UniProt Accession

 VIME_MOUSE; P20152; O08704; Q8CCH1 

Genbank Protein ID

 M24849; X56397; M26251; Z22526; X51438; Y07738; AK033175; D50805 

Genbank Nucleotide ID

 AAA40555.1; CAA39807.1; AAA40556.1; CAA80251.1; CAA35803.1; CAA69019.1; BAC28181.1; BAA19834.1 

Protein Name

 Vimentin 

Protein Synonyms/Alias

  

Gene Name

 Vim 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
104	KNTRTNEKVELQELN	acetylation	[1, 2, 3]
104	KNTRTNEKVELQELN	succinylation	[3]
104	KNTRTNEKVELQELN	ubiquitination	[4]
120	RFANYIDKVRFLEQQ	acetylation	[1, 2, 3]
120	RFANYIDKVRFLEQQ	succinylation	[3]
120	RFANYIDKVRFLEQQ	ubiquitination	[4]
129	RFLEQQNKILLAELE	acetylation	[1, 3]
129	RFLEQQNKILLAELE	succinylation	[3]
139	LAELEQLKGQGKSRL	acetylation	[1, 2, 3]
139	LAELEQLKGQGKSRL	succinylation	[3]
139	LAELEQLKGQGKSRL	ubiquitination	[4]
143	EQLKGQGKSRLGDLY	ubiquitination	[4]
168	VDQLTNDKARVEVER	acetylation	[3]
168	VDQLTNDKARVEVER	succinylation	[3]
168	VDQLTNDKARVEVER	ubiquitination	[4]
188	DIMRLREKLQEEMLQ	acetylation	[1, 3]
188	DIMRLREKLQEEMLQ	succinylation	[3]
188	DIMRLREKLQEEMLQ	ubiquitination	[4]
223	ARLDLERKVESLQEE	acetylation	[1, 3]
223	ARLDLERKVESLQEE	succinylation	[3]
223	ARLDLERKVESLQEE	ubiquitination	[4]
235	QEEIAFLKKLHDEEI	acetylation	[2, 3]
235	QEEIAFLKKLHDEEI	succinylation	[3]
235	QEEIAFLKKLHDEEI	ubiquitination	[4]
282	QYESVAAKNLQEAEE	ubiquitination	[4]
292	QEAEEWYKSKFADLS	ubiquitination	[4]
294	AEEWYKSKFADLSEA	acetylation	[1, 3]
294	AEEWYKSKFADLSEA	succinylation	[3]
294	AEEWYKSKFADLSEA	ubiquitination	[4]
334	TCEVDALKGTNESLE	acetylation	[1]
334	TCEVDALKGTNESLE	ubiquitination	[4]
373	QDEIQNMKEEMARHL	acetylation	[1, 3]
373	QDEIQNMKEEMARHL	succinylation	[3]
373	QDEIQNMKEEMARHL	ubiquitination	[4]
402	IEIATYRKLLEGEES	ubiquitination	[4]
439	PLVDTHSKRTLLIKT	acetylation	[1, 3]
439	PLVDTHSKRTLLIKT	succinylation	[3]
439	PLVDTHSKRTLLIKT	ubiquitination	[4]
445	SKRTLLIKTVETRDG	acetylation	[1, 3]
445	SKRTLLIKTVETRDG	succinylation	[3]
445	SKRTLLIKTVETRDG	ubiquitination	[4]

Reference

 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] 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]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 

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.
 MOD_RES 8 8 Phosphoserine (By similarity).
 MOD_RES 9 9 Phosphoserine; by PKC.
 MOD_RES 10 10 Phosphoserine; by PKC.
 MOD_RES 20 20 Phosphothreonine (By similarity).
 MOD_RES 21 21 Phosphoserine; by PKC.
 MOD_RES 25 25 Phosphoserine; by PKA and PKC.
 MOD_RES 26 26 Phosphoserine; by PKC.
 MOD_RES 29 29 Phosphoserine (By similarity).
 MOD_RES 33 33 Phosphothreonine (By similarity).
 MOD_RES 34 34 Phosphoserine; by PKC.
 MOD_RES 38 38 Phosphotyrosine (By similarity).
 MOD_RES 39 39 Phosphoserine; by CaMK2, PKA, PKC and
 MOD_RES 42 42 Phosphoserine; by PKC.
 MOD_RES 47 47 Phosphoserine; by PKA.
 MOD_RES 49 49 Phosphoserine.
 MOD_RES 51 51 Phosphoserine; by PKA and PKC.
 MOD_RES 53 53 Phosphotyrosine.
 MOD_RES 55 55 Phosphoserine (By similarity).
 MOD_RES 56 56 Phosphoserine; by CDK5 and CDK1 (By
 MOD_RES 61 61 Phosphotyrosine.
 MOD_RES 66 66 Phosphoserine; by PKA and PKC.
 MOD_RES 72 72 Phosphoserine; by AURKB and ROCK2.
 MOD_RES 73 73 Phosphoserine.
 MOD_RES 83 83 Phosphoserine; by CaMK2.
 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.
 MOD_RES 214 214 Phosphoserine.
 MOD_RES 226 226 Phosphoserine.
 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.
 MOD_RES 420 420 Phosphoserine.
 MOD_RES 426 426 Phosphothreonine (By similarity).
 MOD_RES 430 430 Phosphoserine.
 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.  

Keyword

 Acetylation; Coiled coil; Complete proteome; Cytoplasm; Direct protein sequencing; 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; IDA:MGI.
 GO:0042995; C:cell projection; IDA:MGI.
 GO:0005737; C:cytoplasm; IDA:MGI.
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0070062; C:extracellular vesicular exosome; IEA:Compara.
 GO:0005777; C:peroxisome; IEA:Compara.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0045098; C:type III intermediate filament; TAS:MGI.
 GO:0005200; F:structural constituent of cytoskeleton; IEA:Compara.
 GO:0005212; F:structural constituent of eye lens; IDA:MGI.
 GO:0014002; P:astrocyte development; IGI:MGI.
 GO:0060020; P:Bergmann glial cell differentiation; IMP:MGI.
 GO:0045109; P:intermediate filament organization; IGI:MGI.
 GO:0070307; P:lens fiber cell development; IDA:MGI.
 GO:0010977; P:negative regulation of neuron projection development; IGI:MGI. 

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