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Q9UQB8 (BAIP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Brain-specific angiogenesis inhibitor 1-associated protein 2

Short name=BAI-associated protein 2
Short name=BAI1-associated protein 2
Short name=Protein BAP2
Alternative name(s):
Fas ligand-associated factor 3
Short name=FLAF3
Insulin receptor substrate p53/p58
Short name=IRS-58
Short name=IRSp53/58
Insulin receptor substrate protein of 53 kDa
Short name=IRSp53
Short name=Insulin receptor substrate p53
Gene names
Name:BAIAP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length552 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.7 Ref.8 Ref.12 Ref.13 Ref.17

Subunit structure

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. Ref.1 Ref.2 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.16 Ref.17

Subcellular location

Cytoplasm. Membrane; Peripheral membrane protein. Cell projectionfilopodium. Cell projectionruffle. Cytoplasmcytoskeleton. 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. Ref.1 Ref.2 Ref.10 Ref.11 Ref.17

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 isubiquitous, with the highest expression in liver, prostate, testis and placenta. Ref.1 Ref.2 Ref.9

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. Ref.12

The SH3 domain interacts with ATN1, BAI1, WASF1, WASF2, SHANK1, DIAPH1 and ENAH. Ref.12

Post-translational modification

Phosphorylated on tyrosine residues by INSR in response to insulin treatment. Ref.2

Sequence similarities

Contains 1 IMD (IRSp53/MIM homology) domain.

Contains 1 SH3 domain.

Caution

It is uncertain whether Met-1 or Met-59 is the initiator.

Ontologies

Keywords
   Cellular componentCell projection
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
SH3 domain
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

actin crosslink formation

Inferred from sequence or structural similarity. Source: UniProtKB

actin filament bundle assembly

Inferred from sequence or structural similarity. Source: UniProtKB

axonogenesis

Traceable author statement Ref.1. Source: ProtInc

dendrite development

Inferred from electronic annotation. Source: Ensembl

filopodium assembly

Inferred from electronic annotation. Source: InterPro

innate immune response

Traceable author statement. Source: Reactome

insulin receptor signaling pathway

Traceable author statement Ref.1. Source: ProtInc

regulation of actin cytoskeleton organization

Inferred from mutant phenotype Ref.17. Source: UniProtKB

regulation of cell shape

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of synaptic plasticity

Inferred from electronic annotation. Source: Ensembl

response to bacterium

Inferred from mutant phenotype Ref.17. Source: UniProtKB

   Cellular_componentcytoplasm

Traceable author statement Ref.1. Source: ProtInc

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from direct assay Ref.17. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

filopodium

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuron projection

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement Ref.1. Source: ProtInc

ruffle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncytoskeletal adaptor activity

Traceable author statement Ref.1. Source: ProtInc

identical protein binding

Inferred from physical interaction Ref.8Ref.12. Source: IntAct

proline-rich region binding

Inferred from direct assay Ref.17. Source: UniProtKB

protein C-terminus binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UQB8-1)

Also known as: IRSp53(L);

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9UQB8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     529-552: CDLSAQGPEGREHGDGSARTLAGR → SAPLLS
Isoform 3 (identifier: Q9UQB8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     513-552: Missing.
Isoform 4 (identifier: Q9UQB8-4)

Also known as: BAIAP2-alpha;

The sequence of this isoform differs from the canonical sequence as follows:
     512-552: RNPFAHVQLKPTVTNDRCDLSAQGPEGREHGDGSARTLAGR → SGSGTLVSTV
Isoform 5 (identifier: Q9UQB8-5)

Also known as: BAIAP2-beta;

The sequence of this isoform differs from the canonical sequence as follows:
     512-552: RNPFAHVQLKPTVTNDRCDLSAQGPEGREHGDGSARTLAGR → SADVEVARF
Isoform 6 (identifier: Q9UQB8-6)

The sequence of this isoform differs from the canonical sequence as follows:
     356-356: T → TA
     512-552: RNPFAHVQLKPTVTNDRCDLSAQGPEGREHGDGSARTLAGR → SGSGTLVSTV

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 552552Brain-specific angiogenesis inhibitor 1-associated protein 2
PRO_0000064816

Regions

Domain1 – 250250IMD
Domain374 – 43764SH3
Coiled coil132 – 15322 Potential

Amino acid modifications

Modified residue2961Phosphothreonine Ref.2 Ref.14
Modified residue3231Phosphoserine Ref.2 Ref.14
Modified residue3251Phosphoserine Ref.2 Ref.14
Modified residue3401Phosphothreonine Ref.2 Ref.18
Modified residue3461Phosphoserine Ref.2 Ref.14
Modified residue3661Phosphoserine Ref.2 Ref.14
Modified residue4541Phosphoserine Ref.2 Ref.20

Natural variations

Alternative sequence3561T → TA in isoform 6.
VSP_015502
Alternative sequence512 – 55241RNPFA…TLAGR → SGSGTLVSTV in isoform 4 and isoform 6.
VSP_015503
Alternative sequence512 – 55241RNPFA…TLAGR → SADVEVARF in isoform 5.
VSP_015504
Alternative sequence513 – 55240Missing in isoform 3.
VSP_015505
Alternative sequence529 – 55224CDLSA…TLAGR → SAPLLS in isoform 2.
VSP_015506
Natural variant5191Q → R.
Corresponds to variant rs4969391 [ dbSNP | Ensembl ].
VAR_050686

Experimental info

Mutagenesis1421K → E: Abolishes actin-bundling and filopodia formation; when associated with E-143; E-146 and E147. Ref.21
Mutagenesis1431K → E: Abolishes actin-bundling and filopodia formation; when associated with E-142; E-146 and E147. Ref.21
Mutagenesis1461K → E: Abolishes actin-bundling and filopodia formation; when associated with E-142; E-143 and E147. Ref.21
Mutagenesis1471K → E: Abolishes actin-bundling and filopodia formation; when associated with E-142; E-143 and E146. Ref.21
Mutagenesis2671I → N: Loss of interaction with CDC42. Loss of stimulation of neurite growth. Ref.9
Mutagenesis4131W → G: Impairs the SH3 domain and abolishes the interaction with EPS8. Ref.13
Mutagenesis4271F → A: Loss of interaction with ENAH and no induction of filopodia; when associated with A-428. Ref.8
Mutagenesis4281P → A: Loss of interaction with ENAH and no induction of filopodia; when associated with A-427. Ref.8
Sequence conflict841R → W in BAD96390. Ref.4
Sequence conflict4151Y → H in BAD96390. Ref.4
Sequence conflict4731A → T in BAD96390. Ref.4

Secondary structure

................................ 552
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (IRSp53(L)) [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 3B9EDC6405DCC99D

FASTA55260,868
        10         20         30         40         50         60 
MSLSRSEEMH RLTENVYKTI MEQFNPSLRN FIAMGKNYEK ALAGVTYAAK GYFDALVKMG 

        70         80         90        100        110        120 
ELASESQGSK ELGDVLFQMA EVHRQIQNQL EEMLKSFHNE LLTQLEQKVE LDSRYLSAAL 

       130        140        150        160        170        180 
KKYQTEQRSK GDALDKCQAE LKKLRKKSQG SKNPQKYSDK ELQYIDAISN KQGELENYVS 

       190        200        210        220        230        240 
DGYKTALTEE RRRFCFLVEK QCAVAKNSAA YHSKGKELLA QKLPLWQQAC ADPSKIPERA 

       250        260        270        280        290        300 
VQLMQQVASN GATLPSALSA SKSNLVISDP IPGAKPLPVP PELAPFVGRM SAQESTPIMN 

       310        320        330        340        350        360 
GVTGPDGEDY SPWADRKAAQ PKSLSPPQSQ SKLSDSYSNT LPVRKSVTPK NSYATTENKT 

       370        380        390        400        410        420 
LPRSSSMAAG LERNGRMRVK AIFSHAAGDN STLLSFKEGD LITLLVPEAR DGWHYGESEK 

       430        440        450        460        470        480 
TKMRGWFPFS YTRVLDSDGS DRLHMSLQQG KSSSTGNLLD KDDLAIPPPD YGAASRAFPA 

       490        500        510        520        530        540 
QTASGFKQRP YSVAVPAFSQ GLDDYGARSM SRNPFAHVQL KPTVTNDRCD LSAQGPEGRE 

       550 
HGDGSARTLA GR 

« Hide

Isoform 2 [UniParc].

Checksum: E63C4C08C48964B7
Show »

FASTA53459,014
Isoform 3 [UniParc].

Checksum: 985ACC2B8DBEE7C3
Show »

FASTA51256,626
Isoform 4 (BAIAP2-alpha) [UniParc].

Checksum: 618A09FDBEB3A5C3
Show »

FASTA52157,359
Isoform 5 (BAIAP2-beta) [UniParc].

Checksum: FC6852BB490F6C0B
Show »

FASTA52057,445
Isoform 6 [UniParc].

Checksum: 58146A293AF313BC
Show »

FASTA52257,430

References

« Hide 'large scale' references
[1]"Identification of BAIAP2 (BAI-associated protein 2), a novel human homologue of hamster IRSp53, whose SH3 domain interacts with the cytoplasmic domain of BAI1."
Oda K., Shiratsuchi T., Nishimori H., Inazawa J., Yoshikawa H., Taketani Y., Nakamura Y., Tokino T.
Cytogenet. Cell Genet. 84:75-82(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), INTERACTION WITH BAI1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Fetal brain.
[2]"Dentatorubral-pallidoluysian atrophy protein interacts through a proline-rich region near polyglutamine with the SH3 domain of an insulin receptor tyrosine kinase substrate."
Okamura-Oho Y., Miyashita T., Ohmi K., Yamada M.
Hum. Mol. Genet. 8:947-957(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4), PHOSPHORYLATION AT TYROSINE RESIDUES, SUBCELLULAR LOCATION, INTERACTION WITH ATN1, TISSUE SPECIFICITY.
Tissue: Fetal brain.
[3]"Genomic structure and alternative splicing of the insulin receptor tyrosine kinase substrate of 53-kDa protein."
Miyahara A., Okumura-Oho Y., Miyashita T., Hoshika A., Yamada M.
J. Hum. Genet. 48:410-414(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2; 4 AND 5).
[4]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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
Tissue: Brain.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 6).
Tissue: Brain and Duodenum.
[6]"A Fas-ligand associated factor 3, FLAF3, potentiates Fas-ligand stability."
Hachiya T., Kobayasi A., Touji S., Tamai K.
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-328.
Tissue: Placenta.
[7]"IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling."
Miki H., Yamaguchi H., Suetsugu S., Takenawa T.
Nature 408:732-735(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RAC1; CDC42; WASF1 AND WASF2.
[8]"Cdc42 induces filopodia by promoting the formation of an IRSp53:Mena complex."
Krugmann S., Jordens I., Gevaert K., Driessens M., Vandekerckhove J., Hall A.
Curr. Biol. 11:1645-1655(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CDC42 AND ENAH, MUTAGENESIS OF PHE-427 AND PRO-428.
[9]"Cdc42Hs facilitates cytoskeletal reorganization and neurite outgrowth by localizing the 58-kD insulin receptor substrate to filamentous actin."
Govind S., Kozma R., Monfries C., Lim L., Ahmed S.
J. Cell Biol. 152:579-594(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDC42, MUTAGENESIS OF ILE-267, TISSUE SPECIFICITY.
[10]"The insulin receptor substrate IRSp53 links postsynaptic shank1 to the small G-protein cdc42."
Soltau M., Richter D., Kreienkamp H.-J.
Mol. Cell. Neurosci. 21:575-583(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SHANK1; SHANK2; SHANK3 AND CDC42, SUBCELLULAR LOCATION.
[11]"IRSp53/Eps8 complex is important for positive regulation of Rac and cancer cell motility/invasiveness."
Funato Y., Terabayashi T., Suenaga N., Seiki M., Takenawa T., Miki H.
Cancer Res. 64:5237-5244(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EPS8, SUBCELLULAR LOCATION.
[12]"A novel actin bundling/filopodium-forming domain conserved in insulin receptor tyrosine kinase substrate p53 and missing in metastasis protein."
Yamagishi A., Masuda M., Ohki T., Onishi H., Mochizuki N.
J. Biol. Chem. 279:14929-14936(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN, FUNCTION.
[13]"Regulation of cell shape by Cdc42 is mediated by the synergic actin-bundling activity of the Eps8-IRSp53 complex."
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.
Nat. Cell Biol. 8:1337-1347(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EPS8, MUTAGENESIS OF TRP-413.
[14]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-296; SER-323; SER-325; SER-346 AND SER-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"IRSp53 links the enterohemorrhagic E. coli effectors Tir and EspFU for actin pedestal formation."
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.
Cell Host Microbe 5:244-258(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH E.COLI EFFECTOR PROTEIN ESPF(U) AND WITH E.COLI INTIMIN RECEPTOR TIR.
[17]"Insulin receptor tyrosine kinase substrate links the E. coli O157:H7 actin assembly effectors Tir and EspF(U) during pedestal formation."
Vingadassalom D., Kazlauskas A., Skehan B., Cheng H.C., Magoun L., Robbins D., Rosen M.K., Saksela K., Leong J.M.
Proc. Natl. Acad. Sci. U.S.A. 106:6754-6759(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH E.COLI EFFECTOR PROTEIN ESPF(U), SUBCELLULAR LOCATION.
[18]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-340, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-454, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Structural basis of filopodia formation induced by the IRSp53/MIM homology domain of human IRSp53."
Millard T.H., Bompard G., Heung M.Y., Dafforn T.R., Scott D.J., Machesky L.M., Fuetterer K.
EMBO J. 24:240-250(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-250, MUTAGENESIS OF LYS-142; LYS-143; LYS-146 AND LYS-147.
[22]"Crystal structure of RCB domain of IRSP53."
RIKEN structural genomics initiative (RSGI)
Submitted (JUN-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS) OF 1-228.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB015019 mRNA. Translation: BAA36586.1.
AB015020 mRNA. Translation: BAA36587.1.
AB017119 mRNA. Translation: BAA74773.1.
AB017120 mRNA. Translation: BAA74774.1.
AB104726 Genomic DNA. Translation: BAC57945.1.
AB104726 Genomic DNA. Translation: BAC57946.1.
AB104726 Genomic DNA. Translation: BAC57947.1.
AB104726 Genomic DNA. Translation: BAC57948.1.
AK222670 mRNA. Translation: BAD96390.1.
BC014020 mRNA. Translation: AAH14020.1.
BC032559 mRNA. Translation: AAH32559.1.
U70669 mRNA. Translation: AAB93497.1.
RefSeqNP_001138360.1. NM_001144888.1.
NP_006331.1. NM_006340.2.
NP_059344.1. NM_017450.2.
NP_059345.1. NM_017451.2.
XP_005257005.1. XM_005256948.1.
UniGeneHs.128316.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WDZX-ray2.63A/B1-228[»]
1Y2OX-ray2.20A/B1-250[»]
2YKTX-ray2.11A1-250[»]
3RNJX-ray1.50A375-436[»]
4JS0X-ray1.90B260-291[»]
ProteinModelPortalQ9UQB8.
SMRQ9UQB8. Positions 1-248, 374-436.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115721. 25 interactions.
DIPDIP-29272N.
IntActQ9UQB8. 26 interactions.
MINTMINT-92955.
STRING9606.ENSP00000316338.

PTM databases

PhosphoSiteQ9UQB8.

Polymorphism databases

DMDM73917636.

2D gel databases

UCD-2DPAGEQ9UQB8.

Proteomic databases

PaxDbQ9UQB8.
PRIDEQ9UQB8.

Protocols and materials databases

DNASU10458.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000321280; ENSP00000315685; ENSG00000175866. [Q9UQB8-4]
ENST00000321300; ENSP00000316338; ENSG00000175866. [Q9UQB8-1]
ENST00000428708; ENSP00000401022; ENSG00000175866. [Q9UQB8-2]
ENST00000435091; ENSP00000413069; ENSG00000175866. [Q9UQB8-5]
ENST00000575712; ENSP00000458964; ENSG00000175866. [Q9UQB8-3]
GeneID10458.
KEGGhsa:10458.
UCSCuc002jyz.4. human. [Q9UQB8-1]
uc002jza.2. human. [Q9UQB8-4]
uc002jzc.2. human. [Q9UQB8-6]
uc002jzd.2. human. [Q9UQB8-5]
uc002jzf.2. human. [Q9UQB8-2]

Organism-specific databases

CTD10458.
GeneCardsGC17P079008.
HGNCHGNC:947. BAIAP2.
HPAHPA023310.
HPA027421.
MIM605475. gene.
neXtProtNX_Q9UQB8.
PharmGKBPA25251.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG71665.
HOVERGENHBG054462.
InParanoidQ9UQB8.
KOK05627.
OrthoDBEOG7N0C3W.
PhylomeDBQ9UQB8.
TreeFamTF325648.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkQ9UQB8.

Gene expression databases

ArrayExpressQ9UQB8.
BgeeQ9UQB8.
CleanExHS_BAIAP2.
GenevestigatorQ9UQB8.

Family and domain databases

InterProIPR027681. BAIAP2.
IPR013606. IRSp53/MIM_homology_IMD.
IPR001452. SH3_domain.
[Graphical view]
PANTHERPTHR14206. PTHR14206. 1 hit.
PfamPF08397. IMD. 1 hit.
[Graphical view]
SMARTSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS51338. IMD. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9UQB8.
GeneWikiBAIAP2.
GenomeRNAi10458.
NextBio39651.
PROQ9UQB8.
SOURCESearch...

Entry information

Entry nameBAIP2_HUMAN
AccessionPrimary (citable) accession number: Q9UQB8
Secondary accession number(s): O43858 expand/collapse secondary AC list , Q53HB1, Q86WC1, Q8N5C0, Q96CR7, Q9UBR3, Q9UQ43
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

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