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Q8BKX1 (BAIP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 53 kDa substrate
Gene names
Name:Baiap2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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. Ref.9

Subunit structure

Homodimer. Interacts with CDC42 and RAC1 that have been activated by GTP binding. Binds DIAPH1. Interacts with ATN1, BAI1, SHANK1, SHANK2, SHANK3, TIAM1, WASF1 and WASF2. Interacts with ENAH after recruitment of CDC42 By similarity. Interacts with EPS8. Ref.5 Ref.9

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

Detected in liver, brain, olfactory bulb, brain cortex, caudate putamen, hypothalamus and cerebellum. Ref.6

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 By similarity.

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
Reference proteome
Gene Ontology (GO)
   Biological_processRho protein signal transduction

Traceable author statement Ref.5. Source: MGI

actin crosslink formation

Inferred from mutant phenotype Ref.9. Source: UniProtKB

actin filament bundle assembly

Inferred from mutant phenotype Ref.9. Source: UniProtKB

dendrite development

Inferred from mutant phenotype PubMed 19208628. Source: MGI

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 mutant phenotype Ref.9. Source: UniProtKB

regulation of synaptic plasticity

Inferred from mutant phenotype PubMed 19208628. Source: MGI

response to bacterium

Inferred from sequence or structural similarity. Source: UniProtKB

   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 direct assay PubMed 21795692. Source: BHF-UCL

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 Ref.9. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8BKX1-1)

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: Q8BKX1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     513-535: RNPFANVHLKPTVTNDRSAPLLS → SGSGTLVSTV
Isoform 3 (identifier: Q8BKX1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     514-535: Missing.
Isoform 4 (identifier: Q8BKX1-4)

Also known as: Short form;

The sequence of this isoform differs from the canonical sequence as follows:
     290-329: Missing.
     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_0000064817

Regions

Domain1 – 250250IMD
Domain375 – 43864SH3
Coiled coil88 – 15366 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

Natural variations

Alternative sequence290 – 32940Missing in isoform 4.
VSP_015507
Alternative sequence513 – 53523RNPFA…APLLS → SGSGTLVSTV in isoform 2 and isoform 4.
VSP_015508
Alternative sequence514 – 53522Missing in isoform 3.
VSP_015509

Experimental info

Sequence conflict87 – 882QN → HI in BAC33764. Ref.3
Sequence conflict3261S → F in BAC33764. Ref.3
Sequence conflict3301S → F in BAC33764. Ref.3

Sequences

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

Last modified August 30, 2005. Version 2.
Checksum: 45B4C660FBB07F72

FASTA53559,237
        10         20         30         40         50         60 
MSLSRSEEMH RLTENVYKTI MEQFNPSLRN FIAMGKNYEK ALAGVTFAAK GYFDALVKMG 

        70         80         90        100        110        120 
ELASESQGSK ELGDVLFQMA EVHRQIQNQL EETLKSFHNE 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 
VQLMQQMANS NGSILPSALS 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 DKDDLALPPP DYGTSSRAFP 

       490        500        510        520        530 
TQTAGTFKQR PYSVAVPAFS QGLDDYGARS VSRNPFANVH LKPTVTNDRS APLLS 

« Hide

Isoform 2 [UniParc].

Checksum: 8E65752157FD3F99
Show »

FASTA52257,596
Isoform 3 [UniParc].

Checksum: 5EDD57E315AF4005
Show »

FASTA51356,863
Isoform 4 (Short form) [UniParc].

Checksum: F3FA1DFDC1E0D579
Show »

FASTA48253,274

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] (ISOFORMS 2 AND 4).
Strain: C57BL/6J.
Tissue: Brain.
[2]"Genomic structure and alternative splicing of the insulin receptor tyrosine kinase substrate of 53-kDa protein."
Miyahara A., Okumura-Oho Y., Miyashita T., Hoshika A., Yamada M.
J. Hum. Genet. 48:410-414(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 2 AND 4).
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Embryo.
[4]"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 3).
Strain: FVB/N.
Tissue: Mammary gland.
[5]"Rho small G-protein-dependent binding of mDia to an Src homology 3 domain-containing IRSp53/BAIAP2."
Fujiwara T., Mammoto A., Kim Y., Takai Y.
Biochem. Biophys. Res. Commun. 271:626-629(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DIAPH1.
[6]"Novel isoform of insulin receptor substrate p53/p58 is generated by alternative splicing in the CRIB/SH3-binding region."
Alvarez C.E., Sutcliffe J.G., Thomas E.A.
J. Biol. Chem. 277:24728-24734(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[7]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[9]"Regulation of cell shape by Cdc42 is mediated by the synergic actin-bundling activity of the Eps8-IRSp53 complex."
Disanza A., Mantoani S., Hertzog M., Gerboth S., Frittoli E., Steffen A., Berhoerster K., Kreienkamp H.J., Milanesi F., Di Fiore P.P., Ciliberto A., Stradal T.E., Scita G.
Nat. Cell Biol. 8:1337-1347(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EPS8.
[10]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF390178 mRNA. Translation: AAK68153.1.
AF390179 mRNA. Translation: AAK81838.1.
AB105196 Genomic DNA. Translation: BAC65241.1.
AB105196 Genomic DNA. Translation: BAC65242.1.
AK049469 mRNA. Translation: BAC33764.1.
BC006620 mRNA. Translation: AAH06620.1.
BC016411 mRNA. Translation: AAH16411.1.
CCDSCCDS25722.1. [Q8BKX1-1]
CCDS25723.1. [Q8BKX1-4]
CCDS25724.1. [Q8BKX1-2]
RefSeqNP_001032843.1. NM_001037754.3. [Q8BKX1-4]
NP_001032844.2. NM_001037755.3. [Q8BKX1-1]
NP_570932.2. NM_130862.4. [Q8BKX1-2]
UniGeneMm.197534.

3D structure databases

ProteinModelPortalQ8BKX1.
SMRQ8BKX1. Positions 2-229, 264-292, 375-437.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid223833. 1 interaction.
DIPDIP-32392N.
IntActQ8BKX1. 5 interactions.
MINTMINT-4122910.

PTM databases

PhosphoSiteQ8BKX1.

Proteomic databases

MaxQBQ8BKX1.
PaxDbQ8BKX1.
PRIDEQ8BKX1.

Protocols and materials databases

DNASU108100.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026436; ENSMUSP00000026436; ENSMUSG00000025372. [Q8BKX1-1]
ENSMUST00000075180; ENSMUSP00000074674; ENSMUSG00000025372. [Q8BKX1-2]
ENSMUST00000103021; ENSMUSP00000099310; ENSMUSG00000025372. [Q8BKX1-4]
ENSMUST00000106231; ENSMUSP00000101838; ENSMUSG00000025372. [Q8BKX1-3]
GeneID108100.
KEGGmmu:108100.
UCSCuc007mri.1. mouse. [Q8BKX1-1]

Organism-specific databases

CTD10458.
MGIMGI:2137336. Baiap2.

Phylogenomic databases

eggNOGNOG71665.
GeneTreeENSGT00390000005995.
HOGENOMHOG000038005.
HOVERGENHBG054462.
InParanoidQ8BKX1.
KOK05627.
OMAFLAQQMS.
OrthoDBEOG7N0C3W.
PhylomeDBQ8BKX1.
TreeFamTF325648.

Gene expression databases

ArrayExpressQ8BKX1.
BgeeQ8BKX1.
GenevestigatorQ8BKX1.

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

ChiTaRSBAIAP2. mouse.
NextBio360066.
PROQ8BKX1.
SOURCESearch...

Entry information

Entry nameBAIP2_MOUSE
AccessionPrimary (citable) accession number: Q8BKX1
Secondary accession number(s): Q91V97, Q923V9, Q923W0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: August 30, 2005
Last modified: July 9, 2014
This is version 106 of the entry and version 2 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot