Brain-specific angiogenesis inhibitor 1-associated protein 2

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Q60437 (BAIP2_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 72. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)

Taxonomic identifier

10029 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Cricetulus

Protein attributes

Sequence length	521 AA.
Sequence status	Complete.
Protein existence	Evidence 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 projection › filopodium By similarity. Cell projection › ruffle By similarity. Cytoplasm › cytoskeleton 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.

Ontologies

Keywords
Cellular component	Cell projection Cytoplasm Cytoskeleton Membrane
Domain	Coiled coil SH3 domain
PTM	Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	actin crosslink formation Inferred from sequence or structural similarity. Source: UniProtKB actin filament bundle assembly Inferred from sequence or structural similarity. Source: UniProtKB 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 response to bacterium Inferred from sequence or structural similarity. Source: UniProtKB signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from sequence or structural similarity. Source: UniProtKB filopodium Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: UniProtKB-SubCell ruffle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	proline-rich region binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 521

521

Brain-specific angiogenesis inhibitor 1-associated protein 2

PRO_0000064815

Regions

Domain

1 – 250

250

IMD

Domain

375 – 438

SH3

Coiled coil

132 – 153

Potential

Amino acid modifications

Modified residue

324

Phosphoserine By similarity

Modified residue

326

Phosphoserine By similarity

Modified residue

341

Phosphothreonine By similarity

Modified residue

347

Phosphoserine By similarity

Modified residue

367

Phosphoserine By similarity

Modified residue

453

Phosphoserine By similarity

Modified residue

454

Phosphoserine By similarity

Modified residue

455

Phosphoserine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q60437 [UniParc].

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

521

57,639

        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

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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
ProteinModelPortal	Q60437.
SMR	Q60437. Positions 1-248, 379-441.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-5314315.
Proteomic databases
PRIDE	Q60437.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG054462.
Family and domain databases
InterPro	IPR013606. IRSp53/MIM_homology_IMD. IPR011511. SH3_2. IPR001452. SH3_domain. [Graphical view]
Pfam	PF08397. IMD. 1 hit. PF07653. SH3_2. 1 hit. [Graphical view]
SMART	SM00326. SH3. 1 hit. [Graphical view]
SUPFAM	SSF50044. SH3. 1 hit.
PROSITE	PS51338. IMD. 1 hit. PS50002. SH3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BAIP2_CRIGR

Accession

Primary (citable) accession number: Q60437

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents