STT3B
entrez
201595
canonical
uniprot
Q8TCJ2
canonical
ensembl
ENSG00000163527
resolver
ensp
ENSP00000295770
resolver
ensp
ENSP00000520729
resolver
ensp
ENSP00000685235
resolver
enst
ENST00000295770
resolver
enst
ENST00000462235
resolver
genesymbol
STT3B
resolver
genesymbol_syn
SIMP
resolver
hgnc
HGNC:30611
resolver
uniprot
A0ABB0MVB2
resolver
uniprot
Q96JZ4
resolver
uniprot
Q96KY7
resolver
uniprot_entry
A0ABB0MVB2_HUMAN
resolver
uniprot_entry
STT3B_HUMAN
resolver
uniprot_sec
Q96JZ4
resolver
uniprot_sec
Q96KY7
resolver
amino_acid_sequence
MAEPSAPESKHKSSLNSSPWSGLMALGNSRHGHHGPGAQCAHKAAGGAAPPKPAPAGLSGGLSQPAGWQSLLSFTILFLAWLAGFSSRLFAVIRFESIIHEFDPWFNYRSTHHLASHGFYEFLNWFDERAWYPLGRIVGGTVYPGLMITAGLIHWILNTLNITVHIRDVCVFLAPTFSGLTSISTFLLTRELWNQGAGLLAACFIAIVPGYISRSVAGSFDNEGIAIFALQFTYYLWVKSVKTGSVFWTMCCCLSYFYMVSAWGGYVFIINLIPLHVFVLLLMQRYSKRVYIAYSTFYIVGLILSMQIPFVGFQPIRTSEHMAAAGVFALLQAYAFLQYLRDRLTKQEFQTLFFLGVSLAAGAVFLSVIYLTYTGYIAPWSGRFYSLWDTGYAKIHIPIIASVSEHQPTTWVSFFFDLHILVCTFPAGLWFCIKNINDERVFVALYAISAVYFAGVMVRLMLTLTPVVCMLSAIAFSNVFEHYLGDDMKRENPPVEDSSDEDDKRNQGNLYDKAGKVRKHATEQEKTEEGLGPNIKSIVTMLMLMLLMMFAVHCTWVTSNAYSSPSVVLASYNHDGTRNILDDFREAYFWLRQNTDEHARVMSWWDYGYQIAGMANRTTLVDNNTWNNSHIALVGKAMSSNETAAYKIMRTLDVDYVLVIFGGVIGYSGDDINKFLWMVRIAEGEHPKDIRESDYFTPQGEFRVDKAGSPTLLNCLMYKMSYYRFGEMQLDFRTPPGFDRTRNAEIGNKDIKFKHLEEAFTSEHWLVRIYKVKAPDNRETLDHKPRVTNIFPKQKYLSKKTTKRKRGYIKNKLVFKKGKKISKKTV
uniprot
proteins
disease_involvement
DISEASE: Congenital disorder of glycosylation 1X (CDG1X) [MIM:615597]: A form of congenital disorder of glycosylation, a multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions. {ECO:0000269|PubMed:23842455}. Note=The disease is caused by variants affecting the gene represented in this entry.
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 (PubMed:19167329, PubMed:31296534, PubMed:31831667, PubMed:39509507). 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) (PubMed:19167329, PubMed:31296534, PubMed:31831667, PubMed:39509507). 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 (PubMed:19167329, PubMed:31296534, PubMed:31831667, PubMed:39509507). STT3B is present in a small subset of OST complexes (OST-B) 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 (PubMed:19167329, PubMed:22607976, PubMed:31296534, PubMed:39509507). STT3B-containing complexes also act post-translationally and mediate modification of skipped glycosylation sites in unfolded proteins (PubMed:19167329, PubMed:22607976, PubMed:39509507). 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 (PubMed:19167329, PubMed:22607976). Mediates glycosylation of the disease variant AMYL-TTR 'Asp-38' of TTR at 'Asn-118', leading to its degradation (PubMed:19167329, PubMed:22607976). {ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:22607976, ECO:0000269|PubMed:31296534, ECO:0000269|PubMed:31831667, ECO:0000269|PubMed:39509507}.
uniprot
proteins
mass_dalton
93674
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:22607976, ECO:0000269|PubMed:31296534, ECO:0000269|PubMed:31831667, ECO:0000269|PubMed:39509507}.
uniprot
proteins
protein_family
STT3 family
uniprot
proteins
pubmed
12439619
uniprot
proteins
pubmed
12887896
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19167329
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22607976
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23606741
uniprot
proteins
pubmed
23842455
uniprot
proteins
pubmed
25135935
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
31296534
uniprot
proteins
pubmed
31831667
uniprot
proteins
pubmed
39509507
uniprot
proteins
sequence_length
826
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:12887896}. Endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P39007}.
uniprot
proteins
transmembrane_region
TRANSMEM 42..86; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 174..192; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 195..212; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 224..243; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 246..260; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 266..282; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 288..313; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 322..341; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 351..371; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 411..433; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 440..456; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 461..482; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 527..552; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007
uniprot
proteins