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O43516

- WIPF1_HUMAN

UniProt

O43516 - WIPF1_HUMAN

Protein

WAS/WASL-interacting protein family member 1

Gene

WIPF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 3 (30 Nov 2010)
      Previous versions | rss
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    Functioni

    Plays a role in the reorganization of the actin cytoskeleton. Contributes with NCK1 and GRB2 in the recruitment and activation of WASL. May participate in regulating the subcellular localization of WASL, resulting in the disassembly of stress fibers in favor of filopodia formation. Plays a role in the formation of cell ruffles By similarity. Plays an important role in the intracellular motility of vaccinia virus by functioning as an adapter for recruiting WASL to vaccinia virus.By similarity3 Publications

    GO - Molecular functioni

    1. actin binding Source: ProtInc
    2. profilin binding Source: ProtInc
    3. protein binding Source: IntAct

    GO - Biological processi

    1. actin filament-based movement Source: Ensembl
    2. actin polymerization or depolymerization Source: ProtInc
    3. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    4. innate immune response Source: Reactome
    5. protein complex assembly Source: ProtInc
    6. response to other organism Source: Ensembl

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    WAS/WASL-interacting protein family member 1
    Alternative name(s):
    Protein PRPL-2
    Wiskott-Aldrich syndrome protein-interacting protein
    Short name:
    WASP-interacting protein
    Gene namesi
    Name:WIPF1
    Synonyms:WASPIP, WIP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:12736. WIPF1.

    Subcellular locationi

    Cytoplasmic vesicle By similarity. Cytoplasmcytoskeleton By similarity. Cell projectionruffle 1 Publication
    Note: Vesicle surfaces and along actin tails. Colocalizes with actin stress fibers. When coexpressed with WASL, no longer associated with actin filaments but accumulated in perinuclear and cortical areas like WASL By similarity.By similarity

    GO - Cellular componenti

    1. actin cytoskeleton Source: ProtInc
    2. actin filament Source: Ensembl
    3. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
    4. cytosol Source: Reactome
    5. ruffle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton

    Pathology & Biotechi

    Involvement in diseasei

    Wiskott-Aldrich syndrome 2 (WAS2) [MIM:614493]: An immunodeficiency disorder characterized by eczema, thrombocytopenia, recurrent infections, defective T-cell proliferation, and impaired natural killer cell function.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi614493. phenotype.
    Orphaneti906. Wiskott-Aldrich syndrome.
    PharmGKBiPA162409189.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 503503WAS/WASL-interacting protein family member 1PRO_0000065941Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei142 – 1421PhosphoserineBy similarity
    Modified residuei340 – 3401Phosphoserine1 Publication
    Modified residuei345 – 3451Phosphothreonine2 Publications
    Modified residuei350 – 3501Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO43516.
    PaxDbiO43516.
    PRIDEiO43516.

    PTM databases

    PhosphoSiteiO43516.

    Expressioni

    Tissue specificityi

    Highly expressed in peripheral blood mononuclear cells, spleen, placenta, small intestine, colon and thymus. Lower expression in ovary, heart, brain, lung, liver, skeletal muscle, kidney, pancreas, prostate and testis.1 Publication

    Gene expression databases

    ArrayExpressiO43516.
    BgeeiO43516.
    CleanExiHS_WIPF1.
    GenevestigatoriO43516.

    Organism-specific databases

    HPAiCAB009737.
    HPA003739.

    Interactioni

    Subunit structurei

    Binds to WAS, profilin and actin. Binds to WASL By similarity. Interacts with DBNL.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CttnQ605983EBI-346356,EBI-397955From a different organism.
    GRB2P629933EBI-346356,EBI-401755
    HCKP086313EBI-346356,EBI-346340
    HCLS1P143172EBI-346356,EBI-750369
    NCK1P163332EBI-346356,EBI-389883
    WASP4276811EBI-346356,EBI-346375
    WASLO004014EBI-346356,EBI-957615

    Protein-protein interaction databases

    BioGridi113295. 21 interactions.
    DIPiDIP-17015N.
    IntActiO43516. 18 interactions.
    MINTiMINT-238480.
    STRINGi9606.ENSP00000352802.

    Structurei

    Secondary structure

    1
    503
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi33 – 4210

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2A41X-ray2.60C29-60[»]
    ProteinModelPortaliO43516.
    SMRiO43516. Positions 29-60, 461-488.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO43516.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini32 – 4918WH2PROSITE-ProRule annotationAdd
    BLAST
    Repeati352 – 36110XRSGPXPPXP motif 1
    Repeati374 – 38310XRSGPXPPXP motif 2
    Repeati410 – 41910XRSGPXPPXP motif 3

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni45 – 484Binds actin

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi2 – 1312Poly-ProAdd
    BLAST
    Compositional biasi64 – 9633Gly-richAdd
    BLAST
    Compositional biasi241 – 2444Poly-Ser
    Compositional biasi264 – 433170Pro-richAdd
    BLAST

    Domaini

    Binds to WAS within the N-terminal region 170, at a site distinct from the CDC42-binding site.

    Sequence similaritiesi

    Belongs to the verprolin family.Curated
    Contains 1 WH2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG149184.
    HOVERGENiHBG054157.
    InParanoidiO43516.
    OMAiQSSLHNR.
    OrthoDBiEOG7PS1GQ.
    PhylomeDBiO43516.
    TreeFamiTF332135.

    Family and domain databases

    InterProiIPR003124. WH2_dom.
    IPR028295. WIP.
    [Graphical view]
    PANTHERiPTHR23202:SF30. PTHR23202:SF30. 1 hit.
    PfamiPF02205. WH2. 1 hit.
    [Graphical view]
    SMARTiSM00246. WH2. 1 hit.
    [Graphical view]
    PROSITEiPS51082. WH2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O43516-1) [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

    MPVPPPPAPP PPPTFALANT EKPTLNKTEQ AGRNALLSDI SKGKKLKKTV    50
    TNDRSAPILD KPKGAGAGGG GGGFGGGGGF GGGGGGGGGG SFGGGGPPGL 100
    GGLFQAGMPK LRSTANRDND SGGSRPPLLP PGGRSTSAKP FSPPSGPGRF 150
    PVPSPGHRSG PPEPQRNRMP PPRPDVGSKP DSIPPPVPST PRPIQSSPHN 200
    RGSPPVPGGP RQPSPGPTPP PFPGNRGTAL GGGSIRQSPL SSSSPFSNRP 250
    PLPPTPSRAL DDKPPPPPPP VGNRPSIHRE AVPPPPPQNN KPPVPSTPRP 300
    SASSQAPPPP PPPSRPGPPP LPPSSSGNDE TPRLPQRNLS LSSSTPPLPS 350
    PGRSGPLPPP PSERPPPPVR DPPGRSGPLP PPPPVSRNGS TSRALPATPQ 400
    LPSRSGVDSP RSGPRPPLPP DRPSAGAPPP PPPSTSIRNG FQDSPCEDEW 450
    ESRFYFHPIS DLPPPEPYVQ TTKSYPSKLA RNESRSGSNR RERGAPPLPP 500
    IPR 503
    Length:503
    Mass (Da):51,258
    Last modified:November 30, 2010 - v3
    Checksum:i09B7A95E6808A46D
    GO
    Isoform 2 (identifier: O43516-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         487-503: GSNRRERGAPPLPPIPR → EYFCQGF

    Show »
    Length:493
    Mass (Da):50,281
    Checksum:iE6BD4D77F6F2B6F4
    GO
    Isoform 3 (identifier: O43516-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         503-503: R → RPPKQAAE

    Note: No experimental confirmation available.

    Show »
    Length:510
    Mass (Da):51,980
    Checksum:i9AEF92B15E4FE7F9
    GO
    Isoform 4 (identifier: O43516-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         220-364: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:358
    Mass (Da):36,426
    Checksum:i0473FF11AFC330B4
    GO

    Sequence cautioni

    The sequence AAC03767.1 differs from that shown. Reason: Frameshift at positions 302 and 310.
    The sequence CAA60014.1 differs from that shown. Reason: Frameshift at positions 302 and 310.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti119 – 1191N → D in CAE45928. (PubMed:17974005)Curated
    Sequence conflicti120 – 1201D → H in AAH02914. (PubMed:15489334)Curated
    Sequence conflicti360 – 3601P → PV in CAA60014. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti198 – 1981P → L.6 Publications
    Corresponds to variant rs4972450 [ dbSNP | Ensembl ].
    VAR_046526
    Natural varianti495 – 4951A → G.2 Publications
    VAR_010295

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei220 – 364145Missing in isoform 4. 1 PublicationVSP_012964Add
    BLAST
    Alternative sequencei487 – 50317GSNRR…PPIPR → EYFCQGF in isoform 2. 1 PublicationVSP_012965Add
    BLAST
    Alternative sequencei503 – 5031R → RPPKQAAE in isoform 3. 1 PublicationVSP_012966

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF031588 mRNA. Translation: AAC03767.1. Frameshift.
    X86019 mRNA. Translation: CAA60014.1. Frameshift.
    BX640870 mRNA. Translation: CAE45928.1.
    AC010894 Genomic DNA. Translation: AAY14708.1.
    AC104595 Genomic DNA. No translation available.
    CH471058 Genomic DNA. Translation: EAX11131.1.
    CH471058 Genomic DNA. Translation: EAX11132.1.
    CH471058 Genomic DNA. Translation: EAX11133.1.
    BC002914 mRNA. Translation: AAH02914.1.
    AF106062 mRNA. Translation: AAD45972.1.
    CCDSiCCDS2260.1. [O43516-1]
    RefSeqiNP_001070737.1. NM_001077269.1. [O43516-1]
    NP_003378.3. NM_003387.4. [O43516-1]
    XP_006712790.1. XM_006712727.1. [O43516-1]
    UniGeneiHs.128067.

    Genome annotation databases

    EnsembliENST00000272746; ENSP00000272746; ENSG00000115935. [O43516-3]
    ENST00000359761; ENSP00000352802; ENSG00000115935. [O43516-1]
    ENST00000392546; ENSP00000376329; ENSG00000115935. [O43516-1]
    ENST00000392547; ENSP00000376330; ENSG00000115935. [O43516-1]
    ENST00000409891; ENSP00000386431; ENSG00000115935. [O43516-2]
    GeneIDi7456.
    KEGGihsa:7456.
    UCSCiuc002uiz.3. human. [O43516-1]
    uc002ujb.2. human. [O43516-2]
    uc010fqt.1. human. [O43516-3]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF031588 mRNA. Translation: AAC03767.1 . Frameshift.
    X86019 mRNA. Translation: CAA60014.1 . Frameshift.
    BX640870 mRNA. Translation: CAE45928.1 .
    AC010894 Genomic DNA. Translation: AAY14708.1 .
    AC104595 Genomic DNA. No translation available.
    CH471058 Genomic DNA. Translation: EAX11131.1 .
    CH471058 Genomic DNA. Translation: EAX11132.1 .
    CH471058 Genomic DNA. Translation: EAX11133.1 .
    BC002914 mRNA. Translation: AAH02914.1 .
    AF106062 mRNA. Translation: AAD45972.1 .
    CCDSi CCDS2260.1. [O43516-1 ]
    RefSeqi NP_001070737.1. NM_001077269.1. [O43516-1 ]
    NP_003378.3. NM_003387.4. [O43516-1 ]
    XP_006712790.1. XM_006712727.1. [O43516-1 ]
    UniGenei Hs.128067.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2A41 X-ray 2.60 C 29-60 [» ]
    ProteinModelPortali O43516.
    SMRi O43516. Positions 29-60, 461-488.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113295. 21 interactions.
    DIPi DIP-17015N.
    IntActi O43516. 18 interactions.
    MINTi MINT-238480.
    STRINGi 9606.ENSP00000352802.

    PTM databases

    PhosphoSitei O43516.

    Proteomic databases

    MaxQBi O43516.
    PaxDbi O43516.
    PRIDEi O43516.

    Protocols and materials databases

    DNASUi 7456.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000272746 ; ENSP00000272746 ; ENSG00000115935 . [O43516-3 ]
    ENST00000359761 ; ENSP00000352802 ; ENSG00000115935 . [O43516-1 ]
    ENST00000392546 ; ENSP00000376329 ; ENSG00000115935 . [O43516-1 ]
    ENST00000392547 ; ENSP00000376330 ; ENSG00000115935 . [O43516-1 ]
    ENST00000409891 ; ENSP00000386431 ; ENSG00000115935 . [O43516-2 ]
    GeneIDi 7456.
    KEGGi hsa:7456.
    UCSCi uc002uiz.3. human. [O43516-1 ]
    uc002ujb.2. human. [O43516-2 ]
    uc010fqt.1. human. [O43516-3 ]

    Organism-specific databases

    CTDi 7456.
    GeneCardsi GC02M175424.
    H-InvDB HIX0034792.
    HGNCi HGNC:12736. WIPF1.
    HPAi CAB009737.
    HPA003739.
    MIMi 602357. gene.
    614493. phenotype.
    neXtProti NX_O43516.
    Orphaneti 906. Wiskott-Aldrich syndrome.
    PharmGKBi PA162409189.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG149184.
    HOVERGENi HBG054157.
    InParanoidi O43516.
    OMAi QSSLHNR.
    OrthoDBi EOG7PS1GQ.
    PhylomeDBi O43516.
    TreeFami TF332135.

    Enzyme and pathway databases

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

    Miscellaneous databases

    EvolutionaryTracei O43516.
    GeneWikii WIPF1.
    GenomeRNAii 7456.
    NextBioi 29198.
    PROi O43516.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43516.
    Bgeei O43516.
    CleanExi HS_WIPF1.
    Genevestigatori O43516.

    Family and domain databases

    InterProi IPR003124. WH2_dom.
    IPR028295. WIP.
    [Graphical view ]
    PANTHERi PTHR23202:SF30. PTHR23202:SF30. 1 hit.
    Pfami PF02205. WH2. 1 hit.
    [Graphical view ]
    SMARTi SM00246. WH2. 1 hit.
    [Graphical view ]
    PROSITEi PS51082. WH2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "WIP, a protein associated with Wiskott-Aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cells."
      Ramesh N., Anton I.M., Hartwig J.H., Geha R.S.
      Proc. Natl. Acad. Sci. U.S.A. 94:14671-14676(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS LEU-198 AND GLY-495, FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH WASP; PROFILIN AND ACTIN.
    2. Kreideweiss S., Delany-Heiken P., Nordheim A., Ruhlmann A.
      Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS LEU-198 AND GLY-495.
      Tissue: Tonsil.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT LEU-198.
      Tissue: Endometrial tumor.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LEU-198.
    6. "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 4), VARIANT LEU-198.
      Tissue: Skin.
    7. "Mutations that cause the Wiskott-Aldrich syndrome impair the interaction of Wiskott-Aldrich syndrome protein (WASP) with WASP interacting protein."
      Stewart D.M., Tian L., Nelson D.L.
      J. Immunol. 162:5019-5024(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 192-503 (ISOFORM 1), INTERACTION WITH WASP, VARIANT LEU-198.
    8. "A complex of N-WASP and WIP integrates signalling cascades that lead to actin polymerization."
      Moreau V., Frischknecht F., Reckmann I., Vincentelli R., Rabut G., Stewart D.M., Way M.
      Nat. Cell Biol. 2:441-448(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-345 AND SER-350, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "Actin-binding protein-1 interacts with WASp-interacting protein to regulate growth factor-induced dorsal ruffle formation."
      Cortesio C.L., Perrin B.J., Bennin D.A., Huttenlocher A.
      Mol. Biol. Cell 21:186-197(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DBNL.
    13. "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 SER-340; THR-345 AND SER-350, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: INVOLVEMENT IN WAS2.
    16. "Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly."
      Chereau D., Kerff F., Graceffa P., Grabarek Z., Langsetmo K., Dominguez R.
      Proc. Natl. Acad. Sci. U.S.A. 102:16644-16649(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 29-60 IN COMPLEX WITH ACTIN.

    Entry informationi

    Entry nameiWIPF1_HUMAN
    AccessioniPrimary (citable) accession number: O43516
    Secondary accession number(s): B8ZZM1
    , D3DPE4, Q15220, Q53TA9, Q6MZU9, Q9BU37, Q9UNP1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: November 30, 2010
    Last modified: October 1, 2014
    This is version 135 of the entry and version 3 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

    Miscellaneous

    Recruited to PIP5K-induced vesicle surfaces in the absence of functional WASL.By similarity

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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