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Q60437 (BAIP2_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
Alternative name(s):
Insulin receptor substrate protein of 53 kDa
Short name=IRSp53
Short name=Insulin receptor substrate p53
Insulin receptor tyrosine kinase 53 kDa substrate
p58/p53
Gene names
Name:BAIAP2
OrganismCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Protein attributes

Sequence length521 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 By similarity.

Subunit structure

Homodimer. Interacts with CDC42 and RAC1 that have been activated by GTP binding. Interacts with ATN1, BAI1, DIAPH1, EPS8, SHANK1, SHANK2, SHANK3, TIAM1, WASF1 and WASF2. Interacts with ENAH after recruitment of CDC42 By similarity.

Subcellular location

Cytoplasm By similarity. Membrane; Peripheral membrane protein By similarity. Cell projectionfilopodium By similarity. Cell projectionruffle By similarity. Cytoplasmcytoskeleton By similarity. 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 By similarity.

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 By similarity.

The SH3 domain interacts with ATN1, BAI1, WASF1, WASF2, SHANK1, DIAPH1 and ENAH By similarity.

Post-translational modification

Phosphorylated on tyrosine residues by INSR in response to insulin treatment. Ref.1

Sequence similarities

Contains 1 IMD (IRSp53/MIM homology) domain.

Contains 1 SH3 domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NCKIPSDQ9NZQ33EBI-7010040,EBI-745080From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 521521Brain-specific angiogenesis inhibitor 1-associated protein 2
PRO_0000064815

Regions

Domain1 – 250250IMD
Domain375 – 43864SH3
Coiled coil132 – 15322 Potential

Amino acid modifications

Modified residue3241Phosphoserine By similarity
Modified residue3261Phosphoserine By similarity
Modified residue3411Phosphothreonine By similarity
Modified residue3471Phosphoserine By similarity
Modified residue3671Phosphoserine By similarity
Modified residue4551Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q60437 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 58485BD6CAC15DC1

FASTA52157,639
        10         20         30         40         50         60 
MSLSRSEEMH RLTENVYKTI MEQFNPSLRN FIAMGKNYEK ALAGVTFAAK GYFDALVKMG 

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

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

       190        200        210        220        230        240 
DGYKTALTEE RRRFCFLVEK QCAVAKNSAA YHSKGKELLA QKLPVWQQAC ADPNKIPDRA 

       250        260        270        280        290        300 
VQLMQQIASS NGSILPSTLS ASKSNLVISD PIPGAKPLPV PPELAPFVGR MSAQENVPVM 

       310        320        330        340        350        360 
NGVAGPDSED YNPWADRKAA QPKSLSPPQS QSKLSDSYSN TLPVRKSVTP KNSYATTENK 

       370        380        390        400        410        420 
TLPRSSSMAA GLERNGRMRV KAIFSHAAGD NSTLLSFKEG DLITLLVPEA RDGWHYGESE 

       430        440        450        460        470        480 
KTKMRGWFPF SYTRVLDSDG SDRLHMSLQQ GKSSSTGNLL DKDDLAVPPP DYGTSSRAFP 

       490        500        510        520 
TQTAGTFKQR PYSVAVPAFS QGLDDYGARS VSSADVEVAR F 

« Hide

References

[1]"Characterization and cloning of a 58/53-kDa substrate of the insulin receptor tyrosine kinase."
Yeh T.C., Ogawa W., Danielsen A.G., Roth R.A.
J. Biol. Chem. 271:2921-2928(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 71-84 AND 264-285, PHOSPHORYLATION AT TYROSINE RESIDUES.
Tissue: Ovary.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U41899 mRNA. Translation: AAC52436.1.

3D structure databases

ProteinModelPortalQ60437.
SMRQ60437. Positions 1-248, 379-441.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ60437. 1 interaction.
MINTMINT-5314315.

Proteomic databases

PRIDEQ60437.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG054462.

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...

Entry information

Entry nameBAIP2_CRIGR
AccessionPrimary (citable) accession number: Q60437
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: November 1, 1996
Last modified: December 11, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families