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P31000

- VIME_RAT

UniProt

P31000 - VIME_RAT

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Protein

Vimentin

Gene

Vim

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication
Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei351 – 3511StutterBy similarity

GO - Molecular functioni

  1. kinase binding Source: RGD
  2. protein kinase binding Source: RGD
  3. protein phosphatase 2A binding Source: RGD
  4. structural constituent of cytoskeleton Source: UniProtKB
  5. structural molecule activity Source: RGD

GO - Biological processi

  1. aging Source: RGD
  2. cellular response to fibroblast growth factor stimulus Source: RGD
  3. decidualization Source: RGD
  4. fat cell differentiation Source: RGD
  5. positive regulation of glial cell proliferation Source: RGD
  6. regulation of axonogenesis Source: RGD
  7. regulation of Schwann cell migration Source: RGD
  8. response to estradiol Source: RGD
  9. response to radiation Source: RGD
  10. response to selenium ion Source: RGD
  11. response to vitamin D Source: RGD
  12. response to zinc ion Source: RGD
  13. skeletal muscle tissue regeneration Source: RGD
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Vimentin
Gene namesi
Name:Vim
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi621646. Vim.

Subcellular locationi

Nucleus matrix 1 Publication. Cytoplasm By similarity

GO - Cellular componenti

  1. axon Source: RGD
  2. cell body Source: RGD
  3. cell projection Source: RGD
  4. cytoplasm Source: UniProtKB
  5. cytoskeleton Source: RGD
  6. cytosol Source: RGD
  7. intermediate filament Source: UniProtKB
  8. nucleus Source: UniProtKB-KW
  9. perinuclear region of cytoplasm Source: RGD
  10. type III intermediate filament Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Intermediate filament, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi55 – 551S → A: Retains filamentous network during mitosis when transfected alone and when coexpressed with nestin. 1 Publication
Mutagenesisi458 – 4592TS → AA: Induces loss of filamentous network when coexpressed with nestin. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 466465VimentinPRO_0000063759Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei5 – 51PhosphoserineBy similarity
Modified residuei7 – 71Phosphoserine; by PKA and PKC; alternateBy similarity
Glycosylationi7 – 71O-linked (GlcNAc); alternateBy similarity
Modified residuei8 – 81PhosphoserineBy similarity
Modified residuei9 – 91Phosphoserine; by PKCBy similarity
Modified residuei10 – 101Phosphoserine; by PKCBy similarity
Modified residuei20 – 201PhosphothreonineBy similarity
Modified residuei25 – 251PhosphoserineBy similarity
Modified residuei26 – 261PhosphoserineBy similarity
Modified residuei29 – 291PhosphoserineBy similarity
Modified residuei33 – 331Phosphothreonine; alternateBy similarity
Glycosylationi33 – 331O-linked (GlcNAc); alternateBy similarity
Modified residuei34 – 341Phosphoserine; alternateBy similarity
Glycosylationi34 – 341O-linked (GlcNAc); alternateBy similarity
Modified residuei38 – 381PhosphotyrosineBy similarity
Modified residuei39 – 391Phosphoserine; by CaMK2, PKA, PKC and ROCK2By similarity
Modified residuei42 – 421Phosphoserine; by PKCBy similarity
Modified residuei47 – 471Phosphoserine; by PKABy similarity
Modified residuei49 – 491PhosphoserineBy similarity
Modified residuei51 – 511Phosphoserine; by PKA and PKCBy similarity
Modified residuei53 – 531PhosphotyrosineBy similarity
Modified residuei55 – 551Phosphoserine1 Publication
Modified residuei56 – 561Phosphoserine; by CDK5 and CDK1By similarity
Modified residuei61 – 611PhosphotyrosineBy similarity
Modified residuei66 – 661Phosphoserine; by PKA and PKCBy similarity
Modified residuei72 – 721Phosphoserine; by AURKB and ROCK2By similarity
Modified residuei73 – 731PhosphoserineBy similarity
Modified residuei83 – 831Phosphoserine; by CaMK2By similarity
Modified residuei117 – 1171PhosphotyrosineBy similarity
Modified residuei120 – 1201N6-acetyllysine; alternateBy similarity
Modified residuei120 – 1201N6-succinyllysine; alternateBy similarity
Modified residuei129 – 1291N6-acetyllysine; alternateBy similarity
Modified residuei129 – 1291N6-succinyllysine; alternateBy similarity
Modified residuei139 – 1391N6-acetyllysineBy similarity
Modified residuei144 – 1441PhosphoserineBy similarity
Modified residuei168 – 1681N6-acetyllysineBy similarity
Modified residuei188 – 1881N6-acetyllysine; alternateBy similarity
Modified residuei188 – 1881N6-succinyllysine; alternateBy similarity
Modified residuei214 – 2141PhosphoserineBy similarity
Modified residuei223 – 2231N6-acetyllysineBy similarity
Modified residuei226 – 2261PhosphoserineBy similarity
Modified residuei235 – 2351N6-acetyllysineBy similarity
Modified residuei261 – 2611PhosphoserineBy similarity
Modified residuei266 – 2661PhosphothreonineBy similarity
Modified residuei294 – 2941N6-acetyllysine; alternateBy similarity
Modified residuei294 – 2941N6-succinyllysine; alternateBy similarity
Modified residuei299 – 2991PhosphoserineBy similarity
Modified residuei373 – 3731N6-acetyllysineBy similarity
Modified residuei409 – 4091PhosphoserineBy similarity
Modified residuei412 – 4121PhosphoserineBy similarity
Modified residuei419 – 4191PhosphoserineBy similarity
Modified residuei420 – 4201PhosphoserineBy similarity
Modified residuei426 – 4261PhosphothreonineBy similarity
Modified residuei430 – 4301PhosphoserineBy similarity
Modified residuei436 – 4361PhosphothreonineBy similarity
Modified residuei445 – 4451N6-acetyllysine; alternateBy similarity
Modified residuei445 – 4451N6-succinyllysine; alternateBy similarity
Modified residuei446 – 4461PhosphothreonineBy similarity
Modified residuei458 – 4581PhosphothreonineBy similarity
Modified residuei459 – 4591PhosphoserineBy similarity

Post-translational modificationi

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 inhibit the formation of filaments (By similarity). Filament disassembly during mitosis is promoted by phosphorylation at Ser-55 as well as by nestin (Probable). Phosphorylated at Ser-56 by CDK5 during neutrophil secretion in the cytoplasm. Phosphorylated by STK33 (By similarity).By similarityCurated

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP31000.
PRIDEiP31000.

PTM databases

PhosphoSiteiP31000.

Expressioni

Gene expression databases

GenevestigatoriP31000.

Interactioni

Subunit structurei

Homopolymer assembled from elementary dimers. Interacts with HCV core protein. Interacts with BCAS3, LGSN and SYNM. Interacts (via rod region) with PLEC (via CH 1 domain). Interacts with SLC6A4. Interacts with STK33. Interacts with LARP6. Interacts with TOR1A; the interaction associates TOR1A with the cytoskeleton. Interacts with TOR1AIP1 (By similarity). Interacts with RAB8B.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
YwhabP352133EBI-368510,EBI-917309

Protein-protein interaction databases

BioGridi249676. 9 interactions.
IntActiP31000. 6 interactions.
MINTiMINT-4563959.
STRINGi10116.ENSRNOP00000024430.

Structurei

3D structure databases

ProteinModelPortaliP31000.
SMRiP31000. Positions 101-138, 328-406.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 9594HeadAdd
BLAST
Regioni96 – 407312RodAdd
BLAST
Regioni96 – 13136Coil 1AAdd
BLAST
Regioni132 – 15322Linker 1Add
BLAST
Regioni154 – 24592Coil 1BAdd
BLAST
Regioni246 – 26823Linker 12Add
BLAST
Regioni269 – 407139Coil 2Add
BLAST
Regioni408 – 46659TailAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili96 – 13136Add
BLAST
Coiled coili154 – 24592Add
BLAST
Coiled coili303 – 407105Add
BLAST

Domaini

The central alpha-helical coiled-coil rod region mediates elementary homodimerization.By similarity

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG146769.
HOGENOMiHOG000230977.
HOVERGENiHBG013015.
InParanoidiP31000.
KOiK07606.
PhylomeDBiP31000.

Family and domain databases

InterProiIPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
IPR027699. Vimentin.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF27. PTHR23239:SF27. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P31000-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSTRSVSSSS YRRMFGGSGT SSRPSSNRSY VTTSTRTYSL GSALRPSTSR
60 70 80 90 100
SLYSSSPGGA YVTRSSAVRL RSSMPGVRLL QDSVDFSLAD AINTEFKNTR
110 120 130 140 150
TNEKVELQEL NDRFANYIDK VRFLEQQNKI LLAELEQLKG QGKSRLGDLY
160 170 180 190 200
EEEMRELRRQ VDQLTNDKAR VEVERDNLAE DIMRLREKLQ EEMLQREEAE
210 220 230 240 250
STLQSFRQDV DNASLARLDL ERKVESLQEE IAFLKKLHDE EIQELQAQIQ
260 270 280 290 300
EQHVQIDVDV SKPDLTAALR DVRQQYESVA AKNLQEAEEW YKSKFADLSE
310 320 330 340 350
AANRNNDALR QAKQESNEYR RQVQSLTCEV DALKGTNESL ERQMREMEEN
360 370 380 390 400
FALEAANYQD TIGRLQDEIQ NMKEEMARHL REYQDLLNVK MALDIEIATY
410 420 430 440 450
RKLLEGEESR ISLPLPNFSS LNLRETNLES LPLVDTHSKR TLLIKTVETR
460
DGQVINETSQ HHDDLE
Length:466
Mass (Da):53,733
Last modified:January 23, 2007 - v2
Checksum:i501CDCD706166829
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62952 mRNA. Translation: CAA44722.1.
BC061847 mRNA. Translation: AAH61847.1.
M84481 mRNA. Translation: AAA42339.1.
PIRiS22119.
RefSeqiNP_112402.1. NM_031140.1.
UniGeneiRn.2710.

Genome annotation databases

GeneIDi81818.
KEGGirno:81818.
UCSCiRGD:621646. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62952 mRNA. Translation: CAA44722.1 .
BC061847 mRNA. Translation: AAH61847.1 .
M84481 mRNA. Translation: AAA42339.1 .
PIRi S22119.
RefSeqi NP_112402.1. NM_031140.1.
UniGenei Rn.2710.

3D structure databases

ProteinModelPortali P31000.
SMRi P31000. Positions 101-138, 328-406.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 249676. 9 interactions.
IntActi P31000. 6 interactions.
MINTi MINT-4563959.
STRINGi 10116.ENSRNOP00000024430.

PTM databases

PhosphoSitei P31000.

Proteomic databases

PaxDbi P31000.
PRIDEi P31000.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 81818.
KEGGi rno:81818.
UCSCi RGD:621646. rat.

Organism-specific databases

CTDi 7431.
RGDi 621646. Vim.

Phylogenomic databases

eggNOGi NOG146769.
HOGENOMi HOG000230977.
HOVERGENi HBG013015.
InParanoidi P31000.
KOi K07606.
PhylomeDBi P31000.

Miscellaneous databases

NextBioi 615731.
PROi P31000.

Gene expression databases

Genevestigatori P31000.

Family and domain databases

InterProi IPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
IPR027699. Vimentin.
[Graphical view ]
PANTHERi PTHR23239. PTHR23239. 1 hit.
PTHR23239:SF27. PTHR23239:SF27. 1 hit.
Pfami PF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view ]
PROSITEi PS00226. IF. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Fischer.
  2. "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: Prostate.
  3. "Proteome analysis of a rat liver nuclear insoluble protein fraction and localization of a novel protein, ISP36, to compartments in the interchromatin space."
    Segawa M., Niino K., Mineki R., Kaga N., Murayama K., Sugimoto K., Watanabe Y., Furukawa K., Horigome T.
    FEBS J. 272:4327-4338(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 37-50, SUBCELLULAR LOCATION.
    Tissue: Liver.
  4. Lubec G., Afjehi-Sadat L., Kang S.U., Lubec S.
    Submitted (SEP-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 51-64; 123-129; 223-235; 295-304; 321-341; 346-364; 391-401 AND 411-424, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain and Spinal cord.
  5. Paine M.L.
    Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 86-160.
    Tissue: Mammary gland.
  6. "The role of the vimentin intermediate filaments in rat 3Y1 cells elucidated by immunoelectron microscopy and computer-graphic reconstruction."
    Katsumoto T., Mitsushima A., Kurimura T.
    Biol. Cell 68:139-146(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Rab8B GTPase and junction dynamics in the testis."
    Lau A.S., Mruk D.D.
    Endocrinology 144:1549-1563(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAB8B.
  8. "Nestin promotes the phosphorylation-dependent disassembly of vimentin intermediate filaments during mitosis."
    Chou Y.-H., Khuon S., Herrmann H., Goldman R.D.
    Mol. Biol. Cell 14:1468-1478(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-55, MUTAGENESIS OF SER-55 AND 458-THR-SER-459.

Entry informationi

Entry nameiVIME_RAT
AccessioniPrimary (citable) accession number: P31000
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3