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. Component of a complex composed at least of ACTB, AP2M1, AP2A1, AP2A2, MEGF10 and VIM. Interacts with HCV core protein.
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.
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.13 Inferred from direct assay. Source: UniProtKB intermediate filament Ref.29 Inferred from direct assay. Source: UniProtKB
Molecular function	protein binding Ref.29 Inferred from direct assay. Source: UniProtKB structural constituent of cytoskeleton Ref.29 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		3	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

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

Modified residue

5

1

Phosphoserine

Modified residue

7

1

Phosphoserine; by PKA and PKC

Modified residue

8

1

Phosphoserine

Modified residue

9

1

Phosphoserine; by PKC

Modified residue

10

1

Phosphoserine; by PKC

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

Modified residue

34

1

Phosphoserine; by PKC By similarity

Modified residue

38

1

Phosphotyrosine

Modified residue

39

1

Phosphoserine; by CaMK2, PKA and PKC

Modified residue

42

1

Phosphoserine; by PKC

Modified residue

47

1

Phosphoserine

Modified residue

51

1

Phosphoserine; by PKA and PKC By similarity

Modified residue

53

1

Phosphotyrosine

Modified residue

55

1

Phosphoserine

Modified residue

56

1

Phosphoserine

Modified residue

61

1

Phosphotyrosine

Modified residue

66

1

Phosphoserine; by PKA and PKC By similarity

Modified residue

72

1

Phosphoserine

Modified residue

73

1

Phosphoserine

Modified residue

83

1

Phosphoserine; by CaMK2 By similarity

Modified residue

117

1

Phosphotyrosine

Modified residue

214

1

Phosphoserine

Modified residue

412

1

Phosphoserine

Modified residue

420

1

Phosphoserine

Modified residue

430

1

Phosphoserine

Modified residue

446

1

Phosphothreonine

Modified residue

458

1

Phosphothreonine

Modified residue

459

1

Phosphoserine

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.11

Sequence conflict

197

1

E → G in CAG28618. Ref.6

Sequence conflict

201

1

N → S in AAA61281. Ref.15

Sequence conflict

265

1

L → S in AAA61281. Ref.15

Sequence conflict

278

1

S → I in AAA61281. Ref.15

Sequence conflict

339

1

S → C in AAA61281. Ref.15

Sequence conflict

350

1

N → K in AAA61281. Ref.15

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]	"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].
[9]	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].
[10]	"The status, quality, and expansion of the NIH full-length cD