STT3B_HUMAN
ID STT3B_HUMAN Reviewed; 826 AA.
AC Q8TCJ2; Q96JZ4; Q96KY7;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B {ECO:0000305};
DE Short=Oligosaccharyl transferase subunit STT3B;
DE Short=STT3-B;
DE EC=2.4.99.18;
DE AltName: Full=Source of immunodominant MHC-associated peptides homolog;
GN Name=STT3B {ECO:0000312|HGNC:HGNC:30611}; Synonyms=SIMP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12439619; DOI=10.1007/s00251-002-0502-4;
RA McBride K., Baron C., Picard S., Martin S., Boismenu D., Bell A.,
RA Bergeron J., Perreault C.;
RT "The model B6dom1 minor histocompatibility antigen is encoded by a mouse
RT homolog of the yeast STT3 gene.";
RL Immunogenetics 54:562-569(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 510-826.
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 576-826.
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=12887896; DOI=10.1016/s1097-2765(03)00243-0;
RA Kelleher D.J., Karaoglu D., Mandon E.C., Gilmore R.;
RT "Oligosaccharyltransferase isoforms that contain different catalytic STT3
RT subunits have distinct enzymatic properties.";
RL Mol. Cell 12:101-111(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498 AND SER-499, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-29, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP FUNCTION.
RX PubMed=19167329; DOI=10.1016/j.cell.2008.11.047;
RA Ruiz-Canada C., Kelleher D.J., Gilmore R.;
RT "Cotranslational and posttranslational N-glycosylation of polypeptides by
RT distinct mammalian OST isoforms.";
RL Cell 136:272-283(2009).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-623 AND ASN-627.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-498, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP FUNCTION IN ERAD PATHWAY.
RX PubMed=22607976; DOI=10.1016/j.molcel.2012.04.015;
RA Sato T., Sako Y., Sho M., Momohara M., Suico M.A., Shuto T., Nishitoh H.,
RA Okiyoneda T., Kokame K., Kaneko M., Taura M., Miyata M., Chosa K., Koga T.,
RA Morino-Koga S., Wada I., Kai H.;
RT "STT3B-dependent posttranslational N-glycosylation as a surveillance system
RT for secretory protein.";
RL Mol. Cell 47:99-110(2012).
RN [16]
RP INVOLVEMENT IN CDG1X.
RX PubMed=23842455; DOI=10.1093/hmg/ddt312;
RA Shrimal S., Ng B.G., Losfeld M.E., Gilmore R., Freeze H.H.;
RT "Mutations in STT3A and STT3B cause two congenital disorders of
RT glycosylation.";
RL Hum. Mol. Genet. 22:4638-4645(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-498 AND SER-499, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE COMPLEX.
RX PubMed=25135935; DOI=10.1083/jcb.201404083;
RA Cherepanova N.A., Shrimal S., Gilmore R.;
RT "Oxidoreductase activity is necessary for N-glycosylation of cysteine-
RT proximal acceptor sites in glycoproteins.";
RL J. Cell Biol. 206:525-539(2014).
RN [19]
RP IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE COMPLEX.
RX PubMed=23606741; DOI=10.1242/jcs.115410;
RA Dumax-Vorzet A., Roboti P., High S.;
RT "OST4 is a subunit of the mammalian oligosaccharyltransferase required for
RT efficient N-glycosylation.";
RL J. Cell Sci. 126:2595-2606(2013).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [21] {ECO:0007744|PDB:6S7T}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), IDENTIFICATION OF THE
RP OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX, FUNCTION, COFACTOR, AND PATHWAY.
RX PubMed=31831667; DOI=10.1126/science.aaz3505;
RA Ramirez A.S., Kowal J., Locher K.P.;
RT "Cryo-electron microscopy structures of human oligosaccharyltransferase
RT complexes OST-A and OST-B.";
RL Science 366:1372-1375(2019).
CC -!- FUNCTION: Catalytic subunit of the oligosaccharyl transferase (OST)
CC complex that catalyzes the initial transfer of a defined glycan
CC (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-
CC pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr
CC consensus motif in nascent polypeptide chains, the first step in
CC protein N-glycosylation (PubMed:31831667). N-glycosylation occurs
CC cotranslationally and the complex associates with the Sec61 complex at
CC the channel-forming translocon complex that mediates protein
CC translocation across the endoplasmic reticulum (ER). All subunits are
CC required for a maximal enzyme activity. This subunit contains the
CC active site and the acceptor peptide and donor lipid-linked
CC oligosaccharide (LLO) binding pockets (By similarity). STT3B is present
CC in a small subset of OST complexes and mediates both cotranslational
CC and post-translational N-glycosylation of target proteins: STT3B-
CC containing complexes are required for efficient post-translational
CC glycosylation and while they are less competent than STT3A-containing
CC complexes for cotranslational glycosylation, they have the ability to
CC mediate glycosylation of some nascent sites that are not accessible for
CC STT3A. STT3B-containing complexes also act post-translationally and
CC mediate modification of skipped glycosylation sites in unfolded
CC proteins. Plays a role in ER-associated degradation (ERAD) pathway that
CC mediates ubiquitin-dependent degradation of misfolded endoplasmic
CC reticulum proteins by mediating N-glycosylation of unfolded proteins,
CC which are then recognized by the ERAD pathway and targeted for
CC degradation. Mediates glycosylation of the disease variant AMYL-TTR
CC 'Asp-38' of TTR at 'Asn-118', leading to its degradation
CC (PubMed:19167329, PubMed:22607976). {ECO:0000250|UniProtKB:P39007,
CC ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:22607976,
CC ECO:0000269|PubMed:31831667}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl diphosphooligosaccharide + L-asparaginyl-[protein]
CC = a dolichyl diphosphate + H(+) + N(4)-(oligosaccharide-(1->4)-N-
CC acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl)-L-
CC asparaginy-[protein]; Xref=Rhea:RHEA:22980, Rhea:RHEA-COMP:9529,
CC Rhea:RHEA-COMP:12635, Rhea:RHEA-COMP:12804, Rhea:RHEA-COMP:12805,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:50347, ChEBI:CHEBI:57497,
CC ChEBI:CHEBI:57570, ChEBI:CHEBI:132529; EC=2.4.99.18;
CC Evidence={ECO:0000250|UniProtKB:P39007};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:31831667};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:B9KDD4};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:31831667}.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex
CC (PubMed:31831667). OST exists in two different complex forms which
CC contain common core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258,
CC either STT3A or STT3B as catalytic subunits, and form-specific
CC accessory subunits (PubMed:31831667). OST can form stable complexes
CC with the Sec61 complex or with both the Sec61 and TRAP complexes (By
CC similarity). {ECO:0000250|UniProtKB:E2RG47,
CC ECO:0000269|PubMed:23606741, ECO:0000269|PubMed:25135935,
CC ECO:0000269|PubMed:31831667, ECO:0000305}.
CC -!- INTERACTION:
CC Q8TCJ2; Q0VD86: INCA1; NbExp=3; IntAct=EBI-2256290, EBI-6509505;
CC Q8TCJ2; P04843: RPN1; NbExp=2; IntAct=EBI-2256290, EBI-355963;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:12887896}. Endoplasmic reticulum membrane; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:P39007}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver,
CC muscle, kidney and pancreas. Expressed in skin fibroblasts (at protein
CC level). {ECO:0000269|PubMed:12887896}.
CC -!- DOMAIN: Despite low primary sequence conservation between eukaryotic
CC catalytic subunits and bacterial and archaeal single subunit OSTs
CC (ssOST), structural comparison revealed several common motifs at
CC spatially equivalent positions, like the DXD motif 1 on the external
CC loop 1 and the DXD motif 2 on the external loop 2 involved in binding
CC of the metal ion cofactor and the carboxamide group of the acceptor
CC asparagine, the conserved Glu residue of the TIXE/SVSE motif on the
CC external loop 5 involved in catalysis, as well as the WWDYG and the
CC DK/MI motifs in the globular domain that define the binding pocket for
CC the +2 Ser/Thr of the acceptor sequon. In bacterial ssOSTs, an Arg
CC residue was found to interact with a negatively charged side chain at
CC the -2 position of the sequon. This Arg is conserved in bacterial
CC enzymes and correlates with an extended sequon requirement (Asp-X-Asn-
CC X-Ser/Thr) for bacterial N-glycosylation.
CC {ECO:0000250|UniProtKB:P39007}.
CC -!- DISEASE: Congenital disorder of glycosylation 1X (CDG1X) [MIM:615597]:
CC A form of congenital disorder of glycosylation, a multisystem disorder
CC caused by a defect in glycoprotein biosynthesis and characterized by
CC under-glycosylated serum glycoproteins. Congenital disorders of
CC glycosylation result in a wide variety of clinical features, such as
CC defects in the nervous system development, psychomotor retardation,
CC dysmorphic features, hypotonia, coagulation disorders, and
CC immunodeficiency. The broad spectrum of features reflects the critical
CC role of N-glycoproteins during embryonic development, differentiation,
CC and maintenance of cell functions. {ECO:0000269|PubMed:23842455}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the STT3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH15880.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB55370.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC11581.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY074880; AAL71884.1; -; mRNA.
DR EMBL; AC104643; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK027789; BAB55370.1; ALT_INIT; mRNA.
DR EMBL; AK075380; BAC11581.1; ALT_INIT; mRNA.
DR EMBL; BC015880; AAH15880.1; ALT_INIT; mRNA.
DR CCDS; CCDS2650.1; -.
DR RefSeq; NP_849193.1; NM_178862.2.
DR PDB; 6S7T; EM; 3.50 A; A=1-826.
DR PDBsum; 6S7T; -.
DR AlphaFoldDB; Q8TCJ2; -.
DR SMR; Q8TCJ2; -.
DR BioGRID; 128394; 204.
DR ComplexPortal; CPX-5622; Oligosaccharyltransferase complex B.
DR CORUM; Q8TCJ2; -.
DR IntAct; Q8TCJ2; 58.
DR MINT; Q8TCJ2; -.
DR STRING; 9606.ENSP00000295770; -.
DR CAZy; GT66; Glycosyltransferase Family 66.
DR TCDB; 9.B.142.3.17; the integral membrane glycosyltransferase family 39 (gt39) family.
DR GlyConnect; 1189; 14 N-Linked glycans (3 sites).
DR GlyGen; Q8TCJ2; 7 sites, 19 N-linked glycans (4 sites), 1 O-linked glycan (1 site).
DR iPTMnet; Q8TCJ2; -.
DR MetOSite; Q8TCJ2; -.
DR PhosphoSitePlus; Q8TCJ2; -.
DR SwissPalm; Q8TCJ2; -.
DR BioMuta; STT3B; -.
DR DMDM; 74715800; -.
DR EPD; Q8TCJ2; -.
DR jPOST; Q8TCJ2; -.
DR MassIVE; Q8TCJ2; -.
DR MaxQB; Q8TCJ2; -.
DR PaxDb; Q8TCJ2; -.
DR PeptideAtlas; Q8TCJ2; -.
DR PRIDE; Q8TCJ2; -.
DR ProteomicsDB; 74146; -.
DR Antibodypedia; 45312; 48 antibodies from 17 providers.
DR DNASU; 201595; -.
DR Ensembl; ENST00000295770.4; ENSP00000295770.2; ENSG00000163527.10.
DR GeneID; 201595; -.
DR KEGG; hsa:201595; -.
DR MANE-Select; ENST00000295770.4; ENSP00000295770.2; NM_178862.3; NP_849193.1.
DR UCSC; uc011axe.3; human.
DR CTD; 201595; -.
DR DisGeNET; 201595; -.
DR GeneCards; STT3B; -.
DR HGNC; HGNC:30611; STT3B.
DR HPA; ENSG00000163527; Low tissue specificity.
DR MalaCards; STT3B; -.
DR MIM; 608605; gene.
DR MIM; 615597; phenotype.
DR neXtProt; NX_Q8TCJ2; -.
DR OpenTargets; ENSG00000163527; -.
DR Orphanet; 370924; STT3B-CDG.
DR PharmGKB; PA143485625; -.
DR VEuPathDB; HostDB:ENSG00000163527; -.
DR eggNOG; KOG2292; Eukaryota.
DR GeneTree; ENSGT00940000155488; -.
DR HOGENOM; CLU_009279_1_0_1; -.
DR InParanoid; Q8TCJ2; -.
DR OMA; TKELWSP; -.
DR OrthoDB; 187775at2759; -.
DR PhylomeDB; Q8TCJ2; -.
DR TreeFam; TF300822; -.
DR BRENDA; 2.4.99.18; 2681.
DR PathwayCommons; Q8TCJ2; -.
DR SignaLink; Q8TCJ2; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 201595; 108 hits in 1085 CRISPR screens.
DR ChiTaRS; STT3B; human.
DR GeneWiki; STT3B; -.
DR GenomeRNAi; 201595; -.
DR Pharos; Q8TCJ2; Tbio.
DR PRO; PR:Q8TCJ2; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8TCJ2; protein.
DR Bgee; ENSG00000163527; Expressed in ileal mucosa and 194 other tissues.
DR Genevisible; Q8TCJ2; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; IDA:ARUK-UCL.
DR GO; GO:0034998; C:oligosaccharyltransferase I complex; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0004579; F:dolichyl-diphosphooligosaccharide-protein glycotransferase activity; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043686; P:co-translational protein modification; IMP:UniProtKB.
DR GO; GO:0006516; P:glycoprotein catabolic process; IMP:UniProtKB.
DR GO; GO:0043687; P:post-translational protein modification; IMP:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:ComplexPortal.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IMP:UniProtKB.
DR GO; GO:0006986; P:response to unfolded protein; IMP:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:UniProtKB.
DR InterPro; IPR003674; Oligo_trans_STT3.
DR PANTHER; PTHR13872; PTHR13872; 1.
DR Pfam; PF02516; STT3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Congenital disorder of glycosylation;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Magnesium;
KW Manganese; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..826
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit STT3B"
FT /id="PRO_0000246001"
FT TOPO_DOM 2..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 42..86
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 87..173
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 174..192
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 193..194
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 195..212
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 213..223
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 224..243
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 244..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 246..260
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 261..265
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 266..282
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 283..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 288..313
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 314..321
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 322..341
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 342..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..410
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 411..433
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 434..439
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 440..456
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 457..460
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 461..482
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 483..526
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 527..552
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 553..826
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..606
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT MOTIF 101..103
FT /note="DXD motif 1"
FT /evidence="ECO:0000250|UniProtKB:Q5HTX9"
FT MOTIF 221..223
FT /note="DXD motif 2"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT MOTIF 402..405
FT /note="SVSE motif"
FT /evidence="ECO:0000250|UniProtKB:Q5HTX9"
FT MOTIF 604..608
FT /note="WWDYG motif"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT MOTIF 671..678
FT /note="DK motif"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT COMPBIAS 9..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 103
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 221
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 223
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 459
FT /ligand="dolichyl diphosphooligosaccharide"
FT /ligand_id="ChEBI:CHEBI:57570"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 609
FT /ligand="dolichyl diphosphooligosaccharide"
FT /ligand_id="ChEBI:CHEBI:57570"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 103
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 214
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 405
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 674
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3TDQ1"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 499
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT CARBOHYD 616
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 623
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 627
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 641
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 822
FT /note="S -> F (in Ref. 4; AAH15880)"
FT /evidence="ECO:0000305"
FT HELIX 65..86
FT /evidence="ECO:0007829|PDB:6S7T"
FT TURN 90..95
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 104..117
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:6S7T"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:6S7T"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:6S7T"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 146..159
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 166..171
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 173..192
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 195..204
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 223..243
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 246..262
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 266..282
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 288..305
FT /evidence="ECO:0007829|PDB:6S7T"
FT TURN 309..313
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:6S7T"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 322..343
FT /evidence="ECO:0007829|PDB:6S7T"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 350..374
FT /evidence="ECO:0007829|PDB:6S7T"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 382..389
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 392..395
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 398..402
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 411..416
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 421..434
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 438..454
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 461..482
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 534..560
FT /evidence="ECO:0007829|PDB:6S7T"
FT STRAND 566..572
FT /evidence="ECO:0007829|PDB:6S7T"
FT STRAND 578..581
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 583..593
FT /evidence="ECO:0007829|PDB:6S7T"
FT STRAND 600..602
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 605..607
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 608..613
FT /evidence="ECO:0007829|PDB:6S7T"
FT STRAND 618..621
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 628..638
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 642..651
FT /evidence="ECO:0007829|PDB:6S7T"
FT STRAND 656..660
FT /evidence="ECO:0007829|PDB:6S7T"
FT TURN 663..666
FT /evidence="ECO:0007829|PDB:6S7T"
FT TURN 671..674
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 675..685
FT /evidence="ECO:0007829|PDB:6S7T"
FT TURN 687..689
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 692..695
FT /evidence="ECO:0007829|PDB:6S7T"
FT TURN 710..714
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 716..721
FT /evidence="ECO:0007829|PDB:6S7T"
FT STRAND 731..733
FT /evidence="ECO:0007829|PDB:6S7T"
FT TURN 740..743
FT /evidence="ECO:0007829|PDB:6S7T"
FT STRAND 754..761
FT /evidence="ECO:0007829|PDB:6S7T"
FT STRAND 767..772
FT /evidence="ECO:0007829|PDB:6S7T"
FT STRAND 789..791
FT /evidence="ECO:0007829|PDB:6S7T"
FT STRAND 808..811
FT /evidence="ECO:0007829|PDB:6S7T"
SQ SEQUENCE 826 AA; 93674 MW; B70C221C7CBEB798 CRC64;
MAEPSAPESK HKSSLNSSPW SGLMALGNSR HGHHGPGAQC AHKAAGGAAP PKPAPAGLSG
GLSQPAGWQS LLSFTILFLA WLAGFSSRLF AVIRFESIIH EFDPWFNYRS THHLASHGFY
EFLNWFDERA WYPLGRIVGG TVYPGLMITA GLIHWILNTL NITVHIRDVC VFLAPTFSGL
TSISTFLLTR ELWNQGAGLL AACFIAIVPG YISRSVAGSF DNEGIAIFAL QFTYYLWVKS
VKTGSVFWTM CCCLSYFYMV SAWGGYVFII NLIPLHVFVL LLMQRYSKRV YIAYSTFYIV
GLILSMQIPF VGFQPIRTSE HMAAAGVFAL LQAYAFLQYL RDRLTKQEFQ TLFFLGVSLA
AGAVFLSVIY LTYTGYIAPW SGRFYSLWDT GYAKIHIPII ASVSEHQPTT WVSFFFDLHI
LVCTFPAGLW FCIKNINDER VFVALYAISA VYFAGVMVRL MLTLTPVVCM LSAIAFSNVF
EHYLGDDMKR ENPPVEDSSD EDDKRNQGNL YDKAGKVRKH ATEQEKTEEG LGPNIKSIVT
MLMLMLLMMF AVHCTWVTSN AYSSPSVVLA SYNHDGTRNI LDDFREAYFW LRQNTDEHAR
VMSWWDYGYQ IAGMANRTTL VDNNTWNNSH IALVGKAMSS NETAAYKIMR TLDVDYVLVI
FGGVIGYSGD DINKFLWMVR IAEGEHPKDI RESDYFTPQG EFRVDKAGSP TLLNCLMYKM
SYYRFGEMQL DFRTPPGFDR TRNAEIGNKD IKFKHLEEAF TSEHWLVRIY KVKAPDNRET
LDHKPRVTNI FPKQKYLSKK TTKRKRGYIK NKLVFKKGKK ISKKTV
