STT3A (STT3 oligosaccharyltransferase complex catalytic subunit A)

2011-07-01  

Identity

HGNC
LOCATION
11q24.2
LOCUSID
ALIAS
ITM1,STT3-A,TMC
FUSION GENES

Other Information

Locus ID:

NCBI: 3703
MIM: 601134
HGNC: 6172
Ensembl: ENSG00000134910

Variants:

dbSNP: 3703
ClinVar: 3703
TCGA: ENSG00000134910
COSMIC: STT3A

RNA/Proteins

Gene IDTranscript IDUniprot
ENSG00000134910ENST00000392708P46977
ENSG00000134910ENST00000525652A0A0C4DH80
ENSG00000134910ENST00000526726H0YET6
ENSG00000134910ENST00000527606E9PI32
ENSG00000134910ENST00000529196P46977
ENSG00000134910ENST00000529886E9PN73
ENSG00000134910ENST00000531491P46977
ENSG00000134910ENST00000649491P46977

Expression (GTEx)

0
50
100
150

Pathways

PathwaySourceExternal ID
N-Glycan biosynthesisKEGGko00510
N-Glycan biosynthesisKEGGhsa00510
Metabolic pathwaysKEGGhsa01100
Protein processing in endoplasmic reticulumKEGGko04141
Protein processing in endoplasmic reticulumKEGGhsa04141
N-glycosylation by oligosaccharyltransferaseKEGGhsa_M00072
N-glycosylation by oligosaccharyltransferaseKEGGM00072
Metabolism of proteinsREACTOMER-HSA-392499
Post-translational protein modificationREACTOMER-HSA-597592
Asparagine N-linked glycosylationREACTOMER-HSA-446203

Protein levels (Protein atlas)

Not detected
Low
Medium
High

References

Pubmed IDYearTitleCitations
378640322023STT3A-mediated viral N-glycosylation underlies the tumor selectivity of oncolytic virus M1.0
378640322023STT3A-mediated viral N-glycosylation underlies the tumor selectivity of oncolytic virus M1.0
361393502022Proteome and Glycoproteome Analyses Reveal the Protein N-Linked Glycosylation Specificity of STT3A and STT3B.4
361393502022Proteome and Glycoproteome Analyses Reveal the Protein N-Linked Glycosylation Specificity of STT3A and STT3B.4
346533632021Active site variants in STT3A cause a dominant type I congenital disorder of glycosylation with neuromusculoskeletal findings.6
346533632021Active site variants in STT3A cause a dominant type I congenital disorder of glycosylation with neuromusculoskeletal findings.6
312965342019Quantitative glycoproteomics reveals new classes of STT3A- and STT3B-dependent N-glycosylation sites.33
312965342019Quantitative glycoproteomics reveals new classes of STT3A- and STT3B-dependent N-glycosylation sites.33
301812692018Mammalian STT3A/B oligosaccharyltransferases segregate N-glycosylation at the translocon from lipid-linked oligosaccharide hydrolysis.13
301812692018Mammalian STT3A/B oligosaccharyltransferases segregate N-glycosylation at the translocon from lipid-linked oligosaccharide hydrolysis.13
284240032017Phenotypic Heterogeneity in a Congenital Disorder of Glycosylation Caused by Mutations in STT3A.6
288602772017DC2 and KCP2 mediate the interaction between the oligosaccharyltransferase and the ER translocon.24
284240032017Phenotypic Heterogeneity in a Congenital Disorder of Glycosylation Caused by Mutations in STT3A.6
288602772017DC2 and KCP2 mediate the interaction between the oligosaccharyltransferase and the ER translocon.24
250293712014The middle X residue influences cotranslational N-glycosylation consensus site skipping.22

Citation

Dessen P

STT3A (STT3 oligosaccharyltransferase complex catalytic subunit A)

Atlas Genet Cytogenet Oncol Haematol. 2011-07-01

Online version: http://atlasgeneticsoncology.org/gene/52275/gene-fusions-explorer/css/css/lib/dataTables.bootstrap.min.css