Q6GMN2 (BAIP2_RAT) 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 substrate protein p53

Gene names

Name:

Baiap2

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [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 › Rattus

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 By similarity.
Subunit structure	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. Ref.5
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	Ubiquitous. Ref.1 Ref.4
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.4
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 Direct protein sequencing Reference proteome
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 dendrite development Inferred from electronic annotation. Source: Compara 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 regulation of synaptic plasticity Inferred from electronic annotation. Source: Compara response to bacterium Inferred from sequence or structural similarity. Source: UniProtKB signal transduction Inferred from electronic annotation. Source: InterPro
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 electronic annotation. Source: Compara 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...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q6GMN2-1)

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.

Isoform 2 (identifier: Q6GMN2-2)

Also known as: IRSp53S; BAIAP2-alpha;

The sequence of this isoform differs from the canonical sequence as follows:
     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_0000064818
Regions
	Domain	1 – 250	250	IMD
	Domain	375 – 438	64	SH3
	Coiled coil	1 – 251	251	By similarity
Amino acid modifications
	Modified residue	324	1	Phosphoserine By similarity
	Modified residue	326	1	Phosphoserine By similarity
	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 By similarity
	Modified residue	454	1	Phosphoserine By similarity
	Modified residue	455	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	513 – 535	23	RNPFA…APLLS → SGSGTLVSTV in isoform 2.		VSP_015510
Experimental info
	Mutagenesis	17	1	Y → F: Loss of phosphorylation; when associated with F-115 and F-178. Ref.4
	Mutagenesis	115	1	Y → F: Loss of phosphorylation; when associated with F-17 and F-178. Ref.4
	Mutagenesis	178	1	Y → F: Loss of phosphorylation; when associated with F-17 and F-115. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (IRS-58) [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 606CED16E5DFD212	FASTA	535	59,183
	10 20 30 40 50 60 MSLSRSEEMH RLTENVYKTI MEQFNPSLRN FIAMGKNYEK ALAGVTFAAK GYFDALVKMG 70 80 90 100 110 120 ELASESQGSK ELGDVLFQMA EVHRQIQNQL EEMLKAFHNE 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 AQLMQQMANS NGSILPSALS ASKSNLVISD PIPGAKPLPV PPELAPFVGR MSAQENVPVM 310 320 330 340 350 360 NGVAGADSED 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 SQTAGTFKQR PYSVAVPAFS QGLDDYGARS VSRNPFANVH LKPTVTNDRS APLLS
	Isoform 2 (IRSp53S) (BAIAP2-alpha) [UniParc]. Checksum: CCFF96819E52B999	FASTA	522	57,542
	10 20 30 40 50 60 MSLSRSEEMH RLTENVYKTI MEQFNPSLRN FIAMGKNYEK ALAGVTFAAK GYFDALVKMG 70 80 90 100 110 120 ELASESQGSK ELGDVLFQMA EVHRQIQNQL EEMLKAFHNE 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 AQLMQQMANS NGSILPSALS ASKSNLVISD PIPGAKPLPV PPELAPFVGR MSAQENVPVM 310 320 330 340 350 360 NGVAGADSED 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 SQTAGTFKQR 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] (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, 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY037934 mRNA. Translation: AAK72488.1. BC074009 mRNA. Translation: AAH74009.1.
IPI	IPI00203614. IPI00650118.
RefSeq	NP_476544.1. NM_057196.1.
UniGene	Rn.95155.
3D structure databases
ProteinModelPortal	Q6GMN2.
SMR	Q6GMN2. Positions 1-248, 379-441.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-93063.
STRING	10116.ENSRNOP00000005687.
PTM databases
PhosphoSite	Q6GMN2.
Proteomic databases
PaxDb	Q6GMN2.
PRIDE	Q6GMN2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	117542.
KEGG	rno:117542.
Organism-specific databases
CTD	10458.
RGD	619814. Baiap2.
Phylogenomic databases
eggNOG	NOG71665.
HOGENOM	HOG000038005.
HOVERGEN	HBG054462.
KO	K05627.
OrthoDB	EOG45QHCZ.
Gene expression databases
ArrayExpress	Q6GMN2.
Genevestigator	Q6GMN2.
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
NextBio	620361.

Entry information

Entry name

BAIP2_RAT

Accession

Primary (citable) accession number: Q6GMN2
Secondary accession number(s): Q923H3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	July 19, 2004
Last modified:	May 1, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program