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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).By similarity

GO - Molecular functioni

  1. actin filament binding Source: UniProtKB

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.

GO - Cellular componenti

  1. actin cytoskeleton Source: UniProtKB
  2. cell projection Source: UniProtKB-KW
  3. costamere Source: UniProtKB
  4. cytoplasm Source: UniProtKB
  5. focal adhesion Source: UniProtKB
  6. nucleus Source: UniProtKB
  7. plasma membrane Source: UniProtKB
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 – 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

BgeeiO95425.
CleanExiHS_SVIL.
ExpressionAtlasiO95425. baseline and differential.
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. 70 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.
GeneTreeiENSGT00760000119111.
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

        10         20         30         40         50
MKRKERIARR LEGIENDTQP ILLQSCTGLV THRLLEEDTP RYMRASDPAS
60 70 80 90 100
PHIGRSNEEE ETSDSSLEKQ TRSKYCTETS GVHGDSPYGS GTMDTHSLES
110 120 130 140 150
KAERIARYKA ERRRQLAEKY GLTLDPEADS EYLSRYTKSR KEPDAVEKRG
160 170 180 190 200
GKSDKQEESS RDASSLYPGT ETMGLRTCAG ESKDYALHVG DGSSDPEVLL
210 220 230 240 250
NIENQRRGQE LSATRQAHDL SPAAESSSTF SFSGRDSSFT EVPRSPKHAH
260 270 280 290 300
SSSLQQAASR SPSFGDPQLS PEARPSTGKP KHEWFLQKDS EGDTPSLINW
310 320 330 340 350
PSRVKVREKL VKEESARNSP ELASESVTQR RHQPAPVHYV SFQSEHSAFD
360 370 380 390 400
RVPSKAAGST RQPIRGYVQP ADTGHTAKLV TPETPENASE CSWVASATQN
410 420 430 440 450
VPKPPSLTVL EGDGRDSPVL HVCESKAEEE EGEGEGEEKE EDVCFTEALE
460 470 480 490 500
QSKKTLLALE GDGLVRSPED PSRNEDFGKP AVSTVTLEHQ KELENVAQPP
510 520 530 540 550
QAPHQPTERT GRSEMVLYIQ SEPVSQDAKP TGHNREASKK RKVRTRSLSD
560 570 580 590 600
FTGPPQLQAL KYKDPASRRE LELPSSKTEG PYGEISMLDT KVSVAQLRSA
610 620 630 640 650
FLASANACRR PELKSRVERS AEGPGLPTGV ERERGSRKPR RYFSPGESRK
660 670 680 690 700
TSERFRTQPI TSAERKESDR CTSHSETPTV DDEEKVDERA KLSVAAKRLL
710 720 730 740 750
FREMEKSFDE QNVPKRRSRN TAVEQRLRRL QDRSLTQPIT TEEVVIAATE
760 770 780 790 800
PIPASCSGGT HPVMARLPSP TVARSAVQPA RLQASAHQKA LAKDQTNEGK
810 820 830 840 850
ELAEQGEPDS STLSLAEKLA LFNKLSQPVS KAISTRNRID TRQRRMNARY
860 870 880 890 900
QTQPVTLGEV EQVQSGKLIP FSPAVNTSVS TVASTVAPMY AGDLRTKPPL
910 920 930 940 950
DHNASATDYK FSSSIENSDS PVRSILKSQA WQPLVEGSEN KGMLREYGET
960 970 980 990 1000
ESKRALTGRD SGMEKYGSFE EAEASYPILN RAREGDSHKE SKYAVPRRGS
1010 1020 1030 1040 1050
LERANPPITH LGDEPKEFSM AKMNAQGNLD LRDRLPFEEK VEVENVMKRK
1060 1070 1080 1090 1100
FSLRAAEFGE PTSEQTGTAA GKTIAQTTAP VSWKPQDSSE QPQEKLCKNP
1110 1120 1130 1140 1150
CAMFAAGEIK TPTGEGLLDS PSKTMSIKER LALLKKSGEE DWRNRLSRRQ
1160 1170 1180 1190 1200
EGGKAPASSL HTQEAGRSLI KKRVTESRES QMTIEERKQL ITVREEAWKT
1210 1220 1230 1240 1250
RGRGAANDST QFTVAGRMVK KGLASPTAIT PVASPICGKT RGTTPVSKPL
1260 1270 1280 1290 1300
EDIEARPDMQ LESDLKLDRL ETFLRRLNNK VGGMHETVLT VTGKSVKEVM
1310 1320 1330 1340 1350
KPDDDETFAK FYRSVDYNMP RSPVEMDEDF DVIFDPYAPK LTSSVAEHKR
1360 1370 1380 1390 1400
AVRPKRRVQA SKNPLKMLAA REDLLQEYTE QRLNVAFMES KRMKVEKMSS
1410 1420 1430 1440 1450
NSNFSEVTLA GLASKENFSN VSLRSVNLTE QNSNNSAVPY KRLMLLQIKG
1460 1470 1480 1490 1500
RRHVQTRLVE PRASALNSGD CFLLLSPHCC FLWVGEFANV IEKAKASELA
1510 1520 1530 1540 1550
TLIQTKRELG CRATYIQTIE EGINTHTHAA KDFWKLLGGQ TSYQSAGDPK
1560 1570 1580 1590 1600
EDELYEAAII ETNCIYRLMD DKLVPDDDYW GKIPKCSLLQ PKEVLVFDFG
1610 1620 1630 1640 1650
SEVYVWHGKE VTLAQRKIAF QLAKHLWNGT FDYENCDINP LDPGECNPLI
1660 1670 1680 1690 1700
PRKGQGRPDW AIFGRLTEHN ETILFKEKFL DWTELKRSNE KNPGELAQHK
1710 1720 1730 1740 1750
EDPRTDVKAY DVTRMVSMPQ TTAGTILDGV NVGRGYGLVE GHDRRQFEIT
1760 1770 1780 1790 1800
SVSVDVWHIL EFDYSRLPKQ SIGQFHEGDA YVVKWKFMVS TAVGSRQKGE
1810 1820 1830 1840 1850
HSVRAAGKEK CVYFFWQGRH STVSEKGTSA LMTVELDEER GAQVQVLQGK
1860 1870 1880 1890 1900
EPPCFLQCFQ GGMVVHSGRR EEEEENVQSE WRLYCVRGEV PVEGNLLEVA
1910 1920 1930 1940 1950
CHCSSLRSRT SMVVLNVNKA LIYLWHGCKA QAHTKEVGRT AANKIKEQCP
1960 1970 1980 1990 2000
LEAGLHSSSK VTIHECDEGS EPLGFWDALG RRDRKAYDCM LQDPGSFNFA
2010 2020 2030 2040 2050
PRLFILSSSS GDFAATEFVY PARAPSVVSS MPFLQEDLYS APQPALFLVD
2060 2070 2080 2090 2100
NHHEVYLWQG WWPIENKITG SARIRWASDR KSAMETVLQY CKGKNLKKPA
2110 2120 2130 2140 2150
PKSYLIHAGL EPLTFTNMFP SWEHREDIAE ITEMDTEVSN QITLVEDVLA
2160 2170 2180 2190 2200
KLCKTIYPLA DLLARPLPEG VDPLKLEIYL TDEDFEFALD MTRDEYNALP
2210
AWKQVNLKKA KGLF
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. [O95425-4]
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. 70 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 . [O95425-4 ]
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 GC10M029841.
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.
GeneTreei ENSGT00760000119111.
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

Bgeei O95425.
CleanExi HS_SVIL.
ExpressionAtlasi O95425. baseline and differential.
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: October 29, 2014
This is version 127 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