Vimentin (VIM)

The protein contains 466 amino acids for an estimated molecular weight of 53652 Da.

 

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. (updated: March 4, 2015)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  3. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete		TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.
Protein sequence (FASTA)
Protein coevolution profile (FreeContact)
Multiple Sequence Alignment (Muscle)

This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt.


Interpro domains
Total structural coverage: 33%
Model score: 28
MODL_I-TASSER-3.0
MODL_I-TASSER-3.0

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VariantDescription
CTRCT30
CTRCT30

The reference OMIM entry for this protein is 116300

Cataract 30; ctrct30
Cataract 30, pulverulent

A number sign (#) is used with this entry because of evidence that cataract-30 is caused by heterozygous mutation in the VIM gene (193060) on chromosome 10p13.

CLINICAL FEATURES

Muller et al. (2009) screened 90 patients suffering from various types of cataract for mutations in the VIM gene. They identified a mutation (see

MOLECULAR GENETICS

) in only 1 patient, a 45-year-old female with pulverulent (dust-like) opacities.

INHERITANCE

The transmission pattern in the family with cataracts described by Muller et al. (2009) was consistent with autosomal dominant inheritance.

MOLECULAR GENETICS

In a 45-year-old woman with pulverulent cataracts, Muller et al. (2009) identified a heterozygous missense mutation (E151K) in the VIM gene (193060.0001). The patient's mother also had cataracts. The mutation was not found in 192 healthy control individuals. ... More on the omim web site

Subscribe to this protein entry history

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 116300 was added.

Jan. 25, 2016: Protein entry updated
Automatic update: model status changed