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Protein

Vimentin

Gene

VIM

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: 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.
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

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-BTA-264870. Caspase-mediated cleavage of cytoskeletal proteins.
R-BTA-390522. Striated Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Vimentin
Gene namesi
Name:VIM
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 13

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Intermediate filament

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 466465VimentinPRO_0000063751Add
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 – 251Phosphoserine; by PKA and PKCBy similarity
Modified residuei26 – 261Phosphoserine; by PKCBy similarity
Glycosylationi33 – 331O-linked (GlcNAc)By similarity
Modified residuei34 – 341Phosphoserine; by PKC; alternateBy similarity
Glycosylationi34 – 341O-linked (GlcNAc); alternateBy similarity
Modified residuei39 – 391Phosphoserine; by CaMK2, PKA, PKC and ROCK2By similarity
Modified residuei42 – 421Phosphoserine; by PKCBy similarity
Modified residuei49 – 491PhosphoserineBy similarity
Modified residuei53 – 531PhosphotyrosineBy similarity
Modified residuei55 – 551PhosphoserineBy similarity
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 residuei83 – 831Phosphoserine; by CaMK2By similarity
Modified residuei87 – 871PhosphoserineBy 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 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 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 inhibits the formation of filaments. Filament disassembly during mitosis is promoted by phosphorylation at Ser-55 as well as by nestin. Phosphorylated at Ser-56 by CDK5 during neutrophil secretion in the cytoplasm. Phosphorylated by STK33 (By similarity).By similarity
S-nitrosylation is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly implicating the iNOS-S100A8/9 transnitrosylase complex.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein, S-nitrosylation

Proteomic databases

PaxDbiP48616.
PRIDEiP48616.

Interactioni

Subunit structurei

Interacts with BCAS3 (By similarity). Homopolymer assembled from elementary dimers. Interacts with HCV core protein. Interacts with LGSN. Interacts with 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. Interacts with TOR1A; the interaction associates TOR1A with the cytoskeleton. Interacts with TOR1AIP1. Interacts with DIAPH1 (By similarity). Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
TGFB1P183412EBI-1221453,EBI-8537762

Protein-protein interaction databases

IntActiP48616. 3 interactions.
STRINGi9913.ENSBTAP00000024572.

Structurei

3D structure databases

ProteinModelPortaliP48616.
SMRiP48616. 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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi326 – 3294[IL]-x-C-x-x-[DE] motifBy similarity

Domaini

The central alpha-helical coiled-coil rod region mediates elementary homodimerization.By similarity
The [IL]-x-C-x-x-[DE] motif is a proposed target motif for cysteine S-nitrosylation mediated by the iNOS-S100A8/A9 transnitrosylase complex.By similarity

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IFZ1. Eukaryota.
ENOG410XRBS. LUCA.
GeneTreeiENSGT00830000128228.
HOGENOMiHOG000230977.
HOVERGENiHBG013015.
InParanoidiP48616.
KOiK07606.
OMAiNLGEDIM.
OrthoDBiEOG7FV3Q8.
TreeFamiTF330122.

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]
SMARTiSM01391. Filament. 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.

P48616-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTRSVSSSS YRRMFGGPGT ASRPSSTRSY VTTSTRTYSL GSALRPTTSR
60 70 80 90 100
TLYTSSPGGV YATRSSAVRL RSGVPGVRLL 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
EQHVQIDMDV SKPDLTAALR DVRQQYESVA AKNLQEAEEW YKSKFADLSE
310 320 330 340 350
AANRNNDALR QAKQESNEYR RQVQTLTCEV DALKGTNESL ERQMREMEEN
360 370 380 390 400
FSVEAANYQD TIGRLQDEIQ NMKEEMARHL REYQDLLNVK MALDIEIATY
410 420 430 440 450
RKLLEGEESR ISLPLPNFSS LNLRETNLDS LPLVDTHSKR TLLIKTVETR
460
DGQVINETSQ HHDDLE
Length:466
Mass (Da):53,728
Last modified:May 1, 2007 - v3
Checksum:i8722F645FED23BDC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti148 – 1481D → Q in AAA53661 (PubMed:8144034).Curated
Sequence conflicti171 – 1711V → A in AAA53661 (PubMed:8144034).Curated
Sequence conflicti176 – 1761D → H in AAA53661 (PubMed:8144034).Curated
Sequence conflicti240 – 2401E → A in AAA53661 (PubMed:8144034).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13263 mRNA. Translation: AAA53661.1.
BC118269 mRNA. Translation: AAI18270.1.
RefSeqiNP_776394.2. NM_173969.3.
UniGeneiBt.11149.

Genome annotation databases

EnsembliENSBTAT00000024572; ENSBTAP00000024572; ENSBTAG00000018463.
GeneIDi280955.
KEGGibta:280955.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13263 mRNA. Translation: AAA53661.1.
BC118269 mRNA. Translation: AAI18270.1.
RefSeqiNP_776394.2. NM_173969.3.
UniGeneiBt.11149.

3D structure databases

ProteinModelPortaliP48616.
SMRiP48616. Positions 101-138, 328-406.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP48616. 3 interactions.
STRINGi9913.ENSBTAP00000024572.

Proteomic databases

PaxDbiP48616.
PRIDEiP48616.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000024572; ENSBTAP00000024572; ENSBTAG00000018463.
GeneIDi280955.
KEGGibta:280955.

Organism-specific databases

CTDi7431.

Phylogenomic databases

eggNOGiENOG410IFZ1. Eukaryota.
ENOG410XRBS. LUCA.
GeneTreeiENSGT00830000128228.
HOGENOMiHOG000230977.
HOVERGENiHBG013015.
InParanoidiP48616.
KOiK07606.
OMAiNLGEDIM.
OrthoDBiEOG7FV3Q8.
TreeFamiTF330122.

Enzyme and pathway databases

ReactomeiR-BTA-264870. Caspase-mediated cleavage of cytoskeletal proteins.
R-BTA-390522. Striated Muscle Contraction.

Miscellaneous databases

NextBioi20805065.

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]
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the bovine vimentin-encoding cDNA."
    Hess J.F., Casselman J.T., FitzGerald P.G.
    Gene 140:257-259(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Basal ganglia.

Entry informationi

Entry nameiVIME_BOVIN
AccessioniPrimary (citable) accession number: P48616
Secondary accession number(s): Q17QM7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: May 1, 2007
Last modified: May 11, 2016
This is version 126 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.