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O95425

- SVIL_HUMAN

UniProt

O95425 - SVIL_HUMAN

Protein

Supervillin

Gene

SVIL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (07 Jul 2009)
      Previous versions | rss
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    Functioni

    Forms a high-affinity link between the actin cytoskeleton and the membrane. Isoform 1 (archvillin) is among the first costameric proteins to assemble during myogenesis and it contributes to myogenic membrane structure and differentiation. Appears to be involved in myosin II assembly. May modulate myosin II regulation through MLCK during cell spreading, an initial step in cell migration. May play a role in invadopodial function. Isoform 2 may be involved in modulation of focal adhesions. Supervillin-mediated down-regulation of focal adhesions involves binding to TRIP6 By similarity.By similarity

    GO - Molecular functioni

    1. actin filament binding Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. cytoskeleton organization Source: InterPro
    2. skeletal muscle tissue development Source: UniProtKB

    Keywords - Ligandi

    Actin-binding, Calcium

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Supervillin
    Alternative name(s):
    Archvillin
    p205/p250
    Gene namesi
    Name:SVIL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:11480. SVIL.

    Subcellular locationi

    Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcytoskeleton. Cell projectioninvadopodium. Cell projectionpodosome
    Note: Tightly associated with both actin filaments and plasma membranes.

    GO - Cellular componenti

    1. actin cytoskeleton Source: UniProtKB
    2. cell junction Source: UniProtKB-KW
    3. costamere Source: UniProtKB
    4. cytoplasm Source: UniProtKB
    5. invadopodium Source: UniProtKB-SubCell
    6. nucleus Source: UniProtKB
    7. plasma membrane Source: UniProtKB
    8. podosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2176 – 21761L → K: Strongly increased affinity for F-actin. 1 Publication

    Organism-specific databases

    PharmGKBiPA36265.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 22142214SupervillinPRO_0000218740Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei50 – 501Phosphoserine2 Publications
    Modified residuei221 – 2211Phosphoserine3 Publications
    Modified residuei245 – 2451Phosphoserine4 Publications
    Modified residuei270 – 2701Phosphoserine2 Publications
    Modified residuei707 – 7071Phosphoserine2 Publications
    Modified residuei852 – 8521Phosphothreonine1 Publication
    Modified residuei914 – 9141Phosphoserine2 Publications
    Modified residuei920 – 9201Phosphoserine2 Publications
    Modified residuei924 – 9241Phosphoserine1 Publication
    Modified residuei968 – 9681Phosphoserine2 Publications
    Modified residuei1000 – 10001PhosphoserineBy similarity
    Modified residuei1111 – 11111Phosphothreonine1 Publication
    Modified residuei1120 – 11201Phosphoserine2 Publications
    Modified residuei1225 – 12251Phosphoserine2 Publications
    Modified residuei1230 – 12301Phosphothreonine1 Publication
    Modified residuei1322 – 13221Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO95425.
    PaxDbiO95425.
    PRIDEiO95425.

    PTM databases

    PhosphoSiteiO95425.

    Expressioni

    Tissue specificityi

    Expressed in many tissues. Most abundant in muscle, bone marrow, thyroid gland and salivary gland. Isoform 1 (archvillin) is muscle specific.1 Publication

    Gene expression databases

    ArrayExpressiO95425.
    BgeeiO95425.
    CleanExiHS_SVIL.
    GenevestigatoriO95425.

    Organism-specific databases

    HPAiCAB010878.
    HPA020095.
    HPA020138.

    Interactioni

    Subunit structurei

    Associates with F-actin. Interacts with NEB. Interacts with MYH9. Interacts with MYLK. Isoform 2 interacts with TRIP6. Isoform 2 interacts with DYNLT1 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NEBP209294EBI-487145,EBI-1049657

    Protein-protein interaction databases

    BioGridi112707. 69 interactions.
    IntActiO95425. 8 interactions.
    MINTiMINT-1369291.
    STRINGi9606.ENSP00000348128.

    Structurei

    Secondary structure

    1
    2214
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi2159 – 21624
    Beta strandi2169 – 21724
    Helixi2177 – 21793
    Helixi2182 – 21887
    Beta strandi2189 – 21913
    Helixi2193 – 21964
    Helixi2201 – 221111

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2K6MNMR-S2149-2214[»]
    2K6NNMR-A2149-2214[»]
    ProteinModelPortaliO95425.
    SMRiO95425. Positions 1443-2123, 2148-2214.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO95425.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati1441 – 1540100Gelsolin-like 1Add
    BLAST
    Repeati1560 – 1682123Gelsolin-like 2Add
    BLAST
    Repeati1752 – 1862111Gelsolin-like 3Add
    BLAST
    Repeati1881 – 1982102Gelsolin-like 4Add
    BLAST
    Repeati2015 – 2122108Gelsolin-like 5Add
    BLAST
    Domaini2151 – 221464HPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 174174Interaction with MYLKBy similarityAdd
    BLAST
    Regioni1419 – 1687269Interaction with NEBAdd
    BLAST

    Domaini

    As opposed to other villin-type headpiece domains, supervillin HP (SVHP) doesn't bind F-actin due to the absence of a conformationally flexible region (V-loop).1 Publication

    Sequence similaritiesi

    Belongs to the villin/gelsolin family.Curated
    Contains 5 gelsolin-like repeats.Curated
    Contains 1 HP (headpiece) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG324767.
    HOVERGENiHBG052980.
    InParanoidiO95425.
    KOiK10369.
    OMAiRSHTQPI.
    OrthoDBiEOG7WX07J.
    PhylomeDBiO95425.
    TreeFamiTF316081.

    Family and domain databases

    Gene3Di1.10.950.10. 1 hit.
    3.40.20.10. 5 hits.
    InterProiIPR029006. ADF-H/Gelsolin-like_dom.
    IPR007123. Gelsolin-like_dom.
    IPR015628. Supervillin.
    IPR007122. Villin/Gelsolin.
    IPR003128. Villin_headpiece.
    [Graphical view]
    PANTHERiPTHR11977. PTHR11977. 1 hit.
    PTHR11977:SF28. PTHR11977:SF28. 1 hit.
    PfamiPF00626. Gelsolin. 1 hit.
    PF02209. VHP. 1 hit.
    [Graphical view]
    PRINTSiPR00597. GELSOLIN.
    SMARTiSM00262. GEL. 4 hits.
    SM00153. VHP. 1 hit.
    [Graphical view]
    SUPFAMiSSF47050. SSF47050. 1 hit.
    PROSITEiPS51089. HP. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O95425-1) [UniParc]FASTAAdd to Basket

    Also known as: Archvillin, p250, SV2

    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

    MKRKERIARR LEGIENDTQP ILLQSCTGLV THRLLEEDTP RYMRASDPAS     50
    PHIGRSNEEE ETSDSSLEKQ TRSKYCTETS GVHGDSPYGS GTMDTHSLES 100
    KAERIARYKA ERRRQLAEKY GLTLDPEADS EYLSRYTKSR KEPDAVEKRG 150
    GKSDKQEESS RDASSLYPGT ETMGLRTCAG ESKDYALHVG DGSSDPEVLL 200
    NIENQRRGQE LSATRQAHDL SPAAESSSTF SFSGRDSSFT EVPRSPKHAH 250
    SSSLQQAASR SPSFGDPQLS PEARPSTGKP KHEWFLQKDS EGDTPSLINW 300
    PSRVKVREKL VKEESARNSP ELASESVTQR RHQPAPVHYV SFQSEHSAFD 350
    RVPSKAAGST RQPIRGYVQP ADTGHTAKLV TPETPENASE CSWVASATQN 400
    VPKPPSLTVL EGDGRDSPVL HVCESKAEEE EGEGEGEEKE EDVCFTEALE 450
    QSKKTLLALE GDGLVRSPED PSRNEDFGKP AVSTVTLEHQ KELENVAQPP 500
    QAPHQPTERT GRSEMVLYIQ SEPVSQDAKP TGHNREASKK RKVRTRSLSD 550
    FTGPPQLQAL KYKDPASRRE LELPSSKTEG PYGEISMLDT KVSVAQLRSA 600
    FLASANACRR PELKSRVERS AEGPGLPTGV ERERGSRKPR RYFSPGESRK 650
    TSERFRTQPI TSAERKESDR CTSHSETPTV DDEEKVDERA KLSVAAKRLL 700
    FREMEKSFDE QNVPKRRSRN TAVEQRLRRL QDRSLTQPIT TEEVVIAATE 750
    PIPASCSGGT HPVMARLPSP TVARSAVQPA RLQASAHQKA LAKDQTNEGK 800
    ELAEQGEPDS STLSLAEKLA LFNKLSQPVS KAISTRNRID TRQRRMNARY 850
    QTQPVTLGEV EQVQSGKLIP FSPAVNTSVS TVASTVAPMY AGDLRTKPPL 900
    DHNASATDYK FSSSIENSDS PVRSILKSQA WQPLVEGSEN KGMLREYGET 950
    ESKRALTGRD SGMEKYGSFE EAEASYPILN RAREGDSHKE SKYAVPRRGS 1000
    LERANPPITH LGDEPKEFSM AKMNAQGNLD LRDRLPFEEK VEVENVMKRK 1050
    FSLRAAEFGE PTSEQTGTAA GKTIAQTTAP VSWKPQDSSE QPQEKLCKNP 1100
    CAMFAAGEIK TPTGEGLLDS PSKTMSIKER LALLKKSGEE DWRNRLSRRQ 1150
    EGGKAPASSL HTQEAGRSLI KKRVTESRES QMTIEERKQL ITVREEAWKT 1200
    RGRGAANDST QFTVAGRMVK KGLASPTAIT PVASPICGKT RGTTPVSKPL 1250
    EDIEARPDMQ LESDLKLDRL ETFLRRLNNK VGGMHETVLT VTGKSVKEVM 1300
    KPDDDETFAK FYRSVDYNMP RSPVEMDEDF DVIFDPYAPK LTSSVAEHKR 1350
    AVRPKRRVQA SKNPLKMLAA REDLLQEYTE QRLNVAFMES KRMKVEKMSS 1400
    NSNFSEVTLA GLASKENFSN VSLRSVNLTE QNSNNSAVPY KRLMLLQIKG 1450
    RRHVQTRLVE PRASALNSGD CFLLLSPHCC FLWVGEFANV IEKAKASELA 1500
    TLIQTKRELG CRATYIQTIE EGINTHTHAA KDFWKLLGGQ TSYQSAGDPK 1550
    EDELYEAAII ETNCIYRLMD DKLVPDDDYW GKIPKCSLLQ PKEVLVFDFG 1600
    SEVYVWHGKE VTLAQRKIAF QLAKHLWNGT FDYENCDINP LDPGECNPLI 1650
    PRKGQGRPDW AIFGRLTEHN ETILFKEKFL DWTELKRSNE KNPGELAQHK 1700
    EDPRTDVKAY DVTRMVSMPQ TTAGTILDGV NVGRGYGLVE GHDRRQFEIT 1750
    SVSVDVWHIL EFDYSRLPKQ SIGQFHEGDA YVVKWKFMVS TAVGSRQKGE 1800
    HSVRAAGKEK CVYFFWQGRH STVSEKGTSA LMTVELDEER GAQVQVLQGK 1850
    EPPCFLQCFQ GGMVVHSGRR EEEEENVQSE WRLYCVRGEV PVEGNLLEVA 1900
    CHCSSLRSRT SMVVLNVNKA LIYLWHGCKA QAHTKEVGRT AANKIKEQCP 1950
    LEAGLHSSSK VTIHECDEGS EPLGFWDALG RRDRKAYDCM LQDPGSFNFA 2000
    PRLFILSSSS GDFAATEFVY PARAPSVVSS MPFLQEDLYS APQPALFLVD 2050
    NHHEVYLWQG WWPIENKITG SARIRWASDR KSAMETVLQY CKGKNLKKPA 2100
    PKSYLIHAGL EPLTFTNMFP SWEHREDIAE ITEMDTEVSN QITLVEDVLA 2150
    KLCKTIYPLA DLLARPLPEG VDPLKLEIYL TDEDFEFALD MTRDEYNALP 2200
    AWKQVNLKKA KGLF 2214
    Length:2,214
    Mass (Da):247,746
    Last modified:July 7, 2009 - v2
    Checksum:i6C4793D31FCBDF7C
    GO
    Isoform 2 (identifier: O95425-2) [UniParc]FASTAAdd to Basket

    Also known as: Supervillin, p205, SV1

    The sequence of this isoform differs from the canonical sequence as follows:
         276-669: Missing.
         750-781: Missing.

    Note: Contains a phosphoserine at position 270. Contains a phosphoserine at position 261.

    Show »
    Length:1,788
    Mass (Da):200,847
    Checksum:i03BDF48043A3CC8C
    GO
    Isoform SV3 (identifier: O95425-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         276-302: Missing.

    Note: Contains a phosphoserine at position 270. Contains a phosphoserine at position 261.

    Show »
    Length:2,187
    Mass (Da):244,679
    Checksum:i112D7378B67AEED1
    GO
    Isoform SV4 (identifier: O95425-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         750-781: Missing.

    Show »
    Length:2,182
    Mass (Da):244,523
    Checksum:iD0DB0FB611E25EB4
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti189 – 1891V → A.2 Publications
    Corresponds to variant rs10160013 [ dbSNP | Ensembl ].
    VAR_020791
    Natural varianti422 – 4221V → I.2 Publications
    Corresponds to variant rs1247696 [ dbSNP | Ensembl ].
    VAR_058308
    Natural varianti1041 – 10411V → L.
    Corresponds to variant rs7070135 [ dbSNP | Ensembl ].
    VAR_057467
    Natural varianti1235 – 12351P → A.5 Publications
    Corresponds to variant rs2368406 [ dbSNP | Ensembl ].
    VAR_020792
    Natural varianti1688 – 16881S → P.
    Corresponds to variant rs11007612 [ dbSNP | Ensembl ].
    VAR_024691
    Natural varianti2005 – 20051I → V.
    Corresponds to variant rs7921306 [ dbSNP | Ensembl ].
    VAR_057468
    Natural varianti2041 – 20411A → V.
    Corresponds to variant rs17694739 [ dbSNP | Ensembl ].
    VAR_057469

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei276 – 669394Missing in isoform 2. 1 PublicationVSP_012425Add
    BLAST
    Alternative sequencei276 – 30227Missing in isoform SV3. CuratedVSP_053768Add
    BLAST
    Alternative sequencei750 – 78132Missing in isoform 2 and isoform SV4. 2 PublicationsVSP_012426Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF051850 mRNA. Translation: AAC64695.1.
    AF051851 mRNA. Translation: AAC64696.1.
    AF109135 mRNA. Translation: AAD14682.1.
    JX467682 mRNA. Translation: AGE81989.1.
    AL160060, AL158167 Genomic DNA. Translation: CAH71300.1.
    AL160060, AL158167 Genomic DNA. Translation: CAH71301.1.
    AL158167, AL160060 Genomic DNA. Translation: CAI15237.1.
    AL158167, AL160060 Genomic DNA. Translation: CAI15236.1.
    CH471072 Genomic DNA. Translation: EAW86018.1.
    CH471072 Genomic DNA. Translation: EAW86019.1.
    CCDSiCCDS7163.1. [O95425-2]
    CCDS7164.1. [O95425-1]
    RefSeqiNP_003165.2. NM_003174.3. [O95425-2]
    NP_068506.2. NM_021738.2. [O95425-1]
    UniGeneiHs.499209.

    Genome annotation databases

    EnsembliENST00000355867; ENSP00000348128; ENSG00000197321. [O95425-1]
    ENST00000375398; ENSP00000364547; ENSG00000197321. [O95425-1]
    ENST00000375400; ENSP00000364549; ENSG00000197321. [O95425-2]
    GeneIDi6840.
    KEGGihsa:6840.
    UCSCiuc001iut.1. human. [O95425-1]
    uc001iuu.1. human. [O95425-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF051850 mRNA. Translation: AAC64695.1 .
    AF051851 mRNA. Translation: AAC64696.1 .
    AF109135 mRNA. Translation: AAD14682.1 .
    JX467682 mRNA. Translation: AGE81989.1 .
    AL160060 , AL158167 Genomic DNA. Translation: CAH71300.1 .
    AL160060 , AL158167 Genomic DNA. Translation: CAH71301.1 .
    AL158167 , AL160060 Genomic DNA. Translation: CAI15237.1 .
    AL158167 , AL160060 Genomic DNA. Translation: CAI15236.1 .
    CH471072 Genomic DNA. Translation: EAW86018.1 .
    CH471072 Genomic DNA. Translation: EAW86019.1 .
    CCDSi CCDS7163.1. [O95425-2 ]
    CCDS7164.1. [O95425-1 ]
    RefSeqi NP_003165.2. NM_003174.3. [O95425-2 ]
    NP_068506.2. NM_021738.2. [O95425-1 ]
    UniGenei Hs.499209.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2K6M NMR - S 2149-2214 [» ]
    2K6N NMR - A 2149-2214 [» ]
    ProteinModelPortali O95425.
    SMRi O95425. Positions 1443-2123, 2148-2214.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112707. 69 interactions.
    IntActi O95425. 8 interactions.
    MINTi MINT-1369291.
    STRINGi 9606.ENSP00000348128.

    PTM databases

    PhosphoSitei O95425.

    Proteomic databases

    MaxQBi O95425.
    PaxDbi O95425.
    PRIDEi O95425.

    Protocols and materials databases

    DNASUi 6840.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000355867 ; ENSP00000348128 ; ENSG00000197321 . [O95425-1 ]
    ENST00000375398 ; ENSP00000364547 ; ENSG00000197321 . [O95425-1 ]
    ENST00000375400 ; ENSP00000364549 ; ENSG00000197321 . [O95425-2 ]
    GeneIDi 6840.
    KEGGi hsa:6840.
    UCSCi uc001iut.1. human. [O95425-1 ]
    uc001iuu.1. human. [O95425-2 ]

    Organism-specific databases

    CTDi 6840.
    GeneCardsi GC10M029786.
    H-InvDB HIX0008738.
    HGNCi HGNC:11480. SVIL.
    HPAi CAB010878.
    HPA020095.
    HPA020138.
    MIMi 604126. gene.
    neXtProti NX_O95425.
    PharmGKBi PA36265.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG324767.
    HOVERGENi HBG052980.
    InParanoidi O95425.
    KOi K10369.
    OMAi RSHTQPI.
    OrthoDBi EOG7WX07J.
    PhylomeDBi O95425.
    TreeFami TF316081.

    Miscellaneous databases

    ChiTaRSi SVIL. human.
    EvolutionaryTracei O95425.
    GeneWikii SVIL.
    GenomeRNAii 6840.
    NextBioi 26705.
    PROi O95425.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95425.
    Bgeei O95425.
    CleanExi HS_SVIL.
    Genevestigatori O95425.

    Family and domain databases

    Gene3Di 1.10.950.10. 1 hit.
    3.40.20.10. 5 hits.
    InterProi IPR029006. ADF-H/Gelsolin-like_dom.
    IPR007123. Gelsolin-like_dom.
    IPR015628. Supervillin.
    IPR007122. Villin/Gelsolin.
    IPR003128. Villin_headpiece.
    [Graphical view ]
    PANTHERi PTHR11977. PTHR11977. 1 hit.
    PTHR11977:SF28. PTHR11977:SF28. 1 hit.
    Pfami PF00626. Gelsolin. 1 hit.
    PF02209. VHP. 1 hit.
    [Graphical view ]
    PRINTSi PR00597. GELSOLIN.
    SMARTi SM00262. GEL. 4 hits.
    SM00153. VHP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47050. SSF47050. 1 hit.
    PROSITEi PS51089. HP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, characterization, and chromosomal localization of human supervillin (SVIL)."
      Pope R.K., Pestonjamasp K.N., Smith K.P., Wulfkuhle J.D., Strassel C.P., Lawrence J.B., Luna E.J.
      Genomics 52:342-351(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS ALA-189 AND ALA-1235, INTERACTION WITH ACTIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Cervix carcinoma and Kidney.
    2. "Archvillin, a muscle-specific isoform of supervillin, is an early expressed component of the costameric membrane skeleton."
      Oh S.W., Pope R.K., Smith K.P., Crowley J.L., Nebl T., Lawrence J.B., Luna E.J.
      J. Cell Sci. 116:2261-2275(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ALA-189; ILE-422 AND ALA-1235.
    3. "Supervillin-mediated suppression of p53 protein enhances cell survival."
      Fang Z., Luna E.J.
      J. Biol. Chem. 288:7918-7929(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SV4), ALTERNATIVE SPLICING (ISOFORMS SV3 AND SV4).
    4. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ILE-422.
    6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221 AND SER-245, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270 (ISOFORMS 2 AND SV3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-852, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    8. "Archvillin anchors in the Z-line of skeletal muscle via the nebulin C-terminus."
      Lee M.-A., Joo Y.M., Lee Y.M., Kim H.S., Kim J.-H., Choi J.-K., Ahn S.-J., Min B.-I., Kim C.-R.
      Biochem. Biophys. Res. Commun. 374:320-324(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NEB.
    9. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270 (ISOFORMS 2 AND SV3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-221; SER-245; SER-920; THR-1111; SER-1120; SER-1225 AND SER-1322, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261 AND SER-270 (ISOFORMS 2 AND SV3), VARIANT [LARGE SCALE ANALYSIS] ALA-1235, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Supervillin reorganizes the actin cytoskeleton and increases invadopodial efficiency."
      Crowley J.L., Smith T.C., Fang Z., Takizawa N., Luna E.J.
      Mol. Biol. Cell 20:948-962(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "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-50; SER-221; SER-245; SER-270; SER-707; SER-914; SER-920; SER-924; SER-968; SER-1120; SER-1225; THR-1230 AND SER-1322, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261 (ISOFORMS 2 AND SV3), VARIANT [LARGE SCALE ANALYSIS] ALA-1235, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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-245; SER-707; SER-914 AND SER-968, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261 AND SER-270 (ISOFORMS 2 AND SV3), VARIANT [LARGE SCALE ANALYSIS] ALA-1235, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "How to arm a supervillin: designing F-actin binding activity into supervillin headpiece."
      Brown J.W., Vardar-Ulu D., McKnight C.J.
      J. Mol. Biol. 393:608-618(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 2149-2214, MUTAGENESIS OF LEU-2176.

    Entry informationi

    Entry nameiSVIL_HUMAN
    AccessioniPrimary (citable) accession number: O95425
    Secondary accession number(s): D3DRW9
    , M1J557, O60611, O60612, Q5VZK5, Q5VZK6, Q9H1R7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 4, 2005
    Last sequence update: July 7, 2009
    Last modified: October 1, 2014
    This is version 126 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 10
      Human chromosome 10: 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