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Q9UQB8

- BAIP2_HUMAN

UniProt

Q9UQB8 - BAIP2_HUMAN

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Protein
Brain-specific angiogenesis inhibitor 1-associated protein 2
Gene
BAIAP2
Organism
Homo sapiens (Human)
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.5 Publications

GO - Molecular functioni

  1. cytoskeletal adaptor activity Source: ProtInc
  2. identical protein binding Source: IntAct
  3. proline-rich region binding Source: UniProtKB
  4. protein C-terminus binding Source: ProtInc
  5. protein binding Source: IntAct

GO - Biological processi

  1. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  2. actin crosslink formation Source: UniProtKB
  3. actin filament bundle assembly Source: UniProtKB
  4. axonogenesis Source: ProtInc
  5. dendrite development Source: Ensembl
  6. filopodium assembly Source: InterPro
  7. innate immune response Source: Reactome
  8. insulin receptor signaling pathway Source: ProtInc
  9. regulation of actin cytoskeleton organization Source: UniProtKB
  10. regulation of cell shape Source: UniProtKB
  11. regulation of synaptic plasticity Source: Ensembl
  12. response to bacterium Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.
SignaLinkiQ9UQB8.

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
Short name:
Protein BAP2
Alternative name(s):
Fas ligand-associated factor 3
Short name:
FLAF3
Insulin receptor substrate p53/p58
Short name:
IRS-58
Short name:
IRSp53/58
Insulin receptor substrate protein of 53 kDa
Short name:
IRSp53
Short name:
Insulin receptor substrate p53
Gene namesi
Name:BAIAP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:947. BAIAP2.

Subcellular locationi

Cytoplasm. Membrane; Peripheral membrane protein. Cell projectionfilopodium. Cell projectionruffle. Cytoplasmcytoskeleton
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.5 Publications

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. cytoskeleton Source: UniProtKB-SubCell
  3. cytosol Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProt
  5. filopodium Source: UniProtKB-SubCell
  6. neuron projection Source: Ensembl
  7. plasma membrane Source: ProtInc
  8. ruffle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi142 – 1421K → E: Abolishes actin-bundling and filopodia formation; when associated with E-143; E-146 and E147. 1 Publication
Mutagenesisi143 – 1431K → E: Abolishes actin-bundling and filopodia formation; when associated with E-142; E-146 and E147. 1 Publication
Mutagenesisi146 – 1461K → E: Abolishes actin-bundling and filopodia formation; when associated with E-142; E-143 and E147. 1 Publication
Mutagenesisi147 – 1471K → E: Abolishes actin-bundling and filopodia formation; when associated with E-142; E-143 and E146. 1 Publication
Mutagenesisi267 – 2671I → N: Loss of interaction with CDC42. Loss of stimulation of neurite growth. 1 Publication
Mutagenesisi413 – 4131W → G: Impairs the SH3 domain and abolishes the interaction with EPS8. 1 Publication
Mutagenesisi427 – 4271F → A: Loss of interaction with ENAH and no induction of filopodia; when associated with A-428. 1 Publication
Mutagenesisi428 – 4281P → A: Loss of interaction with ENAH and no induction of filopodia; when associated with A-427. 1 Publication

Organism-specific databases

PharmGKBiPA25251.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 552552Brain-specific angiogenesis inhibitor 1-associated protein 2
PRO_0000064816Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei296 – 2961Phosphothreonine2 Publications
Modified residuei323 – 3231Phosphoserine2 Publications
Modified residuei325 – 3251Phosphoserine2 Publications
Modified residuei340 – 3401Phosphothreonine2 Publications
Modified residuei346 – 3461Phosphoserine2 Publications
Modified residuei366 – 3661Phosphoserine2 Publications
Modified residuei454 – 4541Phosphoserine2 Publications

Post-translational modificationi

Phosphorylated on tyrosine residues by INSR in response to insulin treatment.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UQB8.
PaxDbiQ9UQB8.
PRIDEiQ9UQB8.

2D gel databases

UCD-2DPAGEQ9UQB8.

PTM databases

PhosphoSiteiQ9UQB8.

Expressioni

Tissue specificityi

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.3 Publications

Gene expression databases

ArrayExpressiQ9UQB8.
BgeeiQ9UQB8.
CleanExiHS_BAIAP2.
GenevestigatoriQ9UQB8.

Organism-specific databases

HPAiHPA023310.
HPA027421.

Interactioni

Subunit structurei

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. Interacts (via SH3 domain) with E.coli effector protein EspF(U) (via PXXP motifs). Interacts with E.coli intimin receptor Tir.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-525456,EBI-525456
CDC42P609534EBI-6174091,EBI-81752
CDC42P60953-22EBI-525456,EBI-287394
Cdc42Q8CFN22EBI-525456,EBI-7023929From a different organism.
EnahQ031733EBI-525456,EBI-6083294From a different organism.
EPS8Q129294EBI-525456,EBI-375576
Eps8Q085098EBI-525456,EBI-375596From a different organism.
KANK1Q146786EBI-525456,EBI-2556221
KANK1Q14678-24EBI-6174091,EBI-6173812
NCKIPSDQ9NZQ32EBI-525456,EBI-745080
RAC1P630004EBI-525456,EBI-413628
VASPP505526EBI-6174091,EBI-748201
WASF2Q9Y6W55EBI-6174091,EBI-4290615
ZDHHC17Q8IUH53EBI-9091996,EBI-524753

Protein-protein interaction databases

BioGridi115721. 26 interactions.
DIPiDIP-29272N.
IntActiQ9UQB8. 29 interactions.
MINTiMINT-92955.
STRINGi9606.ENSP00000316338.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 2218
Helixi24 – 6441
Beta strandi66 – 683
Helixi70 – 9829
Turni99 – 1013
Helixi102 – 14645
Helixi150 – 1523
Turni154 – 1574
Helixi159 – 22870
Helixi238 – 2469
Helixi281 – 2866
Beta strandi378 – 3836
Beta strandi401 – 4044
Beta strandi406 – 4083
Beta strandi413 – 4186
Turni419 – 4213
Beta strandi424 – 4285
Helixi429 – 4313
Beta strandi432 – 4343

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WDZX-ray2.63A/B1-228[»]
1Y2OX-ray2.20A/B1-250[»]
2YKTX-ray2.11A1-250[»]
3RNJX-ray1.50A375-436[»]
4JS0X-ray1.90B260-291[»]
ProteinModelPortaliQ9UQB8.
SMRiQ9UQB8. Positions 1-248, 263-291, 374-436.

Miscellaneous databases

EvolutionaryTraceiQ9UQB8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 250250IMD
Add
BLAST
Domaini374 – 43764SH3
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili132 – 15322 Reviewed prediction
Add
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.1 Publication
The SH3 domain interacts with ATN1, BAI1, WASF1, WASF2, SHANK1, DIAPH1 and ENAH.1 Publication

Sequence similaritiesi

Contains 1 SH3 domain.

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiNOG71665.
HOVERGENiHBG054462.
InParanoidiQ9UQB8.
KOiK05627.
OrthoDBiEOG7N0C3W.
PhylomeDBiQ9UQB8.
TreeFamiTF325648.

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 (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UQB8-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MSLSRSEEMH RLTENVYKTI MEQFNPSLRN FIAMGKNYEK ALAGVTYAAK    50
GYFDALVKMG ELASESQGSK ELGDVLFQMA EVHRQIQNQL EEMLKSFHNE 100
LLTQLEQKVE LDSRYLSAAL KKYQTEQRSK GDALDKCQAE LKKLRKKSQG 150
SKNPQKYSDK ELQYIDAISN KQGELENYVS DGYKTALTEE RRRFCFLVEK 200
QCAVAKNSAA YHSKGKELLA QKLPLWQQAC ADPSKIPERA VQLMQQVASN 250
GATLPSALSA SKSNLVISDP IPGAKPLPVP PELAPFVGRM SAQESTPIMN 300
GVTGPDGEDY SPWADRKAAQ PKSLSPPQSQ SKLSDSYSNT LPVRKSVTPK 350
NSYATTENKT LPRSSSMAAG LERNGRMRVK AIFSHAAGDN STLLSFKEGD 400
LITLLVPEAR DGWHYGESEK TKMRGWFPFS YTRVLDSDGS DRLHMSLQQG 450
KSSSTGNLLD KDDLAIPPPD YGAASRAFPA QTASGFKQRP YSVAVPAFSQ 500
GLDDYGARSM SRNPFAHVQL KPTVTNDRCD LSAQGPEGRE HGDGSARTLA 550
GR 552
Length:552
Mass (Da):60,868
Last modified:May 1, 2000 - v1
Checksum:i3B9EDC6405DCC99D
GO
Isoform 2 (identifier: Q9UQB8-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:534
Mass (Da):59,014
Checksum:iE63C4C08C48964B7
GO
Isoform 3 (identifier: Q9UQB8-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:512
Mass (Da):56,626
Checksum:i985ACC2B8DBEE7C3
GO
Isoform 4 (identifier: Q9UQB8-4) [UniParc]FASTAAdd to Basket

Also known as: BAIAP2-alpha

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

Show »
Length:521
Mass (Da):57,359
Checksum:i618A09FDBEB3A5C3
GO
Isoform 5 (identifier: Q9UQB8-5) [UniParc]FASTAAdd to Basket

Also known as: BAIAP2-beta

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

Show »
Length:520
Mass (Da):57,445
Checksum:iFC6852BB490F6C0B
GO
Isoform 6 (identifier: Q9UQB8-6) [UniParc]FASTAAdd to Basket

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

Show »
Length:522
Mass (Da):57,430
Checksum:i58146A293AF313BC
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti519 – 5191Q → R.
Corresponds to variant rs4969391 [ dbSNP | Ensembl ].
VAR_050686

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei356 – 3561T → TA in isoform 6.
VSP_015502
Alternative sequencei512 – 55241RNPFA…TLAGR → SGSGTLVSTV in isoform 4 and isoform 6.
VSP_015503Add
BLAST
Alternative sequencei512 – 55241RNPFA…TLAGR → SADVEVARF in isoform 5.
VSP_015504Add
BLAST
Alternative sequencei513 – 55240Missing in isoform 3.
VSP_015505Add
BLAST
Alternative sequencei529 – 55224CDLSA…TLAGR → SAPLLS in isoform 2.
VSP_015506Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841R → W in BAD96390. 1 Publication
Sequence conflicti415 – 4151Y → H in BAD96390. 1 Publication
Sequence conflicti473 – 4731A → T in BAD96390. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS11775.1. [Q9UQB8-1]
CCDS11776.1. [Q9UQB8-5]
CCDS11777.1. [Q9UQB8-4]
CCDS45806.1. [Q9UQB8-2]
RefSeqiNP_001138360.1. NM_001144888.1. [Q9UQB8-2]
NP_006331.1. NM_006340.2. [Q9UQB8-5]
NP_059344.1. NM_017450.2. [Q9UQB8-4]
NP_059345.1. NM_017451.2. [Q9UQB8-1]
XP_005257005.1. XM_005256948.1. [Q9UQB8-6]
UniGeneiHs.128316.

Genome annotation databases

EnsembliENST00000321280; ENSP00000315685; ENSG00000175866. [Q9UQB8-4]
ENST00000321300; ENSP00000316338; ENSG00000175866. [Q9UQB8-1]
ENST00000428708; ENSP00000401022; ENSG00000175866. [Q9UQB8-2]
ENST00000435091; ENSP00000413069; ENSG00000175866. [Q9UQB8-5]
ENST00000575712; ENSP00000458964; ENSG00000175866. [Q9UQB8-3]
GeneIDi10458.
KEGGihsa:10458.
UCSCiuc002jyz.4. human. [Q9UQB8-1]
uc002jza.2. human. [Q9UQB8-4]
uc002jzc.2. human. [Q9UQB8-6]
uc002jzd.2. human. [Q9UQB8-5]
uc002jzf.2. human. [Q9UQB8-2]

Polymorphism databases

DMDMi73917636.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS11775.1. [Q9UQB8-1 ]
CCDS11776.1. [Q9UQB8-5 ]
CCDS11777.1. [Q9UQB8-4 ]
CCDS45806.1. [Q9UQB8-2 ]
RefSeqi NP_001138360.1. NM_001144888.1. [Q9UQB8-2 ]
NP_006331.1. NM_006340.2. [Q9UQB8-5 ]
NP_059344.1. NM_017450.2. [Q9UQB8-4 ]
NP_059345.1. NM_017451.2. [Q9UQB8-1 ]
XP_005257005.1. XM_005256948.1. [Q9UQB8-6 ]
UniGenei Hs.128316.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
2YKT X-ray 2.11 A 1-250 [» ]
3RNJ X-ray 1.50 A 375-436 [» ]
4JS0 X-ray 1.90 B 260-291 [» ]
ProteinModelPortali Q9UQB8.
SMRi Q9UQB8. Positions 1-248, 263-291, 374-436.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115721. 26 interactions.
DIPi DIP-29272N.
IntActi Q9UQB8. 29 interactions.
MINTi MINT-92955.
STRINGi 9606.ENSP00000316338.

PTM databases

PhosphoSitei Q9UQB8.

Polymorphism databases

DMDMi 73917636.

2D gel databases

UCD-2DPAGE Q9UQB8.

Proteomic databases

MaxQBi Q9UQB8.
PaxDbi Q9UQB8.
PRIDEi Q9UQB8.

Protocols and materials databases

DNASUi 10458.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000321280 ; ENSP00000315685 ; ENSG00000175866 . [Q9UQB8-4 ]
ENST00000321300 ; ENSP00000316338 ; ENSG00000175866 . [Q9UQB8-1 ]
ENST00000428708 ; ENSP00000401022 ; ENSG00000175866 . [Q9UQB8-2 ]
ENST00000435091 ; ENSP00000413069 ; ENSG00000175866 . [Q9UQB8-5 ]
ENST00000575712 ; ENSP00000458964 ; ENSG00000175866 . [Q9UQB8-3 ]
GeneIDi 10458.
KEGGi hsa:10458.
UCSCi uc002jyz.4. human. [Q9UQB8-1 ]
uc002jza.2. human. [Q9UQB8-4 ]
uc002jzc.2. human. [Q9UQB8-6 ]
uc002jzd.2. human. [Q9UQB8-5 ]
uc002jzf.2. human. [Q9UQB8-2 ]

Organism-specific databases

CTDi 10458.
GeneCardsi GC17P079008.
HGNCi HGNC:947. BAIAP2.
HPAi HPA023310.
HPA027421.
MIMi 605475. gene.
neXtProti NX_Q9UQB8.
PharmGKBi PA25251.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG71665.
HOVERGENi HBG054462.
InParanoidi Q9UQB8.
KOi K05627.
OrthoDBi EOG7N0C3W.
PhylomeDBi Q9UQB8.
TreeFami TF325648.

Enzyme and pathway databases

Reactomei REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
SignaLinki Q9UQB8.

Miscellaneous databases

EvolutionaryTracei Q9UQB8.
GeneWikii BAIAP2.
GenomeRNAii 10458.
NextBioi 39651.
PROi Q9UQB8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UQB8.
Bgeei Q9UQB8.
CleanExi HS_BAIAP2.
Genevestigatori Q9UQB8.

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. "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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: DOMAIN, FUNCTION.
  13. "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, MUTAGENESIS OF TRP-413.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-296; SER-323; SER-325; SER-346 AND SER-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "IRSp53 links the enterohemorrhagic E. coli effectors Tir and EspFU for actin pedestal formation."
    Weiss S.M., Ladwein M., Schmidt D., Ehinger J., Lommel S., Stading K., Beutling U., Disanza A., Frank R., Jansch L., Scita G., Gunzer F., Rottner K., Stradal T.E.
    Cell Host Microbe 5:244-258(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH E.COLI EFFECTOR PROTEIN ESPF(U) AND WITH E.COLI INTIMIN RECEPTOR TIR.
  17. "Insulin receptor tyrosine kinase substrate links the E. coli O157:H7 actin assembly effectors Tir and EspF(U) during pedestal formation."
    Vingadassalom D., Kazlauskas A., Skehan B., Cheng H.C., Magoun L., Robbins D., Rosen M.K., Saksela K., Leong J.M.
    Proc. Natl. Acad. Sci. U.S.A. 106:6754-6759(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH E.COLI EFFECTOR PROTEIN ESPF(U), SUBCELLULAR LOCATION.
  18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-340, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-454, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-250, MUTAGENESIS OF LYS-142; LYS-143; LYS-146 AND LYS-147.
  22. "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.

Entry informationi

Entry nameiBAIP2_HUMAN
AccessioniPrimary (citable) accession number: Q9UQB8
Secondary accession number(s): O43858
, Q53HB1, Q86WC1, Q8N5C0, Q96CR7, Q9UBR3, Q9UQ43
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: May 1, 2000
Last modified: September 3, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Caution

It is uncertain whether Met-1 or Met-59 is the initiator.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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