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Q6GMN2

- BAIP2_RAT

UniProt

Q6GMN2 - BAIP2_RAT

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Protein

Brain-specific angiogenesis inhibitor 1-associated protein 2

Gene

Baiap2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 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. dendrite development Source: Ensembl
  4. filopodium assembly Source: InterPro
  5. regulation of actin cytoskeleton organization Source: UniProtKB
  6. regulation of cell shape Source: UniProtKB
  7. regulation of synaptic plasticity Source: Ensembl
  8. response to bacterium Source: UniProtKB
  9. signal transduction Source: InterPro
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_196755. Regulation of actin dynamics for phagocytic cup formation.

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 substrate protein p53
Gene namesi
Name:Baiap2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi619814. Baiap2.

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. actin cytoskeleton Source: Ensembl
  2. cytosol Source: UniProtKB
  3. extracellular vesicular exosome Source: Ensembl
  4. membrane Source: UniProtKB-KW
  5. neuron projection Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi17 – 171Y → F: Loss of phosphorylation; when associated with F-115 and F-178. 1 Publication
Mutagenesisi115 – 1151Y → F: Loss of phosphorylation; when associated with F-17 and F-178. 1 Publication
Mutagenesisi178 – 1781Y → F: Loss of phosphorylation; when associated with F-17 and F-115. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 535535Brain-specific angiogenesis inhibitor 1-associated protein 2PRO_0000064818Add
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

PaxDbiQ6GMN2.
PRIDEiQ6GMN2.

PTM databases

PhosphoSiteiQ6GMN2.

Expressioni

Tissue specificityi

Ubiquitous.2 Publications

Gene expression databases

ExpressionAtlasiQ6GMN2. baseline and differential.
GenevestigatoriQ6GMN2.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Lin7bQ9Z2523EBI-6997402,EBI-7001699

Protein-protein interaction databases

BioGridi250757. 6 interactions.
IntActiQ6GMN2. 8 interactions.
MINTiMINT-93063.
STRINGi10116.ENSRNOP00000005687.

Structurei

3D structure databases

ProteinModelPortaliQ6GMN2.
SMRiQ6GMN2. 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 coili1 – 251251By similarityAdd
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

eggNOGiNOG71665.
HOGENOMiHOG000038005.
HOVERGENiHBG054462.
InParanoidiQ6GMN2.
KOiK05627.
PhylomeDBiQ6GMN2.

Family and domain databases

InterProiIPR027681. BAIAP2.
IPR013606. IRSp53/MIM_homology_IMD.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR14206. PTHR14206. 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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q6GMN2-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSLSRSEEMH RLTENVYKTI MEQFNPSLRN FIAMGKNYEK ALAGVTFAAK
60 70 80 90 100
GYFDALVKMG ELASESQGSK ELGDVLFQMA EVHRQIQNQL EEMLKAFHNE
110 120 130 140 150
LLTQLEQKVE LDSRYLSAAL KKYQTEQRSK GDALDKCQAE LKKLRKKSQG
160 170 180 190 200
SKNPQKYSDK ELQYIDAISN KQGELENYVS DGYKTALTEE RRRFCFLVEK
210 220 230 240 250
QCAVAKNSAA YHSKGKELLA QKLPLWQQAC ADPNKIPDRA AQLMQQMANS
260 270 280 290 300
NGSILPSALS ASKSNLVISD PIPGAKPLPV PPELAPFVGR MSAQENVPVM
310 320 330 340 350
NGVAGADSED 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 DKDDLALPPP DYGTSSRAFP SQTAGTFKQR PYSVAVPAFS
510 520 530
QGLDDYGARS VSRNPFANVH LKPTVTNDRS APLLS
Length:535
Mass (Da):59,183
Last modified:July 19, 2004 - v1
Checksum:i606CED16E5DFD212
GO
Isoform 2 (identifier: Q6GMN2-2) [UniParc]FASTAAdd to Basket

Also known as: IRSp53S, BAIAP2-alpha

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

Show »
Length:522
Mass (Da):57,542
Checksum:iCCFF96819E52B999
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei513 – 53523RNPFA…APLLS → SGSGTLVSTV in isoform 2. 1 PublicationVSP_015510Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY037934 mRNA. Translation: AAK72488.1.
BC074009 mRNA. Translation: AAH74009.1.
RefSeqiNP_476544.1. NM_057196.1. [Q6GMN2-2]
XP_006247931.1. XM_006247869.2. [Q6GMN2-1]
UniGeneiRn.95155.

Genome annotation databases

GeneIDi117542.
KEGGirno:117542.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY037934 mRNA. Translation: AAK72488.1 .
BC074009 mRNA. Translation: AAH74009.1 .
RefSeqi NP_476544.1. NM_057196.1. [Q6GMN2-2 ]
XP_006247931.1. XM_006247869.2. [Q6GMN2-1 ]
UniGenei Rn.95155.

3D structure databases

ProteinModelPortali Q6GMN2.
SMRi Q6GMN2. Positions 1-248, 379-441.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 250757. 6 interactions.
IntActi Q6GMN2. 8 interactions.
MINTi MINT-93063.
STRINGi 10116.ENSRNOP00000005687.

PTM databases

PhosphoSitei Q6GMN2.

Proteomic databases

PaxDbi Q6GMN2.
PRIDEi Q6GMN2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 117542.
KEGGi rno:117542.

Organism-specific databases

CTDi 10458.
RGDi 619814. Baiap2.

Phylogenomic databases

eggNOGi NOG71665.
HOGENOMi HOG000038005.
HOVERGENi HBG054462.
InParanoidi Q6GMN2.
KOi K05627.
PhylomeDBi Q6GMN2.

Enzyme and pathway databases

Reactomei REACT_196755. Regulation of actin dynamics for phagocytic cup formation.

Miscellaneous databases

NextBioi 620361.

Gene expression databases

ExpressionAtlasi Q6GMN2. baseline and differential.
Genevestigatori Q6GMN2.

Family and domain databases

InterProi IPR027681. BAIAP2.
IPR013606. IRSp53/MIM_homology_IMD.
IPR001452. SH3_domain.
[Graphical view ]
PANTHERi PTHR14206. PTHR14206. 1 hit.
Pfami PF08397. IMD. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view ]
SMARTi SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
PROSITEi PS51338. IMD. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiBAIP2_RAT
AccessioniPrimary (citable) accession number: Q6GMN2
Secondary accession number(s): Q923H3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: July 19, 2004
Last modified: October 29, 2014
This is version 93 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3