Full text data of STT3B
STT3B
(SIMP)
[Confidence: low (only semi-automatic identification from reviews)]
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B; Oligosaccharyl transferase subunit STT3B; STT3-B; 2.4.99.18 (Source of immunodominant MHC-associated peptides homolog)
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B; Oligosaccharyl transferase subunit STT3B; STT3-B; 2.4.99.18 (Source of immunodominant MHC-associated peptides homolog)
UniProt
Q8TCJ2
ID STT3B_HUMAN Reviewed; 826 AA.
AC Q8TCJ2; Q96JZ4; Q96KY7;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2002, sequence version 1.
DT 22-JAN-2014, entry version 88.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B;
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; Synonyms=SIMP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT mouse 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.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA 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.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX, AND
RP TISSUE SPECIFICITY.
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
RT STT3 subunits have distinct enzymatic properties.";
RL Mol. Cell 12:101-111(2003).
RN [6]
RP IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX.
RX PubMed=15835887; DOI=10.1021/bi047328f;
RA Shibatani T., David L.L., McCormack A.L., Frueh K., Skach W.R.;
RT "Proteomic analysis of mammalian oligosaccharyltransferase reveals
RT multiple subcomplexes that contain Sec61, TRAP, and two potential new
RT subunits.";
RL Biochemistry 44:5982-5992(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498 AND SER-499, AND
RP MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-29, AND MASS
RP SPECTROMETRY.
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
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
RT by distinct mammalian OST isoforms.";
RL Cell 136:272-283(2009).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-623 AND ASN-627, AND MASS
RP SPECTROMETRY.
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
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND MASS
RP SPECTROMETRY.
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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.,
RA Buerckstuemmer T., 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-498, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
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.,
RA Nishitoh H., Okiyoneda T., Kokame K., Kaneko M., Taura M., Miyata M.,
RA Chosa K., Koga T., Morino-Koga S., Wada I., Kai H.;
RT "STT3B-dependent posttranslational N-glycosylation as a surveillance
RT system for secretory protein.";
RL Mol. Cell 47:99-110(2012).
CC -!- FUNCTION: Catalytic subunit of the N-oligosaccharyl transferase
CC (OST) complex which catalyzes the transfer of a high mannose
CC oligosaccharide from a lipid-linked oligosaccharide donor to an
CC asparagine residue within an Asn-X-Ser/Thr consensus motif in
CC nascent polypeptide chains. N-glycosylation occurs
CC cotranslationally and the complex associates with the Sec61
CC complex at the channel-forming translocon complex that mediates
CC protein translocation across the endoplasmic reticulum (ER). STT3B
CC is present in a small subset of OST complexes and mediates both
CC cotranslational and post-translational N-glycosylation of target
CC proteins: STT3B-containing complexes are required for efficient
CC cotranslational glycosylation and while they are less competent
CC than STT3A-containing complexes for cotranslational glycosylation,
CC they have the ability to mediate glycosylation of some nascent
CC sites that are not accessible for STT3A. STT3B-containing
CC complexes also act post-translationally and mediate modification
CC of skipped glycosylation sites in unfolded proteins. Plays a role
CC in ER-associated degradation (ERAD) pathway that mediates
CC ubiquitin-dependent degradation of misfolded endoplasmic reticulum
CC proteins by mediating N-glycosylation of unfolded proteins, which
CC are then recognized by the ERAD pathway and targeted for
CC degradation. Mediates glycosylation of the disease variant AMYL-
CC TTR 'Asp-38' of TTR at 'Asn-118', leading to its degradation.
CC -!- CATALYTIC ACTIVITY: Dolichyl diphosphooligosaccharide + [protein]-
CC L-asparagine = dolichyl diphosphate + a glycoprotein with the
CC oligosaccharide chain attached by N-beta-D-glycosyl linkage to a
CC protein L-asparagine.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex
CC (By similarity). OST seems to exist in different forms which
CC contain at least RPN1, RPN2, OST48, DAD1, OSTC, KRTCAP2 and either
CC STT3A or STT3B. OST can form stable complexes with the Sec61
CC complex or with both the Sec61 and TRAP complexes.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung,
CC liver, muscle, kidney and pancreas. Expressed in skin fibroblasts
CC (at protein level).
CC -!- SIMILARITY: Belongs to the STT3 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH15880.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB55370.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAC11581.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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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 RefSeq; NP_849193.1; NM_178862.1.
DR UniGene; Hs.475812; -.
DR ProteinModelPortal; Q8TCJ2; -.
DR SMR; Q8TCJ2; 582-683.
DR IntAct; Q8TCJ2; 7.
DR STRING; 9606.ENSP00000295770; -.
DR CAZy; GT66; Glycosyltransferase Family 66.
DR PhosphoSite; Q8TCJ2; -.
DR DMDM; 74715800; -.
DR PaxDb; Q8TCJ2; -.
DR PeptideAtlas; Q8TCJ2; -.
DR PRIDE; Q8TCJ2; -.
DR Ensembl; ENST00000295770; ENSP00000295770; ENSG00000163527.
DR GeneID; 201595; -.
DR KEGG; hsa:201595; -.
DR UCSC; uc003cer.1; human.
DR CTD; 201595; -.
DR GeneCards; GC03P031550; -.
DR HGNC; HGNC:30611; STT3B.
DR HPA; HPA036646; -.
DR MIM; 608605; gene.
DR neXtProt; NX_Q8TCJ2; -.
DR PharmGKB; PA143485625; -.
DR eggNOG; COG1287; -.
DR HOGENOM; HOG000157471; -.
DR HOVERGEN; HBG010606; -.
DR InParanoid; Q8TCJ2; -.
DR KO; K07151; -.
DR OMA; TNEMTTS; -.
DR OrthoDB; EOG7VHSWP; -.
DR PhylomeDB; Q8TCJ2; -.
DR SignaLink; Q8TCJ2; -.
DR UniPathway; UPA00378; -.
DR GeneWiki; STT3B; -.
DR GenomeRNAi; 201595; -.
DR NextBio; 90168; -.
DR PRO; PR:Q8TCJ2; -.
DR Bgee; Q8TCJ2; -.
DR CleanEx; HS_STT3B; -.
DR Genevestigator; Q8TCJ2; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; ISS:UniProtKB.
DR GO; GO:0004579; F:dolichyl-diphosphooligosaccharide-protein glycotransferase activity; IMP:UniProtKB.
DR GO; GO:0043686; P:co-translational protein modification; IMP:UniProtKB.
DR GO; GO:0030433; P:ER-associated ubiquitin-dependent protein catabolic process; 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:0018279; P:protein N-linked glycosylation via asparagine; IMP:UniProtKB.
DR GO; GO:0006986; P:response to unfolded protein; IMP:UniProtKB.
DR InterPro; IPR003674; Oligo_trans_STT3.
DR Pfam; PF02516; STT3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Membrane; Phosphoprotein; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 826 Dolichyl-diphosphooligosaccharide--
FT protein glycosyltransferase subunit
FT STT3B.
FT /FTId=PRO_0000246001.
FT TOPO_DOM 2 64 Cytoplasmic (Potential).
FT TRANSMEM 65 85 Helical; (Potential).
FT TOPO_DOM 86 168 Lumenal (Potential).
FT TRANSMEM 169 189 Helical; (Potential).
FT TOPO_DOM 190 223 Cytoplasmic (Potential).
FT TRANSMEM 224 244 Helical; (Potential).
FT TOPO_DOM 245 262 Lumenal (Potential).
FT TRANSMEM 263 283 Helical; (Potential).
FT TOPO_DOM 284 291 Cytoplasmic (Potential).
FT TRANSMEM 292 312 Helical; (Potential).
FT TOPO_DOM 313 319 Lumenal (Potential).
FT TRANSMEM 320 340 Helical; (Potential).
FT TOPO_DOM 341 351 Cytoplasmic (Potential).
FT TRANSMEM 352 372 Helical; (Potential).
FT TOPO_DOM 373 410 Lumenal (Potential).
FT TRANSMEM 411 431 Helical; (Potential).
FT TOPO_DOM 432 440 Cytoplasmic (Potential).
FT TRANSMEM 441 461 Helical; (Potential).
FT TOPO_DOM 462 463 Lumenal (Potential).
FT TRANSMEM 464 484 Helical; (Potential).
FT TOPO_DOM 485 537 Cytoplasmic (Potential).
FT TRANSMEM 538 558 Helical; (Potential).
FT TOPO_DOM 559 826 Lumenal (Potential).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 18 18 Phosphoserine.
FT MOD_RES 29 29 Phosphoserine.
FT MOD_RES 498 498 Phosphoserine.
FT MOD_RES 499 499 Phosphoserine.
FT CARBOHYD 161 161 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 616 616 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 623 623 N-linked (GlcNAc...).
FT CARBOHYD 627 627 N-linked (GlcNAc...).
FT CARBOHYD 641 641 N-linked (GlcNAc...) (Potential).
FT CONFLICT 822 822 S -> F (in Ref. 4; AAH15880).
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
//
ID STT3B_HUMAN Reviewed; 826 AA.
AC Q8TCJ2; Q96JZ4; Q96KY7;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2002, sequence version 1.
DT 22-JAN-2014, entry version 88.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B;
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; Synonyms=SIMP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT mouse 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.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA 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.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX, AND
RP TISSUE SPECIFICITY.
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
RT STT3 subunits have distinct enzymatic properties.";
RL Mol. Cell 12:101-111(2003).
RN [6]
RP IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX.
RX PubMed=15835887; DOI=10.1021/bi047328f;
RA Shibatani T., David L.L., McCormack A.L., Frueh K., Skach W.R.;
RT "Proteomic analysis of mammalian oligosaccharyltransferase reveals
RT multiple subcomplexes that contain Sec61, TRAP, and two potential new
RT subunits.";
RL Biochemistry 44:5982-5992(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498 AND SER-499, AND
RP MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-29, AND MASS
RP SPECTROMETRY.
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
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
RT by distinct mammalian OST isoforms.";
RL Cell 136:272-283(2009).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-623 AND ASN-627, AND MASS
RP SPECTROMETRY.
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
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND MASS
RP SPECTROMETRY.
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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.,
RA Buerckstuemmer T., 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-498, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
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.,
RA Nishitoh H., Okiyoneda T., Kokame K., Kaneko M., Taura M., Miyata M.,
RA Chosa K., Koga T., Morino-Koga S., Wada I., Kai H.;
RT "STT3B-dependent posttranslational N-glycosylation as a surveillance
RT system for secretory protein.";
RL Mol. Cell 47:99-110(2012).
CC -!- FUNCTION: Catalytic subunit of the N-oligosaccharyl transferase
CC (OST) complex which catalyzes the transfer of a high mannose
CC oligosaccharide from a lipid-linked oligosaccharide donor to an
CC asparagine residue within an Asn-X-Ser/Thr consensus motif in
CC nascent polypeptide chains. N-glycosylation occurs
CC cotranslationally and the complex associates with the Sec61
CC complex at the channel-forming translocon complex that mediates
CC protein translocation across the endoplasmic reticulum (ER). STT3B
CC is present in a small subset of OST complexes and mediates both
CC cotranslational and post-translational N-glycosylation of target
CC proteins: STT3B-containing complexes are required for efficient
CC cotranslational glycosylation and while they are less competent
CC than STT3A-containing complexes for cotranslational glycosylation,
CC they have the ability to mediate glycosylation of some nascent
CC sites that are not accessible for STT3A. STT3B-containing
CC complexes also act post-translationally and mediate modification
CC of skipped glycosylation sites in unfolded proteins. Plays a role
CC in ER-associated degradation (ERAD) pathway that mediates
CC ubiquitin-dependent degradation of misfolded endoplasmic reticulum
CC proteins by mediating N-glycosylation of unfolded proteins, which
CC are then recognized by the ERAD pathway and targeted for
CC degradation. Mediates glycosylation of the disease variant AMYL-
CC TTR 'Asp-38' of TTR at 'Asn-118', leading to its degradation.
CC -!- CATALYTIC ACTIVITY: Dolichyl diphosphooligosaccharide + [protein]-
CC L-asparagine = dolichyl diphosphate + a glycoprotein with the
CC oligosaccharide chain attached by N-beta-D-glycosyl linkage to a
CC protein L-asparagine.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex
CC (By similarity). OST seems to exist in different forms which
CC contain at least RPN1, RPN2, OST48, DAD1, OSTC, KRTCAP2 and either
CC STT3A or STT3B. OST can form stable complexes with the Sec61
CC complex or with both the Sec61 and TRAP complexes.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung,
CC liver, muscle, kidney and pancreas. Expressed in skin fibroblasts
CC (at protein level).
CC -!- SIMILARITY: Belongs to the STT3 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH15880.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB55370.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAC11581.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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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 RefSeq; NP_849193.1; NM_178862.1.
DR UniGene; Hs.475812; -.
DR ProteinModelPortal; Q8TCJ2; -.
DR SMR; Q8TCJ2; 582-683.
DR IntAct; Q8TCJ2; 7.
DR STRING; 9606.ENSP00000295770; -.
DR CAZy; GT66; Glycosyltransferase Family 66.
DR PhosphoSite; Q8TCJ2; -.
DR DMDM; 74715800; -.
DR PaxDb; Q8TCJ2; -.
DR PeptideAtlas; Q8TCJ2; -.
DR PRIDE; Q8TCJ2; -.
DR Ensembl; ENST00000295770; ENSP00000295770; ENSG00000163527.
DR GeneID; 201595; -.
DR KEGG; hsa:201595; -.
DR UCSC; uc003cer.1; human.
DR CTD; 201595; -.
DR GeneCards; GC03P031550; -.
DR HGNC; HGNC:30611; STT3B.
DR HPA; HPA036646; -.
DR MIM; 608605; gene.
DR neXtProt; NX_Q8TCJ2; -.
DR PharmGKB; PA143485625; -.
DR eggNOG; COG1287; -.
DR HOGENOM; HOG000157471; -.
DR HOVERGEN; HBG010606; -.
DR InParanoid; Q8TCJ2; -.
DR KO; K07151; -.
DR OMA; TNEMTTS; -.
DR OrthoDB; EOG7VHSWP; -.
DR PhylomeDB; Q8TCJ2; -.
DR SignaLink; Q8TCJ2; -.
DR UniPathway; UPA00378; -.
DR GeneWiki; STT3B; -.
DR GenomeRNAi; 201595; -.
DR NextBio; 90168; -.
DR PRO; PR:Q8TCJ2; -.
DR Bgee; Q8TCJ2; -.
DR CleanEx; HS_STT3B; -.
DR Genevestigator; Q8TCJ2; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; ISS:UniProtKB.
DR GO; GO:0004579; F:dolichyl-diphosphooligosaccharide-protein glycotransferase activity; IMP:UniProtKB.
DR GO; GO:0043686; P:co-translational protein modification; IMP:UniProtKB.
DR GO; GO:0030433; P:ER-associated ubiquitin-dependent protein catabolic process; 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:0018279; P:protein N-linked glycosylation via asparagine; IMP:UniProtKB.
DR GO; GO:0006986; P:response to unfolded protein; IMP:UniProtKB.
DR InterPro; IPR003674; Oligo_trans_STT3.
DR Pfam; PF02516; STT3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Membrane; Phosphoprotein; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 826 Dolichyl-diphosphooligosaccharide--
FT protein glycosyltransferase subunit
FT STT3B.
FT /FTId=PRO_0000246001.
FT TOPO_DOM 2 64 Cytoplasmic (Potential).
FT TRANSMEM 65 85 Helical; (Potential).
FT TOPO_DOM 86 168 Lumenal (Potential).
FT TRANSMEM 169 189 Helical; (Potential).
FT TOPO_DOM 190 223 Cytoplasmic (Potential).
FT TRANSMEM 224 244 Helical; (Potential).
FT TOPO_DOM 245 262 Lumenal (Potential).
FT TRANSMEM 263 283 Helical; (Potential).
FT TOPO_DOM 284 291 Cytoplasmic (Potential).
FT TRANSMEM 292 312 Helical; (Potential).
FT TOPO_DOM 313 319 Lumenal (Potential).
FT TRANSMEM 320 340 Helical; (Potential).
FT TOPO_DOM 341 351 Cytoplasmic (Potential).
FT TRANSMEM 352 372 Helical; (Potential).
FT TOPO_DOM 373 410 Lumenal (Potential).
FT TRANSMEM 411 431 Helical; (Potential).
FT TOPO_DOM 432 440 Cytoplasmic (Potential).
FT TRANSMEM 441 461 Helical; (Potential).
FT TOPO_DOM 462 463 Lumenal (Potential).
FT TRANSMEM 464 484 Helical; (Potential).
FT TOPO_DOM 485 537 Cytoplasmic (Potential).
FT TRANSMEM 538 558 Helical; (Potential).
FT TOPO_DOM 559 826 Lumenal (Potential).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 18 18 Phosphoserine.
FT MOD_RES 29 29 Phosphoserine.
FT MOD_RES 498 498 Phosphoserine.
FT MOD_RES 499 499 Phosphoserine.
FT CARBOHYD 161 161 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 616 616 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 623 623 N-linked (GlcNAc...).
FT CARBOHYD 627 627 N-linked (GlcNAc...).
FT CARBOHYD 641 641 N-linked (GlcNAc...) (Potential).
FT CONFLICT 822 822 S -> F (in Ref. 4; AAH15880).
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
//
MIM
608605
*RECORD*
*FIELD* NO
608605
*FIELD* TI
*608605 OLIGOSACCHARYLTRANSFERASE COMPLEX, CATALYTIC SUBUNIT STT3B; STT3B
;;STT3, S. CEREVISIAE, HOMOLOG OF, B;;
read moreSOURCE OF IMMUNODOMINANT MAJOR HISTOCOMPATIBILITY COMPLEX-ASSOCIATED
PEPTIDES;;
SOURCE OF IMMUNODOMINANT MHC-ASSOCIATED PEPTIDES; SIMP
*FIELD* TX
DESCRIPTION
The STT3B gene encodes a catalytic subunit of the oligosaccharide (OST)
protein complex that carries out glycan chain transfer to proteins in
the endoplasmic reticulum. The STT3 proteins (see also STT3A; 601134)
specifically transfer oligosaccharides onto asparagine residues. STT3A
and STT3B exist in different OST complexes with different kinetic
properties and substrate preferences, but they have overlapping roles
(summary by Shrimal et al., 2013).
CLONING
B6(dom1) is a highly immunogenic minor histocompatibility antigen in
mice. Using the sequence of B6(dom1) suggested by Edman degradation
analysis to search protein and cDNA databases, McBride et al. (2002)
identified a candidate polymorphic mouse gene, which they termed Simp.
The B6(dom1) antigen corresponds to amino acids 770 to 778 of the
823-amino acid Simp protein, and analysis of cytotoxic T-lymphocyte
activity in different mouse strains confirmed the presence of a
polymorphism at amino acid 776. By searching a genomic database and
degenerate PCR analysis, McBride et al. (2002) obtained a human cDNA
encoding SIMP. The 826-amino acid human protein shares 97% identity with
the mouse protein. Sequence analysis of SIMP cDNA from 14 individuals
failed to reveal polymorphism of human SIMP.
MAPPING
By genomic sequence analysis, McBride et al. (2002) mapped the SIMP gene
to chromosome 3p22.3, a region that shows homology of synteny to the
telomeric end of mouse chromosome 9, where the mouse Simp gene is
localized.
MOLECULAR GENETICS
In a boy, born of consanguineous Iraqi parents, with congenital disorder
of glycosylation type Ix (CDG1X; 615597), Shrimal et al. (2013)
identified a homozygous mutation in the STT3B gene (608605.0001). The
mutation was found by homozygosity mapping and candidate gene
sequencing. The patient had severely delayed psychomotor development
with microcephaly, hypotonia, seizures, and optic atrophy, and died at
age 4 years. Serum transferrin showed only a mildly abnormal type I
pattern of glycosylation. Patient cells showed no STT3B mRNA and
severely reduced protein expression. Patient cells also showed
incomplete N-glycosylation of a GFP biomarker that was complemented by
wildtype STT3B, as well as lower glycosylation of the STT3B substrates
SHBG (182205) and beta-glucuronidase (GUSB; 611499) compared to control
cells.
*FIELD* AV
.0001
CONGENITAL DISORDER OF GLYCOSYLATION, TYPE Ix (1 family)
STT3B, c.1539+20G-T
In a boy, born of consanguineous Iraqi parents, with congenital disorder
of glycosylation type Ix (CDG1X; 615597), Shrimal et al. (2013)
identified a homozygous G-to-T transversion in an intron of the STT3B
gene (c.1539+20G-T). The mutation was found by homozygosity mapping and
candidate gene sequencing. It was not present in the dbSNP, 1000 Genomes
Project, or Exome Variant Server databases, or in 1,110 Middle Eastern
control exomes. Patient cells showed no STT3B mRNA and severely reduced
protein expression. The patient had severe developmental and congenital
anomalies, including microcephaly, failure to thrive, lack of visual
tracking and optic nerve hypoplasia, cerebellar atrophy, seizures,
hypotonia, liver involvement, thrombocytopenia, micropenis, hypoplastic
scrotum, and undescended testes. He died at age 4 years. Serum
transferrin showed an only slightly abnormal glycosylation pattern.
Patient cells showed incomplete N-glycosylation of a GFP biomarker
complemented by wildtype STT3B as well as lower glycosylation of the
STT3B substrates SHBG (182205) and beta-glucuronidase (GUSB; 611499)
compared to control cells.
*FIELD* RF
1. McBride, K.; Baron, C.; Picard, S.; Martin, S.; Boismenu, D.; Bell,
A.; Bergeron, J.; Perreault, C.: The model B6(dom1) minor histocompatibility
antigen is encoded by a mouse homolog of the yeast STT3 gene. Immunogenetics 54:
562-569, 2002.
2. Shrimal, S.; Ng, B. G.; Losfeld, M.-E.; Gilmore, R.; Freeze, H.
H.: Mutations in STT3A and STT3B cause two congenital disorders of
glycosylation. Hum. Molec. Genet. 22: 4638-4645, 2013.
*FIELD* CN
Cassandra L. Kniffin - updated: 1/9/2014
*FIELD* CD
Paul J. Converse: 4/23/2004
*FIELD* ED
carol: 01/13/2014
mgross: 1/10/2014
mcolton: 1/10/2014
ckniffin: 1/9/2014
mgross: 4/23/2004
*RECORD*
*FIELD* NO
608605
*FIELD* TI
*608605 OLIGOSACCHARYLTRANSFERASE COMPLEX, CATALYTIC SUBUNIT STT3B; STT3B
;;STT3, S. CEREVISIAE, HOMOLOG OF, B;;
read moreSOURCE OF IMMUNODOMINANT MAJOR HISTOCOMPATIBILITY COMPLEX-ASSOCIATED
PEPTIDES;;
SOURCE OF IMMUNODOMINANT MHC-ASSOCIATED PEPTIDES; SIMP
*FIELD* TX
DESCRIPTION
The STT3B gene encodes a catalytic subunit of the oligosaccharide (OST)
protein complex that carries out glycan chain transfer to proteins in
the endoplasmic reticulum. The STT3 proteins (see also STT3A; 601134)
specifically transfer oligosaccharides onto asparagine residues. STT3A
and STT3B exist in different OST complexes with different kinetic
properties and substrate preferences, but they have overlapping roles
(summary by Shrimal et al., 2013).
CLONING
B6(dom1) is a highly immunogenic minor histocompatibility antigen in
mice. Using the sequence of B6(dom1) suggested by Edman degradation
analysis to search protein and cDNA databases, McBride et al. (2002)
identified a candidate polymorphic mouse gene, which they termed Simp.
The B6(dom1) antigen corresponds to amino acids 770 to 778 of the
823-amino acid Simp protein, and analysis of cytotoxic T-lymphocyte
activity in different mouse strains confirmed the presence of a
polymorphism at amino acid 776. By searching a genomic database and
degenerate PCR analysis, McBride et al. (2002) obtained a human cDNA
encoding SIMP. The 826-amino acid human protein shares 97% identity with
the mouse protein. Sequence analysis of SIMP cDNA from 14 individuals
failed to reveal polymorphism of human SIMP.
MAPPING
By genomic sequence analysis, McBride et al. (2002) mapped the SIMP gene
to chromosome 3p22.3, a region that shows homology of synteny to the
telomeric end of mouse chromosome 9, where the mouse Simp gene is
localized.
MOLECULAR GENETICS
In a boy, born of consanguineous Iraqi parents, with congenital disorder
of glycosylation type Ix (CDG1X; 615597), Shrimal et al. (2013)
identified a homozygous mutation in the STT3B gene (608605.0001). The
mutation was found by homozygosity mapping and candidate gene
sequencing. The patient had severely delayed psychomotor development
with microcephaly, hypotonia, seizures, and optic atrophy, and died at
age 4 years. Serum transferrin showed only a mildly abnormal type I
pattern of glycosylation. Patient cells showed no STT3B mRNA and
severely reduced protein expression. Patient cells also showed
incomplete N-glycosylation of a GFP biomarker that was complemented by
wildtype STT3B, as well as lower glycosylation of the STT3B substrates
SHBG (182205) and beta-glucuronidase (GUSB; 611499) compared to control
cells.
*FIELD* AV
.0001
CONGENITAL DISORDER OF GLYCOSYLATION, TYPE Ix (1 family)
STT3B, c.1539+20G-T
In a boy, born of consanguineous Iraqi parents, with congenital disorder
of glycosylation type Ix (CDG1X; 615597), Shrimal et al. (2013)
identified a homozygous G-to-T transversion in an intron of the STT3B
gene (c.1539+20G-T). The mutation was found by homozygosity mapping and
candidate gene sequencing. It was not present in the dbSNP, 1000 Genomes
Project, or Exome Variant Server databases, or in 1,110 Middle Eastern
control exomes. Patient cells showed no STT3B mRNA and severely reduced
protein expression. The patient had severe developmental and congenital
anomalies, including microcephaly, failure to thrive, lack of visual
tracking and optic nerve hypoplasia, cerebellar atrophy, seizures,
hypotonia, liver involvement, thrombocytopenia, micropenis, hypoplastic
scrotum, and undescended testes. He died at age 4 years. Serum
transferrin showed an only slightly abnormal glycosylation pattern.
Patient cells showed incomplete N-glycosylation of a GFP biomarker
complemented by wildtype STT3B as well as lower glycosylation of the
STT3B substrates SHBG (182205) and beta-glucuronidase (GUSB; 611499)
compared to control cells.
*FIELD* RF
1. McBride, K.; Baron, C.; Picard, S.; Martin, S.; Boismenu, D.; Bell,
A.; Bergeron, J.; Perreault, C.: The model B6(dom1) minor histocompatibility
antigen is encoded by a mouse homolog of the yeast STT3 gene. Immunogenetics 54:
562-569, 2002.
2. Shrimal, S.; Ng, B. G.; Losfeld, M.-E.; Gilmore, R.; Freeze, H.
H.: Mutations in STT3A and STT3B cause two congenital disorders of
glycosylation. Hum. Molec. Genet. 22: 4638-4645, 2013.
*FIELD* CN
Cassandra L. Kniffin - updated: 1/9/2014
*FIELD* CD
Paul J. Converse: 4/23/2004
*FIELD* ED
carol: 01/13/2014
mgross: 1/10/2014
mcolton: 1/10/2014
ckniffin: 1/9/2014
mgross: 4/23/2004