Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O00401

- WASL_HUMAN

UniProt

O00401 - WASL_HUMAN

Protein

Neural Wiskott-Aldrich syndrome protein

Gene

WASL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 2 (01 Feb 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Regulates actin polymerization by stimulating the actin-nucleating activity of the Arp2/3 complex. Involved in mitosis and cytokinesis, via its role in the regulation of actin polymerization. Binds to HSF1/HSTF1 and forms a complex on heat shock promoter elements (HSE) that negatively regulates HSP90 expression.4 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. small GTPase regulator activity Source: ProtInc

    GO - Biological processi

    1. actin polymerization or depolymerization Source: ProtInc
    2. axon guidance Source: Reactome
    3. cellular component movement Source: ProtInc
    4. cellular protein complex localization Source: Ensembl
    5. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    6. innate immune response Source: Reactome
    7. membrane budding Source: BHF-UCL
    8. mitotic nuclear division Source: UniProtKB-KW
    9. nitric oxide metabolic process Source: Reactome
    10. positive regulation of clathrin-mediated endocytosis Source: BHF-UCL
    11. positive regulation of filopodium assembly Source: BHF-UCL
    12. protein complex assembly Source: ProtInc
    13. regulation of nitric-oxide synthase activity Source: Reactome
    14. regulation of protein localization Source: Ensembl
    15. regulation of transcription, DNA-templated Source: UniProtKB-KW
    16. response to bacterium Source: Ensembl
    17. small molecule metabolic process Source: Reactome
    18. spindle localization Source: Ensembl
    19. transcription, DNA-templated Source: UniProtKB-KW
    20. vesicle organization Source: BHF-UCL
    21. vesicle transport along actin filament Source: BHF-UCL

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis, Transcription, Transcription regulation

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    ReactomeiREACT_12541. NOSTRIN mediated eNOS trafficking.
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_22351. DCC mediated attractive signaling.
    REACT_23832. Nephrin interactions.
    SignaLinkiO00401.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neural Wiskott-Aldrich syndrome protein
    Short name:
    N-WASP
    Gene namesi
    Name:WASL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:12735. WASL.

    Subcellular locationi

    Cytoplasmcytoskeleton By similarity. Nucleus By similarity
    Note: Preferentially localized in the cytoplasm when phosphorylated and in the nucleus when unphosphorylated.By similarity

    GO - Cellular componenti

    1. actin cap Source: Ensembl
    2. actin cytoskeleton Source: ProtInc
    3. cytoplasmic membrane-bounded vesicle Source: BHF-UCL
    4. cytosol Source: Reactome
    5. endocytic vesicle membrane Source: Reactome
    6. extracellular vesicular exosome Source: UniProt
    7. lamellipodium Source: Ensembl
    8. nucleus Source: UniProtKB-SubCell
    9. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37346.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 505504Neural Wiskott-Aldrich syndrome proteinPRO_0000189000Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine3 Publications
    Modified residuei242 – 2421Phosphoserine; by TNK21 Publication
    Modified residuei256 – 2561Phosphotyrosine; by FAK1 and TNK22 Publications
    Modified residuei484 – 4841Phosphoserine2 Publications
    Modified residuei485 – 4851Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylation at Ser-242, Tyr-256, Ser-484 and Ser-485 enhances actin polymerization activity.3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO00401.
    PaxDbiO00401.
    PRIDEiO00401.

    PTM databases

    PhosphoSiteiO00401.

    Expressioni

    Gene expression databases

    BgeeiO00401.
    CleanExiHS_WASL.
    GenevestigatoriO00401.

    Organism-specific databases

    HPAiCAB005399.
    HPA005750.

    Interactioni

    Subunit structurei

    Binds actin and the Arp2/3 complex. Interacts with CDC42. Binds to SH3 domains of GRB2. Interacts with the C-terminal SH3 domain of DNMBP. Interacts with SNX9. Interacts with the WW domains of PRPF40A/FBP11. Interacts with PTK2/FAK1. Interacts with PACSIN1, PACSIN2 and PACSIN3 By similarity. Interacts with NOSTRIN. Interacts with Shigella flexneri protein IcsA. The interaction with IcsA enhances the affinity of WASL for Arp2/3, thus assembling a tight complex which has maximal activity in actin assembly. Interacts with E.coli effector protein EspF(U). Identified in a complex containing at least WASL, BAIAP2L1 and E.coli EspF(U). Binds to TNK2. Interacts with SNX33.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ACTR3P611573EBI-957615,EBI-351419From a different organism.
    CDC42P609533EBI-957615,EBI-81752
    CIB1Q998287EBI-957615,EBI-372594
    Fnbp1Q8R5112EBI-957615,EBI-1111424From a different organism.
    GRB2P629933EBI-957615,EBI-401755
    SNX9Q9Y5X12EBI-957615,EBI-77848
    SORBS3O60504-23EBI-957615,EBI-1222956
    WIPF1O435164EBI-957615,EBI-346356

    Protein-protein interaction databases

    BioGridi114466. 47 interactions.
    DIPiDIP-29042N.
    IntActiO00401. 35 interactions.
    MINTiMINT-157215.
    STRINGi9606.ENSP00000223023.

    Structurei

    Secondary structure

    1
    505
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni219 – 2213
    Helixi225 – 2273
    Helixi232 – 2398
    Helixi243 – 2464
    Turni249 – 2513
    Helixi252 – 26211
    Helixi265 – 2695
    Helixi435 – 4439

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FF3X-ray2.00C451-465[»]
    2LNHNMR-A207-270[»]
    2VCPX-ray3.20D/E392-484[»]
    4CC2X-ray1.55B/D346-357[»]
    4CC7X-ray1.97B/D/F/H/J/L/N346-357[»]
    ProteinModelPortaliO00401.
    SMRiO00401. Positions 29-150, 207-270, 403-450, 466-491.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO00401.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini34 – 141108WH1PROSITE-ProRule annotationAdd
    BLAST
    Domaini203 – 21614CRIBPROSITE-ProRule annotationAdd
    BLAST
    Domaini405 – 42218WH2 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini433 – 45018WH2 2PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi277 – 392116Pro-richAdd
    BLAST
    Compositional biasi485 – 50521Asp-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 CRIB domain.PROSITE-ProRule annotation
    Contains 1 WH1 domain.PROSITE-ProRule annotation
    Contains 2 WH2 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG270974.
    HOGENOMiHOG000143378.
    HOVERGENiHBG000222.
    InParanoidiO00401.
    KOiK05747.
    OMAiPTPAGNK.
    OrthoDBiEOG7FJH20.
    PhylomeDBiO00401.
    TreeFamiTF316736.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    3.90.810.10. 1 hit.
    InterProiIPR000095. CRIB_dom.
    IPR011993. PH_like_dom.
    IPR011026. WASP_C.
    IPR000697. WH1/EVH1.
    IPR003124. WH2_dom.
    [Graphical view]
    PfamiPF00786. PBD. 1 hit.
    PF00568. WH1. 1 hit.
    PF02205. WH2. 2 hits.
    [Graphical view]
    SMARTiSM00285. PBD. 1 hit.
    SM00461. WH1. 1 hit.
    SM00246. WH2. 2 hits.
    [Graphical view]
    SUPFAMiSSF47912. SSF47912. 2 hits.
    PROSITEiPS50108. CRIB. 1 hit.
    PS50229. WH1. 1 hit.
    PS51082. WH2. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O00401-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSVQQQPPP PRRVTNVGSL LLTPQENESL FTFLGKKCVT MSSAVVQLYA    50
    ADRNCMWSKK CSGVACLVKD NPQRSYFLRI FDIKDGKLLW EQELYNNFVY 100
    NSPRGYFHTF AGDTCQVALN FANEEEAKKF RKAVTDLLGR RQRKSEKRRD 150
    PPNGPNLPMA TVDIKNPEIT TNRFYGPQVN NISHTKEKKK GKAKKKRLTK 200
    ADIGTPSNFQ HIGHVGWDPN TGFDLNNLDP ELKNLFDMCG ISEAQLKDRE 250
    TSKVIYDFIE KTGGVEAVKN ELRRQAPPPP PPSRGGPPPP PPPPHNSGPP 300
    PPPARGRGAP PPPPSRAPTA APPPPPPSRP SVAVPPPPPN RMYPPPPPAL 350
    PSSAPSGPPP PPPSVLGVGP VAPPPPPPPP PPPGPPPPPG LPSDGDHQVP 400
    TTAGNKAALL DQIREGAQLK KVEQNSRPVS CSGRDALLDQ IRQGIQLKSV 450
    ADGQESTPPT PAPTSGIVGA LMEVMQKRSK AIHSSDEDED EDDEEDFEDD 500
    DEWED 505
    Length:505
    Mass (Da):54,827
    Last modified:February 1, 2005 - v2
    Checksum:iB5895C6055E23049
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti76 – 761Y → H in BAA20128. (PubMed:9322739)Curated
    Sequence conflicti201 – 2011A → G in BAA20128. (PubMed:9322739)Curated
    Sequence conflicti223 – 2231F → S in BAA20128. (PubMed:9322739)Curated
    Sequence conflicti242 – 2421S → L in BAA20128. (PubMed:9322739)Curated
    Sequence conflicti248 – 2481D → E in BAA20128. (PubMed:9322739)Curated
    Sequence conflicti252 – 2521S → L in BAA20128. (PubMed:9322739)Curated
    Sequence conflicti296 – 2961N → S in BAA20128. (PubMed:9322739)Curated
    Sequence conflicti333 – 3331A → E in BAA20128. (PubMed:9322739)Curated
    Sequence conflicti351 – 3511P → L in CAL26602. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D88460 mRNA. Translation: BAA20128.1.
    AM295156 mRNA. Translation: CAL26602.1.
    AC006333 Genomic DNA. Translation: AAQ96857.1.
    BC052955 mRNA. Translation: AAH52955.1.
    CCDSiCCDS34743.1.
    RefSeqiNP_003932.3. NM_003941.3.
    UniGeneiHs.143728.
    Hs.731519.
    Hs.83916.

    Genome annotation databases

    EnsembliENST00000223023; ENSP00000223023; ENSG00000106299.
    GeneIDi8976.
    KEGGihsa:8976.
    UCSCiuc003vkz.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D88460 mRNA. Translation: BAA20128.1 .
    AM295156 mRNA. Translation: CAL26602.1 .
    AC006333 Genomic DNA. Translation: AAQ96857.1 .
    BC052955 mRNA. Translation: AAH52955.1 .
    CCDSi CCDS34743.1.
    RefSeqi NP_003932.3. NM_003941.3.
    UniGenei Hs.143728.
    Hs.731519.
    Hs.83916.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FF3 X-ray 2.00 C 451-465 [» ]
    2LNH NMR - A 207-270 [» ]
    2VCP X-ray 3.20 D/E 392-484 [» ]
    4CC2 X-ray 1.55 B/D 346-357 [» ]
    4CC7 X-ray 1.97 B/D/F/H/J/L/N 346-357 [» ]
    ProteinModelPortali O00401.
    SMRi O00401. Positions 29-150, 207-270, 403-450, 466-491.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114466. 47 interactions.
    DIPi DIP-29042N.
    IntActi O00401. 35 interactions.
    MINTi MINT-157215.
    STRINGi 9606.ENSP00000223023.

    PTM databases

    PhosphoSitei O00401.

    Proteomic databases

    MaxQBi O00401.
    PaxDbi O00401.
    PRIDEi O00401.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000223023 ; ENSP00000223023 ; ENSG00000106299 .
    GeneIDi 8976.
    KEGGi hsa:8976.
    UCSCi uc003vkz.3. human.

    Organism-specific databases

    CTDi 8976.
    GeneCardsi GC07M123321.
    HGNCi HGNC:12735. WASL.
    HPAi CAB005399.
    HPA005750.
    MIMi 605056. gene.
    neXtProti NX_O00401.
    PharmGKBi PA37346.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG270974.
    HOGENOMi HOG000143378.
    HOVERGENi HBG000222.
    InParanoidi O00401.
    KOi K05747.
    OMAi PTPAGNK.
    OrthoDBi EOG7FJH20.
    PhylomeDBi O00401.
    TreeFami TF316736.

    Enzyme and pathway databases

    Reactomei REACT_12541. NOSTRIN mediated eNOS trafficking.
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_22351. DCC mediated attractive signaling.
    REACT_23832. Nephrin interactions.
    SignaLinki O00401.

    Miscellaneous databases

    ChiTaRSi WASL. human.
    EvolutionaryTracei O00401.
    GeneWikii WASL_(gene).
    GenomeRNAii 8976.
    NextBioi 33689.
    PROi O00401.
    SOURCEi Search...

    Gene expression databases

    Bgeei O00401.
    CleanExi HS_WASL.
    Genevestigatori O00401.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    3.90.810.10. 1 hit.
    InterProi IPR000095. CRIB_dom.
    IPR011993. PH_like_dom.
    IPR011026. WASP_C.
    IPR000697. WH1/EVH1.
    IPR003124. WH2_dom.
    [Graphical view ]
    Pfami PF00786. PBD. 1 hit.
    PF00568. WH1. 1 hit.
    PF02205. WH2. 2 hits.
    [Graphical view ]
    SMARTi SM00285. PBD. 1 hit.
    SM00461. WH1. 1 hit.
    SM00246. WH2. 2 hits.
    [Graphical view ]
    SUPFAMi SSF47912. SSF47912. 2 hits.
    PROSITEi PS50108. CRIB. 1 hit.
    PS50229. WH1. 1 hit.
    PS51082. WH2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of N-WASP homologs in human and rat brain."
      Fukuoka M., Miki H., Takenawa T.
      Gene 196:43-48(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "Analysis of the anti-tumor T cell repertoire of melanoma patients vaccinated with a mixed tumor cell/DC vaccine."
      Lennerz V., Fatho M., Eberts D., Woelfel C., Schreiber S., Huber C., van der Bruggen P., Schmidt C.W., Woelfel T.
      Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Melanoma.
    3. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [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].
      Tissue: Brain.
    5. "Neural Wiskott-Aldrich syndrome protein is implicated in the actin-based motility of Shigella flexneri."
      Suzuki T., Miki H., Takenawa T., Sasakawa C.
      EMBO J. 17:2767-2776(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SHIGELLA FLEXNERI ICSA.
    6. "Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility."
      Egile C., Loisel T.P., Laurent V., Li R., Pantaloni D., Sansonetti P.J., Carlier M.-F.
      J. Cell Biol. 146:1319-1332(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SHIGELLA FLEXNERI ICSA.
    7. "Phosphorylation of WASP by the Cdc42-associated kinase ACK1: dual hydroxyamino acid specificity in a tyrosine kinase."
      Yokoyama N., Lougheed J., Miller W.T.
      J. Biol. Chem. 280:42219-42226(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-242 AND TYR-256 BY TNK2, INTERACTION WITH WASL.
    8. "NOSTRIN functions as a homotrimeric adaptor protein facilitating internalization of eNOS."
      Icking A., Matt S., Opitz N., Wiesenthal A., Mueller-Esterl W., Schilling K.
      J. Cell Sci. 118:5059-5069(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NOSTRIN.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    11. "Sorting nexin 33 induces mammalian cell micronucleated phenotype and actin polymerization by interacting with Wiskott-Aldrich syndrome protein."
      Zhang J., Zhang X., Guo Y., Xu L., Pei D.
      J. Biol. Chem. 284:21659-21669(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SNX33.
    12. "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), IDENTIFICATION IN A COMPLEX WITH BAIAP2L1 AND E.COLI EFFECTOR PROTEIN ESPF(U).
    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 TYR-256; SER-484 AND SER-485, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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-484 AND SER-485, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "The structural basis of actin interaction with multiple WH2/beta-thymosin motif-containing proteins."
      Aguda A.H., Xue B., Irobi E., Preat T., Robinson R.C.
      Structure 14:469-476(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 451-465.
    19. "Interactions of isolated C-terminal fragments of neural Wiskott-Aldrich syndrome protein (N-WASP) with actin and Arp2/3 complex."
      Gaucher J.F., Mauge C., Didry D., Guichard B., Renault L., Carlier M.F.
      J. Biol. Chem. 287:34646-34659(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 392-484 IN COMPLEX WITH ACTIN, FUNCTION, SUBUNIT, INTERACTION WITH THE ARP2/3 COMPLEX, ACTIN-BINDING.
    20. "Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly."
      Aitio O., Hellman M., Skehan B., Kesti T., Leong J.M., Saksela K., Permi P.
      Structure 20:1692-1703(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 207-270 IN COMPLEX WITH BAIAP2L1 AND THE E.COLI SECRETED EFFECTOR PROTEIN ESPF(U), IDENTIFICATION IN A COMPLEX WITH BAIAP2L1 AND E.COLI EFFECTOR PROTEIN ESPF(U), FUNCTION.

    Entry informationi

    Entry nameiWASL_HUMAN
    AccessioniPrimary (citable) accession number: O00401
    Secondary accession number(s): A1JUI9, Q7Z746
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: February 1, 2005
    Last modified: October 1, 2014
    This is version 146 of the entry and version 2 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 7
      Human chromosome 7: 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