CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010584
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Vinculin 
Protein Synonyms/Alias
 Metavinculin 
Gene Name
 Vcl 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
59SNLVRVGKETVQTTEacetylation[1]
71TTEDQILKRDMPPAFacetylation[1]
170NLGPGMTKMAKMIDEacetylation[1]
173PGMTKMAKMIDERQQacetylation[1]
219FVTTKNSKNQGIEEAubiquitination[2]
228QGIEEALKNRNFTVGacetylation[1]
276ALASIDSKLNQAKGWacetylation[1]
366GLDVLTAKVENAARKacetylation[1]
444EIAALTSKLGDLRRQacetylation[1]
496AAVHLEGKIEQAQRWacetylation[1]
699YEHFETMKNQWIDNVacetylation[1]
732ASEEAIKKDLDKCKVacetylation[1]
768NRILLVAKREVENSEacetylation[1]
778VENSEDPKFREAVKAacetylation[1]
784PKFREAVKAASDELSacetylation[1]
802SPMVMDAKAVAGNISacetylation[1]
815ISDPGLQKSFLDSGYacetylation[1]
915EARKWSSKGNDIIAAacetylation[1]
924NDIIAAAKRMALLMAacetylation[1]
952RALIQCAKDIAKASDacetylation[1]
956QCAKDIAKASDEVTRacetylation[1]
966DEVTRLAKEVAKQCTacetylation[1]
1035QNLMQSVKETVREAEacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [2] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113] 
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 (By similarity). 
Sequence Annotation
 REPEAT 259 369 1.
 REPEAT 370 479 2.
 REPEAT 480 589 3.
 REGION 2 835 N-terminal globular head (By similarity).
 REGION 168 208 Talin-interaction (By similarity).
 REGION 259 589 3 X 112 AA tandem repeats.
 REGION 836 878 Linker (Pro-rich) (By similarity).
 REGION 879 1066 C-terminal tail (By similarity).
 REGION 935 978 Facilitates phospholipid membrane
 REGION 1052 1066 Facilitates phospholipid membrane
 MOD_RES 173 173 N6-acetyllysine (By similarity).
 MOD_RES 290 290 Phosphoserine.
 MOD_RES 324 324 Phosphothreonine (By similarity).
 MOD_RES 346 346 Phosphoserine (By similarity).
 MOD_RES 434 434 Phosphoserine (By similarity).
 MOD_RES 496 496 N6-acetyllysine (By similarity).
 MOD_RES 721 721 Phosphoserine (By similarity).
 MOD_RES 774 774 Phosphoserine (By similarity).
 MOD_RES 822 822 Phosphotyrosine (By similarity).
 MOD_RES 1065 1065 Phosphotyrosine; by SRC-type Tyr-kinases  
Keyword
 Acetylation; Actin-binding; Cell adhesion; Cell junction; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Lipoprotein; Membrane; Palmitate; Phosphoprotein; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1066 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 NFTVGKMSAE 240
INEIIRVLQL TSWDEDAWAS KDTEAMKRAL ASIDSKLNQA KGWLRDPNAS PGDAGEQAIR 300
QILDEAGKVG ELCAGKERRE ILGTCKMLGQ MTDQVADLRA RGQGASPVAM QKAQQVSQGL 360
DVLTAKVENA ARKLEAMTNS KQSIAKKIDA AQNWLADPNG GPEGEEQIRG ALAEARKIAE 420
LCDDPKERDD ILRSLGEIAA LTSKLGDLRR QGKGDSPEAR ALAKQVATAL QNLQTKTNRA 480
VANSRPAKAA VHLEGKIEQA QRWIDNPTVD DRGVGQAAIR GLVAEGHRLA NVMMGPYRQD 540
LLAKCDRVDQ LAAQLADLAA RGEGESPQAR ALASQLQDSL KDLKTQMQEA MTQEVSDVFS 600
DTTTPIKLLA VAATAPPDAP NREEVFDERA ANFENHSGRL GATAEKAAAV GAANKSTVEG 660
IQASVKTARE LTPQVISAAR 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 KWSSKGNDII AAAKRMALLM AEMSRLVRGG SGTKRALIQC AKDIAKASDE 960
VTRLAKEVAK QCTDKRIRTN LLQVCERIPT ISTQLKILST VKATMLGRTN ISDEESEQAT 1020
EMLVHNAQNL MQSVKETVRE AEAASIKIRT DAGFTLRWVR KTPWYQ 1066 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; IEA:InterPro.
 GO:0043034; C:costamere; IEA:Compara.
 GO:0005916; C:fascia adherens; IEA:Compara.
 GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
 GO:0014704; C:intercalated disc; IDA:BHF-UCL.
 GO:0043234; C:protein complex; IEA:Compara.
 GO:0042383; C:sarcolemma; IDA:BHF-UCL.
 GO:0030018; C:Z disc; IDA:BHF-UCL.
 GO:0005198; F:structural molecule activity; IEA:InterPro.
 GO:0034333; P:adherens junction assembly; IEA:Compara.
 GO:0043297; P:apical junction assembly; IEA:Compara.
 GO:0090136; P:epithelial cell-cell adhesion; IEA:Compara.
 GO:0030032; P:lamellipodium assembly; IEA:Compara.
 GO:0002009; P:morphogenesis of an epithelium; IEA:Compara.
 GO:0034394; P:protein localization to cell surface; IEA:Compara.
 GO:0030334; P:regulation of cell migration; IEA:Compara. 
Interpro
 IPR017997; Vinculin.
 IPR006077; Vinculin/catenin.
 IPR000633; Vinculin_CS. 
Pfam
 PF01044; Vinculin 
SMART
  
PROSITE
 PS00663; VINCULIN_1
 PS00664; VINCULIN_2 
PRINTS
 PR00806; VINCULIN.