O95425 (SVIL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Supervillin

Alternative name(s):
Archvillin
p205/p250

Gene names

Name:

SVIL

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2214 AA.
Sequence status	Complete.
Protein existence	Evidence 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 adehesions involves binding to TRIP6 By similarity. Ref.11
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.7
Subcellular location	Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm › cytoskeleton. Cell projection › invadopodium. Cell projection › podosome. Note: Tightly associated with both actin filaments and plasma membranes. Ref.1 Ref.11
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
Sequence similarities	Belongs to the villin/gelsolin family. Contains 5 gelsolin-like repeats. Contains 1 HP (headpiece) domain.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	Actin-binding Calcium
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cytoskeleton organization Inferred from electronic annotation. Source: InterPro skeletal muscle tissue development Inferred from mutant phenotype Ref.2. Source: UniProtKB
Cellular_component	actin cytoskeleton Non-traceable author statement Ref.1. Source: UniProtKB cell junction Inferred from electronic annotation. Source: UniProtKB-KW costamere Inferred from direct assay Ref.2. Source: UniProtKB invadopodium Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.2. Source: UniProtKB plasma membrane Inferred from direct assay Ref.2. Source: UniProtKB podosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	actin filament binding Inferred from direct assay Ref.2. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O95425-1)

Also known as: Archvillin; p250;

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;

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2214

2214

Supervillin

PRO_0000218740

Regions

Repeat

1441 – 1540

100

Gelsolin-like 1

Repeat

1560 – 1682

123

Gelsolin-like 2

Repeat

1752 – 1862

111

Gelsolin-like 3

Repeat

1881 – 1982

102

Gelsolin-like 4

Repeat

2015 – 2122

108

Gelsolin-like 5

Domain

2151 – 2214

64

HP

Region

1 – 174

174

Interaction with MYLK By similarity

Region

1419 – 1687

269

Interaction with NEB

Amino acid modifications

Modified residue

50

1

Phosphoserine Ref.10 Ref.13

Modified residue

221

1

Phosphoserine Ref.5 Ref.10 Ref.13

Modified residue

245

1

Phosphoserine Ref.5 Ref.10 Ref.13 Ref.14

Modified residue

270

1

Phosphoserine Ref.5 Ref.8 Ref.9 Ref.10 Ref.13 Ref.14

Modified residue

673

1

Phosphoserine By similarity

Modified residue

675

1

Phosphoserine By similarity

Modified residue

707

1

Phosphoserine Ref.13 Ref.14

Modified residue

852

1

Phosphothreonine Ref.6

Modified residue

914

1

Phosphoserine Ref.13 Ref.14

Modified residue

920

1

Phosphoserine Ref.10 Ref.13

Modified residue

924

1

Phosphoserine Ref.13

Modified residue

968

1

Phosphoserine Ref.13 Ref.14

Modified residue

1000

1

Phosphoserine By similarity

Modified residue

1052

1

Phosphoserine By similarity

Modified residue

1111

1

Phosphothreonine Ref.10

Modified residue

1120

1

Phosphoserine Ref.10 Ref.13

Modified residue

1225

1

Phosphoserine Ref.10 Ref.13

Modified residue

1230

1

Phosphothreonine Ref.13

Modified residue

1322

1

Phosphoserine Ref.10 Ref.13

Natural variations

Alternative sequence

276 – 669

394

Missing in isoform 2.

VSP_012425

Alternative sequence

750 – 781

32

Missing in isoform 2.

VSP_012426

Natural variant

189

1

V → A. Ref.1 Ref.2
Corresponds to variant rs10160013 [ dbSNP | Ensembl ].

VAR_020791

Natural variant

422

1

V → I. Ref.2 Ref.4
Corresponds to variant rs1247696 [ dbSNP | Ensembl ].

VAR_058308

Natural variant

1041

1

V → L.
Corresponds to variant rs7070135 [ dbSNP | Ensembl ].

VAR_057467

Natural variant

1235

1

P → A. Ref.1 Ref.2 Ref.10 Ref.13 Ref.14
Corresponds to variant rs2368406 [ dbSNP | Ensembl ].

VAR_020792

Natural variant

1688

1

S → P.
Corresponds to variant rs11007612 [ dbSNP | Ensembl ].

VAR_024691

Natural variant

2005

1

I → V.
Corresponds to variant rs7921306 [ dbSNP | Ensembl ].

VAR_057468

Natural variant

2041

1

A → V.
Corresponds to variant rs17694739 [ dbSNP | Ensembl ].

VAR_057469

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

2214

Helix Strand Turn

Details...

Helix

2159 – 2162

4

Beta strand

2169 – 2172

4

Helix

2177 – 2179

3

Helix

2182 – 2188

7

Beta strand

2189 – 2191

3

Helix

2193 – 2196

4

Helix

2201 – 2211

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Archvillin) (p250) [UniParc]. Last modified July 7, 2009. Version 2. Checksum: 6C4793D31FCBDF7C	FASTA	2,214	247,746
	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
	Isoform 2 (Supervillin) (p205) [UniParc]. Checksum: 03BDF48043A3CC8C	FASTA	1,788	200,847
	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 PEARPRCTSH SETPTVDDEE KVDERAKLSV 310 320 330 340 350 360 AAKRLLFREM EKSFDEQNVP KRRSRNTAVE QRLRRLQDRS LTQPITTEEV VIAATLQASA 370 380 390 400 410 420 HQKALAKDQT NEGKELAEQG EPDSSTLSLA EKLALFNKLS QPVSKAISTR NRIDTRQRRM 430 440 450 460 470 480 NARYQTQPVT LGEVEQVQSG KLIPFSPAVN TSVSTVASTV APMYAGDLRT KPPLDHNASA 490 500 510 520 530 540 TDYKFSSSIE NSDSPVRSIL KSQAWQPLVE GSENKGMLRE YGETESKRAL TGRDSGMEKY 550 560 570 580 590 600 GSFEEAEASY PILNRAREGD SHKESKYAVP RRGSLERANP PITHLGDEPK EFSMAKMNAQ 610 620 630 640 650 660 GNLDLRDRLP FEEKVEVENV MKRKFSLRAA EFGEPTSEQT GTAAGKTIAQ TTAPVSWKPQ 670 680 690 700 710 720 DSSEQPQEKL CKNPCAMFAA GEIKTPTGEG LLDSPSKTMS IKERLALLKK SGEEDWRNRL 730 740 750 760 770 780 SRRQEGGKAP ASSLHTQEAG RSLIKKRVTE SRESQMTIEE RKQLITVREE AWKTRGRGAA 790 800 810 820 830 840 NDSTQFTVAG RMVKKGLASP TAITPVASPI CGKTRGTTPV SKPLEDIEAR PDMQLESDLK 850 860 870 880 890 900 LDRLETFLRR LNNKVGGMHE TVLTVTGKSV KEVMKPDDDE TFAKFYRSVD YNMPRSPVEM 910 920 930 940 950 960 DEDFDVIFDP YAPKLTSSVA EHKRAVRPKR RVQASKNPLK MLAAREDLLQ EYTEQRLNVA 970 980 990 1000 1010 1020 FMESKRMKVE KMSSNSNFSE VTLAGLASKE NFSNVSLRSV NLTEQNSNNS AVPYKRLMLL 1030 1040 1050 1060 1070 1080 QIKGRRHVQT RLVEPRASAL NSGDCFLLLS PHCCFLWVGE FANVIEKAKA SELATLIQTK 1090 1100 1110 1120 1130 1140 RELGCRATYI QTIEEGINTH THAAKDFWKL LGGQTSYQSA GDPKEDELYE AAIIETNCIY 1150 1160 1170 1180 1190 1200 RLMDDKLVPD DDYWGKIPKC SLLQPKEVLV FDFGSEVYVW HGKEVTLAQR KIAFQLAKHL 1210 1220 1230 1240 1250 1260 WNGTFDYENC DINPLDPGEC NPLIPRKGQG RPDWAIFGRL TEHNETILFK EKFLDWTELK 1270 1280 1290 1300 1310 1320 RSNEKNPGEL AQHKEDPRTD VKAYDVTRMV SMPQTTAGTI LDGVNVGRGY GLVEGHDRRQ 1330 1340 1350 1360 1370 1380 FEITSVSVDV WHILEFDYSR LPKQSIGQFH EGDAYVVKWK FMVSTAVGSR QKGEHSVRAA 1390 1400 1410 1420 1430 1440 GKEKCVYFFW QGRHSTVSEK GTSALMTVEL DEERGAQVQV LQGKEPPCFL QCFQGGMVVH 1450 1460 1470 1480 1490 1500 SGRREEEEEN VQSEWRLYCV RGEVPVEGNL LEVACHCSSL RSRTSMVVLN VNKALIYLWH 1510 1520 1530 1540 1550 1560 GCKAQAHTKE VGRTAANKIK EQCPLEAGLH SSSKVTIHEC DEGSEPLGFW DALGRRDRKA 1570 1580 1590 1600 1610 1620 YDCMLQDPGS FNFAPRLFIL SSSSGDFAAT EFVYPARAPS VVSSMPFLQE DLYSAPQPAL 1630 1640 1650 1660 1670 1680 FLVDNHHEVY LWQGWWPIEN KITGSARIRW ASDRKSAMET VLQYCKGKNL KKPAPKSYLI 1690 1700 1710 1720 1730 1740 HAGLEPLTFT NMFPSWEHRE DIAEITEMDT EVSNQITLVE DVLAKLCKTI YPLADLLARP 1750 1760 1770 1780 LPEGVDPLKL EIYLTDEDFE FALDMTRDEY NALPAWKQVN LKKAKGLF

References

	« Hide 'large scale' referencesShow '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]	"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].
[4]	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. , 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.
[5]	"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 (ISOFORM 2), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"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, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[7]	"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.
[8]	"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 (ISOFORM 2), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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, MASS SPECTROMETRY. Tissue: Platelet.
[10]	"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 (ISOFORM 2), VARIANT [LARGE SCALE ANALYSIS] ALA-1235, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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.
[12]	"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.
[13]	"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 (ISOFORM 2), VARIANT [LARGE SCALE ANALYSIS] ALA-1235, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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 (ISOFORM 2), VARIANT [LARGE SCALE ANALYSIS] ALA-1235, MASS SPECTROMETRY.
+	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.
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.

IPI

IPI00018370.
IPI00412650.

RefSeq

NP_003165.2. NM_003174.3.
NP_068506.2. NM_021738.2.

UniGene

Hs.499209.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2K6M	NMR	-	S	2149-2214	[»]
2K6N	NMR	-	A	2149-2214	[»]

ProteinModelPortal

O95425.

ModBase

Search...

Protein-protein interaction databases

IntAct

O95425. 6 interactions.

MINT

MINT-1369291.

STRING

9606.ENSP00000348128.

PTM databases

PhosphoSite

O95425.

Proteomic databases

PaxDb

O95425.

PRIDE

O95425.

Protocols and materials databases

DNASU

6840.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000355867; ENSP00000348128; ENSG00000197321.
ENST00000375398; ENSP00000364547; ENSG00000197321.
ENST00000375400; ENSP00000364549; ENSG00000197321.

GeneID

6840.

KEGG

hsa:6840.

UCSC

uc001iut.1. human.
uc001iuu.1. human.

Organism-specific databases

CTD

6840.

GeneCards

GC10M029786.

H-InvDB

HIX0008738.

HGNC

HGNC:11480. SVIL.

HPA

CAB010878.
HPA020095.
HPA020138.

MIM

604126. gene.

neXtProt

NX_O95425.

PharmGKB

PA36265.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG324767.

HOVERGEN

HBG052980.

InParanoid

O95425.

KO

K10369.

OMA

VNLTEQN.

PhylomeDB

O95425.

Enzyme and pathway databases

Pathway_Interaction_DB

ar_pathway. Coregulation of Androgen receptor activity.

Gene expression databases

ArrayExpress

O95425.

Bgee

O95425.

CleanEx

HS_SVIL.

Genevestigator

O95425.

GermOnline

ENSG00000197321. Homo sapiens.

Family and domain databases

Gene3D

1.10.950.10. 1 hit.

InterPro

IPR007123. Gelsolin_dom.
IPR015628. Supervillin.
IPR007122. Villin/Gelsolin.
IPR003128. Villin_headpiece.
[Graphical view]

PANTHER

PTHR11977. PTHR11977. 1 hit.
PTHR11977:SF4. PTHR11977:SF4. 1 hit.

Pfam

PF00626. Gelsolin. 1 hit.
PF02209. VHP. 1 hit.
[Graphical view]

PRINTS

PR00597. GELSOLIN.

SMART

SM00262. GEL. 4 hits.
SM00153. VHP. 1 hit.
[Graphical view]

SUPFAM

SSF47050. VHP. 1 hit.

PROSITE

PS51089. HP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SVIL. human.

EvolutionaryTrace

O95425.

GenomeRNAi

6840.

NextBio

26705.

SOURCE

Search...

Entry information

Entry name

SVIL_HUMAN

Accession

Primary (citable) accession number: O95425
Secondary accession number(s): D3DRW9 , O60611, O60612, Q5VZK5, Q5VZK6, Q9H1R7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 4, 2005
Last sequence update:	July 7, 2009
Last modified:	May 1, 2013
This is version 114 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.