UniProt Accession

 STT3B_MOUSE; Q3TDQ1; Q7TT24; Q921E3; Q99LL0; Q9D2V2 

Genbank Protein ID

 AK018758; AK145674; AK154979; AK152899; AK170079; BC003206; BC013054; BC052433 

Genbank Nucleotide ID

 BAB31390.1; BAE26582.1; BAE32968.1; BAE31580.1; BAE41550.1; AAH03206.1; AAH13054.2; AAH52433.1 

Protein Name

 Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B 

Protein Synonyms/Alias

 Oligosaccharyl transferase subunit STT3B; STT3-B; B6dom1 antigen; Source of immunodominant MHC-associated peptides 

Gene Name

 Stt3b 

Gene Synonyms/Alias

 Simp 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
510	NPGNLYDKAGKVRKH	ubiquitination	[1]

Reference

 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 

Functional Description

 Catalytic component of oligosaccharyltransferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). STT3B is present in a small subset of OST complexes and mediates both cotranslational and post-translational N-glycosylation of target proteins: STT3B-containing complexes are required for efficient cotranslational glycosylation and while they are less competent than STT3A-containing complexes for cotranslational glycosylation, they have the ability to mediate glycosylation of some nascent sites that are not accessible for STT3A. STT3B-containing complexes also act post-translationally and mediate modification of skipped glycosylation sites in unfolded proteins. Plays a role in ER-associated degradation (ERAD) pathway that mediates ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins by mediating N-glycosylation of unfolded proteins, which are then recognized by the ERAD pathway and targeted for degradation (By similarity). 

Sequence Annotation

 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 18 18 Phosphoserine (By similarity).
 MOD_RES 29 29 Phosphoserine (By similarity).
 MOD_RES 495 495 Phosphoserine.
 MOD_RES 496 496 Phosphoserine.
 CARBOHYD 624 624 N-linked (GlcNAc...).
 CARBOHYD 638 638 N-linked (GlcNAc...).  

Keyword

 Acetylation; Complete proteome; Direct protein sequencing; Endoplasmic reticulum; Glycoprotein; Membrane; Phosphoprotein; Polymorphism; Reference proteome; Transferase; Transmembrane; Transmembrane helix. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 823 AA 

Protein Sequence

Gene Ontology

 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0008250; C:oligosaccharyltransferase complex; ISS:UniProtKB.
 GO:0004579; F:dolichyl-diphosphooligosaccharide-protein glycotransferase activity; ISS:UniProtKB.
 GO:0043686; P:co-translational protein modification; ISS:UniProtKB.
 GO:0030433; P:ER-associated protein catabolic process; ISS:UniProtKB.
 GO:0006516; P:glycoprotein catabolic process; ISS:UniProtKB.
 GO:0043687; P:post-translational protein modification; ISS:UniProtKB.
 GO:0018279; P:protein N-linked glycosylation via asparagine; ISS:UniProtKB.
 GO:0006986; P:response to unfolded protein; ISS:UniProtKB. 

Interpro

 IPR003674; Oligo_trans_STT3. 

Pfam

 PF02516; STT3 

SMART

  

PROSITE

  

PRINTS