Q8TCJ2 (STT3B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
Short name=Oligosaccharyl transferase subunit STT3B
Short name=STT3-B
EC=2.4.99.18

Alternative name(s):
Source of immunodominant MHC-associated peptides homolog

Gene names

Name:	STT3B
Synonyms:	SIMP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	826 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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). 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 cotranslational 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. Mediates glycosylation of the disease variant AMYL-TTR 'Asp-38' of TTR at 'Asn-118', leading to its degradation. Ref.9 Ref.15
Catalytic activity	Dolichyl diphosphooligosaccharide + [protein]-L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.
Pathway	Protein modification; protein glycosylation.
Subunit structure	Component of the oligosaccharyltransferase (OST) complex By similarity. OST seems to exist in different forms which contain at least RPN1, RPN2, OST48, DAD1, OSTC, KRTCAP2 and either STT3A or STT3B. OST can form stable complexes with the Sec61 complex or with both the Sec61 and TRAP complexes. Ref.5 Ref.6
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein.
Tissue specificity	Expressed in heart, brain, placenta, lung, liver, muscle, kidney and pancreas. Expressed in skin fibroblasts (at protein level). Ref.5
Sequence similarities	Belongs to the STT3 family.
Sequence caution	The sequence AAH15880.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAB55370.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAC11581.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ER-associated protein catabolic process Inferred from mutant phenotype Ref.15. Source: UniProtKB co-translational protein modification Inferred from mutant phenotype Ref.9. Source: UniProtKB glycoprotein catabolic process Inferred from mutant phenotype Ref.15. Source: UniProtKB post-translational protein modification Inferred from mutant phenotype Ref.9Ref.15. Source: UniProtKB protein N-linked glycosylation via asparagine Inferred from mutant phenotype Ref.9Ref.15. Source: UniProtKB response to unfolded protein Inferred from mutant phenotype Ref.9Ref.15. Source: UniProtKB
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW oligosaccharyltransferase complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	dolichyl-diphosphooligosaccharide-protein glycotransferase activity Inferred from mutant phenotype Ref.9Ref.15. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 826	826	Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B		PRO_0000246001
Regions
	Topological domain	1 – 64	64	Cytoplasmic Potential
	Transmembrane	65 – 85	21	Helical; Potential
	Topological domain	86 – 168	83	Lumenal Potential
	Transmembrane	169 – 189	21	Helical; Potential
	Topological domain	190 – 223	34	Cytoplasmic Potential
	Transmembrane	224 – 244	21	Helical; Potential
	Topological domain	245 – 262	18	Lumenal Potential
	Transmembrane	263 – 283	21	Helical; Potential
	Topological domain	284 – 291	8	Cytoplasmic Potential
	Transmembrane	292 – 312	21	Helical; Potential
	Topological domain	313 – 319	7	Lumenal Potential
	Transmembrane	320 – 340	21	Helical; Potential
	Topological domain	341 – 351	11	Cytoplasmic Potential
	Transmembrane	352 – 372	21	Helical; Potential
	Topological domain	373 – 410	38	Lumenal Potential
	Transmembrane	411 – 431	21	Helical; Potential
	Topological domain	432 – 440	9	Cytoplasmic Potential
	Transmembrane	441 – 461	21	Helical; Potential
	Topological domain	462 – 463	2	Lumenal Potential
	Transmembrane	464 – 484	21	Helical; Potential
	Topological domain	485 – 537	53	Cytoplasmic Potential
	Transmembrane	538 – 558	21	Helical; Potential
	Topological domain	559 – 826	268	Lumenal Potential
Amino acid modifications
	Modified residue	18	1	Phosphoserine Ref.8 Ref.12
	Modified residue	29	1	Phosphoserine Ref.8 Ref.11 Ref.14
	Modified residue	498	1	Phosphoserine Ref.7 Ref.14
	Modified residue	499	1	Phosphoserine Ref.7
	Glycosylation	161	1	N-linked (GlcNAc...) Potential
	Glycosylation	616	1	N-linked (GlcNAc...) Potential
	Glycosylation	623	1	N-linked (GlcNAc...) Ref.10
	Glycosylation	627	1	N-linked (GlcNAc...) Ref.10
	Glycosylation	641	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	822	1	S → F in AAH15880. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q8TCJ2 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: B70C221C7CBEB798	FASTA	826	93,674
	10 20 30 40 50 60 MAEPSAPESK HKSSLNSSPW SGLMALGNSR HGHHGPGAQC AHKAAGGAAP PKPAPAGLSG 70 80 90 100 110 120 GLSQPAGWQS LLSFTILFLA WLAGFSSRLF AVIRFESIIH EFDPWFNYRS THHLASHGFY 130 140 150 160 170 180 EFLNWFDERA WYPLGRIVGG TVYPGLMITA GLIHWILNTL NITVHIRDVC VFLAPTFSGL 190 200 210 220 230 240 TSISTFLLTR ELWNQGAGLL AACFIAIVPG YISRSVAGSF DNEGIAIFAL QFTYYLWVKS 250 260 270 280 290 300 VKTGSVFWTM CCCLSYFYMV SAWGGYVFII NLIPLHVFVL LLMQRYSKRV YIAYSTFYIV 310 320 330 340 350 360 GLILSMQIPF VGFQPIRTSE HMAAAGVFAL LQAYAFLQYL RDRLTKQEFQ TLFFLGVSLA 370 380 390 400 410 420 AGAVFLSVIY LTYTGYIAPW SGRFYSLWDT GYAKIHIPII ASVSEHQPTT WVSFFFDLHI 430 440 450 460 470 480 LVCTFPAGLW FCIKNINDER VFVALYAISA VYFAGVMVRL MLTLTPVVCM LSAIAFSNVF 490 500 510 520 530 540 EHYLGDDMKR ENPPVEDSSD EDDKRNQGNL YDKAGKVRKH ATEQEKTEEG LGPNIKSIVT 550 560 570 580 590 600 MLMLMLLMMF AVHCTWVTSN AYSSPSVVLA SYNHDGTRNI LDDFREAYFW LRQNTDEHAR 610 620 630 640 650 660 VMSWWDYGYQ IAGMANRTTL VDNNTWNNSH IALVGKAMSS NETAAYKIMR TLDVDYVLVI 670 680 690 700 710 720 FGGVIGYSGD DINKFLWMVR IAEGEHPKDI RESDYFTPQG EFRVDKAGSP TLLNCLMYKM 730 740 750 760 770 780 SYYRFGEMQL DFRTPPGFDR TRNAEIGNKD IKFKHLEEAF TSEHWLVRIY KVKAPDNRET 790 800 810 820 LDHKPRVTNI FPKQKYLSKK TTKRKRGYIK NKLVFKKGKK ISKKTV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The model B6dom1 minor histocompatibility antigen is encoded by a mouse homolog of the yeast STT3 gene." McBride K., Baron C., Picard S., Martin S., Boismenu D., Bell A., Bergeron J., Perreault C. Immunogenetics 54:562-569(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 510-826. Tissue: Placenta.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 576-826. Tissue: Placenta.
[5]	"Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties." Kelleher D.J., Karaoglu D., Mandon E.C., Gilmore R. Mol. Cell 12:101-111(2003) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX, TISSUE SPECIFICITY.
[6]	"Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits." Shibatani T., David L.L., McCormack A.L., Frueh K., Skach W.R. Biochemistry 44:5982-5992(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498 AND SER-499, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-29, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms." Ruiz-Canada C., Kelleher D.J., Gilmore R. Cell 136:272-283(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-623 AND ASN-627, MASS SPECTROMETRY. Tissue: Liver.
[11]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-498, MASS SPECTROMETRY.
[15]	"STT3B-dependent posttranslational N-glycosylation as a surveillance system for secretory protein." Sato T., Sako Y., Sho M., Momohara M., Suico M.A., Shuto T., Nishitoh H., Okiyoneda T., Kokame K., Kaneko M., Taura M., Miyata M., Chosa K., Koga T., Morino-Koga S., Wada I., Kai H. Mol. Cell 47:99-110(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN ERAD PATHWAY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY074880 mRNA. Translation: AAL71884.1. AC104643 Genomic DNA. No translation available. AK027789 mRNA. Translation: BAB55370.1. Different initiation. AK075380 mRNA. Translation: BAC11581.1. Different initiation. BC015880 mRNA. Translation: AAH15880.1. Different initiation.
IPI	IPI00152377.
RefSeq	NP_849193.1. NM_178862.1.
UniGene	Hs.475812.
3D structure databases
ProteinModelPortal	Q8TCJ2.
SMR	Q8TCJ2. Positions 584-656.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8TCJ2. 6 interactions.
STRING	9606.ENSP00000295770.
Protein family/group databases
CAZy	GT66. Glycosyltransferase Family 66.
PTM databases
PhosphoSite	Q8TCJ2.
Polymorphism databases
DMDM	74715800.
Proteomic databases
PaxDb	Q8TCJ2.
PeptideAtlas	Q8TCJ2.
PRIDE	Q8TCJ2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000295770; ENSP00000295770; ENSG00000163527.
GeneID	201595.
KEGG	hsa:201595.
UCSC	uc003cer.1. human.
Organism-specific databases
CTD	201595.
GeneCards	GC03P031550.
HGNC	HGNC:30611. STT3B.
HPA	HPA036646.
MIM	608605. gene.
neXtProt	NX_Q8TCJ2.
PharmGKB	PA143485625.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1287.
HOGENOM	HOG000157471.
HOVERGEN	HBG010606.
InParanoid	Q8TCJ2.
KO	K07151.
OMA	TNIVPKQ.
OrthoDB	EOG4VT5WM.
PhylomeDB	Q8TCJ2.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
Bgee	Q8TCJ2.
CleanEx	HS_STT3B.
Genevestigator	Q8TCJ2.
GermOnline	ENSG00000163527. Homo sapiens.
Family and domain databases
InterPro	IPR003674. Oligo_trans_STT3. [Graphical view]
Pfam	PF02516. STT3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	201595.
NextBio	90168.
SOURCE	Search...

Entry information

Entry name

STT3B_HUMAN

Accession

Primary (citable) accession number: Q8TCJ2
Secondary accession number(s): Q96JZ4, Q96KY7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2006
Last sequence update:	June 1, 2002
Last modified:	May 1, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.