Q8BKX1 (BAIP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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

Gene names

Name:

Baiap2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	535 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. Ref.7
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.7
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.
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 component	Cell projection Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing
Domain	Coiled coil SH3 domain
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Rho protein signal transduction Traceable author statement Ref.5. Source: MGI actin crosslink formation Inferred from mutant phenotype Ref.7. Source: UniProtKB actin filament bundle assembly Inferred from mutant phenotype Ref.7. 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.7. 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_component	actin cytoskeleton Inferred from electronic annotation. Source: Compara cell junction Inferred from electronic annotation. Source: Compara 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: Compara plasma membrane Inferred from electronic annotation. Source: Compara 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Diaph1	O08808	3	EBI-771498,EBI-1026445
Dlg4	Q62108	3	EBI-771498,EBI-300895

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 535	535	Brain-specific angiogenesis inhibitor 1-associated protein 2		PRO_0000064817
Regions
	Domain	1 – 250	250	IMD
	Domain	375 – 438	64	SH3
	Coiled coil	88 – 153	66	Potential
Amino acid modifications
	Modified residue	324	1	Phosphoserine By similarity
	Modified residue	326	1	Phosphoserine Ref.8
	Modified residue	341	1	Phosphothreonine By similarity
	Modified residue	347	1	Phosphoserine By similarity
	Modified residue	367	1	Phosphoserine By similarity
	Modified residue	453	1	Phosphoserine Ref.9
	Modified residue	454	1	Phosphoserine Ref.9
	Modified residue	455	1	Phosphoserine Ref.9
Natural variations
	Alternative sequence	290 – 329	40	Missing in isoform 4.		VSP_015507
	Alternative sequence	513 – 535	23	RNPFA…APLLS → SGSGTLVSTV in isoform 2 and isoform 4.		VSP_015508
	Alternative sequence	514 – 535	22	Missing in isoform 3.		VSP_015509
Experimental info
	Sequence conflict	87 – 88	2	QN → HI in BAC33764. Ref.3
	Sequence conflict	326	1	S → F in BAC33764. Ref.3
	Sequence conflict	330	1	S → F in BAC33764. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 30, 2005. Version 2. Checksum: 45B4C660FBB07F72	FASTA	535	59,237
	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
	Isoform 2 [UniParc]. Checksum: 8E65752157FD3F99	FASTA	522	57,596
	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 TQTAGTFKQR PYSVAVPAFS QGLDDYGARS VSSGSGTLVS TV
	Isoform 3 [UniParc]. Checksum: 5EDD57E315AF4005	FASTA	513	56,863
	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 TQTAGTFKQR PYSVAVPAFS QGLDDYGARS VSR
	Isoform 4 (Short form) [UniParc]. Checksum: F3FA1DFDC1E0D579	FASTA	482	53,274
	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 PPELAPFVGS QSKLSDSYSN 310 320 330 340 350 360 TLPVRKSVTP KNSYATTENK TLPRSSSMAA GLERNGRMRV KAIFSHAAGD NSTLLSFKEG 370 380 390 400 410 420 DLITLLVPEA RDGWHYGESE KTKMRGWFPF SYTRVLDSDG SDRLHMSLQQ GKSSSTGNLL 430 440 450 460 470 480 DKDDLALPPP DYGTSSRAFP TQTAGTFKQR PYSVAVPAFS QGLDDYGARS VSSGSGTLVS TV

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.
[8]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, MASS SPECTROMETRY. Tissue: Brain cortex.
[9]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453; SER-454 AND SER-455, MASS SPECTROMETRY. 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.
IPI	IPI00124778. IPI00222731. IPI00459465. IPI00649474.
RefSeq	NP_001032843.1. NM_001037754.3. NP_001032844.2. NM_001037755.3. NP_570932.2. NM_130862.4.
UniGene	Mm.197534.
3D structure databases
ProteinModelPortal	Q8BKX1.
SMR	Q8BKX1. Positions 2-229, 375-437.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-32392N.
IntAct	Q8BKX1. 3 interactions.
PTM databases
PhosphoSite	Q8BKX1.
Proteomic databases
PaxDb	Q8BKX1.
PRIDE	Q8BKX1.
Protocols and materials databases
DNASU	108100.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000026436; ENSMUSP00000026436; ENSMUSG00000025372. ENSMUST00000075180; ENSMUSP00000074674; ENSMUSG00000025372. ENSMUST00000103021; ENSMUSP00000099310; ENSMUSG00000025372. ENSMUST00000106231; ENSMUSP00000101838; ENSMUSG00000025372.
GeneID	108100.
KEGG	mmu:108100.
Organism-specific databases
CTD	10458.
MGI	MGI:2137336. Baiap2.
Phylogenomic databases
eggNOG	NOG71665.
GeneTree	ENSGT00390000005995.
HOGENOM	HOG000038005.
HOVERGEN	HBG054462.
InParanoid	Q8BKX1.
KO	K05627.
OMA	FLAQQMS.
OrthoDB	EOG45QHCZ.
Gene expression databases
ArrayExpress	Q8BKX1.
Bgee	Q8BKX1.
Genevestigator	Q8BKX1.
GermOnline	ENSMUSG00000025372. Mus musculus.
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...
Other
ChiTaRS	BAIAP2. mouse.
NextBio	360066.
SOURCE	Search...

Entry information

Entry name

BAIP2_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program