CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007870
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A 
Protein Synonyms/Alias
 Oligosaccharyl transferase subunit STT3A; STT3-A; B5; Integral membrane protein 1; Transmembrane protein TMC 
Gene Name
 STT3A 
Gene Synonyms/Alias
 ITM1; TMC 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
3*****MTKFGFLRLSubiquitination[1, 2, 3, 4]
13FLRLSYEKQDTLLKLubiquitination[1, 2, 4, 5]
67LAEEGFYKFHNWFDDubiquitination[1, 2, 3, 4, 5, 6, 7]
139YHLTKELKDAGAGLLubiquitination[5]
289FVDYLRSKLNPQQFEubiquitination[2, 5]
440LDISRPDKKSKKQQDubiquitination[2]
441DISRPDKKSKKQQDSubiquitination[3]
444RPDKKSKKQQDSTYPubiquitination[2, 5]
565AMASTEEKAYEIMREubiquitination[2, 3, 5]
610GGSTDTGKHIKENDYubiquitination[2, 3, 5]
613TDTGKHIKENDYYTPubiquitination[1, 2, 3, 4, 5]
641LLNCLMYKMCYYRFGubiquitination[2]
655GQVYTEAKRPPGFDRubiquitination[1, 2, 3, 4, 5, 8]
671RNAEIGNKDFELDVLubiquitination[2, 5]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] 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]
 [3] 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]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [6] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [7] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [8] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 
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). SST3A seems to be involved in complex substrate specificity. STT3A is present in the majority of OST complexes and mediates cotranslational N-glycosylation of most sites on target proteins, while STT3B-containing complexes are required for efficient cotranslational glycosylation and mediate glycosylation of sites that have been skipped by STT3A. 
Sequence Annotation
 CARBOHYD 537 537 N-linked (GlcNAc...).
 CARBOHYD 544 544 N-linked (GlcNAc...).
 CARBOHYD 548 548 N-linked (GlcNAc...).  
Keyword
 Complete proteome; Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane; Reference proteome; Transferase; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 705 AA 
Protein Sequence
MTKFGFLRLS YEKQDTLLKL LILSMAAVLS FSTRLFAVLR FESVIHEFDP YFNYRTTRFL 60
AEEGFYKFHN WFDDRAWYPL GRIIGGTIYP GLMITSAAIY HVLHFFHITI DIRNVCVFLA 120
PLFSSFTTIV TYHLTKELKD AGAGLLAAAM IAVVPGYISR SVAGSYDNEG IAIFCMLLTY 180
YMWIKAVKTG SICWAAKCAL AYFYMVSSWG GYVFLINLIP LHVLVLMLTG RFSHRIYVAY 240
CTVYCLGTIL SMQISFVGFQ PVLSSEHMAA FGVFGLCQIH AFVDYLRSKL NPQQFEVLFR 300
SVISLVGFVL LTVGALLMLT GKISPWTGRF YSLLDPSYAK NNIPIIASVS EHQPTTWSSY 360
YFDLQLLVFM FPVGLYYCFS NLSDARIFII MYGVTSMYFS AVMVRLMLVL APVMCILSGI 420
GVSQVLSTYM KNLDISRPDK KSKKQQDSTY PIKNEVASGM ILVMAFFLIT YTFHSTWVTS 480
EAYSSPSIVL SARGGDGSRI IFDDFREAYY WLRHNTPEDA KVMSWWDYGY QITAMANRTI 540
LVDNNTWNNT HISRVGQAMA STEEKAYEIM RELDVSYVLV IFGGLTGYSS DDINKFLWMV 600
RIGGSTDTGK HIKENDYYTP TGEFRVDREG SPVLLNCLMY KMCYYRFGQV YTEAKRPPGF 660
DRVRNAEIGN KDFELDVLEE AYTTEHWLVR IYKVKDLDNR GLSRT 705 
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:0043687; P:post-translational protein modification; TAS:Reactome.
 GO:0018279; P:protein N-linked glycosylation via asparagine; IMP:UniProtKB. 
Interpro
 IPR003674; Oligo_trans_STT3. 
Pfam
 PF02516; STT3 
SMART
  
PROSITE
  
PRINTS