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Protein

Brain-specific angiogenesis inhibitor 1-associated protein 2

Gene

BAIAP2

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  1. proline-rich region binding Source: UniProtKB

GO - Biological processi

  1. actin crosslink formation Source: UniProtKB
  2. actin filament bundle assembly Source: UniProtKB
  3. plasma membrane organization Source: InterPro
  4. regulation of actin cytoskeleton organization Source: UniProtKB
  5. regulation of cell shape Source: UniProtKB
  6. response to bacterium Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
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 namesi
Name:BAIAP2
OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifieri10029 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Subcellular locationi

Cytoplasm By similarity. Membrane By similarity; 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).By similarity

GO - Cellular componenti

  1. cytoskeleton Source: UniProtKB-SubCell
  2. cytosol Source: UniProtKB
  3. filopodium Source: UniProtKB-SubCell
  4. membrane Source: UniProtKB-SubCell
  5. ruffle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 521521Brain-specific angiogenesis inhibitor 1-associated protein 2PRO_0000064815Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei324 – 3241PhosphoserineBy similarity
Modified residuei326 – 3261PhosphoserineBy similarity
Modified residuei341 – 3411PhosphothreonineBy similarity
Modified residuei347 – 3471PhosphoserineBy similarity
Modified residuei367 – 3671PhosphoserineBy similarity
Modified residuei455 – 4551PhosphoserineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ60437.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
NCKIPSDQ9NZQ33EBI-7010040,EBI-745080From a different organism.

Protein-protein interaction databases

IntActiQ60437. 1 interaction.
MINTiMINT-5314315.

Structurei

3D structure databases

ProteinModelPortaliQ60437.
SMRiQ60437. Positions 1-248, 379-441.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 250250IMDPROSITE-ProRule annotationAdd
BLAST
Domaini375 – 43864SH3PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili132 – 15322Sequence AnalysisAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 IMD (IRSp53/MIM homology) domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

HOVERGENiHBG054462.

Family and domain databases

InterProiIPR013606. I-BAR_dom.
IPR030128. IRSp53.
IPR027681. IRSp53/IRTKS/Pinkbar.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR14206. PTHR14206. 1 hit.
PTHR14206:SF3. PTHR14206:SF3. 1 hit.
PfamiPF08397. IMD. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51338. IMD. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q60437-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLSRSEEMH RLTENVYKTI MEQFNPSLRN FIAMGKNYEK ALAGVTFAAK
60 70 80 90 100
GYFDALVKMG ELASESQGSK ELGDVLFQMA EVHRQIQNQL EEMLKSFHNE
110 120 130 140 150
LLTQLEQKVE LDSRYLSAAL KKYQAEQRSK GDALDKCQAE LKKLRKKSQG
160 170 180 190 200
SKNPQKYSDK ELQYIDAISN KQGELENYVS DGYKTALTEE RRRFCFLVEK
210 220 230 240 250
QCAVAKNSAA YHSKGKELLA QKLPVWQQAC ADPNKIPDRA VQLMQQIASS
260 270 280 290 300
NGSILPSTLS ASKSNLVISD PIPGAKPLPV PPELAPFVGR MSAQENVPVM
310 320 330 340 350
NGVAGPDSED YNPWADRKAA QPKSLSPPQS QSKLSDSYSN TLPVRKSVTP
360 370 380 390 400
KNSYATTENK TLPRSSSMAA GLERNGRMRV KAIFSHAAGD NSTLLSFKEG
410 420 430 440 450
DLITLLVPEA RDGWHYGESE KTKMRGWFPF SYTRVLDSDG SDRLHMSLQQ
460 470 480 490 500
GKSSSTGNLL DKDDLAVPPP DYGTSSRAFP TQTAGTFKQR PYSVAVPAFS
510 520
QGLDDYGARS VSSADVEVAR F
Length:521
Mass (Da):57,639
Last modified:November 1, 1996 - v1
Checksum:i58485BD6CAC15DC1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41899 mRNA. Translation: AAC52436.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41899 mRNA. Translation: AAC52436.1.

3D structure databases

ProteinModelPortaliQ60437.
SMRiQ60437. Positions 1-248, 379-441.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ60437. 1 interaction.
MINTiMINT-5314315.

Proteomic databases

PRIDEiQ60437.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG054462.

Family and domain databases

InterProiIPR013606. I-BAR_dom.
IPR030128. IRSp53.
IPR027681. IRSp53/IRTKS/Pinkbar.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR14206. PTHR14206. 1 hit.
PTHR14206:SF3. PTHR14206:SF3. 1 hit.
PfamiPF08397. IMD. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51338. IMD. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiBAIP2_CRIGR
AccessioniPrimary (citable) accession number: Q60437
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: November 1, 1996
Last modified: March 4, 2015
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.