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O95425 (SVIL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Supervillin
Alternative name(s):
Archvillin
p205/p250
Gene names
Name:SVIL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2214 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.12

Subunit structure

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. Ref.1 Ref.8

Subcellular location

Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcytoskeleton. Cell projectioninvadopodium. Cell projectionpodosome. Note: Tightly associated with both actin filaments and plasma membranes. Ref.1 Ref.12

Tissue specificity

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

Domain

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) (Ref.16).

Sequence similarities

Belongs to the villin/gelsolin family.

Contains 5 gelsolin-like repeats.

Contains 1 HP (headpiece) domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NEBP209294EBI-487145,EBI-1049657

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O95425-1)

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.
Isoform 2 (identifier: O95425-2)

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.
Isoform SV3 (identifier: O95425-3)

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.
Isoform SV4 (identifier: O95425-4)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 22142214Supervillin
PRO_0000218740

Regions

Repeat1441 – 1540100Gelsolin-like 1
Repeat1560 – 1682123Gelsolin-like 2
Repeat1752 – 1862111Gelsolin-like 3
Repeat1881 – 1982102Gelsolin-like 4
Repeat2015 – 2122108Gelsolin-like 5
Domain2151 – 221464HP
Region1 – 174174Interaction with MYLK By similarity
Region1419 – 1687269Interaction with NEB

Amino acid modifications

Modified residue501Phosphoserine Ref.11 Ref.14
Modified residue2211Phosphoserine Ref.6 Ref.11 Ref.14
Modified residue2451Phosphoserine Ref.6 Ref.11 Ref.14 Ref.15
Modified residue2701Phosphoserine Ref.6 Ref.9 Ref.10 Ref.11 Ref.14 Ref.15
Modified residue7071Phosphoserine Ref.14 Ref.15
Modified residue8521Phosphothreonine Ref.7
Modified residue9141Phosphoserine Ref.14 Ref.15
Modified residue9201Phosphoserine Ref.11 Ref.14
Modified residue9241Phosphoserine Ref.14
Modified residue9681Phosphoserine Ref.14 Ref.15
Modified residue10001Phosphoserine By similarity
Modified residue11111Phosphothreonine Ref.11
Modified residue11201Phosphoserine Ref.11 Ref.14
Modified residue12251Phosphoserine Ref.11 Ref.14
Modified residue12301Phosphothreonine Ref.14
Modified residue13221Phosphoserine Ref.11 Ref.14

Natural variations

Alternative sequence276 – 669394Missing in isoform 2.
VSP_012425
Alternative sequence276 – 30227Missing in isoform SV3.
VSP_053768
Alternative sequence750 – 78132Missing in isoform 2 and isoform SV4.
VSP_012426
Natural variant1891V → A. Ref.1 Ref.2
Corresponds to variant rs10160013 [ dbSNP | Ensembl ].
VAR_020791
Natural variant4221V → I. Ref.2 Ref.5
Corresponds to variant rs1247696 [ dbSNP | Ensembl ].
VAR_058308
Natural variant10411V → L.
Corresponds to variant rs7070135 [ dbSNP | Ensembl ].
VAR_057467
Natural variant12351P → A. Ref.1 Ref.2 Ref.11 Ref.14 Ref.15
Corresponds to variant rs2368406 [ dbSNP | Ensembl ].
VAR_020792
Natural variant16881S → P.
Corresponds to variant rs11007612 [ dbSNP | Ensembl ].
VAR_024691
Natural variant20051I → V.
Corresponds to variant rs7921306 [ dbSNP | Ensembl ].
VAR_057468
Natural variant20411A → V.
Corresponds to variant rs17694739 [ dbSNP | Ensembl ].
VAR_057469

Experimental info

Mutagenesis21761L → K: Strongly increased affinity for F-actin. Ref.16

Secondary structure

.............. 2214
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Archvillin) (p250) (SV2) [UniParc].

Last modified July 7, 2009. Version 2.
Checksum: 6C4793D31FCBDF7C

FASTA2,214247,746
        10         20         30         40         50         60 
MKRKERIARR LEGIENDTQP ILLQSCTGLV THRLLEEDTP RYMRASDPAS PHIGRSNEEE 

        70         80         90        100        110        120 
ETSDSSLEKQ TRSKYCTETS GVHGDSPYGS GTMDTHSLES KAERIARYKA ERRRQLAEKY 

       130        140        150        160        170        180 
GLTLDPEADS EYLSRYTKSR KEPDAVEKRG GKSDKQEESS RDASSLYPGT ETMGLRTCAG 

       190        200        210        220        230        240 
ESKDYALHVG DGSSDPEVLL NIENQRRGQE LSATRQAHDL SPAAESSSTF SFSGRDSSFT 

       250        260        270        280        290        300 
EVPRSPKHAH SSSLQQAASR SPSFGDPQLS PEARPSTGKP KHEWFLQKDS EGDTPSLINW 

       310        320        330        340        350        360 
PSRVKVREKL VKEESARNSP ELASESVTQR RHQPAPVHYV SFQSEHSAFD RVPSKAAGST 

       370        380        390        400        410        420 
RQPIRGYVQP ADTGHTAKLV TPETPENASE CSWVASATQN VPKPPSLTVL EGDGRDSPVL 

       430        440        450        460        470        480 
HVCESKAEEE EGEGEGEEKE EDVCFTEALE QSKKTLLALE GDGLVRSPED PSRNEDFGKP 

       490        500        510        520        530        540 
AVSTVTLEHQ KELENVAQPP QAPHQPTERT GRSEMVLYIQ SEPVSQDAKP TGHNREASKK 

       550        560        570        580        590        600 
RKVRTRSLSD FTGPPQLQAL KYKDPASRRE LELPSSKTEG PYGEISMLDT KVSVAQLRSA 

       610        620        630        640        650        660 
FLASANACRR PELKSRVERS AEGPGLPTGV ERERGSRKPR RYFSPGESRK TSERFRTQPI 

       670        680        690        700        710        720 
TSAERKESDR CTSHSETPTV DDEEKVDERA KLSVAAKRLL FREMEKSFDE QNVPKRRSRN 

       730        740        750        760        770        780 
TAVEQRLRRL QDRSLTQPIT TEEVVIAATE PIPASCSGGT HPVMARLPSP TVARSAVQPA 

       790        800        810        820        830        840 
RLQASAHQKA LAKDQTNEGK ELAEQGEPDS STLSLAEKLA LFNKLSQPVS KAISTRNRID 

       850        860        870        880        890        900 
TRQRRMNARY QTQPVTLGEV EQVQSGKLIP FSPAVNTSVS TVASTVAPMY AGDLRTKPPL 

       910        920        930        940        950        960 
DHNASATDYK FSSSIENSDS PVRSILKSQA WQPLVEGSEN KGMLREYGET ESKRALTGRD 

       970        980        990       1000       1010       1020 
SGMEKYGSFE EAEASYPILN RAREGDSHKE SKYAVPRRGS LERANPPITH LGDEPKEFSM 

      1030       1040       1050       1060       1070       1080 
AKMNAQGNLD LRDRLPFEEK VEVENVMKRK FSLRAAEFGE PTSEQTGTAA GKTIAQTTAP 

      1090       1100       1110       1120       1130       1140 
VSWKPQDSSE QPQEKLCKNP CAMFAAGEIK TPTGEGLLDS PSKTMSIKER LALLKKSGEE 

      1150       1160       1170       1180       1190       1200 
DWRNRLSRRQ EGGKAPASSL HTQEAGRSLI KKRVTESRES QMTIEERKQL ITVREEAWKT 

      1210       1220       1230       1240       1250       1260 
RGRGAANDST QFTVAGRMVK KGLASPTAIT PVASPICGKT RGTTPVSKPL EDIEARPDMQ 

      1270       1280       1290       1300       1310       1320 
LESDLKLDRL ETFLRRLNNK VGGMHETVLT VTGKSVKEVM KPDDDETFAK FYRSVDYNMP 

      1330       1340       1350       1360       1370       1380 
RSPVEMDEDF DVIFDPYAPK LTSSVAEHKR AVRPKRRVQA SKNPLKMLAA REDLLQEYTE 

      1390       1400       1410       1420       1430       1440 
QRLNVAFMES KRMKVEKMSS NSNFSEVTLA GLASKENFSN VSLRSVNLTE QNSNNSAVPY 

      1450       1460       1470       1480       1490       1500 
KRLMLLQIKG RRHVQTRLVE PRASALNSGD CFLLLSPHCC FLWVGEFANV IEKAKASELA 

      1510       1520       1530       1540       1550       1560 
TLIQTKRELG CRATYIQTIE EGINTHTHAA KDFWKLLGGQ TSYQSAGDPK EDELYEAAII 

      1570       1580       1590       1600       1610       1620 
ETNCIYRLMD DKLVPDDDYW GKIPKCSLLQ PKEVLVFDFG SEVYVWHGKE VTLAQRKIAF 

      1630       1640       1650       1660       1670       1680 
QLAKHLWNGT FDYENCDINP LDPGECNPLI PRKGQGRPDW AIFGRLTEHN ETILFKEKFL 

      1690       1700       1710       1720       1730       1740 
DWTELKRSNE KNPGELAQHK EDPRTDVKAY DVTRMVSMPQ TTAGTILDGV NVGRGYGLVE 

      1750       1760       1770       1780       1790       1800 
GHDRRQFEIT SVSVDVWHIL EFDYSRLPKQ SIGQFHEGDA YVVKWKFMVS TAVGSRQKGE 

      1810       1820       1830       1840       1850       1860 
HSVRAAGKEK CVYFFWQGRH STVSEKGTSA LMTVELDEER GAQVQVLQGK EPPCFLQCFQ 

      1870       1880       1890       1900       1910       1920 
GGMVVHSGRR EEEEENVQSE WRLYCVRGEV PVEGNLLEVA CHCSSLRSRT SMVVLNVNKA 

      1930       1940       1950       1960       1970       1980 
LIYLWHGCKA QAHTKEVGRT AANKIKEQCP LEAGLHSSSK VTIHECDEGS EPLGFWDALG 

      1990       2000       2010       2020       2030       2040 
RRDRKAYDCM LQDPGSFNFA PRLFILSSSS GDFAATEFVY PARAPSVVSS MPFLQEDLYS 

      2050       2060       2070       2080       2090       2100 
APQPALFLVD NHHEVYLWQG WWPIENKITG SARIRWASDR KSAMETVLQY CKGKNLKKPA 

      2110       2120       2130       2140       2150       2160 
PKSYLIHAGL EPLTFTNMFP SWEHREDIAE ITEMDTEVSN QITLVEDVLA KLCKTIYPLA 

      2170       2180       2190       2200       2210 
DLLARPLPEG VDPLKLEIYL TDEDFEFALD MTRDEYNALP AWKQVNLKKA KGLF 

« Hide

Isoform 2 (Supervillin) (p205) (SV1) [UniParc].

Checksum: 03BDF48043A3CC8C
Show »

FASTA1,788200,847
Isoform SV3 [UniParc].

Checksum: 112D7378B67AEED1
Show »

FASTA2,187244,679
Isoform SV4 [UniParc].

Checksum: D0DB0FB611E25EB4
Show »

FASTA2,182244,523

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS7163.1. [O95425-2]
CCDS7164.1. [O95425-1]
RefSeqNP_003165.2. NM_003174.3. [O95425-2]
NP_068506.2. NM_021738.2. [O95425-1]
UniGeneHs.499209.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2K6MNMR-S2149-2214[»]
2K6NNMR-A2149-2214[»]
ProteinModelPortalO95425.
SMRO95425. Positions 1443-2123, 2148-2214.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112707. 69 interactions.
IntActO95425. 8 interactions.
MINTMINT-1369291.
STRING9606.ENSP00000348128.

PTM databases

PhosphoSiteO95425.

Proteomic databases

MaxQBO95425.
PaxDbO95425.
PRIDEO95425.

Protocols and materials databases

DNASU6840.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355867; ENSP00000348128; ENSG00000197321. [O95425-1]
ENST00000375398; ENSP00000364547; ENSG00000197321. [O95425-1]
ENST00000375400; ENSP00000364549; ENSG00000197321. [O95425-2]
GeneID6840.
KEGGhsa:6840.
UCSCuc001iut.1. human. [O95425-1]
uc001iuu.1. human. [O95425-2]

Organism-specific databases

CTD6840.
GeneCardsGC10M029786.
H-InvDBHIX0008738.
HGNCHGNC:11480. SVIL.
HPACAB010878.
HPA020095.
HPA020138.
MIM604126. gene.
neXtProtNX_O95425.
PharmGKBPA36265.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG324767.
HOVERGENHBG052980.
InParanoidO95425.
KOK10369.
OMARSHTQPI.
OrthoDBEOG7WX07J.
PhylomeDBO95425.
TreeFamTF316081.

Gene expression databases

ArrayExpressO95425.
BgeeO95425.
CleanExHS_SVIL.
GenevestigatorO95425.

Family and domain databases

Gene3D1.10.950.10. 1 hit.
3.40.20.10. 5 hits.
InterProIPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. Gelsolin-like_dom.
IPR015628. Supervillin.
IPR007122. Villin/Gelsolin.
IPR003128. Villin_headpiece.
[Graphical view]
PANTHERPTHR11977. PTHR11977. 1 hit.
PTHR11977:SF28. PTHR11977:SF28. 1 hit.
PfamPF00626. Gelsolin. 1 hit.
PF02209. VHP. 1 hit.
[Graphical view]
PRINTSPR00597. GELSOLIN.
SMARTSM00262. GEL. 4 hits.
SM00153. VHP. 1 hit.
[Graphical view]
SUPFAMSSF47050. SSF47050. 1 hit.
PROSITEPS51089. HP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSVIL. human.
EvolutionaryTraceO95425.
GeneWikiSVIL.
GenomeRNAi6840.
NextBio26705.
PROO95425.
SOURCESearch...

Entry information

Entry nameSVIL_HUMAN
AccessionPrimary (citable) accession number: O95425
Secondary accession number(s): D3DRW9 expand/collapse secondary AC list , M1J557, O60611, O60612, Q5VZK5, Q5VZK6, Q9H1R7
Entry history
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 statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM