Stt3b
entrez
68292
canonical
uniprot
Q3TDQ1
canonical
ensembl
ENSMUSG00000032437
resolver
ensp
ENSMUSP00000035010
resolver
enst
ENSMUST00000035010
resolver
genesymbol
Stt3b
resolver
genesymbol_syn
Simp
resolver
uniprot
A0A0R4J0D3
resolver
uniprot
Q7TT24
resolver
uniprot
Q921E3
resolver
uniprot
Q99LL0
resolver
uniprot
Q9D2V2
resolver
uniprot_entry
A0A0R4J0D3_MOUSE
resolver
uniprot_entry
STT3B_MOUSE
resolver
uniprot_sec
Q7TT24
resolver
uniprot_sec
Q921E3
resolver
uniprot_sec
Q99LL0
resolver
uniprot_sec
Q9D2V2
resolver
amino_acid_sequence
MAEPSAPESKHKSSLNSSPWSGLMALGNSRHGHHGPGTQSASSAAAPKPGPPAGLSGGLSQPAGWQSLLSFTILFLAWLAGFSSRLFAVIRFESIIHEFDPWFNYRSTHHLASHGFYEFLNWFDERAWYPLGRIVGGTVYPGLMITAGLIHWILNTLNITVHIRDVCVFLAPTFSGLTSISTFLLTRELWNQGAGLLAACFIAIVPGYISRSVAGSFDNEGIAIFALQFTYYLWVKSVKTGSVFWTMCCCLSYFYMVSAWGGYVFIINLIPLHVFVLLLMQRYSKRVYIAYSTFYIVGLILSMQIPFVGFQPIRTSEHMAAAGVFALLQAYAFLQYLRDRLTKQEFQTLFFLGVSLAAGAVFLSVIYLTYTGYIAPWSGRFYSLWDTGYAKIHIPIIASVSEHQPTTWVSFFFDLHILVCTFPAGLWFCIKNINDERVFVALYAISAVYFAGVMVRLMLTLTPVVCMLSAIAFSNVFEHYLGDDMKRENPPVEDSSDEDDKRNPGNLYDKAGKVRKHVTEQEKPEEGLGPNIKSIVTMLMLMLLMMFAVHCTWVTSNAYSSPSVVLASYNHDGTRNILDDFREAYFWLRQNTDEHARVMSWWDYGYQIAGMANRTTLVDNNTWNNSHIALVGKAMSSNETAAYKIMRSLDVDYVLVIFGGVIGYSGDDINKFLWMVRIAEGEHPKDIREGDYFTQQGEFRVDKAGSPTLLNCLMYKMSYYRFGEMQLDFRTPPGFDRTRNAEIGNKDIKFKHLEEAFTSEHWLVRIYKVKAPDNRETLGHKPRVTNIVPKQKYLSKKTTKRKRGYVKNKLVFKKGKKTSKKTV
uniprot
proteins
ec_number
2.4.99.18
uniprot
proteins
function
FUNCTION: Catalytic subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (By similarity). 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). All subunits are required for a maximal enzyme activity. This subunit contains the active site and the acceptor peptide and donor lipid-linked oligosaccharide (LLO) binding pockets (By similarity). 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 post-translational 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). {ECO:0000250|UniProtKB:E2RG47, ECO:0000250|UniProtKB:P39007, ECO:0000250|UniProtKB:Q8TCJ2}.
uniprot
proteins
mass_dalton
93246
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:Q8TCJ2}.
uniprot
proteins
protein_family
STT3 family
uniprot
proteins
pubmed
12439619
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
19131326
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
21183079
uniprot
proteins
sequence_length
823
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8TCJ2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P39007}.
uniprot
proteins
transmembrane_region
TRANSMEM 42..83; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 171..189; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 192..209; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 221..240; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 243..257; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 263..279; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 285..310; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 319..338; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 348..368; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 408..430; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 437..453; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 458..479; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 524..549; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007
uniprot
proteins