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Q9Y6W5

- WASF2_HUMAN

UniProt

Q9Y6W5 - WASF2_HUMAN

Protein

Wiskott-Aldrich syndrome protein family member 2

Gene

WASF2

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 3 (01 Feb 2005)
      Previous versions | rss
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    Functioni

    Downstream effector molecule involved in the transmission of signals from tyrosine kinase receptors and small GTPases to the actin cytoskeleton. Promotes formation of actin filaments. Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex.2 Publications

    GO - Molecular functioni

    1. actin binding Source: ProtInc
    2. protein binding Source: UniProtKB
    3. protein complex binding Source: UniProt

    GO - Biological processi

    1. actin cytoskeleton organization Source: ProtInc
    2. actin filament-based movement Source: Ensembl
    3. adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: ProtInc
    4. ameboidal cell migration Source: Ensembl
    5. angiogenesis Source: Ensembl
    6. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    7. innate immune response Source: Reactome
    8. lamellipodium assembly Source: Ensembl
    9. lamellipodium morphogenesis Source: Ensembl
    10. megakaryocyte development Source: Ensembl
    11. negative regulation of stress fiber assembly Source: UniProt
    12. positive regulation of lamellipodium assembly Source: UniProt
    13. Rac protein signal transduction Source: Ensembl

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    SignaLinkiQ9Y6W5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Wiskott-Aldrich syndrome protein family member 2
    Short name:
    WASP family protein member 2
    Alternative name(s):
    Protein WAVE-2
    Verprolin homology domain-containing protein 2
    Gene namesi
    Name:WASF2
    Synonyms:WAVE2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:12733. WASF2.

    Subcellular locationi

    Cytoplasmcytoskeleton By similarity. Cell projectionlamellipodium By similarity
    Note: At the interface between the lamellipodial actin meshwork and the membrane.By similarity

    GO - Cellular componenti

    1. actin cytoskeleton Source: ProtInc
    2. cytosol Source: Reactome
    3. early endosome Source: Ensembl
    4. extracellular vesicular exosome Source: UniProt
    5. intracellular Source: MGI
    6. lamellipodium Source: MGI
    7. ruffle Source: Ensembl
    8. SCAR complex Source: UniProt

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi40 – 401L → D: Decreased interaction with WAVE complex; when associated with D-51. 1 Publication
    Mutagenesisi50 – 501I → D: Decreased interaction with WAVE complex; when associated with D-54. 1 Publication
    Mutagenesisi51 – 511F → D: Decreased interaction with WAVE complex; when associated with D-40. 1 Publication
    Mutagenesisi54 – 541L → D: Decreased interaction with WAVE complex; when associated with D-50. 1 Publication
    Mutagenesisi124 – 1241Y → D: Constitutive induction of the formation of actin filaments. Strongly enhances formation of lamellipodia. 1 Publication
    Mutagenesisi150 – 1501Y → D: Constitutive induction of the formation of actin filaments. Strongly enhances formation of lamellipodia. 1 Publication
    Mutagenesisi160 – 1612WK → ED: Constitutive induction of the formation of actin filaments. Strongly enhances formation of lamellipodia.

    Organism-specific databases

    PharmGKBiPA37344.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 498498Wiskott-Aldrich syndrome protein family member 2PRO_0000188994Add
    BLAST

    Proteomic databases

    MaxQBiQ9Y6W5.
    PaxDbiQ9Y6W5.
    PeptideAtlasiQ9Y6W5.
    PRIDEiQ9Y6W5.

    PTM databases

    PhosphoSiteiQ9Y6W5.

    Miscellaneous databases

    PMAP-CutDBQ9Y6W5.

    Expressioni

    Tissue specificityi

    Expressed in all tissues with strongest expression in placenta, lung, and peripheral blood leukocytes, but not in skeletal muscle.1 Publication

    Gene expression databases

    ArrayExpressiQ9Y6W5.
    BgeeiQ9Y6W5.
    CleanExiHS_WASF2.
    GenevestigatoriQ9Y6W5.

    Organism-specific databases

    HPAiCAB022632.
    HPA045288.

    Interactioni

    Subunit structurei

    Binds actin and the Arp2/3 complex. Interacts with BAIAP2. Component of the WAVE2 complex composed of ABI1, CYFIP1/SRA1, NCKAP1/NAP1 and WASF2/WAVE2. Directly interacts with BRK1.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BAIAP2Q9UQB8-45EBI-4290615,EBI-6174091
    SORBS3O60504-23EBI-4290615,EBI-1222956
    ZDHHC17Q8IUH52EBI-4290615,EBI-524753

    Protein-protein interaction databases

    BioGridi115465. 13 interactions.
    DIPiDIP-41817N.
    IntActiQ9Y6W5. 8 interactions.
    MINTiMINT-5005787.
    STRINGi9606.ENSP00000396211.

    Structurei

    Secondary structure

    1
    498
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi436 – 44611

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2A40X-ray1.80C/F433-464[»]
    ProteinModelPortaliQ9Y6W5.
    SMRiQ9Y6W5. Positions 21-197, 435-482.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y6W5.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini436 – 45318WH2PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi268 – 2714Poly-Pro
    Compositional biasi318 – 32811Poly-ProAdd
    BLAST
    Compositional biasi333 – 3386Poly-Pro
    Compositional biasi347 – 3504Poly-Pro
    Compositional biasi364 – 3718Poly-Pro
    Compositional biasi379 – 3824Poly-Pro
    Compositional biasi391 – 40616Poly-ProAdd
    BLAST

    Domaini

    Binds and activates the Arp2/3 complex via the C-terminal domain. Interacts with actin via the WH2 domain.2 Publications

    Sequence similaritiesi

    Belongs to the SCAR/WAVE family.Curated
    Contains 1 WH2 domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG299696.
    HOGENOMiHOG000021456.
    HOVERGENiHBG058482.
    InParanoidiQ9Y6W5.
    KOiK05748.
    OMAiDTSELEC.
    OrthoDBiEOG7VHSXK.
    PhylomeDBiQ9Y6W5.
    TreeFamiTF315031.

    Family and domain databases

    InterProiIPR028288. SCAR/WAVE_fam.
    IPR003124. WH2_dom.
    [Graphical view]
    PANTHERiPTHR12902. PTHR12902. 1 hit.
    PfamiPF02205. WH2. 1 hit.
    [Graphical view]
    SMARTiSM00246. WH2. 1 hit.
    [Graphical view]
    PROSITEiPS51082. WH2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y6W5-1) [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

    MPLVTRNIEP RHLCRQTLPS VRSELECVTN ITLANVIRQL GSLSKYAEDI    50
    FGELFTQANT FASRVSSLAE RVDRLQVKVT QLDPKEEEVS LQGINTRKAF 100
    RSSTIQDQKL FDRNSLPVPV LETYNTCDTP PPLNNLTPYR DDGKEALKFY 150
    TDPSYFFDLW KEKMLQDTKD IMKEKRKHRK EKKDNPNRGN VNPRKIKTRK 200
    EEWEKMKMGQ EFVESKEKLG TSGYPPTLVY QNGSIGCVEN VDASSYPPPP 250
    QSDSASSPSP SFSEDNLPPP PAEFSYPVDN QRGSGLAGPK RSSVVSPSHP 300
    PPAPPLGSPP GPKPGFAPPP APPPPPPPMI GIPPPPPPVG FGSPGTPPPP 350
    SPPSFPPHPD FAAPPPPPPP PAADYPTLPP PPLSQPTGGA PPPPPPPPPP 400
    GPPPPPFTGA DGQPAIPPPL SDTTKPKSSL PAVSDARSDL LSAIRQGFQL 450
    RRVEEQREQE KRDVVGNDVA TILSRRIAVE YSDSEDDSSE FDEDDWSD 498
    Length:498
    Mass (Da):54,284
    Last modified:February 1, 2005 - v3
    Checksum:iC737CE963016DE94
    GO
    Isoform 2 (identifier: Q9Y6W5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         275-281: SYPVDNQ → RFSAAQG
         282-498: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:281
    Mass (Da):31,979
    Checksum:iC5E79110854FAF56
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei275 – 2817SYPVDNQ → RFSAAQG in isoform 2. 1 PublicationVSP_042514
    Alternative sequencei282 – 498217Missing in isoform 2. 1 PublicationVSP_042515Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB026542 mRNA. Translation: BAA81795.1.
    AK303011 mRNA. Translation: BAG64142.1.
    AL096774 Genomic DNA. Translation: CAC18518.1.
    AL663122 Genomic DNA. No translation available.
    BX293535 Genomic DNA. No translation available.
    BC040943 mRNA. Translation: AAH40943.1.
    CCDSiCCDS304.1. [Q9Y6W5-1]
    CCDS55582.1. [Q9Y6W5-2]
    RefSeqiNP_001188333.1. NM_001201404.1. [Q9Y6W5-2]
    NP_008921.1. NM_006990.3. [Q9Y6W5-1]
    UniGeneiHs.469244.

    Genome annotation databases

    EnsembliENST00000536657; ENSP00000439883; ENSG00000158195. [Q9Y6W5-2]
    GeneIDi10163.
    KEGGihsa:10163.
    UCSCiuc001bof.2. human. [Q9Y6W5-1]
    uc010ofl.2. human. [Q9Y6W5-2]

    Polymorphism databases

    DMDMi59800456.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB026542 mRNA. Translation: BAA81795.1 .
    AK303011 mRNA. Translation: BAG64142.1 .
    AL096774 Genomic DNA. Translation: CAC18518.1 .
    AL663122 Genomic DNA. No translation available.
    BX293535 Genomic DNA. No translation available.
    BC040943 mRNA. Translation: AAH40943.1 .
    CCDSi CCDS304.1. [Q9Y6W5-1 ]
    CCDS55582.1. [Q9Y6W5-2 ]
    RefSeqi NP_001188333.1. NM_001201404.1. [Q9Y6W5-2 ]
    NP_008921.1. NM_006990.3. [Q9Y6W5-1 ]
    UniGenei Hs.469244.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2A40 X-ray 1.80 C/F 433-464 [» ]
    ProteinModelPortali Q9Y6W5.
    SMRi Q9Y6W5. Positions 21-197, 435-482.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115465. 13 interactions.
    DIPi DIP-41817N.
    IntActi Q9Y6W5. 8 interactions.
    MINTi MINT-5005787.
    STRINGi 9606.ENSP00000396211.

    PTM databases

    PhosphoSitei Q9Y6W5.

    Polymorphism databases

    DMDMi 59800456.

    Proteomic databases

    MaxQBi Q9Y6W5.
    PaxDbi Q9Y6W5.
    PeptideAtlasi Q9Y6W5.
    PRIDEi Q9Y6W5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000536657 ; ENSP00000439883 ; ENSG00000158195 . [Q9Y6W5-2 ]
    GeneIDi 10163.
    KEGGi hsa:10163.
    UCSCi uc001bof.2. human. [Q9Y6W5-1 ]
    uc010ofl.2. human. [Q9Y6W5-2 ]

    Organism-specific databases

    CTDi 10163.
    GeneCardsi GC01M027730.
    HGNCi HGNC:12733. WASF2.
    HPAi CAB022632.
    HPA045288.
    MIMi 605875. gene.
    neXtProti NX_Q9Y6W5.
    PharmGKBi PA37344.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG299696.
    HOGENOMi HOG000021456.
    HOVERGENi HBG058482.
    InParanoidi Q9Y6W5.
    KOi K05748.
    OMAi DTSELEC.
    OrthoDBi EOG7VHSXK.
    PhylomeDBi Q9Y6W5.
    TreeFami TF315031.

    Enzyme and pathway databases

    Reactomei REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    SignaLinki Q9Y6W5.

    Miscellaneous databases

    ChiTaRSi WASF2. human.
    EvolutionaryTracei Q9Y6W5.
    GeneWikii WASF2.
    GenomeRNAii 10163.
    NextBioi 38478.
    PMAP-CutDB Q9Y6W5.
    PROi Q9Y6W5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y6W5.
    Bgeei Q9Y6W5.
    CleanExi HS_WASF2.
    Genevestigatori Q9Y6W5.

    Family and domain databases

    InterProi IPR028288. SCAR/WAVE_fam.
    IPR003124. WH2_dom.
    [Graphical view ]
    PANTHERi PTHR12902. PTHR12902. 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. "Identification of two human WAVE/SCAR homologues as general actin regulatory molecules which associate with the Arp2/3 complex."
      Suetsugu S., Miki H., Takenawa T.
      Biochem. Biophys. Res. Commun. 260:296-302(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH ACTIN AND THE ARP2/3 COMPLEX, SUBUNIT, DOMAIN, TISSUE SPECIFICITY.
      Tissue: T-cell lymphoma.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Testis.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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 1).
      Tissue: Lymph.
    5. "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: INTERACTION WITH BAIAP2.
    6. Cited for: INTERACTION WITH C3ORF10.
    7. Cited for: MUTAGENESIS OF LEU-40; ILE-50; PHE-51 AND LEU-54, SUBUNIT.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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 (1.8 ANGSTROMS) OF 433-464 IN COMPLEX WITH ACTIN, FUNCTION, DOMAIN, MUTAGENESIS OF TYR-124; TYR-150 AND 160-TRP-LYS-161, SUBUNIT.

    Entry informationi

    Entry nameiWASF2_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y6W5
    Secondary accession number(s): B4DZN0, O60794, Q9UDY7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: February 1, 2005
    Last modified: October 1, 2014
    This is version 131 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3