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Q9UI08

- EVL_HUMAN

UniProt

Q9UI08 - EVL_HUMAN

Protein

Ena/VASP-like protein

Gene

EVL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (15 Nov 2002)
      Previous versions | rss
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    Functioni

    Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. EVL enhances actin nucleation and polymerization.

    GO - Molecular functioni

    1. profilin binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. SH3 domain binding Source: UniProtKB

    GO - Biological processi

    1. actin filament organization Source: ProtInc
    2. actin polymerization or depolymerization Source: UniProtKB
    3. axon guidance Source: Reactome
    4. cell surface receptor signaling pathway Source: UniProtKB
    5. negative regulation of epithelial cell migration Source: UniProt
    6. negative regulation of ruffle assembly Source: UniProt
    7. nervous system development Source: UniProtKB
    8. organ morphogenesis Source: UniProtKB
    9. positive regulation of stress fiber assembly Source: UniProt
    10. protein homotetramerization Source: InterPro

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    ReactomeiREACT_12623. Generation of second messenger molecules.
    REACT_19351. Signaling by Robo receptor.
    SignaLinkiQ9UI08.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ena/VASP-like protein
    Alternative name(s):
    Ena/vasodilator-stimulated phosphoprotein-like
    Gene namesi
    Name:EVL
    Synonyms:RNB6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:20234. EVL.

    Subcellular locationi

    Cytoplasmcytoskeleton By similarity. Cell projectionlamellipodium By similarity
    Note: Targeted to the leading edge of lamellipodia and the dital tip of stress fibers through interaction with a number of proteins. In activated T-cells, localizes to the F-actin collar and the distal tip of microspikes By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoskeleton Source: UniProtKB-SubCell
    3. cytosol Source: Reactome
    4. focal adhesion Source: UniProtKB
    5. lamellipodium Source: UniProtKB
    6. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134890866.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 416416Ena/VASP-like proteinPRO_0000087104Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei246 – 2461Phosphoserine1 Publication
    Modified residuei304 – 3041Phosphoserine2 Publications
    Modified residuei306 – 3061Phosphoserine1 Publication
    Modified residuei329 – 3291Phosphoserine1 Publication
    Modified residuei331 – 3311Phosphoserine1 Publication
    Modified residuei341 – 3411Phosphoserine1 Publication
    Modified residuei349 – 3491Phosphoserine2 Publications
    Modified residuei354 – 3541Phosphoserine1 Publication
    Modified residuei369 – 3691Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated by PKA; phosphorylation abolishes binding to SH3 domains of ABL and SRC.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UI08.
    PaxDbiQ9UI08.
    PRIDEiQ9UI08.

    PTM databases

    PhosphoSiteiQ9UI08.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UI08.
    BgeeiQ9UI08.
    CleanExiHS_EVL.
    GenevestigatoriQ9UI08.

    Organism-specific databases

    HPAiHPA018849.

    Interactioni

    Subunit structurei

    Homotetramer By similarity. Binds to the SH3 domains of ABL1, LYN and SRC. Also binds to profilin, with preference for isoform IIa of PFN2, and the WW domain of APBB1/FE65. Binds to SEMA6A. Interacts, via the Pro-rich region, with the C-terminal SH3 domain of DNMBP. Interacts with RAPH1. Binds, via the EVH1 domain, the Pro-rich domain of Listeria monocytogenes actA By similarity. Binds, via the EVH1 domain, the Pro-rich domain of ZYX.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HTTP428582EBI-6448852,EBI-466029
    SPTAN1Q138134EBI-346653,EBI-351450
    ZDHHC17Q8IUH52EBI-6448852,EBI-524753

    Protein-protein interaction databases

    BioGridi119556. 18 interactions.
    IntActiQ9UI08. 9 interactions.
    MINTiMINT-3080348.
    STRINGi9606.ENSP00000376652.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UI08.
    SMRiQ9UI08. Positions 1-113.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 112112WH1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni222 – 413192EVH2Add
    BLAST
    Regioni222 – 24221EVH2 block AAdd
    BLAST
    Regioni265 – 28218EVH2 block BAdd
    BLAST
    Regioni379 – 41335EVH2 block CAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi231 – 2344KLKR

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi162 – 20645Pro-richAdd
    BLAST

    Domaini

    The EVH2 domain is comprised of 3 regions. Block A is a thymosin-like domain required for G-actin binding. The KLKR motif within this block is essential for the G-actin binding and for actin polymerization. Block B is required for F-actin binding and subcellular location, and Block C for tetramerization.

    Sequence similaritiesi

    Belongs to the Ena/VASP family.Curated
    Contains 1 WH1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH3-binding

    Phylogenomic databases

    eggNOGiNOG265043.
    HOVERGENiHBG006655.
    OMAiQHRQESL.
    OrthoDBiEOG72JWGQ.
    PhylomeDBiQ9UI08.
    TreeFamiTF321411.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR011993. PH_like_dom.
    IPR017354. Vasodilator_phosphoprotein.
    IPR014885. VASP_tetra.
    IPR000697. WH1/EVH1.
    [Graphical view]
    PfamiPF08776. VASP_tetra. 1 hit.
    PF00568. WH1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038010. Vasodilator_Phospo. 1 hit.
    SMARTiSM00461. WH1. 1 hit.
    [Graphical view]
    PROSITEiPS50229. WH1. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 2 (identifier: Q9UI08-1) [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

    MSEQSICQAR ASVMVYDDTS KKWVPIKPGQ QGFSRINIYH NTASNTFRVV    50
    GVKLQDQQVV INYSIVKGLK YNQATPTFHQ WRDARQVYGL NFASKEEATT 100
    FSNAMLFALN IMNSQEGGPS SQRQVQNGPS PDEMDIQRRQ VMEQHQQQRQ 150
    ESLERRTSAT GPILPPGHPS SAASAPVSCS GPPPPPPPPV PPPPTGATPP 200
    PPPPLPAGGA QGSSHDESSM SGLAAAIAGA KLRRVQRPED ASGGSSPSGT 250
    SKSDANRASS GGGGGGLMEE MNKLLAKRRK AASQSDKPAE KKEDESQMED 300
    PSTSPSPGTR AASQPPNSSE AGRKPWERSN SVEKPVSSIL SRTPSVAKSP 350
    EAKSPLQSQP HSRMKPAGSV NDMALDAFDL DRMKQEILEE VVRELHKVKE 400
    EIIDAIRQEL SGISTT 416
    Length:416
    Mass (Da):44,620
    Last modified:November 15, 2002 - v2
    Checksum:iAD5B67458755D659
    GO
    Isoform 1 (identifier: Q9UI08-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MAT

    Show »
    Length:418
    Mass (Da):44,792
    Checksum:iBFCCF68CF923720C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti201 – 2011P → S in AAF17197. (PubMed:10931946)Curated
    Sequence conflicti329 – 3291S → N in AAP97156. 1 PublicationCurated
    Sequence conflicti364 – 3641M → Y in CAB63763. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti188 – 1881P → L in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036464
    Natural varianti247 – 2471P → L in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036465

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MAT in isoform 1. 3 PublicationsVSP_004044

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF052504 mRNA. Translation: AAF21709.1.
    AF087843 mRNA. Translation: AAP97156.1.
    AF112209 mRNA. Translation: AAF17197.1.
    AK289720 mRNA. Translation: BAF82409.1.
    CH471061 Genomic DNA. Translation: EAW81684.1.
    BC023997 mRNA. Translation: AAH23997.1.
    BC032358 mRNA. Translation: AAH32358.1.
    AF131766 mRNA. Translation: AAD20040.1.
    AL133642 mRNA. Translation: CAB63763.2.
    CCDSiCCDS9955.1. [Q9UI08-2]
    RefSeqiNP_057421.1. NM_016337.2. [Q9UI08-2]
    UniGeneiHs.125867.

    Genome annotation databases

    EnsembliENST00000392920; ENSP00000376652; ENSG00000196405. [Q9UI08-2]
    ENST00000402714; ENSP00000384720; ENSG00000196405. [Q9UI08-1]
    GeneIDi51466.
    KEGGihsa:51466.
    UCSCiuc001ygt.3. human. [Q9UI08-1]
    uc001ygu.3. human. [Q9UI08-2]

    Polymorphism databases

    DMDMi25090276.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF052504 mRNA. Translation: AAF21709.1 .
    AF087843 mRNA. Translation: AAP97156.1 .
    AF112209 mRNA. Translation: AAF17197.1 .
    AK289720 mRNA. Translation: BAF82409.1 .
    CH471061 Genomic DNA. Translation: EAW81684.1 .
    BC023997 mRNA. Translation: AAH23997.1 .
    BC032358 mRNA. Translation: AAH32358.1 .
    AF131766 mRNA. Translation: AAD20040.1 .
    AL133642 mRNA. Translation: CAB63763.2 .
    CCDSi CCDS9955.1. [Q9UI08-2 ]
    RefSeqi NP_057421.1. NM_016337.2. [Q9UI08-2 ]
    UniGenei Hs.125867.

    3D structure databases

    ProteinModelPortali Q9UI08.
    SMRi Q9UI08. Positions 1-113.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119556. 18 interactions.
    IntActi Q9UI08. 9 interactions.
    MINTi MINT-3080348.
    STRINGi 9606.ENSP00000376652.

    PTM databases

    PhosphoSitei Q9UI08.

    Polymorphism databases

    DMDMi 25090276.

    Proteomic databases

    MaxQBi Q9UI08.
    PaxDbi Q9UI08.
    PRIDEi Q9UI08.

    Protocols and materials databases

    DNASUi 51466.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000392920 ; ENSP00000376652 ; ENSG00000196405 . [Q9UI08-2 ]
    ENST00000402714 ; ENSP00000384720 ; ENSG00000196405 . [Q9UI08-1 ]
    GeneIDi 51466.
    KEGGi hsa:51466.
    UCSCi uc001ygt.3. human. [Q9UI08-1 ]
    uc001ygu.3. human. [Q9UI08-2 ]

    Organism-specific databases

    CTDi 51466.
    GeneCardsi GC14P101159.
    H-InvDB HIX0011964.
    HGNCi HGNC:20234. EVL.
    HPAi HPA018849.
    neXtProti NX_Q9UI08.
    PharmGKBi PA134890866.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG265043.
    HOVERGENi HBG006655.
    OMAi QHRQESL.
    OrthoDBi EOG72JWGQ.
    PhylomeDBi Q9UI08.
    TreeFami TF321411.

    Enzyme and pathway databases

    Reactomei REACT_12623. Generation of second messenger molecules.
    REACT_19351. Signaling by Robo receptor.
    SignaLinki Q9UI08.

    Miscellaneous databases

    ChiTaRSi EVL. human.
    GeneWikii Enah/Vasp-like.
    GenomeRNAii 51466.
    NextBioi 55097.
    PROi Q9UI08.

    Gene expression databases

    ArrayExpressi Q9UI08.
    Bgeei Q9UI08.
    CleanExi HS_EVL.
    Genevestigatori Q9UI08.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR011993. PH_like_dom.
    IPR017354. Vasodilator_phosphoprotein.
    IPR014885. VASP_tetra.
    IPR000697. WH1/EVH1.
    [Graphical view ]
    Pfami PF08776. VASP_tetra. 1 hit.
    PF00568. WH1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038010. Vasodilator_Phospo. 1 hit.
    SMARTi SM00461. WH1. 1 hit.
    [Graphical view ]
    PROSITEi PS50229. WH1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Ohta S., Mineta T., Kimoto M., Tabuchi K.
      Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    2. "Cloning of a new human cDNA homologous to R.norvegicus RNB6 mRNA."
      Wan Y.Z., Yu L., Yue P., Tu Q., Fu S.N., Zhao S.Y.
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Adrenal gland.
    4. "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].
      Tissue: Brain.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORMS 1 AND 2).
      Tissue: Lung and Pancreas.
    7. Mei G., Yu W., Gibbs R.A.
      Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 55-416.
      Tissue: Brain.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 163-364.
      Tissue: Uterus.
    9. "The orthologous human and murine semaphorin 6A-1 proteins (SEMA6A-1/Sema6A-1) bind to the enabled/vasodilator-stimulated phosphoprotein-like protein (EVL) via a novel carboxyl-terminal zyxin-like domain."
      Klostermann A., Lutz B., Gertler F., Behl C.
      J. Biol. Chem. 275:39647-39653(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SEMA6A.
    10. Cited for: INTERACTION WITH RAPH1.
    11. "Tes, a specific Mena interacting partner, breaks the rules for EVH1 binding."
      Boeda B., Briggs D.C., Higgins T., Garvalov B.K., Fadden A.J., McDonald N.Q., Way M.
      Mol. Cell 28:1071-1082(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZYX.
    12. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349 AND SER-369, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-304; SER-306; SER-329; SER-331 AND SER-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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-304; SER-341 AND SER-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-188 AND LEU-247.

    Entry informationi

    Entry nameiEVL_HUMAN
    AccessioniPrimary (citable) accession number: Q9UI08
    Secondary accession number(s): A8K105
    , O95884, Q7Z522, Q8TBV1, Q9UF25, Q9UIC2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 15, 2002
    Last sequence update: November 15, 2002
    Last modified: October 1, 2014
    This is version 132 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

    Miscellaneous

    Required to transform actin polymerization into active movement for the propulsive force of Listeria monocytogenes.By similarity

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3