UniProt Accession

 STT3B_HUMAN; Q8TCJ2; Q96JZ4; Q96KY7 

Genbank Protein ID

 AY074880; AC104643; AK027789; AK075380; BC015880 

Genbank Nucleotide ID

 AAL71884.1; BAB55370.1; BAC11581.1; AAH15880.1 

Protein Name

 Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B 

Protein Synonyms/Alias

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

Gene Name

 STT3B 

Gene Synonyms/Alias

 SIMP 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
10	EPSAPESKHKSSLNS	ubiquitination	[1]
12	SAPESKHKSSLNSSP	ubiquitination	[1, 2]
504	DSSDEDDKRNQGNLY	ubiquitination	[1, 2, 3]
513	NQGNLYDKAGKVRKH	acetylation	[4]
513	NQGNLYDKAGKVRKH	ubiquitination	[1, 3]
647	SNETAAYKIMRTLDV	ubiquitination	[1, 5]
688	IAEGEHPKDIRESDY	ubiquitination	[1, 2, 3, 5]
706	QGEFRVDKAGSPTLL	ubiquitination	[1, 6]
719	LLNCLMYKMSYYRFG	ubiquitination	[1, 6]
749	RNAEIGNKDIKFKHL	ubiquitination	[1, 2]
752	EIGNKDIKFKHLEEA	ubiquitination	[1, 2]
754	GNKDIKFKHLEEAFT	ubiquitination	[1, 6]
793	RVTNIFPKQKYLSKK	ubiquitination	[1]
795	TNIFPKQKYLSKKTT	ubiquitination	[1]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094] 

Functional Description

 Catalytic subunit of the N-oligosaccharyl transferase (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. Mediates glycosylation of the disease variant AMYL- TTR 'Asp-38' of TTR at 'Asn-118', leading to its degradation. 

Sequence Annotation

 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 18 18 Phosphoserine.
 MOD_RES 29 29 Phosphoserine.
 MOD_RES 498 498 Phosphoserine.
 MOD_RES 499 499 Phosphoserine.
 CARBOHYD 161 161 N-linked (GlcNAc...) (Potential).
 CARBOHYD 616 616 N-linked (GlcNAc...) (Potential).
 CARBOHYD 623 623 N-linked (GlcNAc...).
 CARBOHYD 627 627 N-linked (GlcNAc...).
 CARBOHYD 641 641 N-linked (GlcNAc...) (Potential).  

Keyword

 Acetylation; Complete proteome; Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane; Phosphoprotein; Reference proteome; Transferase; Transmembrane; Transmembrane helix. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 826 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; IMP:UniProtKB.
 GO:0043686; P:co-translational protein modification; IMP:UniProtKB.
 GO:0030433; P:ER-associated protein catabolic process; IMP:UniProtKB.
 GO:0006516; P:glycoprotein catabolic process; IMP:UniProtKB.
 GO:0043687; P:post-translational protein modification; IMP:UniProtKB.
 GO:0018279; P:protein N-linked glycosylation via asparagine; IMP:UniProtKB.
 GO:0006986; P:response to unfolded protein; IMP:UniProtKB. 

Interpro

 IPR003674; Oligo_trans_STT3. 

Pfam

 PF02516; STT3 

SMART

  

PROSITE

  

PRINTS