P08670 (VIME_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Vimentin

Gene names

Name:

VIM

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	466 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.36 Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. Ref.36
Subunit structure	Homopolymer assembled from elementary dimers. Interacts with HCV core protein. Interacts with LGSN and SYNM. Interacts (via rod region) with PLEC (via CH 1 domain) By similarity. Interacts with SLC6A4. Interacts with STK33. Interacts with LARP6. Interacts with RAB8B By similarity. Ref.23 Ref.27 Ref.31 Ref.36 Ref.41
Subcellular location	Cytoplasm Ref.38.
Tissue specificity	Highly expressed in fibroblasts, some expression in T- and B-lymphocytes, and little or no expression in Burkitt's lymphoma cell lines. Expressed in many hormone-independent mammary carcinoma cell lines. Ref.12 Ref.17
Domain	The central alpha-helical coiled-coil rod region mediates elementary homodimerization. Ref.41
Post-translational modification	Filament disassembly during mitosis is promoted by phosphorylation at Ser-55 as well as by nestin By similarity. One of the most prominent phosphoproteins in various cells of mesenchymal origin. Phosphorylation is enhanced during cell division, at which time vimentin filaments are significantly reorganized. Phosphorylation by PKN1 inhibits the formation of filaments. Phosphorylated at Ser-56 by CDK5 during neutrophil secretion in the cytoplasm. Phosphorylated by STK33. Ref.14 Ref.19 Ref.20 Ref.21 Ref.27 Ref.38
Sequence similarities	Belongs to the intermediate filament family.
Sequence caution	The sequence BAB71275.1 differs from that shown. Reason: Intron retention.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cytoplasm Intermediate filament
Domain	Coiled coil
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Bergmann glial cell differentiation Inferred from electronic annotation. Source: Compara astrocyte development Inferred from electronic annotation. Source: Compara cellular component disassembly involved in execution phase of apoptosis Traceable author statement. Source: Reactome intermediate filament organization Inferred from electronic annotation. Source: Compara lens fiber cell development Inferred from electronic annotation. Source: Compara muscle filament sliding Traceable author statement. Source: Reactome negative regulation of neuron projection development Inferred from electronic annotation. Source: Compara virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cell leading edge Inferred from electronic annotation. Source: Compara cell projection Inferred from electronic annotation. Source: Compara cytosol Inferred from direct assay Ref.31. Source: UniProtKB extracellular vesicular exosome Inferred from direct assay PubMed 21362503. Source: UniProtKB intermediate filament Inferred from direct assay Ref.40. Source: UniProtKB peroxisome Inferred from direct assay PubMed 17881773. Source: UniProtKB
Molecular_function	structural constituent of cytoskeleton Inferred from direct assay Ref.40. Source: UniProtKB structural constituent of eye lens Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		5	EBI-353844,EBI-353844
AKT1	P31749	29	EBI-353844,EBI-296087
AKT2	P31751	6	EBI-353844,EBI-296058
BCAS3	Q9H6U6	3	EBI-353844,EBI-6083685
CRMP1	Q14194	2	EBI-353844,EBI-473101
KAT7	O95251	3	EBI-353844,EBI-473199
TRIM16	O95361	3	EBI-353844,EBI-727384

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.13

Chain

2 – 466

465

Vimentin

PRO_0000063754

Regions

Region

2 – 95

94

Head

Region

96 – 407

312

Rod

Region

96 – 131

36

Coil 1A

Region

132 – 153

22

Linker 1

Region

154 – 245

92

Coil 1B

Region

246 – 268

23

Linker 12

Region

269 – 407

139

Coil 2

Region

408 – 466

59

Tail

Coiled coil

96 – 131

36

Ref.41

Coiled coil

154 – 245

92

Ref.41

Coiled coil

303 – 407

105

Ref.41

Sites

Site

351

1

Stutter

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.13

Modified residue

5

1

Phosphoserine Ref.21 Ref.30

Modified residue

7

1

Phosphoserine; by PKA and PKC Ref.21

Modified residue

8

1

Phosphoserine Ref.21

Modified residue

9

1

Phosphoserine; by PKC Ref.21

Modified residue

10

1

Phosphoserine; by PKC Ref.21

Modified residue

20

1

Phosphothreonine Ref.34

Modified residue

25

1

Phosphoserine Ref.30

Modified residue

26

1

Phosphoserine; by PKC By similarity

Modified residue

27

1

Phosphoserine

Modified residue

29

1

Phosphoserine

Modified residue

33

1

Phosphothreonine

Modified residue

34

1

Phosphoserine Ref.30

Modified residue

38

1

Phosphotyrosine

Modified residue

39

1

Phosphoserine; by CaMK2, PKA, PKC and ROCK2 Ref.21 Ref.30

Modified residue

42

1

Phosphoserine; by PKC Ref.21 Ref.30 Ref.34

Modified residue

47

1

Phosphoserine Ref.34

Modified residue

49

1

Phosphoserine By similarity

Modified residue

51

1

Phosphoserine Ref.30 Ref.32 Ref.34 Ref.37

Modified residue

53

1

Phosphotyrosine

Modified residue

55

1

Phosphoserine

Modified residue

56

1

Phosphoserine; by CDK5 and CDK1 Ref.14 Ref.25 Ref.30 Ref.32 Ref.34 Ref.38

Modified residue

61

1

Phosphotyrosine Ref.30 Ref.32

Modified residue

66

1

Phosphoserine; by PKA and PKC By similarity

Modified residue

72

1

Phosphoserine; by AURKB and ROCK2 Ref.20 Ref.21 Ref.30

Modified residue

73

1

Phosphoserine Ref.21 Ref.30 Ref.34

Modified residue

83

1

Phosphoserine Ref.30 Ref.34

Modified residue

104

1

N6-acetyllysine

Modified residue

117

1

Phosphotyrosine Ref.22

Modified residue

120

1

N6-acetyllysine Ref.33

Modified residue

139

1

N6-acetyllysine Ref.33

Modified residue

144

1

Phosphoserine Ref.30 Ref.34 Ref.37

Modified residue

214

1

Phosphoserine Ref.24 Ref.34

Modified residue

226

1

Phosphoserine Ref.34

Modified residue

261

1

Phosphoserine

Modified residue

266

1

Phosphothreonine

Modified residue

292

1

N6-acetyllysine

Modified residue

299

1

Phosphoserine Ref.34

Modified residue

373

1

N6-acetyllysine Ref.33

Modified residue

402

1

N6-acetyllysine

Modified residue

409

1

Phosphoserine Ref.30

Modified residue

412

1

Phosphoserine Ref.24 Ref.26 Ref.29 Ref.30 Ref.34

Modified residue

419

1

Phosphoserine Ref.34

Modified residue

420

1

Phosphoserine Ref.21 Ref.34

Modified residue

426

1

Phosphothreonine Ref.34

Modified residue

430

1

Phosphoserine Ref.21 Ref.34

Modified residue

436

1

Phosphothreonine Ref.34

Modified residue

445

1

N6-acetyllysine Ref.33

Modified residue

446

1

Phosphothreonine

Modified residue

458

1

Phosphothreonine Ref.21

Modified residue

459

1

Phosphoserine Ref.21 Ref.30 Ref.34 Ref.37

Experimental info

Sequence conflict

39 – 50

12

Missing in BAB71275. Ref.5

Sequence conflict

42

1

S → D in AAA61279. Ref.1

Sequence conflict

68 – 76

9

Missing in BAB71275. Ref.5

Sequence conflict

113

1

R → P in CAA34499. Ref.12

Sequence conflict

197

1

E → G in CAG28618. Ref.6

Sequence conflict

201

1

N → S in AAA61281. Ref.17

Sequence conflict

265

1

L → S in AAA61281. Ref.17

Sequence conflict

278

1

S → I in AAA61281. Ref.17

Sequence conflict

339

1

S → C in AAA61281. Ref.17

Sequence conflict

350

1

N → K in AAA61281. Ref.17

Sequence conflict

442

1

L → F in AAA61279. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

466

Helix Strand Turn

Details...

Helix

102 – 135

34

Helix

155 – 207

53

Helix

210 – 234

25

Turn

244 – 248

5

Helix

266 – 334

69

Helix

385 – 405

21

Sequences

	Sequence		Length	Mass (Da)
	P08670 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: BAB54026665B015A	FASTA	466	53,652
	10 20 30 40 50 60 MSTRSVSSSS YRRMFGGPGT ASRPSSSRSY VTTSTRTYSL GSALRPSTSR SLYASSPGGV 70 80 90 100 110 120 YATRSSAVRL RSSVPGVRLL QDSVDFSLAD AINTEFKNTR TNEKVELQEL NDRFANYIDK 130 140 150 160 170 180 VRFLEQQNKI LLAELEQLKG QGKSRLGDLY EEEMRELRRQ VDQLTNDKAR VEVERDNLAE 190 200 210 220 230 240 DIMRLREKLQ EEMLQREEAE NTLQSFRQDV DNASLARLDL ERKVESLQEE IAFLKKLHEE 250 260 270 280 290 300 EIQELQAQIQ EQHVQIDVDV SKPDLTAALR DVRQQYESVA AKNLQEAEEW YKSKFADLSE 310 320 330 340 350 360 AANRNNDALR QAKQESTEYR RQVQSLTCEV DALKGTNESL ERQMREMEEN FAVEAANYQD 370 380 390 400 410 420 TIGRLQDEIQ NMKEEMARHL REYQDLLNVK MALDIEIATY RKLLEGEESR ISLPLPNFSS 430 440 450 460 LNLRETNLDS LPLVDTHSKR TLLIKTVETR DGQVINETSQ HHDDLE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Coding sequence and growth regulation of the human vimentin gene." Ferrari S., Battini R., Kaczmarek L., Rittling S., Calabretta B., de Riel J.K., Philiponis V., Wei J.-F., Baserga R. Mol. Cell. Biol. 6:3614-3620(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Nucleotide sequence of cDNA covering the complete coding part of the human vimentin gene." Honore B., Madsen P., Basse B., Andersen A., Walbum E., Celis J.E., Leffers H. Nucleic Acids Res. 18:6692-6692(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"SEREX identification of new tumour-associated antigens in cutaneous T-cell lymphoma." Hartmann T.B., Thiel D., Dummer R., Schadendorf D., Eichmueller S. Br. J. Dermatol. 150:252-258(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lymphoma.
[4]	Zimbelmann R. Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Embryo, Placenta and Stomach.
[6]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Adipose tissue and Coronary artery.
[8]	NHLBI resequencing and genotyping service (RS&G) Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[9]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cervix, Placenta and Testis.
[12]	"Vimentin rather than keratin expression in some hormone-independent breast cancer cell lines and in oncogene-transformed mammary epithelial cells." Sommers C.L., Walker-Jones D., Heckford S.E., Worland P., Valverius E., Clark R., McCormick F., Stampfer M., Abularach S., Gelmann E.P. Cancer Res. 49:4258-4263(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-135, TISSUE SPECIFICITY. Tissue: Mammary carcinoma.
[13]	Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M. Submitted (MAY-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-11; 87-96; 129-138; 188-195; 223-234; 282-291; 322-333 AND 381-389, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY. Tissue: T-cell.
[14]	Bienvenut W.V., Fleming J., Leug H.Y. Submitted (JAN-2010) to UniProtKB Cited for: PROTEIN SEQUENCE OF 5-12; 14-45; 51-64; 72-78; 105-113; 123-143; 159-184; 187-217; 223-236; 271-292; 295-313; 322-390 AND 403-466, PHOSPHORYLATION AT SER-56, MASS SPECTROMETRY. Tissue: Hepatoma.
[15]	"Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2." Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E., Simpson R.J., Dorow D.S. Electrophoresis 18:588-598(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 17-25 AND 55-70. Tissue: Mammary carcinoma.
[16]	Lubec G., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 51-64; 79-97; 105-113; 130-139; 146-155; 176-184; 189-207; 223-235; 283-292; 295-304; 322-334; 346-373; 382-401 AND 411-439, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[17]	"Nucleotide sequence of the human vimentin gene and regulation of its transcription in tissues and cultured cells." Perreau J., Lilienbaum A., Vasseur M., Paulin D. Gene 62:7-16(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 113-466, TISSUE SPECIFICITY. Tissue: Fibroblast.
[18]	"Isolation of a human vimentin cDNA with a long 3'-noncoding region from a human osteosarcoma cell line (MG-63)." Gupta A.K., Aubin J.E., Waye M.M.Y. Gene 86:303-304(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 167-466. Tissue: Osteosarcoma.
[19]	"Domain-specific phosphorylation of vimentin and glial fibrillary acidic protein by PKN." Matsuzawa K., Kosako H., Inagaki N., Shibata H., Mukai H., Ono Y., Amano M., Kaibuchi K., Matsuura Y., Azuma I., Inagaki M. Biochem. Biophys. Res. Commun. 234:621-625(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION.
[20]	"Aurora-B regulates the cleavage furrow-specific vimentin phosphorylation in the cytokinetic process." Goto H., Yasui Y., Kawajiri A., Nigg E.A., Terada Y., Tatsuka M., Nagata K., Inagaki M. J. Biol. Chem. 278:8526-8530(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-72.
[21]	"Specific in vivo phosphorylation sites determine the assembly dynamics of vimentin intermediate filaments." Eriksson J.E., He T., Trejo-Skalli A.V., Harmala-Brasken A.-S., Hellman J., Chou Y.-H., Goldman R.D. J. Cell Sci. 117:919-932(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-5; SER-7; SER-8; SER-9; SER-10; SER-39; SER-42; SER-72; SER-73; SER-420; SER-430; THR-458 AND SER-459, MASS SPECTROMETRY.
[22]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-117, MASS SPECTROMETRY.
[23]	"Proteomic profiling of cellular proteins interacting with the hepatitis C virus core protein." Kang S.-M., Shin M.-J., Kim J.-H., Oh J.-W. Proteomics 5:2227-2237(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HCV CORE PROTEIN.
[24]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214 AND SER-412, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[25]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[26]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[27]	"The serine/threonine kinase Stk33 exhibits autophosphorylation and phosphorylates the intermediate filament protein Vimentin." Brauksiepe B., Mujica A.O., Herrmann H., Schmidt E.R. BMC Biochem. 9:25-25(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH STK33, PHOSPHORYLATION BY STK33.
[28]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[29]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[30]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-25; SER-34; SER-39; SER-42; SER-51; SER-56; TYR-61; SER-72; SER-73; SER-83; SER-144; SER-409; SER-412 AND SER-459, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[31]	"The cellular distribution of serotonin transporter is impeded on serotonin-altered vimentin network." Ahmed B.A., Bukhari I.A., Jeffus B.C., Harney J.T., Thyparambil S., Ziu E., Fraer M., Rusch N.J., Zimniak P., Lupashin V., Tang D., Kilic F. PLoS ONE 4:E4730-E4730(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SLC6A4.
[32]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-56 AND TYR-61, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[33]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-120; LYS-139; LYS-373 AND LYS-445, MASS SPECTROMETRY.
[34]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; SER-42; SER-47; SER-51; SER-56; SER-73; SER-83; SER-144; SER-214; SER-226; SER-299; SER-412; SER-419; SER-420; THR-426; SER-430; THR-436 AND SER-459, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[35]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[36]	"A novel role of vimentin filaments: binding and stabilization of collagen mRNAs." Challa A.A., Stefanovic B. Mol. Cell. Biol. 31:3773-3789(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN COLLAGEN MRNA STABILIZATION, INTERACTION WITH LARP6.
[37]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-144 AND SER-459, MASS SPECTROMETRY.
[38]	"Cdk5 mediates vimentin Ser56 phosphorylation during GTP-induced secretion by neutrophils." Lee K.Y., Liu L., Jin Y., Fu S.B., Rosales J.L. J. Cell. Physiol. 227:739-750(2012) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-56, SUBCELLULAR LOCATION.
[39]	"Divide-and-conquer crystallographic approach towards an atomic structure of intermediate filaments." Strelkov S.V., Herrmann H., Geisler N., Lustig A., Ivaninskii S., Zimbelmann R., Burkhard P., Aebi U. J. Mol. Biol. 306:773-781(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 102-138.
[40]	"Conserved segments 1A and 2B of the intermediate filament dimer: their atomic structures and role in filament assembly." Strelkov S.V., Herrmann H., Geisler N., Wedig T., Zimbelmann R., Aebi U., Burkhard P. EMBO J. 21:1255-1266(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 103-139 AND 328-411.
[41]	"Atomic structure of vimentin coil 2." Nicolet S., Herrmann H., Aebi U., Strelkov S.V. J. Struct. Biol. 170:369-376(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 263-334, COILED-COIL DOMAINS, SUBUNIT.
[42]	"Stabilization of vimentin coil2 fragment via an engineered disulfide." Chernyatina A.A., Strelkov S.V. J. Struct. Biol. 177:46-53(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 261-335 OF MUTANT CYS-265.
+	Additional computationally mapped references.

Web resources

Wikipedia

Vimentin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M14144 Genomic DNA. Translation: AAA61279.1.
X56134 mRNA. Translation: CAA39600.1.
AF328728 mRNA. Translation: AAN09720.1.
Z19554 mRNA. Translation: CAA79613.2.
AK056766 mRNA. Translation: BAB71275.1. Frameshift.
AK097336 mRNA. Translation: BAC05002.1.
AK290643 mRNA. Translation: BAF83332.1.
CR407690 mRNA. Translation: CAG28618.1.
AK222507 mRNA. Translation: BAD96227.1.
AK222602 mRNA. Translation: BAD96322.1.
EF445046 Genomic DNA. Translation: ACA06101.1.
EF445046 Genomic DNA. Translation: ACA06102.1.
AL133415 Genomic DNA. Translation: CAB87963.1.
CH471072 Genomic DNA. Translation: EAW86215.1.
CH471072 Genomic DNA. Translation: EAW86216.1.
BC000163 mRNA. Translation: AAH00163.2.
BC030573 mRNA. Translation: AAH30573.1.
BC066956 mRNA. Translation: AAH66956.1.
X16478 mRNA. Translation: CAA34499.1.
M18895 , M18888, M18889, M18890, M18891, M18892, M18893, M18894 Genomic DNA. Translation: AAA61281.2.
M25246 mRNA. Translation: AAA61282.1.

IPI

IPI00418471.

PIR

A25074. S13115.

RefSeq

NP_003371.2. NM_003380.3.

UniGene

Hs.455493.
Hs.691131.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GK4	X-ray	2.30	A/B/C/D/E/F	328-411	[»]
1GK6	X-ray	1.90	A/B	385-412	[»]
1GK7	X-ray	1.40	A	102-138	[»]
3G1E	X-ray	1.83	A/B	102-138	[»]
3KLT	X-ray	2.70	A/B/C/D	263-334	[»]
3S4R	X-ray	2.45	A/B	99-189	[»]
3SSU	X-ray	2.60	A/B	99-189	[»]
3SWK	X-ray	1.70	A/B	153-238	[»]
3TRT	X-ray	2.30	A/B	261-335	[»]
3UF1	X-ray	2.81	A/B/C/D	144-251	[»]

ProteinModelPortal

P08670.

ModBase

Search...

Protein-protein interaction databases

IntAct

P08670. 101 interactions.

MINT

MINT-118802.

PTM databases

PhosphoSite

P08670.

Polymorphism databases

DMDM

55977767.

2D gel databases

DOSAC-COBS-2DPAGE

P08670.

OGP

P08670.

REPRODUCTION-2DPAGE

IPI00418471.
P08670.

SWISS-2DPAGE

P08670.

UCD-2DPAGE

P08670.

Proteomic databases

PaxDb

P08670.

PeptideAtlas

P08670.

PRIDE

P08670.

Protocols and materials databases

DNASU

7431.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000224237; ENSP00000224237; ENSG00000026025.
ENST00000544301; ENSP00000446007; ENSG00000026025.

GeneID

7431.

KEGG

hsa:7431.

UCSC

uc001iou.2. human.

Organism-specific databases

CTD

7431.

GeneCards

GC10P017310.

H-InvDB

HIX0035657.

HGNC

HGNC:12692. VIM.

HPA

CAB000080.
CAB058687.
HPA001762.

MIM

193060. gene.

neXtProt

NX_P08670.

Orphanet

98984. Pulverulent cataract.

PharmGKB

PA37311.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG146769.

HOVERGEN

HBG013015.

InParanoid

P08670.

KO

K07606.

OMA

INTEFKA.

OrthoDB

EOG4GHZPD.

PhylomeDB

P08670.

Enzyme and pathway databases

Pathway_Interaction_DB

aurora_b_pathway. Aurora B signaling.
caspase_pathway. Caspase cascade in apoptosis.

Reactome

REACT_17044. Muscle contraction.
REACT_578. Apoptosis.

Gene expression databases

ArrayExpress

P08670.

Bgee

P08670.

Genevestigator

P08670.

GermOnline

ENSG00000026025. Homo sapiens.

Family and domain databases

InterPro

IPR016044. F.
IPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
[Graphical view]

PANTHER

PTHR23239. PTHR23239. 1 hit.

Pfam

PF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]

PROSITE

PS00226. IF. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

VIM. human.

EvolutionaryTrace

P08670.

GenomeRNAi

7431.

NextBio

29104.

PMAP-CutDB

P08670.

SOURCE

Search...

Entry information

Entry name

VIME_HUMAN

Accession

Primary (citable) accession number: P08670
Secondary accession number(s): B0YJC2 , D3DRU4, Q15867, Q15868, Q15869, Q548L2, Q6LER9, Q8N850, Q96ML2, Q9NTM3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 178 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.