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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)DescriptionActionsGraphical viewLength
Sitei351StutterBy similarity1

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000637512 – 466VimentinAdd BLAST465

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei5PhosphoserineBy similarity1
Modified residuei7Phosphoserine; by PKA and PKC; alternateBy similarity1
Glycosylationi7O-linked (GlcNAc); alternateBy similarity1
Modified residuei8PhosphoserineBy similarity1
Modified residuei9Phosphoserine; by PKCBy similarity1
Modified residuei10Phosphoserine; by PKCBy similarity1
Modified residuei11Nitrated tyrosineBy similarity1
Modified residuei20PhosphothreonineBy similarity1
Modified residuei22PhosphoserineBy similarity1
Modified residuei25Phosphoserine; by PKA and PKCBy similarity1
Modified residuei26Phosphoserine; by PKCBy similarity1
Glycosylationi33O-linked (GlcNAc)By similarity1
Modified residuei34Phosphoserine; by PKC; alternateBy similarity1
Glycosylationi34O-linked (GlcNAc); alternateBy similarity1
Modified residuei39Phosphoserine; by CaMK2, PKA, PKC and ROCK2By similarity1
Modified residuei42Phosphoserine; by PKCBy similarity1
Modified residuei49PhosphoserineBy similarity1
Modified residuei53PhosphotyrosineBy similarity1
Modified residuei55PhosphoserineBy similarity1
Modified residuei56Phosphoserine; by CDK5 and CDK1By similarity1
Modified residuei61PhosphotyrosineBy similarity1
Modified residuei66Phosphoserine; by PKA and PKCBy similarity1
Modified residuei72Phosphoserine; by AURKB and ROCK2By similarity1
Modified residuei83Phosphoserine; by CaMK2By similarity1
Modified residuei87PhosphoserineBy similarity1
Modified residuei117PhosphotyrosineBy similarity1
Modified residuei120N6-acetyllysine; alternateBy similarity1
Modified residuei120N6-succinyllysine; alternateBy similarity1
Modified residuei129N6-acetyllysine; alternateBy similarity1
Modified residuei129N6-succinyllysine; alternateBy similarity1
Modified residuei139N6-acetyllysineBy similarity1
Modified residuei144PhosphoserineBy similarity1
Modified residuei168N6-acetyllysineBy similarity1
Modified residuei188N6-acetyllysine; alternateBy similarity1
Modified residuei188N6-succinyllysine; alternateBy similarity1
Modified residuei214PhosphoserineBy similarity1
Modified residuei223N6-acetyllysineBy similarity1
Modified residuei226PhosphoserineBy similarity1
Modified residuei235N6-acetyllysineBy similarity1
Modified residuei294N6-acetyllysine; alternateBy similarity1
Modified residuei294N6-succinyllysine; alternateBy similarity1
Modified residuei299PhosphoserineBy similarity1
Modified residuei373N6-acetyllysineBy similarity1
Modified residuei383Nitrated tyrosineBy similarity1
Modified residuei409PhosphoserineBy similarity1
Modified residuei412PhosphoserineBy similarity1
Modified residuei419PhosphoserineBy similarity1
Modified residuei420PhosphoserineBy similarity1
Modified residuei426PhosphothreonineBy similarity1
Modified residuei430PhosphoserineBy similarity1
Modified residuei436PhosphothreonineBy similarity1
Modified residuei438PhosphoserineBy similarity1
Modified residuei445N6-acetyllysine; alternateBy similarity1
Modified residuei445N6-succinyllysine; alternateBy similarity1
Cross-linki445Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki445Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei446PhosphothreonineBy similarity1
Modified residuei458PhosphothreonineBy similarity1
Modified residuei459PhosphoserineBy similarity1

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, Isopeptide bond, Nitration, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

PaxDbiP48616.
PeptideAtlasiP48616.
PRIDEiP48616.

PTM databases

iPTMnetiP48616.

Expressioni

Gene expression databases

BgeeiENSBTAG00000018463.

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). Interacts with EPPK1; interaction is dependent of higher-order structure of intermediate filament (By similarity).By similarity

Binary interactionsi

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

Protein-protein interaction databases

IntActiP48616. 3 interactors.
STRINGi9913.ENSBTAP00000024572.

Structurei

3D structure databases

ProteinModelPortaliP48616.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 95HeadAdd BLAST94
Regioni96 – 407RodAdd BLAST312
Regioni96 – 131Coil 1AAdd BLAST36
Regioni132 – 153Linker 1Add BLAST22
Regioni154 – 245Coil 1BAdd BLAST92
Regioni246 – 268Linker 12Add BLAST23
Regioni269 – 407Coil 2Add BLAST139
Regioni408 – 466TailAdd BLAST59

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili96 – 131Add BLAST36
Coiled coili154 – 245Add BLAST92
Coiled coili303 – 407Add BLAST105

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi326 – 329[IL]-x-C-x-x-[DE] motifBy similarity4

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.
OMAiDVDNACL.
OrthoDBiEOG091G12MK.
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)DescriptionActionsGraphical viewLength
Sequence conflicti148D → Q in AAA53661 (PubMed:8144034).Curated1
Sequence conflicti171V → A in AAA53661 (PubMed:8144034).Curated1
Sequence conflicti176D → H in AAA53661 (PubMed:8144034).Curated1
Sequence conflicti240E → A in AAA53661 (PubMed:8144034).Curated1

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP48616. 3 interactors.
STRINGi9913.ENSBTAP00000024572.

PTM databases

iPTMnetiP48616.

Proteomic databases

PaxDbiP48616.
PeptideAtlasiP48616.
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.
OMAiDVDNACL.
OrthoDBiEOG091G12MK.
TreeFamiTF330122.

Enzyme and pathway databases

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

Gene expression databases

BgeeiENSBTAG00000018463.

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...

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: November 30, 2016
This is version 131 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.