Reviewed, UniProtKB/Swiss-Prot P08670 (VIME_HUMAN)

Names and origin

Protein names

Recommended name:
    Vimentin

Gene names

Name:

VIM

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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.
Subunit structure	Homopolymer. Interacts with HCV core protein. Interacts with LGSN and SYNM By similarity.
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.16
Post-translational modification	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.
Sequence similarities	Belongs to the intermediate filament family.
Sequence caution	The sequence BAB71275.1 differs from that shown. Reason: Miscellaneous discrepancy. Intron retention.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Intermediate filament
Domain	Coiled coil
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cell motion Traceable author statement. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Ref.14 Inferred from direct assay. Source: UniProtKB intermediate filament Ref.32 Inferred from direct assay. Source: UniProtKB
Molecular function	protein binding Ref.32 Inferred from direct assay. Source: UniProtKB structural constituent of cytoskeleton Ref.32 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-353844,EBI-353844
CRMP1	Q14194	1	EBI-353844,EBI-473101
MDM2	Q00987	1	EBI-353844,EBI-389668
MYST2	O95251	2	EBI-353844,EBI-473199

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

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.13

Modified residue

5

1

Phosphoserine Ref.18 Ref.29

Modified residue

7

1

Phosphoserine; by PKA and PKC Ref.18

Modified residue

8

1

Phosphoserine Ref.18

Modified residue

9

1

Phosphoserine; by PKC Ref.18

Modified residue

10

1

Phosphoserine; by PKC Ref.18

Modified residue

25

1

Phosphoserine; by PKA and PKC By similarity

Modified residue

26

1

Phosphoserine; by PKC By similarity

Modified residue

27

1

Phosphoserine Ref.21

Modified residue

34

1

Phosphoserine Ref.29

Modified residue

38

1

Phosphotyrosine Ref.24

Modified residue

39

1

Phosphoserine; by CaMK2, PKA and PKC Ref.18 Ref.29 Ref.26

Modified residue

42

1

Phosphoserine; by PKC Ref.18 Ref.29

Modified residue

47

1

Phosphoserine Ref.26

Modified residue

49

1

Phosphoserine By similarity

Modified residue

51

1

Phosphoserine; by PKA and PKC By similarity

Modified residue

53

1

Phosphotyrosine Ref.24

Modified residue

55

1

Phosphoserine Ref.26

Modified residue

56

1

Phosphoserine Ref.29 Ref.21 Ref.26 Ref.22 Ref.23 Ref.25 Ref.28

Modified residue

61

1

Phosphotyrosine Ref.29 Ref.24 Ref.26

Modified residue

66

1

Phosphoserine; by PKA and PKC By similarity

Modified residue

72

1

Phosphoserine Ref.18 Ref.29

Modified residue

73

1

Phosphoserine Ref.18 Ref.29 Ref.21

Modified residue

83

1

Phosphoserine Ref.29

Modified residue

117

1

Phosphotyrosine Ref.24 Ref.19

Modified residue

144

1

Phosphoserine Ref.29

Modified residue

214

1

Phosphoserine Ref.21

Modified residue

226

1

Phosphoserine Ref.29

Modified residue

299

1

Phosphoserine Ref.29

Modified residue

409

1

Phosphoserine Ref.29

Modified residue

412

1

Phosphoserine Ref.29 Ref.21 Ref.25 Ref.28 Ref.27

Modified residue

419

1

Phosphoserine By similarity

Modified residue

420

1

Phosphoserine Ref.18

Modified residue

430

1

Phosphoserine Ref.18 Ref.26

Modified residue

446

1

Phosphothreonine Ref.25

Modified residue

458

1

Phosphothreonine Ref.18 Ref.26

Modified residue

459

1

Phosphoserine Ref.18 Ref.29 Ref.26 Ref.25 Ref.28

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.16

Sequence conflict

265

1

L → S in AAA61281. Ref.16

Sequence conflict

278

1

S → I in AAA61281. Ref.16

Sequence conflict

339

1

S → C in AAA61281. Ref.16

Sequence conflict

350

1

N → K in AAA61281. Ref.16

Sequence conflict

442

1

L → F in AAA61279. Ref.1

Secondary structure

1

.

.

.

.

.

466

Helix Strand Turn

Details...

Helix

102 – 135

34

Helix

329 – 404

76

Sequences

	Sequence		Length	Mass (Da)
	P08670-1 [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: 3467175] [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: 2251132] [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: 14996095] [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: 14702039] [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: 15164054] [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: 15489334] [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: 2472876] [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]	"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: 9150946] [Abstract] Cited for: PROTEIN SEQUENCE OF 17-25 AND 55-70. Tissue: Mammary carcinoma.
[15]	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.
[16]	"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: 3371665] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 113-466, TISSUE SPECIFICITY. Tissue: Fibroblast.
[17]	"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: 2323579] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 167-466. Tissue: Osteosarcoma.
[18]	"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: 14762106] [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.
[19]	"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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-117, MASS SPECTROMETRY.
[20]	"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: 15846844] [Abstract] Cited for: INTERACTION WITH HCV CORE PROTEIN.
[21]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-56; SER-73; SER-214 AND SER-412, MASS SPECTROMETRY. Tissue: Epithelium.
[22]	"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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, MASS SPECTROMETRY. Tissue: Epithelium.
[23]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, MASS SPECTROMETRY. Tissue: Epithelium.
[24]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-38; TYR-53; TYR-61 AND TYR-117, MASS SPECTROMETRY.
[25]	"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: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56; SER-412; THR-446 AND SER-459, MASS SPECTROMETRY. Tissue: Epithelium.
[26]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-47; SER-55; SER-56; TYR-61; SER-430; THR-458 AND SER-459, MASS SPECTROMETRY.
[27]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-412, MASS SPECTROMETRY.
[28]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56; SER-412 AND SER-459, MASS SPECTROMETRY.
[29]	"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: 18669648] [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-226; SER-299; SER-409; SER-412 AND SER-459, MASS SPECTROMETRY.
[30]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[31]	"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: 11243787] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 102-138.
[32]	"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: 11889032] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 103-139 AND 328-411.
+	Additional computationally mapped references.

Web resources

Wikipedia

Vimentin entry

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.
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.

UniGene

Hs.642813

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P08670. 86 interactions.

PTM databases

PhosphoSite

P08670.

2-D gel databases

SWISS-2DPAGE

P08670.

Aarhus/Ghent-2DPAGE

8417. IEF.

Cornea-2DPAGE

P08670.

DOSAC-COBS-2DPAGE

P08670.

HSC-2DPAGE

P08670.

OGP

P08670.

PHCI-2DPAGE

P08670.

REPRODUCTION-2DPAGE

IPI00418471.
P08670.

Proteomic databases

PeptideAtlas

P08670.

PRIDE

P08670.

Genome annotation databases

Ensembl

ENSG00000026025. Homo sapiens. [Contig view]

GeneID

7431.

KEGG

hsa:7431.

Organism-specific databases

GeneCards

GC10P017310.

H-InvDB

HIX0008682.
HIX0035657.

HGNC

HGNC:12692. VIM.

HPA

CAB000080.
HPA001762.

MIM

193060. gene.

PharmGKB

PA37311.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P08670.

OMA

P08670. ANRTNEK.

Enzyme and pathway databases

Pathway_Interaction_DB

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

Reactome

REACT_578. Apoptosis.

Gene expression databases

ArrayExpress

P08670.

Bgee

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. IF. 1 hit.

Pfam

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

PROSITE

PS00226. IF. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

29104.

PMAP-CutDB

P08670.

SOURCE

Search...

Entry information

Entry name

VIME_HUMAN

Accession

Primary (citable) accession number: P08670
Secondary accession number(s): B0YJC2 , 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:	June 16, 2009
This is version 132 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)