CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004659
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Vinculin 
Protein Synonyms/Alias
 Metavinculin; MV 
Gene Name
 VCL 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
173PGMTKMAKMIDERQQacetylation[1, 2]
199VNSMNTVKELLPVLIubiquitination[3]
219FVTTKNSKNQGIEEAubiquitination[3, 4, 5, 6, 7, 8, 9]
276ALASIDSKLNQAKGWacetylation[2, 10]
326REILGTCKMLGQMTDacetylation[10]
366GLDVLTAKVENAARKubiquitination[8]
444EISALTSKLADLRRQacetylation[10]
444EISALTSKLADLRRQubiquitination[3, 4, 7, 9]
464PEARALAKQVATALQubiquitination[4, 9]
476ALQNLQTKTNRAVANubiquitination[4, 5, 7, 8, 9]
496AAVHLEGKIEQAQRWacetylation[1, 2, 10]
581SQLQDSLKDLKARMQubiquitination[4, 9]
655AAVGTANKSTVEGIQubiquitination[5]
699YEHFETMKNQWIDNVacetylation[10]
699YEHFETMKNQWIDNVubiquitination[4, 5, 6, 8, 9]
720VDEAIDTKSLLDASEubiquitination[6]
778VENSEDPKFREAVKAubiquitination[7]
784PKFREAVKAASDELSubiquitination[8]
792AASDELSKTISPMVMubiquitination[5, 8]
802SPMVMDAKAVAGNISubiquitination[8]
815ISDPGLQKSFLDSGYubiquitination[3, 4, 5, 7, 8, 9]
983EATKWSSKGNDIIAAubiquitination[4, 7, 9]
1064PTISTQLKILSTVKAubiquitination[7]
1070LKILSTVKATMLGRTubiquitination[5, 7]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [3] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [7] 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]
 [8] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [9] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [10] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 
Functional Description
 Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell- surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion. 
Sequence Annotation
 REPEAT 259 369 1.
 REPEAT 370 479 2.
 REPEAT 480 589 3.
 REGION 2 835 N-terminal globular head.
 REGION 168 208 Talin-interaction (By similarity).
 REGION 259 589 3 X 112 AA tandem repeats.
 REGION 836 878 Linker (Pro-rich).
 REGION 879 1134 C-terminal tail.
 REGION 1003 1046 Facilitates phospholipid membrane
 REGION 1120 1134 Facilitates phospholipid membrane
 MOD_RES 173 173 N6-acetyllysine.
 MOD_RES 288 288 Phosphoserine.
 MOD_RES 290 290 Phosphoserine.
 MOD_RES 324 324 Phosphothreonine (By similarity).
 MOD_RES 346 346 Phosphoserine.
 MOD_RES 434 434 Phosphoserine.
 MOD_RES 496 496 N6-acetyllysine.
 MOD_RES 537 537 Phosphotyrosine (Potential).
 MOD_RES 721 721 Phosphoserine.
 MOD_RES 774 774 Phosphoserine (By similarity).
 MOD_RES 822 822 Phosphotyrosine.
 MOD_RES 1133 1133 Phosphotyrosine; by SRC-type Tyr-kinases.  
Keyword
 3D-structure; Acetylation; Actin-binding; Alternative splicing; Cardiomyopathy; Cell adhesion; Cell junction; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease mutation; Lipoprotein; Membrane; Palmitate; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1134 AA 
Protein Sequence
MPVFHTRTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL TAPVAAVQAA VSNLVRVGKE 60
TVQTTEDQIL KRDMPPAFIK VENACTKLVQ AAQMLQSDPY SVPARDYLID GSRGILSGTS 120
DLLLTFDEAE VRKIIRVCKG ILEYLTVAEV VETMEDLVTY TKNLGPGMTK MAKMIDERQQ 180
ELTHQEHRVM LVNSMNTVKE LLPVLISAMK IFVTTKNSKN QGIEEALKNR NFTVEKMSAE 240
INEIIRVLQL TSWDEDAWAS KDTEAMKRAL ASIDSKLNQA KGWLRDPSAS PGDAGEQAIR 300
QILDEAGKVG ELCAGKERRE ILGTCKMLGQ MTDQVADLRA RGQGSSPVAM QKAQQVSQGL 360
DVLTAKVENA ARKLEAMTNS KQSIAKKIDA AQNWLADPNG GPEGEEQIRG ALAEARKIAE 420
LCDDPKERDD ILRSLGEISA LTSKLADLRR QGKGDSPEAR ALAKQVATAL QNLQTKTNRA 480
VANSRPAKAA VHLEGKIEQA QRWIDNPTVD DRGVGQAAIR GLVAEGHRLA NVMMGPYRQD 540
LLAKCDRVDQ LTAQLADLAA RGEGESPQAR ALASQLQDSL KDLKARMQEA MTQEVSDVFS 600
DTTTPIKLLA VAATAPPDAP NREEVFDERA ANFENHSGKL GATAEKAAAV GTANKSTVEG 660
IQASVKTARE LTPQVVSAAR ILLRNPGNQA AYEHFETMKN QWIDNVEKMT GLVDEAIDTK 720
SLLDASEEAI KKDLDKCKVA MANIQPQMLV AGATSIARRA NRILLVAKRE VENSEDPKFR 780
EAVKAASDEL SKTISPMVMD AKAVAGNISD PGLQKSFLDS GYRILGAVAK VREAFQPQEP 840
DFPPPPPDLE QLRLTDELAP PKPPLPEGEV PPPRPPPPEE KDEEFPEQKA GEVINQPMMM 900
AARQLHDEAR KWSSKPGIPA AEVGIGVVAE ADAADAAGFP VPPDMEDDYE PELLLMPSNQ 960
PVNQPILAAA QSLHREATKW SSKGNDIIAA AKRMALLMAE MSRLVRGGSG TKRALIQCAK 1020
DIAKASDEVT RLAKEVAKQC TDKRIRTNLL QVCERIPTIS TQLKILSTVK ATMLGRTNIS 1080
DEESEQATEM LVHNAQNLMQ SVKETVREAE AASIKIRTDA GFTLRWVRKT PWYQ 1134 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; IEA:InterPro.
 GO:0005913; C:cell-cell adherens junction; IDA:BHF-UCL.
 GO:0043034; C:costamere; ISS:UniProtKB.
 GO:0005856; C:cytoskeleton; TAS:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005576; C:extracellular region; TAS:Reactome.
 GO:0005916; C:fascia adherens; IEA:Compara.
 GO:0005925; C:focal adhesion; ISS:UniProtKB.
 GO:0043234; C:protein complex; IDA:UniProtKB.
 GO:0042383; C:sarcolemma; IEA:Compara.
 GO:0030018; C:Z disc; IEA:Compara.
 GO:0003779; F:actin binding; IDA:BHF-UCL.
 GO:0008013; F:beta-catenin binding; ISS:BHF-UCL.
 GO:0045296; F:cadherin binding; ISS:BHF-UCL.
 GO:0005198; F:structural molecule activity; IEA:InterPro.
 GO:0034333; P:adherens junction assembly; IMP:BHF-UCL.
 GO:0043297; P:apical junction assembly; IMP:UniProtKB.
 GO:0007160; P:cell-matrix adhesion; TAS:BHF-UCL.
 GO:0006928; P:cellular component movement; TAS:UniProtKB.
 GO:0090136; P:epithelial cell-cell adhesion; IMP:BHF-UCL.
 GO:0030032; P:lamellipodium assembly; ISS:UniProtKB.
 GO:0002009; P:morphogenesis of an epithelium; IMP:BHF-UCL.
 GO:0006936; P:muscle contraction; TAS:Reactome.
 GO:0030336; P:negative regulation of cell migration; TAS:UniProtKB.
 GO:0030168; P:platelet activation; TAS:Reactome.
 GO:0002576; P:platelet degranulation; TAS:Reactome.
 GO:0034394; P:protein localization to cell surface; IMP:BHF-UCL. 
Interpro
 IPR017997; Vinculin.
 IPR006077; Vinculin/catenin.
 IPR000633; Vinculin_CS. 
Pfam
 PF01044; Vinculin 
SMART
  
PROSITE
 PS00663; VINCULIN_1
 PS00664; VINCULIN_2 
PRINTS
 PR00806; VINCULIN.