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Q8TCJ2 (STT3B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length826 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.10 Ref.16

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 826825Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
PRO_0000246001

Regions

Topological domain2 – 6463Cytoplasmic Potential
Transmembrane65 – 8521Helical; Potential
Topological domain86 – 16883Lumenal Potential
Transmembrane169 – 18921Helical; Potential
Topological domain190 – 22334Cytoplasmic Potential
Transmembrane224 – 24421Helical; Potential
Topological domain245 – 26218Lumenal Potential
Transmembrane263 – 28321Helical; Potential
Topological domain284 – 2918Cytoplasmic Potential
Transmembrane292 – 31221Helical; Potential
Topological domain313 – 3197Lumenal Potential
Transmembrane320 – 34021Helical; Potential
Topological domain341 – 35111Cytoplasmic Potential
Transmembrane352 – 37221Helical; Potential
Topological domain373 – 41038Lumenal Potential
Transmembrane411 – 43121Helical; Potential
Topological domain432 – 4409Cytoplasmic Potential
Transmembrane441 – 46121Helical; Potential
Topological domain462 – 4632Lumenal Potential
Transmembrane464 – 48421Helical; Potential
Topological domain485 – 53753Cytoplasmic Potential
Transmembrane538 – 55821Helical; Potential
Topological domain559 – 826268Lumenal Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.9
Modified residue181Phosphoserine Ref.8 Ref.13
Modified residue291Phosphoserine Ref.8 Ref.12 Ref.15
Modified residue4981Phosphoserine Ref.7 Ref.15
Modified residue4991Phosphoserine Ref.7
Glycosylation1611N-linked (GlcNAc...) Potential
Glycosylation6161N-linked (GlcNAc...) Potential
Glycosylation6231N-linked (GlcNAc...) Ref.11
Glycosylation6271N-linked (GlcNAc...) Ref.11
Glycosylation6411N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict8221S → F in AAH15880. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q8TCJ2 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: B70C221C7CBEB798

FASTA82693,674
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[10]"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.
[11]"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.
Tissue: Liver.
[12]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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].
[15]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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.
RefSeqNP_849193.1. NM_178862.1.
UniGeneHs.475812.

3D structure databases

ProteinModelPortalQ8TCJ2.
SMRQ8TCJ2. Positions 103-272, 584-656.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid128394. 22 interactions.
IntActQ8TCJ2. 7 interactions.
STRING9606.ENSP00000295770.

Protein family/group databases

CAZyGT66. Glycosyltransferase Family 66.

PTM databases

PhosphoSiteQ8TCJ2.

Polymorphism databases

DMDM74715800.

Proteomic databases

PaxDbQ8TCJ2.
PeptideAtlasQ8TCJ2.
PRIDEQ8TCJ2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295770; ENSP00000295770; ENSG00000163527.
GeneID201595.
KEGGhsa:201595.
UCSCuc003cer.1. human.

Organism-specific databases

CTD201595.
GeneCardsGC03P031550.
HGNCHGNC:30611. STT3B.
HPAHPA036646.
MIM608605. gene.
neXtProtNX_Q8TCJ2.
Orphanet370924. STT3B-CDG.
PharmGKBPA143485625.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1287.
HOGENOMHOG000157471.
HOVERGENHBG010606.
InParanoidQ8TCJ2.
KOK07151.
OMATNEMTTS.
OrthoDBEOG7VHSWP.
PhylomeDBQ8TCJ2.
TreeFamTF300822.

Enzyme and pathway databases

SignaLinkQ8TCJ2.
UniPathwayUPA00378.

Gene expression databases

BgeeQ8TCJ2.
CleanExHS_STT3B.
GenevestigatorQ8TCJ2.

Family and domain databases

InterProIPR003674. Oligo_trans_STT3.
[Graphical view]
PfamPF02516. STT3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiSTT3B.
GenomeRNAi201595.
NextBio90168.
PROQ8TCJ2.
SOURCESearch...

Entry information

Entry nameSTT3B_HUMAN
AccessionPrimary (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: March 19, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM