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P48616 (VIME_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Vimentin
Gene names
Name:VIM
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Homopolymer assembled from elementary dimers. Interacts with LGSN and SYNM. Interacts (via rod region) with PLEC (via CH 1 domain). Interacts with SLC6A4 By similarity. Interacts with STK33 By similarity. Interacts with LARP6 By similarity. Interacts with RAB8B By similarity.

Subcellular location

Cytoplasm By similarity.

Domain

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

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. 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.

Sequence similarities

Belongs to the intermediate filament family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 466465Vimentin
PRO_0000063751

Regions

Region2 – 9594Head
Region96 – 407312Rod
Region96 – 13136Coil 1A
Region132 – 15322Linker 1
Region154 – 24592Coil 1B
Region246 – 26823Linker 12
Region269 – 407139Coil 2
Region408 – 46659Tail
Coiled coil96 – 13136
Coiled coil154 – 24592
Coiled coil303 – 407105

Sites

Site3511Stutter By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue51Phosphoserine By similarity
Modified residue71Phosphoserine; by PKA and PKC
Modified residue81Phosphoserine By similarity
Modified residue91Phosphoserine; by PKC
Modified residue101Phosphoserine; by PKC
Modified residue201Phosphothreonine By similarity
Modified residue251Phosphoserine; by PKA and PKC By similarity
Modified residue261Phosphoserine; by PKC By similarity
Modified residue291Phosphoserine By similarity
Modified residue331Phosphothreonine By similarity
Modified residue341Phosphoserine; by PKC By similarity
Modified residue381Phosphotyrosine By similarity
Modified residue391Phosphoserine; by CaMK2, PKA, PKC and ROCK2 By similarity
Modified residue421Phosphoserine; by PKC
Modified residue491Phosphoserine By similarity
Modified residue531Phosphotyrosine By similarity
Modified residue551Phosphoserine By similarity
Modified residue561Phosphoserine; by CDK5 and CDK1 By similarity
Modified residue611Phosphotyrosine By similarity
Modified residue661Phosphoserine; by PKA and PKC By similarity
Modified residue721Phosphoserine; by AURKB and ROCK2 By similarity
Modified residue831Phosphoserine; by CaMK2 By similarity
Modified residue1041N6-acetyllysine By similarity
Modified residue1171Phosphotyrosine By similarity
Modified residue1201N6-acetyllysine By similarity
Modified residue1391N6-acetyllysine By similarity
Modified residue1441Phosphoserine By similarity
Modified residue2141Phosphoserine By similarity
Modified residue2261Phosphoserine By similarity
Modified residue2611Phosphoserine By similarity
Modified residue2661Phosphothreonine By similarity
Modified residue2921N6-acetyllysine By similarity
Modified residue2991Phosphoserine By similarity
Modified residue3731N6-acetyllysine By similarity
Modified residue4021N6-acetyllysine By similarity
Modified residue4091Phosphoserine By similarity
Modified residue4121Phosphoserine By similarity
Modified residue4191Phosphoserine By similarity
Modified residue4201Phosphoserine By similarity
Modified residue4261Phosphothreonine By similarity
Modified residue4301Phosphoserine By similarity
Modified residue4361Phosphothreonine By similarity
Modified residue4451N6-acetyllysine By similarity
Modified residue4461Phosphothreonine By similarity
Modified residue4581Phosphothreonine By similarity
Modified residue4591Phosphoserine By similarity

Experimental info

Sequence conflict1481D → Q in AAA53661. Ref.1
Sequence conflict1711V → A in AAA53661. Ref.1
Sequence conflict1761D → H in AAA53661. Ref.1
Sequence conflict2401E → A in AAA53661. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P48616 [UniParc].

Last modified May 1, 2007. Version 3.
Checksum: 8722F645FED23BDC

FASTA46653,728
        10         20         30         40         50         60 
MSTRSVSSSS YRRMFGGPGT ASRPSSTRSY VTTSTRTYSL GSALRPTTSR TLYTSSPGGV 

        70         80         90        100        110        120 
YATRSSAVRL RSGVPGVRLL QDSVDFSLAD AINTEFKNTR TNEKVELQEL NDRFANYIDK 

       130        140        150        160        170        180 
VRFLEQQNKI LLAELEQLKG QGKSRLGDLY EEEMRELRRQ VDQLTNDKAR VEVERDNLAE 

       190        200        210        220        230        240 
DIMRLREKLQ EEMLQREEAE STLQSFRQDV DNASLARLDL ERKVESLQEE IAFLKKLHDE 

       250        260        270        280        290        300 
EIQELQAQIQ EQHVQIDMDV SKPDLTAALR DVRQQYESVA AKNLQEAEEW YKSKFADLSE 

       310        320        330        340        350        360 
AANRNNDALR QAKQESNEYR RQVQTLTCEV DALKGTNESL ERQMREMEEN FSVEAANYQD 

       370        380        390        400        410        420 
TIGRLQDEIQ NMKEEMARHL REYQDLLNVK MALDIEIATY RKLLEGEESR ISLPLPNFSS 

       430        440        450        460 
LNLRETNLDS LPLVDTHSKR TLLIKTVETR DGQVINETSQ HHDDLE

« Hide

References

« Hide 'large scale' references
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L13263 mRNA. Translation: AAA53661.1.
BC118269 mRNA. Translation: AAI18270.1.
IPIIPI00689228.
RefSeqNP_776394.2. NM_173969.3.
UniGeneBt.11149.

3D structure databases

ProteinModelPortalP48616.
SMRP48616. Positions 101-138, 328-406.
ModBaseSearch...

Protein-protein interaction databases

IntActP48616. 1 interaction.

Proteomic databases

PaxDbP48616.
PRIDEP48616.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000024572; ENSBTAP00000024572; ENSBTAG00000018463.
GeneID280955.
KEGGbta:280955.

Organism-specific databases

CTD7431.

Phylogenomic databases

eggNOGNOG146769.
GeneTreeENSGT00660000095344.
HOGENOMHOG000230977.
HOVERGENHBG013015.
InParanoidP48616.
KOK07606.
OMAINTEFKA.
OrthoDBEOG4GHZPD.

Gene expression databases

ArrayExpressP48616.

Family and domain databases

InterProIPR016044. F.
IPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
[Graphical view]
PANTHERPTHR23239. PTHR23239. 1 hit.
PfamPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20805065.

Entry information

Entry nameVIME_BOVIN
AccessionPrimary (citable) accession number: P48616
Secondary accession number(s): Q17QM7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: May 1, 2007
Last modified: April 3, 2013
This is version 98 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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