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Q9UQB8

- BAIP2_HUMAN

UniProt

Q9UQB8 - BAIP2_HUMAN

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
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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 binding Source: IntAct
    5. protein C-terminus binding Source: ProtInc

    GO - Biological processi

    1. actin crosslink formation Source: UniProtKB
    2. actin filament bundle assembly Source: UniProtKB
    3. axonogenesis Source: ProtInc
    4. dendrite development Source: Ensembl
    5. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    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

    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.

    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

    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 2PRO_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.4 Publications

    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.By similarity10 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

    1
    552
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UQB8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 250250IMDPROSITE-ProRule annotationAdd
    BLAST
    Domaini374 – 43764SH3PROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili132 – 15322Sequence AnalysisAdd
    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 IMD (IRSp53/MIM homology) domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    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

    Experimental Info

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

    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. 2 PublicationsVSP_015502
    Alternative sequencei512 – 55241RNPFA…TLAGR → SGSGTLVSTV in isoform 4 and isoform 6. 4 PublicationsVSP_015503Add
    BLAST
    Alternative sequencei512 – 55241RNPFA…TLAGR → SADVEVARF in isoform 5. 1 PublicationVSP_015504Add
    BLAST
    Alternative sequencei513 – 55240Missing in isoform 3. 1 PublicationVSP_015505Add
    BLAST
    Alternative sequencei529 – 55224CDLSA…TLAGR → SAPLLS in isoform 2. CuratedVSP_015506Add
    BLAST

    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

    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

    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

    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: October 1, 2014
    This is version 131 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.Curated

    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