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vimentin (VIM)

Function: - class-3 intermediate filament proteins - phosphoprotein; phosphorylation is enhanced during cell division, at which time vimentin filaments are significantly reorganized - component of a complex composed at least of ACTB, AP2M1, AP2A1, AP2A2, MEGF10 & VIM - interacts with LGSN & SYNM (putative) - belongs to the intermediate filament family Structure: - homopolymer - intermediate filament protein Expression: - highly expressed in fibroblasts, some expression in T-cells & B-cells - found in various non-epithelial cells, especially mesenchymal cells Pathology: - little or no expression in Burkitt's lymphoma cell lines - expressed in many hormone-independent mammary carcinoma cell lines - interacts with HCV core protein. - co-expressed with cytokeratins in > 50% of - renal cell carcinoma - endometrial adenocarcinoma - spindle cell carcinoma - thyroid follicular carcinoma - salivary gland carcinoma - co-expressed with cytokeratins in < 10% of - colorectal adenocarcinoma - breast ductal-lobular carcinoma - lung non-small cell carcinoma - prostate adenocarcinoma - endocervical adenocarcinoma Laboratory: - vimentin Ab in serum - mutated citrullinated vimentin Ab in serum

Interactions

molecular events

Related

vimentin Ag in tissue

General

intermediate filament protein oligomerizing protein PEST protein

Properties

SIZE: entity length = 466 aa MW = 54 kD COMPARTMENT: cytoplasm MOTIF: Head {2-95} acetylation site SITE: N-TERMINUS EFFECTOR-BOUND: acetyl Ser phosphorylation site {S5} Ser phosphorylation site {S7} Ser phosphorylation site {S8} Ser phosphorylation site {S9} Ser phosphorylation site {S10} Ser phosphorylation site {S25} Ser phosphorylation site {S26} Ser phosphorylation site {S27} Ser phosphorylation site {S34} Tyr phosphorylation site {Y38} Ser phosphorylation site {S39} Ser phosphorylation site {S42} Ser phosphorylation site {S47} Ser phosphorylation site {S49} Ser phosphorylation site {S51} Tyr phosphorylation site {Y53} Ser phosphorylation site {S55} Ser phosphorylation site {S56} Tyr phosphorylation site {Y61} Ser phosphorylation site {S66} Ser phosphorylation site {S72} Ser phosphorylation site {S73} Ser phosphorylation site {S83} Rod {96-407} MOTIF: Coil 1A {96-131} Tyr phosphorylation site {Y117} Linker 1 {132-153} Ser phosphorylation site {S144} Coil 1B {154-245} Ser phosphorylation site {S214} Ser phosphorylation site {S226} Linker 12 {246-268} Coil 2 {269-407} Ser phosphorylation site {S299} Tail {408-466} MOTIF: Ser phosphorylation site {S409} Ser phosphorylation site {S412} Ser phosphorylation site {S419} Ser phosphorylation site {S420} Ser phosphorylation site {S430} Thr phosphorylation site {T446} Thr phosphorylation site {T458} Ser phosphorylation site {S459}

Database Correlations

OMIM 193060 UniProt P08670 PFAM correlations Entrez Gene 7431 Kegg hsa:7431

References

  1. Wang KK et al Calmodulin-binding proteins as calpain substrates. Biochem J 262:693 1989 PMID: 2556106
  2. Bourne HR. Colon cancer. Consider the coiled coil.... Nature. 1991 May 16;351(6323):188-90. PMID: 1645848 (dimer)
  3. Dabbs. Diagnostic Immunohistochemistry. Churchill-Livingstone, 2002. page 175.
  4. Entrez Gene :accession 7431
  5. UniProt :accession P08670
  6. Wikipedia; Note: Vimentin entry http://en.wikipedia.org/wiki/Vimentin