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Q6GMN2 (BAIP2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 90. 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·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
Alternative name(s):
Insulin receptor substrate protein of 53 kDa
Short name=IRSp53
Short name=Insulin receptor substrate p53
Insulin receptor tyrosine kinase substrate protein p53
Gene names
Name:Baiap2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length535 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. Binds TIAM1. Interacts with ATN1, BAI1, DIAPH1, EPS8, SHANK1, SHANK2, SHANK3, WASF1 and WASF2. Interacts with ENAH after recruitment of CDC42 By similarity. Ref.5

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.

Tissue specificity

Ubiquitous. Ref.1 Ref.4

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.4

Sequence similarities

Contains 1 IMD (IRSp53/MIM homology) domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Cellular componentCell projection
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
SH3 domain
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin crosslink formation

Inferred from sequence or structural similarity. Source: UniProtKB

actin filament bundle assembly

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite development

Inferred from electronic annotation. Source: Ensembl

filopodium assembly

Inferred from electronic annotation. Source: InterPro

regulation of actin cytoskeleton organization

Inferred from sequence or structural similarity. 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 sequence or structural similarity. Source: UniProtKB

signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentactin cytoskeleton

Inferred from electronic annotation. Source: Ensembl

cell junction

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

filopodium

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuron projection

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: Ensembl

ruffle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionproline-rich region binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 14596909. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Lin7bQ9Z2523EBI-6997402,EBI-7001699

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6GMN2-1)

Also known as: IRS-58;

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: Q6GMN2-2)

Also known as: IRSp53S; BAIAP2-alpha;

The sequence of this isoform differs from the canonical sequence as follows:
     513-535: RNPFANVHLKPTVTNDRSAPLLS → SGSGTLVSTV

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 535535Brain-specific angiogenesis inhibitor 1-associated protein 2
PRO_0000064818

Regions

Domain1 – 250250IMD
Domain375 – 43864SH3
Coiled coil1 – 251251 By similarity

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

Natural variations

Alternative sequence513 – 53523RNPFA…APLLS → SGSGTLVSTV in isoform 2.
VSP_015510

Experimental info

Mutagenesis171Y → F: Loss of phosphorylation; when associated with F-115 and F-178. Ref.4
Mutagenesis1151Y → F: Loss of phosphorylation; when associated with F-17 and F-178. Ref.4
Mutagenesis1781Y → F: Loss of phosphorylation; when associated with F-17 and F-115. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (IRS-58) [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 606CED16E5DFD212

FASTA53559,183
        10         20         30         40         50         60 
MSLSRSEEMH RLTENVYKTI MEQFNPSLRN FIAMGKNYEK ALAGVTFAAK GYFDALVKMG 

        70         80         90        100        110        120 
ELASESQGSK ELGDVLFQMA EVHRQIQNQL EEMLKAFHNE 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 ADPNKIPDRA 

       250        260        270        280        290        300 
AQLMQQMANS NGSILPSALS ASKSNLVISD PIPGAKPLPV PPELAPFVGR MSAQENVPVM 

       310        320        330        340        350        360 
NGVAGADSED 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 DKDDLALPPP DYGTSSRAFP 

       490        500        510        520        530 
SQTAGTFKQR PYSVAVPAFS QGLDDYGARS VSRNPFANVH LKPTVTNDRS APLLS 

« Hide

Isoform 2 (IRSp53S) (BAIAP2-alpha) [UniParc].

Checksum: CCFF96819E52B999
Show »

FASTA52257,542

References

« Hide 'large scale' references
[1]"Insulin receptor substrate protein p53 localization in rats suggests mechanism for specific polyglutamine neurodegeneration."
Thomas E.A., Foye P.E., Alvarez C.E., Usui H., Sutcliffe J.G.
Neurosci. Lett. 309:145-148(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
Strain: Sprague-Dawley.
[2]"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] (ISOFORM 1).
Tissue: Lung.
[3]Lubec G., Chen W.-Q.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 12-18 AND 41-50, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus.
[4]"Distinctive tissue distribution and phosphorylation of IRSp53 isoforms."
Okamura-Oho Y., Miyashita T., Yamada M.
Biochem. Biophys. Res. Commun. 289:957-960(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, MUTAGENESIS OF TYR-17; TYR-115 AND TYR-178, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[5]"Tiam1-IRSp53 complex formation directs specificity of rac-mediated actin cytoskeleton regulation."
Connolly B.A., Rice J., Feig L.A., Buchsbaum R.J.
Mol. Cell. Biol. 25:4602-4614(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TIAM1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY037934 mRNA. Translation: AAK72488.1.
BC074009 mRNA. Translation: AAH74009.1.
RefSeqNP_476544.1. NM_057196.1. [Q6GMN2-2]
XP_006247931.1. XM_006247869.1. [Q6GMN2-1]
UniGeneRn.95155.

3D structure databases

ProteinModelPortalQ6GMN2.
SMRQ6GMN2. Positions 1-248, 379-441.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid250757. 6 interactions.
IntActQ6GMN2. 8 interactions.
MINTMINT-93063.
STRING10116.ENSRNOP00000005687.

PTM databases

PhosphoSiteQ6GMN2.

Proteomic databases

PaxDbQ6GMN2.
PRIDEQ6GMN2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID117542.
KEGGrno:117542.

Organism-specific databases

CTD10458.
RGD619814. Baiap2.

Phylogenomic databases

eggNOGNOG71665.
HOGENOMHOG000038005.
HOVERGENHBG054462.
KOK05627.
PhylomeDBQ6GMN2.

Gene expression databases

GenevestigatorQ6GMN2.

Family and domain databases

InterProIPR027681. BAIAP2.
IPR013606. IRSp53/MIM_homology_IMD.
IPR001452. SH3_domain.
[Graphical view]
PANTHERPTHR14206. PTHR14206. 1 hit.
PfamPF08397. IMD. 1 hit.
PF14604. SH3_9. 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

NextBio620361.

Entry information

Entry nameBAIP2_RAT
AccessionPrimary (citable) accession number: Q6GMN2
Secondary accession number(s): Q923H3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: July 19, 2004
Last modified: June 11, 2014
This is version 90 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