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O95425

- SVIL_HUMAN

UniProt

O95425 - SVIL_HUMAN

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Protein

Supervillin

Gene
SVIL
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.1 Publication

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
Complete GO annotation...

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.2 Publications

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
Complete GO annotation...

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 – 2701Phosphoserine6 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 – 10001Phosphoserine By 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.2 Publications

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.

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 – 221464HPAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 174174Interaction with MYLK By 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.

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. VSP_012425Add
BLAST
Alternative sequencei276 – 30227Missing in isoform SV3. VSP_053768Add
BLAST
Alternative sequencei750 – 78132Missing in isoform 2 and isoform SV4. VSP_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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 125 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

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