CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005935
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Vimentin 
Protein Synonyms/Alias
  
Gene Name
 Vim 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
143EQLKGQGKSRLGDLYmethylation[1]
168VDQLTNDKARVEVERubiquitination[2]
188DIMRLREKLQEEMLQubiquitination[2]
402IEIATYRKLLEGEESubiquitination[2]
439PLVDTHSKRTLLIKTubiquitination[2]
445SKRTLLIKTVETRDGubiquitination[2]
Reference
 [1] A method for the comprehensive proteomic analysis of membrane proteins.
 Wu CC, MacCoss MJ, Howell KE, Yates JR 3rd.
 Nat Biotechnol. 2003 May;21(5):532-8. [PMID: 12692561]
 [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
 Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. 
Sequence Annotation
 REGION 2 95 Head.
 REGION 96 407 Rod.
 REGION 96 131 Coil 1A.
 REGION 132 153 Linker 1.
 REGION 154 245 Coil 1B.
 REGION 246 268 Linker 12.
 REGION 269 407 Coil 2.
 REGION 408 466 Tail.
 MOD_RES 2 2 N-acetylserine (By similarity).
 MOD_RES 5 5 Phosphoserine (By similarity).
 MOD_RES 7 7 Phosphoserine; by PKA and PKC (By
 MOD_RES 8 8 Phosphoserine (By similarity).
 MOD_RES 9 9 Phosphoserine; by PKC (By similarity).
 MOD_RES 10 10 Phosphoserine; by PKC (By similarity).
 MOD_RES 20 20 Phosphothreonine (By similarity).
 MOD_RES 21 21 Phosphoserine (By similarity).
 MOD_RES 25 25 Phosphoserine (By similarity).
 MOD_RES 26 26 Phosphoserine (By similarity).
 MOD_RES 29 29 Phosphoserine (By similarity).
 MOD_RES 33 33 Phosphothreonine (By similarity).
 MOD_RES 34 34 Phosphoserine (By similarity).
 MOD_RES 38 38 Phosphotyrosine (By similarity).
 MOD_RES 39 39 Phosphoserine; by CaMK2, PKA, PKC and
 MOD_RES 42 42 Phosphoserine; by PKC (By similarity).
 MOD_RES 47 47 Phosphoserine; by PKA (By similarity).
 MOD_RES 49 49 Phosphoserine (By similarity).
 MOD_RES 51 51 Phosphoserine; by PKA and PKC (By
 MOD_RES 53 53 Phosphotyrosine (By similarity).
 MOD_RES 55 55 Phosphoserine (Probable).
 MOD_RES 56 56 Phosphoserine; by CDK5 and CDK1 (By
 MOD_RES 61 61 Phosphotyrosine (By similarity).
 MOD_RES 66 66 Phosphoserine; by PKA and PKC (By
 MOD_RES 72 72 Phosphoserine; by AURKB and ROCK2 (By
 MOD_RES 73 73 Phosphoserine (By similarity).
 MOD_RES 83 83 Phosphoserine; by CaMK2 (By similarity).
 MOD_RES 104 104 N6-acetyllysine (By similarity).
 MOD_RES 117 117 Phosphotyrosine (By similarity).
 MOD_RES 120 120 N6-acetyllysine (By similarity).
 MOD_RES 139 139 N6-acetyllysine (By similarity).
 MOD_RES 144 144 Phosphoserine (By similarity).
 MOD_RES 214 214 Phosphoserine (By similarity).
 MOD_RES 226 226 Phosphoserine (By similarity).
 MOD_RES 261 261 Phosphoserine (By similarity).
 MOD_RES 266 266 Phosphothreonine (By similarity).
 MOD_RES 292 292 N6-acetyllysine (By similarity).
 MOD_RES 299 299 Phosphoserine (By similarity).
 MOD_RES 373 373 N6-acetyllysine (By similarity).
 MOD_RES 402 402 N6-acetyllysine (By similarity).
 MOD_RES 409 409 Phosphoserine (By similarity).
 MOD_RES 412 412 Phosphoserine (By similarity).
 MOD_RES 419 419 Phosphoserine (By similarity).
 MOD_RES 420 420 Phosphoserine (By similarity).
 MOD_RES 426 426 Phosphothreonine (By similarity).
 MOD_RES 430 430 Phosphoserine (By similarity).
 MOD_RES 436 436 Phosphothreonine (By similarity).
 MOD_RES 445 445 N6-acetyllysine (By similarity).
 MOD_RES 446 446 Phosphothreonine (By similarity).
 MOD_RES 458 458 Phosphothreonine (By similarity).
 MOD_RES 459 459 Phosphoserine (By similarity).  
Keyword
 Acetylation; Coiled coil; Complete proteome; Cytoplasm; Direct protein sequencing; Intermediate filament; Nucleus; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 466 AA 
Protein Sequence
MSTRSVSSSS YRRMFGGSGT SSRPSSNRSY VTTSTRTYSL GSALRPSTSR SLYSSSPGGA 60
YVTRSSAVRL RSSMPGVRLL QDSVDFSLAD AINTEFKNTR TNEKVELQEL NDRFANYIDK 120
VRFLEQQNKI LLAELEQLKG QGKSRLGDLY EEEMRELRRQ VDQLTNDKAR VEVERDNLAE 180
DIMRLREKLQ EEMLQREEAE STLQSFRQDV DNASLARLDL ERKVESLQEE IAFLKKLHDE 240
EIQELQAQIQ EQHVQIDVDV SKPDLTAALR DVRQQYESVA AKNLQEAEEW YKSKFADLSE 300
AANRNNDALR QAKQESNEYR RQVQSLTCEV DALKGTNESL ERQMREMEEN FALEAANYQD 360
TIGRLQDEIQ NMKEEMARHL REYQDLLNVK MALDIEIATY RKLLEGEESR ISLPLPNFSS 420
LNLRETNLES LPLVDTHSKR TLLIKTVETR DGQVINETSQ HHDDLE 466 
Gene Ontology
 GO:0030424; C:axon; IDA:RGD.
 GO:0044297; C:cell body; IDA:RGD.
 GO:0005829; C:cytosol; IDA:RGD.
 GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
 GO:0045098; C:type III intermediate filament; TAS:RGD.
 GO:0051721; F:protein phosphatase 2A binding; IDA:RGD.
 GO:0005200; F:structural constituent of cytoskeleton; ISS:UniProtKB.
 GO:0007568; P:aging; IEP:RGD.
 GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEP:RGD.
 GO:0046697; P:decidualization; IEP:RGD.
 GO:0045444; P:fat cell differentiation; IEP:RGD.
 GO:0060252; P:positive regulation of glial cell proliferation; IMP:RGD.
 GO:0050770; P:regulation of axonogenesis; IDA:RGD.
 GO:1900147; P:regulation of Schwann cell migration; IDA:RGD.
 GO:0032355; P:response to estradiol stimulus; IEP:RGD.
 GO:0009314; P:response to radiation; IEP:RGD.
 GO:0010269; P:response to selenium ion; IEP:RGD.
 GO:0033280; P:response to vitamin D; IEP:RGD.
 GO:0010043; P:response to zinc ion; IEP:RGD.
 GO:0043403; P:skeletal muscle tissue regeneration; IEP:RGD. 
Interpro
 IPR016044; F.
 IPR001664; IF.
 IPR006821; Intermed_filament_DNA-bd.
 IPR018039; Intermediate_filament_CS. 
Pfam
 PF00038; Filament
 PF04732; Filament_head 
SMART
  
PROSITE
 PS00226; IF 
PRINTS