Syntaxin-2 (STX2)

The protein contains 288 amino acids for an estimated molecular weight of 33341 Da.

 

Essential for epithelial morphogenesis. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm. (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.
  4. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
  5. Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.

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 predicted to be membranous by TOPCONS.

Topcons

Interpro domains
Total structural coverage: 100%
Model score: 68
MODL_MODELLER-9.18

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VariantDescription
dbSNP:rs17564
dbSNP:rs7301926

The reference OMIM entry for this protein is 132350

Syntaxin 2; stx2
Epimorphin; epim
Syntaxin 2a; stx2a
Syntaxin 2b; stx2b
Syntaxin 2c; stx2c

CLONING

Hirai et al. (1992) identified a novel 150-kD protein expressed on the surface of mesenchymal cells of mouse embryonic tissues. A monoclonal antibody to this molecule inhibited various processes of epithelial morphogenesis, such as hair follicle growth and lung epithelial tubular formation, in organ cultures of these tissues. Sequence analysis of cDNA encoding this protein showed that it had 289 amino acids with a hydrophobic stretch at the C terminus. NIH-3T3 cells transfected with the cDNA expressed the exogenous 150-kD protein on their surface. When lung epithelial cells were cocultured with these transfected cells, they showed normal tubular morphogenesis, but not when cocultured with untransfected NIH-3T3 cells. Hirai et al. (1992) interpreted these results as indicating that the protein, termed epimorphin, plays a central role in epithelial-mesenchymal interactions.

GENE FUNCTION

Low et al. (2003) found that 2 members of the SNARE membrane fusion machinery, syntaxin-2 and Vamp8 (603177), localized to the midbody during cytokinesis in rat and canine kidney cell lines. Inhibition of syntaxin-2 and Vamp8 function by overexpression of nonmembrane-anchored mutants caused failure of cytokinesis leading to the formation of binucleated cells. Time-lapse microscopy showed that only midbody abscission and not further upstream events, such as furrowing, were affected.

MAPPING

Zha et al. (1996) mapped the rat, mouse, and human epimorphin genes. They used a rat epimorphin DNA probe, mouse rat somatic cell hybrids, and fluorescence in situ hybridization to map epimorphin to rat chromosome 12q16. By analyzing epimorphin RFLPs segregating in 2 genetic crosses, Zha et al. (1996) mapped epimorphin to mouse chromosome 5, a region homologous to parts of human chromosomes 7 and 12. They determined that epimorphin is a new member of the synteny group conserved between mouse chromosome 5 and rat chromosome 5 that also includes Tcf1 (142410), Mdh2 (154100), and Gus. Zha et al. (1996) noted that mouse epimorphin maps near the developmental mutation bf (buff), which is characterized by alteration of coat color in non-agouti mice. Zha et al. (1996) mapped the epimorphin gene to human chromosome 7 by in situ hybridization.

ANIMAL MODEL

Wang et al. (2006) found that male Epim -/- mice were sterile due to abnormal testicular development and impaired spermatogenesis. Intestinal growth was increased in Epim -/- mice due to augmented crypt cell proliferation and crypt fission during the suckling period that was mediated, at least in part, by changes in Bmp (see BMP1; 112264) and Wnt (see WNT1; 164820) signaling pathways. Colonic mucosal injury and colitis induced by dextran sodium sulfate were ameliorated in Epim -/- mice, likely due to the increased proliferative capacity of the Epim -/- colon. ... 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

June 20, 2017: Protein entry updated
Automatic update: comparative model was added.

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 132350 was added.