648; -.
Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs.
SignaLink; Q9UQB8; -.
SIGNOR; Q9UQB8; -.
ChiTaRS; BAIAP2; human.
EvolutionaryTrace; Q9UQB8; -.
GeneWiki; BAIAP2; -.
GenomeRNAi; 10458; -.
PRO; PR:Q9UQB8; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000175866; -.
CleanEx; HS_BAIAP2; -.
ExpressionAtlas; Q9UQB8; baseline and differential.
Genevisible; Q9UQB8; HS.
GO; GO:0005913; C:cell-cell adherens junction; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0043198; C:dendritic shaft; IEA:Ensembl.
GO; GO:0061846; C:dendritic spine cytoplasm; IEA:Ensembl.
GO; GO:0060076; C:excitatory synapse; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0005874; C:microtubule; IEA:Ensembl.
GO; GO:0061845; C:neuron projection branch point; IEA:Ensembl.
GO; GO:0044306; C:neuron projection terminus; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
GO; GO:0098793; C:presynapse; IEA:Ensembl.
GO; GO:0005791; C:rough endoplasmic reticulum; IEA:Ensembl.
GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
GO; GO:0030141; C:secretory granule; IEA:Ensembl.
GO; GO:0097060; C:synaptic membrane; IEA:Ensembl.
GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0008093; F:cytoskeletal adaptor activity; TAS:ProtInc.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
GO; GO:0070064; F:proline-rich region binding; IDA:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; TAS:ProtInc.
GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
GO; GO:0001221; F:transcription cofactor binding; IEA:Ensembl.
GO; GO:0051764; P:actin crosslink formation; ISS:UniProtKB.
GO; GO:0051017; P:actin filament bundle assembly; ISS:UniProtKB.
GO; GO:0007409; P:axonogenesis; TAS:ProtInc.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl.
GO; GO:1905232; P:cellular response to L-glutamate; IEA:Ensembl.
GO; GO:0016358; P:dendrite development; IEA:Ensembl.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0008286; P:insulin receptor signaling pathway; TAS:ProtInc.
GO; GO:0007009; P:plasma membrane organization; IEA:InterPro.
GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IBA:GO_Central.
GO; GO:0030838; P:positive regulation of actin filament polymerization; IBA:GO_Central.
GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IEA:Ensembl.
GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IEA:Ensembl.
GO; GO:0035418; P:protein localization to synapse; IEA:Ensembl.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
GO; GO:0048167; P:regulation of synaptic plasticity; IEA:Ensembl.
GO; GO:0009617; P:response to bacterium; IMP:UniProtKB.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
CDD; cd11915; SH3_Irsp53; 1.
Gene3D; 1.20.1270.60; -; 1.
InterPro; IPR027267; AH/BAR_dom_sf.
InterPro; IPR013606; I-BAR_dom.
InterPro; IPR030128; IRSp53.
InterPro; IPR027681; IRSp53/IRTKS/Pinkbar.
InterPro; IPR035594; Irsp53_SH3.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
PANTHER; PTHR14206; PTHR14206; 1.
PANTHER; PTHR14206:SF3; PTHR14206:SF3; 1.
Pfam; PF08397; IMD; 1.
Pfam; PF14604; SH3_9; 1.
SMART; SM00326; SH3; 1.
SUPFAM; SSF103657; SSF103657; 1.
SUPFAM; SSF50044; SSF50044; 1.
PROSITE; PS51338; IMD; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell projection; Coiled coil;
Complete proteome; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein;
Polymorphism; Reference proteome; SH3 domain.
CHAIN 1 552 Brain-specific angiogenesis inhibitor 1-
associated protein 2.
/FTId=PRO_0000064816.
DOMAIN 1 250 IMD. {ECO:0000255|PROSITE-
ProRule:PRU00668}.
DOMAIN 374 437 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
COILED 132 153 {ECO:0000255}.
MOD_RES 261 261 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 296 296 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 323 323 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 325 325 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 336 336 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 340 340 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 346 346 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 360 360 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 366 366 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 384 384 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 395 395 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BKX1}.
MOD_RES 454 454 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
VAR_SEQ 356 356 T -> TA (in isoform 6).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.4}.
/FTId=VSP_015502.
VAR_SEQ 512 552 RNPFAHVQLKPTVTNDRCDLSAQGPEGREHGDGSARTLAGR
-> SGSGTLVSTV (in isoform 4 and isoform
6). {ECO:0000303|PubMed:10332026,
ECO:0000303|PubMed:10343108,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.4}.
/FTId=VSP_015503.
VAR_SEQ 512 552 RNPFAHVQLKPTVTNDRCDLSAQGPEGREHGDGSARTLAGR
-> SADVEVARF (in isoform 5).
{ECO:0000303|PubMed:10343108}.
/FTId=VSP_015504.
VAR_SEQ 513 552 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_015505.
VAR_SEQ 529 552 CDLSAQGPEGREHGDGSARTLAGR -> SAPLLS (in
isoform 2). {ECO:0000305}.
/FTId=VSP_015506.
VARIANT 519 519 Q -> R (in dbSNP:rs4969391).
/FTId=VAR_050686.
MUTAGEN 142 142 K->E: Abolishes actin-bundling and
filopodia formation; when associated with
E-143; E-146 and E147.
{ECO:0000269|PubMed:15635447}.
MUTAGEN 143 143 K->E: Abolishes actin-bundling and
filopodia formation; when associated with
E-142; E-146 and E147.
{ECO:0000269|PubMed:15635447}.
MUTAGEN 146 146 K->E: Abolishes actin-bundling and
filopodia formation; when associated with
E-142; E-143 and E147.
{ECO:0000269|PubMed:15635447}.
MUTAGEN 147 147 K->E: Abolishes actin-bundling and
filopodia formation; when associated with
E-142; E-143 and E146.
{ECO:0000269|PubMed:15635447}.
MUTAGEN 267 267 I->N: Loss of interaction with CDC42.
Loss of stimulation of neurite growth.
{ECO:0000269|PubMed:11157984}.
MUTAGEN 413 413 W->G: Impairs the SH3 domain and
abolishes the interaction with EPS8.
{ECO:0000269|PubMed:17115031}.
MUTAGEN 427 427 F->A: Loss of interaction with ENAH and
no induction of filopodia; when
associated with A-428.
{ECO:0000269|PubMed:11696321}.
MUTAGEN 428 428 P->A: Loss of interaction with ENAH and
no induction of filopodia; when
associated with A-427.
{ECO:0000269|PubMed:11696321}.
CONFLICT 84 84 R -> W (in Ref. 4; BAD96390).
{ECO:0000305}.
CONFLICT 415 415 Y -> H (in Ref. 4; BAD96390).
{ECO:0000305}.
CONFLICT 473 473 A -> T (in Ref. 4; BAD96390).
{ECO:0000305}.
HELIX 5 22 {ECO:0000244|PDB:2YKT}.
HELIX 24 64 {ECO:0000244|PDB:2YKT}.
STRAND 66 68 {ECO:0000244|PDB:2YKT}.
HELIX 70 98 {ECO:0000244|PDB:2YKT}.
TURN 99 101 {ECO:0000244|PDB:2YKT}.
HELIX 102 146 {ECO:0000244|PDB:2YKT}.
HELIX 150 152 {ECO:0000244|PDB:1WDZ}.
TURN 154 157 {ECO:0000244|PDB:1Y2O}.
HELIX 159 228 {ECO:0000244|PDB:2YKT}.
HELIX 238 246 {ECO:0000244|PDB:1Y2O}.
HELIX 281 286 {ECO:0000244|PDB:4JS0}.
STRAND 378 383 {ECO:0000244|PDB:3RNJ}.
STRAND 401 404 {ECO:0000244|PDB:3RNJ}.
STRAND 406 408 {ECO:0000244|PDB:3RNJ}.
STRAND 413 418 {ECO:0000244|PDB:3RNJ}.
TURN 419 421 {ECO:0000244|PDB:3RNJ}.
STRAND 424 428 {ECO:0000244|PDB:3RNJ}.
HELIX 429 431 {ECO:0000244|PDB:3RNJ}.
STRAND 432 434 {ECO:0000244|PDB:3RNJ}.
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


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