UniProt Accession

 VIME_HUMAN; P08670; B0YJC2; D3DRU4; Q15867; Q15868; Q15869; Q548L2; Q6LER9; Q8N850; Q96ML2; Q9NTM3 

Genbank Protein ID

 M14144; X56134; AF328728; Z19554; AK056766; AK097336; AK290643; CR407690; AK222507; AK222602; EF445046; EF445046; AL133415; CH471072; CH471072; BC000163; BC030573; BC066956; X16478; M18895; M18888; M18889; M18890; M18891; M18892; M18893; M18894; M25246 

Genbank Nucleotide ID

 AAA61279.1; CAA39600.1; AAN09720.1; CAA79613.2; BAB71275.1; BAC05002.1; BAF83332.1; CAG28618.1; BAD96227.1; BAD96322.1; ACA06101.1; ACA06102.1; CAB87963.1; EAW86215.1; EAW86216.1; AAH00163.2; AAH30573.1; AAH66956.1; CAA34499.1; AAA61281.2; AAA61281.2; AAA61281.2; AAA61281.2; AAA61281.2; AAA61281.2; AAA61281.2; AAA61281.2; AAA61282.1 

Protein Name

 Vimentin 

Protein Synonyms/Alias

  

Gene Name

 VIM 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
97	DAINTEFKNTRTNEK	ubiquitination	[1, 2, 3, 4, 5, 6, 7]
104	KNTRTNEKVELQELN	acetylation	[8]
104	KNTRTNEKVELQELN	ubiquitination	[1, 2, 4, 5, 6, 7, 9]
120	RFANYIDKVRFLEQQ	acetylation	[8]
120	RFANYIDKVRFLEQQ	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 9]
129	RFLEQQNKILLAELE	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 9, 10]
139	LAELEQLKGQGKSRL	acetylation	[8]
139	LAELEQLKGQGKSRL	glycation	[11]
139	LAELEQLKGQGKSRL	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 9, 10]
143	EQLKGQGKSRLGDLY	glycation	[11]
143	EQLKGQGKSRLGDLY	ubiquitination	[1, 2, 4, 5, 7, 9]
168	VDQLTNDKARVEVER	glycation	[11]
168	VDQLTNDKARVEVER	ubiquitination	[1, 2, 4, 5, 7, 9]
188	DIMRLREKLQEEMLQ	ubiquitination	[1, 2, 4, 5, 6, 7, 9]
223	ARLDLERKVESLQEE	ubiquitination	[9]
235	QEEIAFLKKLHEEEI	acetylation	[8]
235	QEEIAFLKKLHEEEI	ubiquitination	[1, 2, 6, 7, 9]
236	EEIAFLKKLHEEEIQ	ubiquitination	[9]
262	QIDVDVSKPDLTAAL	glycation	[11]
282	QYESVAAKNLQEAEE	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 9]
292	QEAEEWYKSKFADLS	acetylation	[8]
292	QEAEEWYKSKFADLS	ubiquitination	[1, 2, 3, 4, 6, 7, 9]
294	AEEWYKSKFADLSEA	ubiquitination	[1, 2, 4, 5, 6, 7, 9]
313	NDALRQAKQESTEYR	glycation	[11]
313	NDALRQAKQESTEYR	ubiquitination	[1, 2, 5, 7, 9]
334	TCEVDALKGTNESLE	ubiquitination	[2, 3, 4, 5, 6, 9]
373	QDEIQNMKEEMARHL	acetylation	[8]
373	QDEIQNMKEEMARHL	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 9]
402	IEIATYRKLLEGEES	ubiquitination	[4, 7, 9, 12]
439	PLVDTHSKRTLLIKT	ubiquitination	[1, 3, 4, 5, 6, 7, 9, 13]
445	SKRTLLIKTVETRDG	acetylation	[8, 14]
445	SKRTLLIKTVETRDG	glycation	[11]
445	SKRTLLIKTVETRDG	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 9, 12, 13, 15]

Reference

 [1] 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]
 [2] 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]
 [3] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [10] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [11] Vimentin is the specific target in skin glycation. Structural prerequisites, functional consequences, and role in skin aging.
 Kueper T, Grune T, Prahl S, Lenz H, Welge V, Biernoth T, Vogt Y, Muhr GM, Gaemlich A, Jung T, Boemke G, Elsässer HP, Wittern KP, Wenck H, Stäb F, Blatt T.
 J Biol Chem. 2007 Aug 10;282(32):23427-36. [PMID: 17567584]
 [12] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [13] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [14] 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]
 [15] 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] 

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.
 MOD_RES 5 5 Phosphoserine.
 MOD_RES 7 7 Phosphoserine; by PKA and PKC.
 MOD_RES 8 8 Phosphoserine.
 MOD_RES 9 9 Phosphoserine; by PKC.
 MOD_RES 10 10 Phosphoserine; by PKC.
 MOD_RES 20 20 Phosphothreonine.
 MOD_RES 25 25 Phosphoserine.
 MOD_RES 26 26 Phosphoserine; by PKC (By similarity).
 MOD_RES 27 27 Phosphoserine.
 MOD_RES 29 29 Phosphoserine.
 MOD_RES 33 33 Phosphothreonine.
 MOD_RES 34 34 Phosphoserine.
 MOD_RES 38 38 Phosphotyrosine.
 MOD_RES 39 39 Phosphoserine; by CaMK2, PKA, PKC and
 MOD_RES 42 42 Phosphoserine; by PKC.
 MOD_RES 47 47 Phosphoserine.
 MOD_RES 49 49 Phosphoserine (By similarity).
 MOD_RES 51 51 Phosphoserine.
 MOD_RES 53 53 Phosphotyrosine.
 MOD_RES 55 55 Phosphoserine.
 MOD_RES 56 56 Phosphoserine; by CDK5 and CDK1.
 MOD_RES 61 61 Phosphotyrosine.
 MOD_RES 66 66 Phosphoserine; by PKA and PKC (By
 MOD_RES 72 72 Phosphoserine; by AURKB and ROCK2.
 MOD_RES 73 73 Phosphoserine.
 MOD_RES 83 83 Phosphoserine.
 MOD_RES 104 104 N6-acetyllysine.
 MOD_RES 117 117 Phosphotyrosine.
 MOD_RES 120 120 N6-acetyllysine.
 MOD_RES 139 139 N6-acetyllysine.
 MOD_RES 144 144 Phosphoserine.
 MOD_RES 214 214 Phosphoserine.
 MOD_RES 226 226 Phosphoserine.
 MOD_RES 261 261 Phosphoserine.
 MOD_RES 266 266 Phosphothreonine.
 MOD_RES 292 292 N6-acetyllysine.
 MOD_RES 299 299 Phosphoserine.
 MOD_RES 373 373 N6-acetyllysine.
 MOD_RES 402 402 N6-acetyllysine.
 MOD_RES 409 409 Phosphoserine.
 MOD_RES 412 412 Phosphoserine.
 MOD_RES 419 419 Phosphoserine.
 MOD_RES 420 420 Phosphoserine.
 MOD_RES 426 426 Phosphothreonine.
 MOD_RES 430 430 Phosphoserine.
 MOD_RES 436 436 Phosphothreonine.
 MOD_RES 445 445 N6-acetyllysine.
 MOD_RES 446 446 Phosphothreonine.
 MOD_RES 458 458 Phosphothreonine.
 MOD_RES 459 459 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Coiled coil; Complete proteome; Cytoplasm; Direct protein sequencing; Host-virus interaction; Intermediate filament; Phosphoprotein; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 466 AA 

Protein Sequence

Gene Ontology

 GO:0031252; C:cell leading edge; IEA:Compara.
 GO:0042995; C:cell projection; IEA:Compara.
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
 GO:0005882; C:intermediate filament; IDA:UniProtKB.
 GO:0005777; C:peroxisome; IDA:UniProtKB.
 GO:0005200; F:structural constituent of cytoskeleton; IDA:UniProtKB.
 GO:0005212; F:structural constituent of eye lens; IEA:Compara.
 GO:0014002; P:astrocyte development; IEA:Compara.
 GO:0060020; P:Bergmann glial cell differentiation; IEA:Compara.
 GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; TAS:Reactome.
 GO:0045109; P:intermediate filament organization; IEA:Compara.
 GO:0070307; P:lens fiber cell development; IEA:Compara.
 GO:0030049; P:muscle filament sliding; TAS:Reactome.
 GO:0010977; P:negative regulation of neuron projection development; IEA:Compara.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 

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