CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001599
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Supervillin 
Protein Synonyms/Alias
 Archvillin; p205/p250 
Gene Name
 SVIL 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
824EKLALFNKLSQPVSKubiquitination[1]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 
Functional Description
 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). 
Sequence Annotation
 REPEAT 1441 1540 Gelsolin-like 1.
 REPEAT 1560 1682 Gelsolin-like 2.
 REPEAT 1752 1862 Gelsolin-like 3.
 REPEAT 1881 1982 Gelsolin-like 4.
 REPEAT 2015 2122 Gelsolin-like 5.
 DOMAIN 2151 2214 HP.
 REGION 1 174 Interaction with MYLK (By similarity).
 REGION 1419 1687 Interaction with NEB.
 MOD_RES 50 50 Phosphoserine.
 MOD_RES 221 221 Phosphoserine.
 MOD_RES 245 245 Phosphoserine.
 MOD_RES 270 270 Phosphoserine.
 MOD_RES 673 673 Phosphoserine (By similarity).
 MOD_RES 675 675 Phosphoserine (By similarity).
 MOD_RES 707 707 Phosphoserine.
 MOD_RES 852 852 Phosphothreonine.
 MOD_RES 914 914 Phosphoserine.
 MOD_RES 920 920 Phosphoserine.
 MOD_RES 924 924 Phosphoserine.
 MOD_RES 968 968 Phosphoserine.
 MOD_RES 1000 1000 Phosphoserine (By similarity).
 MOD_RES 1052 1052 Phosphoserine (By similarity).
 MOD_RES 1111 1111 Phosphothreonine.
 MOD_RES 1120 1120 Phosphoserine.
 MOD_RES 1225 1225 Phosphoserine.
 MOD_RES 1230 1230 Phosphothreonine.
 MOD_RES 1322 1322 Phosphoserine.  
Keyword
 3D-structure; Actin-binding; Alternative splicing; Calcium; Cell junction; Cell membrane; Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2214 AA 
Protein Sequence
MKRKERIARR LEGIENDTQP ILLQSCTGLV THRLLEEDTP RYMRASDPAS PHIGRSNEEE 60
ETSDSSLEKQ TRSKYCTETS GVHGDSPYGS GTMDTHSLES KAERIARYKA ERRRQLAEKY 120
GLTLDPEADS EYLSRYTKSR KEPDAVEKRG GKSDKQEESS RDASSLYPGT ETMGLRTCAG 180
ESKDYALHVG DGSSDPEVLL NIENQRRGQE LSATRQAHDL SPAAESSSTF SFSGRDSSFT 240
EVPRSPKHAH SSSLQQAASR SPSFGDPQLS PEARPSTGKP KHEWFLQKDS EGDTPSLINW 300
PSRVKVREKL VKEESARNSP ELASESVTQR RHQPAPVHYV SFQSEHSAFD RVPSKAAGST 360
RQPIRGYVQP ADTGHTAKLV TPETPENASE CSWVASATQN VPKPPSLTVL EGDGRDSPVL 420
HVCESKAEEE EGEGEGEEKE EDVCFTEALE QSKKTLLALE GDGLVRSPED PSRNEDFGKP 480
AVSTVTLEHQ KELENVAQPP QAPHQPTERT GRSEMVLYIQ SEPVSQDAKP TGHNREASKK 540
RKVRTRSLSD FTGPPQLQAL KYKDPASRRE LELPSSKTEG PYGEISMLDT KVSVAQLRSA 600
FLASANACRR PELKSRVERS AEGPGLPTGV ERERGSRKPR RYFSPGESRK TSERFRTQPI 660
TSAERKESDR CTSHSETPTV DDEEKVDERA KLSVAAKRLL FREMEKSFDE QNVPKRRSRN 720
TAVEQRLRRL QDRSLTQPIT TEEVVIAATE PIPASCSGGT HPVMARLPSP TVARSAVQPA 780
RLQASAHQKA LAKDQTNEGK ELAEQGEPDS STLSLAEKLA LFNKLSQPVS KAISTRNRID 840
TRQRRMNARY QTQPVTLGEV EQVQSGKLIP FSPAVNTSVS TVASTVAPMY AGDLRTKPPL 900
DHNASATDYK FSSSIENSDS PVRSILKSQA WQPLVEGSEN KGMLREYGET ESKRALTGRD 960
SGMEKYGSFE EAEASYPILN RAREGDSHKE SKYAVPRRGS LERANPPITH LGDEPKEFSM 1020
AKMNAQGNLD LRDRLPFEEK VEVENVMKRK FSLRAAEFGE PTSEQTGTAA GKTIAQTTAP 1080
VSWKPQDSSE QPQEKLCKNP CAMFAAGEIK TPTGEGLLDS PSKTMSIKER LALLKKSGEE 1140
DWRNRLSRRQ EGGKAPASSL HTQEAGRSLI KKRVTESRES QMTIEERKQL ITVREEAWKT 1200
RGRGAANDST QFTVAGRMVK KGLASPTAIT PVASPICGKT RGTTPVSKPL EDIEARPDMQ 1260
LESDLKLDRL ETFLRRLNNK VGGMHETVLT VTGKSVKEVM KPDDDETFAK FYRSVDYNMP 1320
RSPVEMDEDF DVIFDPYAPK LTSSVAEHKR AVRPKRRVQA SKNPLKMLAA REDLLQEYTE 1380
QRLNVAFMES KRMKVEKMSS NSNFSEVTLA GLASKENFSN VSLRSVNLTE QNSNNSAVPY 1440
KRLMLLQIKG RRHVQTRLVE PRASALNSGD CFLLLSPHCC FLWVGEFANV IEKAKASELA 1500
TLIQTKRELG CRATYIQTIE EGINTHTHAA KDFWKLLGGQ TSYQSAGDPK EDELYEAAII 1560
ETNCIYRLMD DKLVPDDDYW GKIPKCSLLQ PKEVLVFDFG SEVYVWHGKE VTLAQRKIAF 1620
QLAKHLWNGT FDYENCDINP LDPGECNPLI PRKGQGRPDW AIFGRLTEHN ETILFKEKFL 1680
DWTELKRSNE KNPGELAQHK EDPRTDVKAY DVTRMVSMPQ TTAGTILDGV NVGRGYGLVE 1740
GHDRRQFEIT SVSVDVWHIL EFDYSRLPKQ SIGQFHEGDA YVVKWKFMVS TAVGSRQKGE 1800
HSVRAAGKEK CVYFFWQGRH STVSEKGTSA LMTVELDEER GAQVQVLQGK EPPCFLQCFQ 1860
GGMVVHSGRR EEEEENVQSE WRLYCVRGEV PVEGNLLEVA CHCSSLRSRT SMVVLNVNKA 1920
LIYLWHGCKA QAHTKEVGRT AANKIKEQCP LEAGLHSSSK VTIHECDEGS EPLGFWDALG 1980
RRDRKAYDCM LQDPGSFNFA PRLFILSSSS GDFAATEFVY PARAPSVVSS MPFLQEDLYS 2040
APQPALFLVD NHHEVYLWQG WWPIENKITG SARIRWASDR KSAMETVLQY CKGKNLKKPA 2100
PKSYLIHAGL EPLTFTNMFP SWEHREDIAE ITEMDTEVSN QITLVEDVLA KLCKTIYPLA 2160
DLLARPLPEG VDPLKLEIYL TDEDFEFALD MTRDEYNALP AWKQVNLKKA KGLF 2214 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; NAS:UniProtKB.
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0043034; C:costamere; IDA:UniProtKB.
 GO:0071437; C:invadopodium; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
 GO:0051015; F:actin filament binding; IDA:UniProtKB.
 GO:0007010; P:cytoskeleton organization; IEA:InterPro.
 GO:0007519; P:skeletal muscle tissue development; IMP:UniProtKB. 
Interpro
 IPR007123; Gelsolin_dom.
 IPR015628; Supervillin.
 IPR007122; Villin/Gelsolin.
 IPR003128; Villin_headpiece. 
Pfam
 PF00626; Gelsolin
 PF02209; VHP 
SMART
 SM00262; GEL
 SM00153; VHP 
PROSITE
 PS51089; HP 
PRINTS
 PR00597; GELSOLIN.