VASH1

VASH1 (Vasohibin 1) is a Protein Coding gene. An important paralog of this gene is VASH2.

Full Name

vasohibin 1

Function

Tyrosine carboxypeptidase that removes the C-terminal tyrosine residue of alpha-tubulin, thereby regulating microtubule dynamics and function (PubMed:29146869, PubMed:31270470, PubMed:31235910, PubMed:31171830, PubMed:31235911).
Critical for spindle function and accurate chromosome segregation during mitosis since microtuble detyronisation regulates mitotic spindle length and postioning (PubMed:31171830).
Acts as an angiogenesis inhibitor: inhibits migration, proliferation and network formation by endothelial cells as well as angiogenesis (PubMed:15467828, PubMed:16488400, PubMed:16707096, PubMed:19204325).
This inhibitory effect is selective to endothelial cells as it does not affect the migration of smooth muscle cells or fibroblasts (PubMed:15467828, PubMed:16488400, PubMed:16707096).

Biological Process

Biological Process angiogenesis Source:MGI1 Publication
Biological Process cell cycle Source:UniProtKB-KW
Biological Process labyrinthine layer blood vessel development Source:Ensembl
Biological Process negative regulation of angiogenesis Source:UniProtKB1 Publication
Biological Process negative regulation of blood vessel endothelial cell migration Source:UniProtKB1 Publication
Biological Process negative regulation of endothelial cell proliferation Source:UniProtKB1 Publication
Biological Process negative regulation of lymphangiogenesis Source:MGI2 Publications
Biological Process proteolysis Source:UniProtKB1 Publication
Biological Process regulation of angiogenesis Source:GO_Central1 Publication
Biological Process regulation of cell cycle Source:UniProtKB-KW
Biological Process regulation of cellular senescence Source:MGI1 Publication
Biological Process response to wounding Source:MGI1 Publication

Cellular Location

Cytoplasm
Secreted
Mainly localizes in the cytoplasm (PubMed:27879017).
Some fraction is secreted via a non-canonical secretion system; interaction with SVBP promotes secretion (PubMed:27879017).

PTM

2 major forms (42 and 36 kDa) and 2 minors (32 and 27 kDa) may be processed by proteolytic cleavage (PubMed:16488400).
The largest form (42 kDa) seems to be secreted and the other major form (63 kDa) seems to accumulate within the cells or pericellular milieu (PubMed:16488400).
Polypeptide consisting of Met-77 to Arg-318 may correspond to the 27 kDa form and that consisting of Met-77 to Val-365 may correspond to the 36 kDa form (PubMed:16488400).
Ubiquitinated in vitro.