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Q8BKX1

- BAIP2_MOUSE

UniProt

Q8BKX1 - BAIP2_MOUSE

Protein

Brain-specific angiogenesis inhibitor 1-associated protein 2

Gene

Baiap2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 2 (30 Aug 2005)
      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.1 Publication

    GO - Molecular functioni

    1. proline-rich region binding Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. actin crosslink formation Source: UniProtKB
    2. actin filament bundle assembly Source: UniProtKB
    3. dendrite development Source: MGI
    4. filopodium assembly Source: InterPro
    5. regulation of actin cytoskeleton organization Source: UniProtKB
    6. regulation of cell shape Source: UniProtKB
    7. regulation of synaptic plasticity Source: MGI
    8. response to bacterium Source: UniProtKB
    9. Rho protein signal transduction Source: MGI

    Enzyme and pathway databases

    ReactomeiREACT_198374. Regulation of actin dynamics for phagocytic cup formation.

    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
    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 namesi
    Name:Baiap2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:2137336. Baiap2.

    Subcellular locationi

    Cytoplasm By similarity. Membrane By similarity; Peripheral membrane protein By similarity. Cell projectionfilopodium By similarity. Cell projectionruffle By similarity. Cytoplasmcytoskeleton 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.By similarity

    GO - Cellular componenti

    1. actin cytoskeleton Source: Ensembl
    2. cell junction Source: Ensembl
    3. cytosol Source: UniProtKB
    4. filopodium Source: UniProtKB-SubCell
    5. neuron projection Source: BHF-UCL
    6. nucleus Source: Ensembl
    7. plasma membrane Source: Ensembl
    8. ruffle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Cytoskeleton, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 535535Brain-specific angiogenesis inhibitor 1-associated protein 2PRO_0000064817Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei324 – 3241PhosphoserineBy similarity
    Modified residuei326 – 3261PhosphoserineBy similarity
    Modified residuei341 – 3411PhosphothreonineBy similarity
    Modified residuei347 – 3471PhosphoserineBy similarity
    Modified residuei367 – 3671PhosphoserineBy similarity
    Modified residuei455 – 4551PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated on tyrosine residues by INSR in response to insulin treatment.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8BKX1.
    PaxDbiQ8BKX1.
    PRIDEiQ8BKX1.

    PTM databases

    PhosphoSiteiQ8BKX1.

    Expressioni

    Tissue specificityi

    Detected in liver, brain, olfactory bulb, brain cortex, caudate putamen, hypothalamus and cerebellum.1 Publication

    Gene expression databases

    ArrayExpressiQ8BKX1.
    BgeeiQ8BKX1.
    GenevestigatoriQ8BKX1.

    Interactioni

    Subunit structurei

    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.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Diaph1O088083EBI-771498,EBI-1026445
    Dlg4Q621083EBI-771498,EBI-300895
    Iqsec2A4GZ267EBI-771498,EBI-8526464

    Protein-protein interaction databases

    BioGridi223833. 1 interaction.
    DIPiDIP-32392N.
    IntActiQ8BKX1. 5 interactions.
    MINTiMINT-4122910.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BKX1.
    SMRiQ8BKX1. Positions 2-229, 264-292, 375-437.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 250250IMDPROSITE-ProRule annotationAdd
    BLAST
    Domaini375 – 43864SH3PROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili88 – 15366Sequence 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 By similarity.By similarity
    The SH3 domain interacts with ATN1, BAI1, WASF1, WASF2, SHANK1, DIAPH1 and ENAH.By similarity

    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.
    GeneTreeiENSGT00390000005995.
    HOGENOMiHOG000038005.
    HOVERGENiHBG054462.
    InParanoidiQ8BKX1.
    KOiK05627.
    OMAiFLAQQMS.
    OrthoDBiEOG7N0C3W.
    PhylomeDBiQ8BKX1.
    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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8BKX1-1) [UniParc]FASTAAdd to Basket

    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 ALAGVTFAAK    50
    GYFDALVKMG ELASESQGSK ELGDVLFQMA EVHRQIQNQL EETLKSFHNE 100
    LLTQLEQKVE LDSRYLSAAL KKYQTEQRSK GDALDKCQAE LKKLRKKSQG 150
    SKNPQKYSDK ELQYIDAISN KQGELENYVS DGYKTALTEE RRRFCFLVEK 200
    QCAVAKNSAA YHSKGKELLA QKLPLWQQAC ADPNKIPDRA VQLMQQMANS 250
    NGSILPSALS ASKSNLVISD PIPGAKPLPV PPELAPFVGR MSAQENVPVM 300
    NGVAGPDSED YNPWADRKAA QPKSLSPPQS QSKLSDSYSN TLPVRKSVTP 350
    KNSYATTENK TLPRSSSMAA GLERNGRMRV KAIFSHAAGD NSTLLSFKEG 400
    DLITLLVPEA RDGWHYGESE KTKMRGWFPF SYTRVLDSDG SDRLHMSLQQ 450
    GKSSSTGNLL DKDDLALPPP DYGTSSRAFP TQTAGTFKQR PYSVAVPAFS 500
    QGLDDYGARS VSRNPFANVH LKPTVTNDRS APLLS 535
    Length:535
    Mass (Da):59,237
    Last modified:August 30, 2005 - v2
    Checksum:i45B4C660FBB07F72
    GO
    Isoform 2 (identifier: Q8BKX1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         513-535: RNPFANVHLKPTVTNDRSAPLLS → SGSGTLVSTV

    Show »
    Length:522
    Mass (Da):57,596
    Checksum:i8E65752157FD3F99
    GO
    Isoform 3 (identifier: Q8BKX1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         514-535: Missing.

    Show »
    Length:513
    Mass (Da):56,863
    Checksum:i5EDD57E315AF4005
    GO
    Isoform 4 (identifier: Q8BKX1-4) [UniParc]FASTAAdd to Basket

    Also known as: Short form

    The sequence of this isoform differs from the canonical sequence as follows:
         290-329: Missing.
         513-535: RNPFANVHLKPTVTNDRSAPLLS → SGSGTLVSTV

    Show »
    Length:482
    Mass (Da):53,274
    Checksum:iF3FA1DFDC1E0D579
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti87 – 882QN → HI in BAC33764. (PubMed:16141072)Curated
    Sequence conflicti326 – 3261S → F in BAC33764. (PubMed:16141072)Curated
    Sequence conflicti330 – 3301S → F in BAC33764. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei290 – 32940Missing in isoform 4. 1 PublicationVSP_015507Add
    BLAST
    Alternative sequencei513 – 53523RNPFA…APLLS → SGSGTLVSTV in isoform 2 and isoform 4. 1 PublicationVSP_015508Add
    BLAST
    Alternative sequencei514 – 53522Missing in isoform 3. 1 PublicationVSP_015509Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS25722.1. [Q8BKX1-1]
    CCDS25723.1. [Q8BKX1-4]
    CCDS25724.1. [Q8BKX1-2]
    RefSeqiNP_001032843.1. NM_001037754.3. [Q8BKX1-4]
    NP_001032844.2. NM_001037755.3. [Q8BKX1-1]
    NP_570932.2. NM_130862.4. [Q8BKX1-2]
    UniGeneiMm.197534.

    Genome annotation databases

    EnsembliENSMUST00000026436; ENSMUSP00000026436; ENSMUSG00000025372. [Q8BKX1-1]
    ENSMUST00000075180; ENSMUSP00000074674; ENSMUSG00000025372. [Q8BKX1-2]
    ENSMUST00000103021; ENSMUSP00000099310; ENSMUSG00000025372. [Q8BKX1-4]
    ENSMUST00000106231; ENSMUSP00000101838; ENSMUSG00000025372. [Q8BKX1-3]
    GeneIDi108100.
    KEGGimmu:108100.
    UCSCiuc007mri.1. mouse. [Q8BKX1-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS25722.1. [Q8BKX1-1 ]
    CCDS25723.1. [Q8BKX1-4 ]
    CCDS25724.1. [Q8BKX1-2 ]
    RefSeqi NP_001032843.1. NM_001037754.3. [Q8BKX1-4 ]
    NP_001032844.2. NM_001037755.3. [Q8BKX1-1 ]
    NP_570932.2. NM_130862.4. [Q8BKX1-2 ]
    UniGenei Mm.197534.

    3D structure databases

    ProteinModelPortali Q8BKX1.
    SMRi Q8BKX1. Positions 2-229, 264-292, 375-437.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 223833. 1 interaction.
    DIPi DIP-32392N.
    IntActi Q8BKX1. 5 interactions.
    MINTi MINT-4122910.

    PTM databases

    PhosphoSitei Q8BKX1.

    Proteomic databases

    MaxQBi Q8BKX1.
    PaxDbi Q8BKX1.
    PRIDEi Q8BKX1.

    Protocols and materials databases

    DNASUi 108100.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000026436 ; ENSMUSP00000026436 ; ENSMUSG00000025372 . [Q8BKX1-1 ]
    ENSMUST00000075180 ; ENSMUSP00000074674 ; ENSMUSG00000025372 . [Q8BKX1-2 ]
    ENSMUST00000103021 ; ENSMUSP00000099310 ; ENSMUSG00000025372 . [Q8BKX1-4 ]
    ENSMUST00000106231 ; ENSMUSP00000101838 ; ENSMUSG00000025372 . [Q8BKX1-3 ]
    GeneIDi 108100.
    KEGGi mmu:108100.
    UCSCi uc007mri.1. mouse. [Q8BKX1-1 ]

    Organism-specific databases

    CTDi 10458.
    MGIi MGI:2137336. Baiap2.

    Phylogenomic databases

    eggNOGi NOG71665.
    GeneTreei ENSGT00390000005995.
    HOGENOMi HOG000038005.
    HOVERGENi HBG054462.
    InParanoidi Q8BKX1.
    KOi K05627.
    OMAi FLAQQMS.
    OrthoDBi EOG7N0C3W.
    PhylomeDBi Q8BKX1.
    TreeFami TF325648.

    Enzyme and pathway databases

    Reactomei REACT_198374. Regulation of actin dynamics for phagocytic cup formation.

    Miscellaneous databases

    ChiTaRSi BAIAP2. mouse.
    NextBioi 360066.
    PROi Q8BKX1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8BKX1.
    Bgeei Q8BKX1.
    Genevestigatori Q8BKX1.

    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. "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. "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] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
      Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
      Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    9. "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.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiBAIP2_MOUSE
    AccessioniPrimary (citable) accession number: Q8BKX1
    Secondary accession number(s): Q91V97, Q923V9, Q923W0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: August 30, 2005
    Last modified: October 1, 2014
    This is version 108 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3