Reviewed, UniProtKB/Swiss-Prot Q9UQB8 (BAIP2_HUMAN)

Names and origin

Protein names

Recommended name:
    Brain-specific angiogenesis inhibitor 1-associated protein 2
      Short name=BAI1-associated protein 2
      Short name=BAI-associated protein 2
      Short name=Protein BAP2
Alternative name(s):
    Insulin receptor substrate protein of 53 kDa
      Short name=Insulin receptor substrate p53
      Short name=IRSp53
    Insulin receptor substrate p53/p58
      Short name=IRSp53/58
      Short name=IRS-58
    Fas ligand-associated factor 3
      Short name=FLAF3

Gene names

Name:

BAIAP2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	552 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. Ref.7 Ref.8 Ref.12
Subunit structure	Homodimer. Interacts with CDC42 and RAC1 that have been activated by GTP binding. Interacts with ATN1, BAI1, EPS8, SHANK1, SHANK2, SHANK3, WASF1 and WASF2. Interacts with ENAH after recruitment of CDC42. Interacts with TIAM1 and DIAPH1 By similarity. Ref.7 Ref.8 Ref.1 Ref.2 Ref.9 Ref.10 Ref.11
Subcellular location	Cytoplasm. Membrane; Peripheral membrane protein. Cell projection › filopodium. Cell projection › ruffle. Note: Detected throughout the cytoplasm in the absence of specific binding partners. Detected in filopodia and close to membrane ruffles. Ref.1 Ref.2 Ref.10 Ref.11
Tissue specificity	Isoform 1 and isoform 4 are expressed almost exclusively in brain. Isoform 4 is barely detectable in placenta, prostate and testis. A short isoform is ubiquitous, with the highest expression in liver, prostate, testis and placenta. Ref.1 Ref.2 Ref.9
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. Ref.12 The SH3 domain interacts with ATN1, BAI1, WASF1, WASF2, SHANK1, DIAPH1 and ENAH. Ref.12
Post-translational modification	Phosphorylated on tyrosine residues by INSR in response to insulin treatment. Ref.2 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17
Sequence similarities	Contains 1 IMD (IRSp53/MIM homology) domain. Contains 1 SH3 domain.
Caution	It is uncertain whether Met-1 or Met-59 is the initiator.

Ontologies

Keywords
Cellular component	Cell projection Cytoplasm Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil SH3 domain
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	axonogenesis Ref.1 Traceable author statement. Source: ProtInc filopodium assembly Inferred from electronic annotation. Source: InterPro insulin receptor signaling pathway Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Ref.1 Traceable author statement. Source: ProtInc extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell filopodium Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Ref.1 Traceable author statement. Source: ProtInc ruffle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	SH3 domain binding Inferred from electronic annotation. Source: InterPro cytoskeletal adaptor activity Ref.1 Traceable author statement. Source: ProtInc protein C-terminus binding Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ABI1	Q8IZP0	1	EBI-525456,EBI-375446
EPS8	Q12929	1	EBI-525456,EBI-375576
Eps8	Q08509	6	EBI-525456,EBI-375596	From a different organism.
PBX2	P40425	1	EBI-525456,EBI-348489
YWHAG	P61981	1	EBI-525456,EBI-359832

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UQB8-1)

Also known as: IRSp53(L);

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: Q9UQB8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     529-552: CDLSAQGPEGREHGDGSARTLAGR → SAPLLS

Isoform 3 (identifier: Q9UQB8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     513-552: Missing.

Isoform 4 (identifier: Q9UQB8-4)

Also known as: BAIAP2-alpha;

The sequence of this isoform differs from the canonical sequence as follows:
     512-552: RNPFAHVQLKPTVTNDRCDLSAQGPEGREHGDGSARTLAGR → SGSGTLVSTV

Isoform 5 (identifier: Q9UQB8-5)

Also known as: BAIAP2-beta;

The sequence of this isoform differs from the canonical sequence as follows:
     512-552: RNPFAHVQLKPTVTNDRCDLSAQGPEGREHGDGSARTLAGR → SADVEVARF

Isoform 6 (identifier: Q9UQB8-6)

The sequence of this isoform differs from the canonical sequence as follows:
     356-356: T → TA
     512-552: RNPFAHVQLKPTVTNDRCDLSAQGPEGREHGDGSARTLAGR → SGSGTLVSTV

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 552

552

Brain-specific angiogenesis inhibitor 1-associated protein 2

PRO_0000064816

Regions

Domain

1 – 250

250

IMD

Domain

374 – 437

64

SH3

Coiled coil

132 – 153

22

Potential

Amino acid modifications

Modified residue

157

1

Phosphotyrosine By similarity

Modified residue

296

1

Phosphothreonine Ref.2 Ref.15

Modified residue

310

1

Phosphotyrosine Ref.2 Ref.15

Modified residue

323

1

Phosphoserine Ref.2 Ref.15

Modified residue

325

1

Phosphoserine Ref.2 Ref.14 Ref.15 Ref.16

Modified residue

337

1

Phosphotyrosine Ref.2 Ref.13 Ref.17

Modified residue

346

1

Phosphoserine Ref.2 Ref.15

Modified residue

348

1

Phosphothreonine Ref.2 Ref.15

Modified residue

366

1

Phosphoserine Ref.2 Ref.15

Modified residue

452

1

Phosphoserine By similarity

Modified residue

453

1

Phosphoserine By similarity

Modified residue

454

1

Phosphoserine Ref.2 Ref.16

Modified residue

491

1

Phosphotyrosine Ref.2 Ref.13

Modified residue

505

1

Phosphotyrosine Ref.2 Ref.13

Natural variations

Alternative sequence

356

1

T → TA in isoform 6.

VSP_015502

Alternative sequence

512 – 552

41

RNPFA…TLAGR → SGSGTLVSTV in isoform 4 and isoform 6.

VSP_015503

Alternative sequence

512 – 552

41

RNPFA…TLAGR → SADVEVARF in isoform 5.

VSP_015504

Alternative sequence

513 – 552

40

Missing in isoform 3.

VSP_015505

Alternative sequence

529 – 552

24

CDLSA…TLAGR → SAPLLS in isoform 2.

VSP_015506

Natural variant

519

1

Q → R: dbSNP rs4969391.

VAR_050686

Experimental info

Mutagenesis

142

1

K → E: Abolishes actin-bundling and filopodia formation; when associated with E-143; E-146 and E147. Ref.18

Mutagenesis

143

1

K → E: Abolishes actin-bundling and filopodia formation; when associated with E-142; E-146 and E147. Ref.18

Mutagenesis

146

1

K → E: Abolishes actin-bundling and filopodia formation; when associated with E-142; E-143 and E147. Ref.18

Mutagenesis

147

1

K → E: Abolishes actin-bundling and filopodia formation; when associated with E-142; E-143 and E146. Ref.18

Mutagenesis

267

1

I → N: Loss of interaction with CDC42. Loss of stimulation of neurite growth. Ref.9

Mutagenesis

427

1

F → A: Loss of interaction with ENAH and no induction of filopodia; when associated with A-428. Ref.8

Mutagenesis

428

1

P → A: Loss of interaction with ENAH and no induction of filopodia; when associated with A-427. Ref.8

Sequence conflict

84

1

R → W in BAD96390. Ref.4

Sequence conflict

415

1

Y → H in BAD96390. Ref.4

Sequence conflict

473

1

A → T in BAD96390. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

552

Helix Strand Turn

Details...

Helix

2 – 22

21

Helix

24 – 64

41

Beta strand

66 – 68

3

Helix

70 – 99

30

Helix

102 – 149

48

Turn

154 – 157

4

Helix

158 – 229

72

Helix

238 – 246

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (IRSp53(L)) [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 3B9EDC6405DCC99D	FASTA	552	60,868
	10 20 30 40 50 60 MSLSRSEEMH RLTENVYKTI MEQFNPSLRN FIAMGKNYEK ALAGVTYAAK GYFDALVKMG 70 80 90 100 110 120 ELASESQGSK ELGDVLFQMA EVHRQIQNQL EEMLKSFHNE 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 ADPSKIPERA 250 260 270 280 290 300 VQLMQQVASN GATLPSALSA SKSNLVISDP IPGAKPLPVP PELAPFVGRM SAQESTPIMN 310 320 330 340 350 360 GVTGPDGEDY SPWADRKAAQ PKSLSPPQSQ SKLSDSYSNT LPVRKSVTPK NSYATTENKT 370 380 390 400 410 420 LPRSSSMAAG LERNGRMRVK AIFSHAAGDN STLLSFKEGD LITLLVPEAR DGWHYGESEK 430 440 450 460 470 480 TKMRGWFPFS YTRVLDSDGS DRLHMSLQQG KSSSTGNLLD KDDLAIPPPD YGAASRAFPA 490 500 510 520 530 540 QTASGFKQRP YSVAVPAFSQ GLDDYGARSM SRNPFAHVQL KPTVTNDRCD LSAQGPEGRE 550 HGDGSARTLA GR
	Isoform 2. Checksum: E63C4C08C48964B7	FASTA	534	59,014
	10 20 30 40 50 60 MSLSRSEEMH RLTENVYKTI MEQFNPSLRN FIAMGKNYEK ALAGVTYAAK GYFDALVKMG 70 80 90 100 110 120 ELASESQGSK ELGDVLFQMA EVHRQIQNQL EEMLKSFHNE 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 ADPSKIPERA 250 260 270 280 290 300 VQLMQQVASN GATLPSALSA SKSNLVISDP IPGAKPLPVP PELAPFVGRM SAQESTPIMN 310 320 330 340 350 360 GVTGPDGEDY SPWADRKAAQ PKSLSPPQSQ SKLSDSYSNT LPVRKSVTPK NSYATTENKT 370 380 390 400 410 420 LPRSSSMAAG LERNGRMRVK AIFSHAAGDN STLLSFKEGD LITLLVPEAR DGWHYGESEK 430 440 450 460 470 480 TKMRGWFPFS YTRVLDSDGS DRLHMSLQQG KSSSTGNLLD KDDLAIPPPD YGAASRAFPA 490 500 510 520 530 QTASGFKQRP YSVAVPAFSQ GLDDYGARSM SRNPFAHVQL KPTVTNDRSA PLLS
	Isoform 3. Checksum: 985ACC2B8DBEE7C3	FASTA	512	56,626
	10 20 30 40 50 60 MSLSRSEEMH RLTENVYKTI MEQFNPSLRN FIAMGKNYEK ALAGVTYAAK GYFDALVKMG 70 80 90 100 110 120 ELASESQGSK ELGDVLFQMA EVHRQIQNQL EEMLKSFHNE 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 ADPSKIPERA 250 260 270 280 290 300 VQLMQQVASN GATLPSALSA SKSNLVISDP IPGAKPLPVP PELAPFVGRM SAQESTPIMN 310 320 330 340 350 360 GVTGPDGEDY SPWADRKAAQ PKSLSPPQSQ SKLSDSYSNT LPVRKSVTPK NSYATTENKT 370 380 390 400 410 420 LPRSSSMAAG LERNGRMRVK AIFSHAAGDN STLLSFKEGD LITLLVPEAR DGWHYGESEK 430 440 450 460 470 480 TKMRGWFPFS YTRVLDSDGS DRLHMSLQQG KSSSTGNLLD KDDLAIPPPD YGAASRAFPA 490 500 510 QTASGFKQRP YSVAVPAFSQ GLDDYGARSM SR
	Isoform 4 (BAIAP2-alpha). Checksum: 618A09FDBEB3A5C3	FASTA	521	57,359
	10 20 30 40 50 60 MSLSRSEEMH RLTENVYKTI MEQFNPSLRN FIAMGKNYEK ALAGVTYAAK GYFDALVKMG 70 80 90 100 110 120 ELASESQGSK ELGDVLFQMA EVHRQIQNQL EEMLKSFHNE 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 ADPSKIPERA 250 260 270 280 290 300 VQLMQQVASN GATLPSALSA SKSNLVISDP IPGAKPLPVP PELAPFVGRM SAQESTPIMN 310 320 330 340 350 360 GVTGPDGEDY SPWADRKAAQ PKSLSPPQSQ SKLSDSYSNT LPVRKSVTPK NSYATTENKT 370 380 390 400 410 420 LPRSSSMAAG LERNGRMRVK AIFSHAAGDN STLLSFKEGD LITLLVPEAR DGWHYGESEK 430 440 450 460 470 480 TKMRGWFPFS YTRVLDSDGS DRLHMSLQQG KSSSTGNLLD KDDLAIPPPD YGAASRAFPA 490 500 510 520 QTASGFKQRP YSVAVPAFSQ GLDDYGARSM SSGSGTLVST V
	Isoform 5 (BAIAP2-beta). Checksum: FC6852BB490F6C0B	FASTA	520	57,445
	10 20 30 40 50 60 MSLSRSEEMH RLTENVYKTI MEQFNPSLRN FIAMGKNYEK ALAGVTYAAK GYFDALVKMG 70 80 90 100 110 120 ELASESQGSK ELGDVLFQMA EVHRQIQNQL EEMLKSFHNE 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 ADPSKIPERA 250 260 270 280 290 300 VQLMQQVASN GATLPSALSA SKSNLVISDP IPGAKPLPVP PELAPFVGRM SAQESTPIMN 310 320 330 340 350 360 GVTGPDGEDY SPWADRKAAQ PKSLSPPQSQ SKLSDSYSNT LPVRKSVTPK NSYATTENKT 370 380 390 400 410 420 LPRSSSMAAG LERNGRMRVK AIFSHAAGDN STLLSFKEGD LITLLVPEAR DGWHYGESEK 430 440 450 460 470 480 TKMRGWFPFS YTRVLDSDGS DRLHMSLQQG KSSSTGNLLD KDDLAIPPPD YGAASRAFPA 490 500 510 520 QTASGFKQRP YSVAVPAFSQ GLDDYGARSM SSADVEVARF
	Isoform 6. Checksum: 58146A293AF313BC	FASTA	522	57,430
	10 20 30 40 50 60 MSLSRSEEMH RLTENVYKTI MEQFNPSLRN FIAMGKNYEK ALAGVTYAAK GYFDALVKMG 70 80 90 100 110 120 ELASESQGSK ELGDVLFQMA EVHRQIQNQL EEMLKSFHNE 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 ADPSKIPERA 250 260 270 280 290 300 VQLMQQVASN GATLPSALSA SKSNLVISDP IPGAKPLPVP PELAPFVGRM SAQESTPIMN 310 320 330 340 350 360 GVTGPDGEDY SPWADRKAAQ PKSLSPPQSQ SKLSDSYSNT LPVRKSVTPK NSYATTAENK 370 380 390 400 410 420 TLPRSSSMAA GLERNGRMRV KAIFSHAAGD NSTLLSFKEG DLITLLVPEA RDGWHYGESE 430 440 450 460 470 480 KTKMRGWFPF SYTRVLDSDG SDRLHMSLQQ GKSSSTGNLL DKDDLAIPPP DYGAASRAFP 490 500 510 520 AQTASGFKQR PYSVAVPAFS QGLDDYGARS MSSGSGTLVS TV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of BAIAP2 (BAI-associated protein 2), a novel human homologue of hamster IRSp53, whose SH3 domain interacts with the cytoplasmic domain of BAI1." Oda K., Shiratsuchi T., Nishimori H., Inazawa J., Yoshikawa H., Taketani Y., Nakamura Y., Tokino T. Cytogenet. Cell Genet. 84:75-82(1999) [PubMed: 10343108] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), INTERACTION WITH BAI1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Fetal brain.
[2]	"Dentatorubral-pallidoluysian atrophy protein interacts through a proline-rich region near polyglutamine with the SH3 domain of an insulin receptor tyrosine kinase substrate." Okamura-Oho Y., Miyashita T., Ohmi K., Yamada M. Hum. Mol. Genet. 8:947-957(1999) [PubMed: 10332026] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4), PHOSPHORYLATION AT TYROSINE RESIDUES, SUBCELLULAR LOCATION, INTERACTION WITH ATN1, TISSUE SPECIFICITY. Tissue: Fetal brain.
[3]	"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: 12884081] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2; 4 AND 5).
[4]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6). Tissue: Brain.
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 6). Tissue: Brain and Duodenum.
[6]	"A Fas-ligand associated factor 3, FLAF3, potentiates Fas-ligand stability." Hachiya T., Kobayasi A., Touji S., Tamai K. Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-328. Tissue: Placenta.
[7]	"IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling." Miki H., Yamaguchi H., Suetsugu S., Takenawa T. Nature 408:732-735(2000) [PubMed: 11130076] [Abstract] Cited for: FUNCTION, INTERACTION WITH RAC1; CDC42; WASF1 AND WASF2.
[8]	"Cdc42 induces filopodia by promoting the formation of an IRSp53:Mena complex." Krugmann S., Jordens I., Gevaert K., Driessens M., Vandekerckhove J., Hall A. Curr. Biol. 11:1645-1655(2001) [PubMed: 11696321] [Abstract] Cited for: FUNCTION, INTERACTION WITH CDC42 AND ENAH, MUTAGENESIS OF PHE-427 AND PRO-428.
[9]	"Cdc42Hs facilitates cytoskeletal reorganization and neurite outgrowth by localizing the 58-kD insulin receptor substrate to filamentous actin." Govind S., Kozma R., Monfries C., Lim L., Ahmed S. J. Cell Biol. 152:579-594(2001) [PubMed: 11157984] [Abstract] Cited for: INTERACTION WITH CDC42, MUTAGENESIS OF ILE-267, TISSUE SPECIFICITY.
[10]	"The insulin receptor substrate IRSp53 links postsynaptic shank1 to the small G-protein cdc42." Soltau M., Richter D., Kreienkamp H.-J. Mol. Cell. Neurosci. 21:575-583(2002) [PubMed: 12504591] [Abstract] Cited for: INTERACTION WITH SHANK1; SHANK2; SHANK3 AND CDC42, SUBCELLULAR LOCATION.
[11]	"IRSp53/Eps8 complex is important for positive regulation of Rac and cancer cell motility/invasiveness." Funato Y., Terabayashi T., Suenaga N., Seiki M., Takenawa T., Miki H. Cancer Res. 64:5237-5244(2004) [PubMed: 15289329] [Abstract] Cited for: INTERACTION WITH EPS8, SUBCELLULAR LOCATION.
[12]	"A novel actin bundling/filopodium-forming domain conserved in insulin receptor tyrosine kinase substrate p53 and missing in metastasis protein." Yamagishi A., Masuda M., Ohki T., Onishi H., Mochizuki N. J. Biol. Chem. 279:14929-14936(2004) [PubMed: 14752106] [Abstract] Cited for: DOMAIN, FUNCTION.
[13]	"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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-337; TYR-491 AND TYR-505, MASS SPECTROMETRY.
[14]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325, MASS SPECTROMETRY.
[15]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-296; TYR-310; SER-323; SER-325; SER-346; THR-348 AND SER-366, MASS SPECTROMETRY.
[16]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325 AND SER-454, MASS SPECTROMETRY.
[17]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-337, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[18]	"Structural basis of filopodia formation induced by the IRSp53/MIM homology domain of human IRSp53." Millard T.H., Bompard G., Heung M.Y., Dafforn T.R., Scott D.J., Machesky L.M., Fuetterer K. EMBO J. 24:240-250(2005) [PubMed: 15635447] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-250, MUTAGENESIS OF LYS-142; LYS-143; LYS-146 AND LYS-147.
[19]	"Crystal structure of RCB domain of IRSP53." RIKEN structural genomics initiative (RSGI) Submitted (JUN-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS) OF 1-228.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB015019 mRNA. Translation: BAA36586.1.
AB015020 mRNA. Translation: BAA36587.1.
AB017119 mRNA. Translation: BAA74773.1.
AB017120 mRNA. Translation: BAA74774.1.
AB104726 Genomic DNA. Translation: BAC57945.1.
AB104726 Genomic DNA. Translation: BAC57946.1.
AB104726 Genomic DNA. Translation: BAC57947.1.
AB104726 Genomic DNA. Translation: BAC57948.1.
AK222670 mRNA. Translation: BAD96390.1.
BC014020 mRNA. Translation: AAH14020.1.
BC032559 mRNA. Translation: AAH32559.1.
U70669 mRNA. Translation: AAB93497.1.

IPI

IPI00180292.
IPI00185159.
IPI00299088.
IPI00642333.
IPI00644120.
IPI00647603.

RefSeq

NP_001138360.1.
NP_006331.1.
NP_059344.1.
NP_059345.1.

UniGene

Hs.128316

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WDZ	X-ray	2.63	A/B	1-228	[»]
1Y2O	X-ray	2.20	A/B	1-250	[»]

SMR

Q9UQB8. Positions 378-440.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29272N.

IntAct

Q9UQB8. 9 interactions.

STRING

Q9UQB8.

PTM databases

PhosphoSite

Q9UQB8.

Proteomic databases

PRIDE

Q9UQB8.

Genome annotation databases

Ensembl

ENST00000321300; ENSP00000316338; ENSG00000175866; Homo sapiens. [Genome view]

GeneID

10458.

KEGG

hsa:10458.

UCSC

uc002jyz.2. human.
uc002jza.1. human.
uc002jzc.1. human.
uc002jzd.1. human.
uc002jzf.1. human.
uc002jzg.1. human.

Organism-specific databases

CTD

10458.

GeneCards

GC17P076623.

H-InvDB

HIX0020031.

HGNC

HGNC:947. BAIAP2.

HPA

HPA023310.

MIM

605475. gene.

PharmGKB

PA25251.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG13810.

HOVERGEN

Q9UQB8.

InParanoid

Q9UQB8.

OMA

AVSRNPF.

OrthoDB

EOG9XKXS9.

PhylomeDB

Q9UQB8.

Enzyme and pathway databases

Reactome

REACT_14797. Signaling by GPCR.

Gene expression databases

ArrayExpress

Q9UQB8.

Bgee

Q9UQB8.

CleanEx

HS_BAIAP2.

Genevestigator

Q9UQB8.

GermOnline

ENSG00000175866. Homo sapiens.

Family and domain databases

InterPro

IPR013606. IRSp53/MIM_homology_IMD.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]

Gene3D

G3DSA:1.20.1270.80. IRSp53/MIM_homology_IMD. 1 hit.

Pfam

PF08397. IMD. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]

SMART

SM00326. SH3. 1 hit.
[Graphical view]

PROSITE

PS51338. IMD. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

39651.

SOURCE

Search...

Entry information

Entry name

BAIP2_HUMAN

Accession

Primary (citable) accession number: Q9UQB8
Secondary accession number(s): O43858 , Q53HB1, Q86WC1, Q8N5C0, Q96CR7, Q9UBR3, Q9UQ43

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	May 1, 2000
Last modified:	February 9, 2010
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.