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Q92558

- WASF1_HUMAN

UniProt

Q92558 - WASF1_HUMAN

Protein

Wiskott-Aldrich syndrome protein family member 1

Gene

WASF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      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.

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. protein complex binding Source: UniProt

    GO - Biological processi

    1. actin filament polymerization Source: ProtInc
    2. cellular component movement Source: ProtInc
    3. lamellipodium morphogenesis Source: Ensembl
    4. positive regulation of Arp2/3 complex-mediated actin nucleation Source: UniProt
    5. protein complex assembly Source: ProtInc
    6. Rac protein signal transduction Source: UniProt

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Wiskott-Aldrich syndrome protein family member 1
    Short name:
    WASP family protein member 1
    Alternative name(s):
    Protein WAVE-1
    Verprolin homology domain-containing protein 1
    Gene namesi
    Name:WASF1
    Synonyms:KIAA0269, SCAR1, WAVE1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:12732. WASF1.

    Subcellular locationi

    Cytoplasmcytoskeleton. Cell junctionsynapse By similarity
    Note: Dot-like pattern in the cytoplasm. Concentrated in Rac-regulated membrane-ruffling areas.

    GO - Cellular componenti

    1. actin cytoskeleton Source: ProtInc
    2. cell junction Source: UniProtKB-KW
    3. cytoskeleton Source: ProtInc
    4. lamellipodium Source: Ensembl
    5. mitochondrial outer membrane Source: Ensembl
    6. SCAR complex Source: UniProt
    7. synapse Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cytoplasm, Cytoskeleton, Synapse

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37343.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 559559Wiskott-Aldrich syndrome protein family member 1PRO_0000188992Add
    BLAST

    Proteomic databases

    MaxQBiQ92558.
    PaxDbiQ92558.
    PRIDEiQ92558.

    PTM databases

    PhosphoSiteiQ92558.

    Miscellaneous databases

    PMAP-CutDBQ92558.

    Expressioni

    Tissue specificityi

    Highly expressed in brain. Lowly expressed in testis, ovary, colon, kidney, pancreas, thymus, small intestine and peripheral blood.

    Gene expression databases

    ArrayExpressiQ92558.
    BgeeiQ92558.
    CleanExiHS_WASF1.
    GenevestigatoriQ92558.

    Organism-specific databases

    HPAiCAB022161.
    HPA004105.

    Interactioni

    Subunit structurei

    Component of the WAVE1 complex composed of ABI2, CYFIP1 or CYFIP2, BRK1, NCKAP1 and WASF1/WAVE1. Within the complex, a heterdimer containing NCKAP1 and CYFIP1 interacts with a heterotrimer formed by WAVE1, ABI2 and BRK1. CYFIP2 binds to activated RAC1 which causes the complex to dissociate, releasing activated WASF1. The complex can also be activated by NCK1. Binds actin and the Arp2/3 complex. Interacts with BAIAP2. Interacts with SHANK3; the interaction mediates the association of SHANK3 with the WAVE1 complex. Interacts with ABI1 (via N-terminus).2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PFN1P077372EBI-1548747,EBI-713780

    Protein-protein interaction databases

    BioGridi114449. 14 interactions.
    DIPiDIP-39391N.
    IntActiQ92558. 19 interactions.
    MINTiMINT-144109.
    STRINGi9606.ENSP00000352425.

    Structurei

    Secondary structure

    1
    559
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi26 – 8156
    Turni85 – 873
    Helixi93 – 964
    Helixi114 – 1163
    Helixi119 – 1279
    Helixi134 – 1407
    Helixi147 – 1504
    Helixi156 – 18126
    Helixi500 – 51314
    Helixi531 – 54010
    Turni541 – 5433

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3P8CX-ray2.29D1-186[»]
    D485-559[»]
    4N78X-ray2.43D1-559[»]
    ProteinModelPortaliQ92558.
    SMRiQ92558. Positions 21-227, 496-544.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ92558.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini497 – 51418WH2PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi278 – 2836Poly-Pro
    Compositional biasi322 – 33211Poly-ProAdd
    BLAST
    Compositional biasi348 – 35912Poly-ProAdd
    BLAST
    Compositional biasi369 – 3746Poly-Pro
    Compositional biasi424 – 43512Poly-ProAdd
    BLAST

    Domaini

    Binds the Arp2/3 complex through the C-terminal region and actin through verprolin homology (VPH) domain.

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG299696.
    HOGENOMiHOG000021456.
    HOVERGENiHBG058482.
    InParanoidiQ92558.
    KOiK05753.
    OMAiYMEHLDG.
    OrthoDBiEOG7VHSXK.
    PhylomeDBiQ92558.
    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]

    Sequencei

    Sequence statusi: Complete.

    Q92558-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPLVKRNIDP RHLCHTALPR GIKNELECVT NISLANIIRQ LSSLSKYAED    50
    IFGELFNEAH SFSFRVNSLQ ERVDRLSVSV TQLDPKEEEL SLQDITMRKA 100
    FRSSTIQDQQ LFDRKTLPIP LQETYDVCEQ PPPLNILTPY RDDGKEGLKF 150
    YTNPSYFFDL WKEKMLQDTE DKRKEKRKQK QKNLDRPHEP EKVPRAPHDR 200
    RREWQKLAQG PELAEDDANL LHKHIEVANG PASHFETRPQ TYVDHMDGSY 250
    SLSALPFSQM SELLTRAEER VLVRPHEPPP PPPMHGAGDA KPIPTCISSA 300
    TGLIENRPQS PATGRTPVFV SPTPPPPPPP LPSALSTSSL RASMTSTPPP 350
    PVPPPPPPPA TALQAPAVPP PPAPLQIAPG VLHPAPPPIA PPLVQPSPPV 400
    ARAAPVCETV PVHPLPQGEV QGLPPPPPPP PLPPPGIRPS SPVTVTALAH 450
    PPSGLHPTPS TAPGPHVPLM PPSPPSQVIP ASEPKRHPST LPVISDARSV 500
    LLEAIRKGIQ LRKVEEQREQ EAKHERIEND VATILSRRIA VEYSDSEDDS 550
    EFDEVDWLE 559
    Length:559
    Mass (Da):61,652
    Last modified:February 1, 1997 - v1
    Checksum:i44B4527BDB77BC6E
    GO

    Sequence cautioni

    The sequence BAA13399.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF134303 mRNA. Translation: AAD33052.1.
    D87459 mRNA. Translation: BAA13399.2. Different initiation.
    AL590009 Genomic DNA. Translation: CAI12485.1.
    CH471051 Genomic DNA. Translation: EAW48325.1.
    CH471051 Genomic DNA. Translation: EAW48326.1.
    CH471051 Genomic DNA. Translation: EAW48327.1.
    CH471051 Genomic DNA. Translation: EAW48328.1.
    CH471051 Genomic DNA. Translation: EAW48329.1.
    BC044591 mRNA. Translation: AAH44591.1.
    CCDSiCCDS5080.1.
    RefSeqiNP_001020105.1. NM_001024934.1.
    NP_001020106.1. NM_001024935.1.
    NP_001020107.1. NM_001024936.1.
    NP_003922.1. NM_003931.2.
    XP_005267260.1. XM_005267203.2.
    XP_005267261.1. XM_005267204.1.
    XP_005267262.1. XM_005267205.1.
    XP_005267263.1. XM_005267206.1.
    XP_005267264.1. XM_005267207.1.
    XP_006715658.1. XM_006715595.1.
    UniGeneiHs.75850.

    Genome annotation databases

    EnsembliENST00000359451; ENSP00000352425; ENSG00000112290.
    ENST00000392586; ENSP00000376365; ENSG00000112290.
    ENST00000392587; ENSP00000376366; ENSG00000112290.
    ENST00000392588; ENSP00000376367; ENSG00000112290.
    ENST00000392589; ENSP00000376368; ENSG00000112290.
    GeneIDi8936.
    KEGGihsa:8936.
    UCSCiuc003ptv.1. human.

    Polymorphism databases

    DMDMi2495730.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF134303 mRNA. Translation: AAD33052.1 .
    D87459 mRNA. Translation: BAA13399.2 . Different initiation.
    AL590009 Genomic DNA. Translation: CAI12485.1 .
    CH471051 Genomic DNA. Translation: EAW48325.1 .
    CH471051 Genomic DNA. Translation: EAW48326.1 .
    CH471051 Genomic DNA. Translation: EAW48327.1 .
    CH471051 Genomic DNA. Translation: EAW48328.1 .
    CH471051 Genomic DNA. Translation: EAW48329.1 .
    BC044591 mRNA. Translation: AAH44591.1 .
    CCDSi CCDS5080.1.
    RefSeqi NP_001020105.1. NM_001024934.1.
    NP_001020106.1. NM_001024935.1.
    NP_001020107.1. NM_001024936.1.
    NP_003922.1. NM_003931.2.
    XP_005267260.1. XM_005267203.2.
    XP_005267261.1. XM_005267204.1.
    XP_005267262.1. XM_005267205.1.
    XP_005267263.1. XM_005267206.1.
    XP_005267264.1. XM_005267207.1.
    XP_006715658.1. XM_006715595.1.
    UniGenei Hs.75850.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3P8C X-ray 2.29 D 1-186 [» ]
    D 485-559 [» ]
    4N78 X-ray 2.43 D 1-559 [» ]
    ProteinModelPortali Q92558.
    SMRi Q92558. Positions 21-227, 496-544.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114449. 14 interactions.
    DIPi DIP-39391N.
    IntActi Q92558. 19 interactions.
    MINTi MINT-144109.
    STRINGi 9606.ENSP00000352425.

    PTM databases

    PhosphoSitei Q92558.

    Polymorphism databases

    DMDMi 2495730.

    Proteomic databases

    MaxQBi Q92558.
    PaxDbi Q92558.
    PRIDEi Q92558.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000359451 ; ENSP00000352425 ; ENSG00000112290 .
    ENST00000392586 ; ENSP00000376365 ; ENSG00000112290 .
    ENST00000392587 ; ENSP00000376366 ; ENSG00000112290 .
    ENST00000392588 ; ENSP00000376367 ; ENSG00000112290 .
    ENST00000392589 ; ENSP00000376368 ; ENSG00000112290 .
    GeneIDi 8936.
    KEGGi hsa:8936.
    UCSCi uc003ptv.1. human.

    Organism-specific databases

    CTDi 8936.
    GeneCardsi GC06M110421.
    HGNCi HGNC:12732. WASF1.
    HPAi CAB022161.
    HPA004105.
    MIMi 605035. gene.
    neXtProti NX_Q92558.
    PharmGKBi PA37343.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG299696.
    HOGENOMi HOG000021456.
    HOVERGENi HBG058482.
    InParanoidi Q92558.
    KOi K05753.
    OMAi YMEHLDG.
    OrthoDBi EOG7VHSXK.
    PhylomeDBi Q92558.
    TreeFami TF315031.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi WASF1. human.
    EvolutionaryTracei Q92558.
    GeneWikii WASF1.
    GenomeRNAii 8936.
    NextBioi 33600.
    PMAP-CutDB Q92558.
    PROi Q92558.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92558.
    Bgeei Q92558.
    CleanExi HS_WASF1.
    Genevestigatori Q92558.

    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. "SCAR, a WASP-related protein, isolated as a suppressor of receptor defects in late Dictyostelium development."
      Bear J.E., Rawls J.F., Saxe C.L. III
      J. Cell Biol. 142:1325-1335(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
      Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
      DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Bone marrow.
    3. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Tissue: Testis.
    6. "Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex."
      Machesky L.M., Insall R.H.
      Curr. Biol. 8:1347-1356(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    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: INTERACTION WITH BAIAP2.
    8. Cited for: X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF WAVE1 COMPLEX, SUBUNIT.

    Entry informationi

    Entry nameiWASF1_HUMAN
    AccessioniPrimary (citable) accession number: Q92558
    Secondary accession number(s): E1P5F2, Q5SZK7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 117 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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