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Q8TCJ2

- STT3B_HUMAN

UniProt

Q8TCJ2 - STT3B_HUMAN

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Protein

Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B

Gene

STT3B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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.

Pathwayi

GO - Molecular functioni

  1. dolichyl-diphosphooligosaccharide-protein glycotransferase activity Source: UniProtKB

GO - Biological processi

  1. co-translational protein modification Source: UniProtKB
  2. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  3. glycoprotein catabolic process Source: UniProtKB
  4. post-translational protein modification Source: UniProtKB
  5. protein N-linked glycosylation via asparagine Source: UniProtKB
  6. response to unfolded protein Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

SignaLinkiQ8TCJ2.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT66. Glycosyltransferase Family 66.

Names & Taxonomyi

Protein namesi
Recommended name:
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B (EC:2.4.99.18)
Short name:
Oligosaccharyl transferase subunit STT3B
Short name:
STT3-B
Alternative name(s):
Source of immunodominant MHC-associated peptides homolog
Gene namesi
Name:STT3B
Synonyms:SIMP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:30611. STT3B.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 6463CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei65 – 8521HelicalSequence AnalysisAdd
BLAST
Topological domaini86 – 16883LumenalSequence AnalysisAdd
BLAST
Transmembranei169 – 18921HelicalSequence AnalysisAdd
BLAST
Topological domaini190 – 22334CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei224 – 24421HelicalSequence AnalysisAdd
BLAST
Topological domaini245 – 26218LumenalSequence AnalysisAdd
BLAST
Transmembranei263 – 28321HelicalSequence AnalysisAdd
BLAST
Topological domaini284 – 2918CytoplasmicSequence Analysis
Transmembranei292 – 31221HelicalSequence AnalysisAdd
BLAST
Topological domaini313 – 3197LumenalSequence Analysis
Transmembranei320 – 34021HelicalSequence AnalysisAdd
BLAST
Topological domaini341 – 35111CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei352 – 37221HelicalSequence AnalysisAdd
BLAST
Topological domaini373 – 41038LumenalSequence AnalysisAdd
BLAST
Transmembranei411 – 43121HelicalSequence AnalysisAdd
BLAST
Topological domaini432 – 4409CytoplasmicSequence Analysis
Transmembranei441 – 46121HelicalSequence AnalysisAdd
BLAST
Topological domaini462 – 4632LumenalSequence Analysis
Transmembranei464 – 48421HelicalSequence AnalysisAdd
BLAST
Topological domaini485 – 53753CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei538 – 55821HelicalSequence AnalysisAdd
BLAST
Topological domaini559 – 826268LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. membrane Source: UniProtKB
  3. oligosaccharyltransferase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Congenital disorder of glycosylation 1X (CDG1X) [MIM:615597]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Keywords - Diseasei

Congenital disorder of glycosylation

Organism-specific databases

MIMi615597. phenotype.
Orphaneti370924. STT3B-CDG.
PharmGKBiPA143485625.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 826825Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3BPRO_0000246001Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei18 – 181Phosphoserine2 Publications
Modified residuei29 – 291Phosphoserine3 Publications
Glycosylationi161 – 1611N-linked (GlcNAc...)Sequence Analysis
Modified residuei498 – 4981Phosphoserine2 Publications
Modified residuei499 – 4991Phosphoserine1 Publication
Glycosylationi616 – 6161N-linked (GlcNAc...)Sequence Analysis
Glycosylationi623 – 6231N-linked (GlcNAc...)1 Publication
Glycosylationi627 – 6271N-linked (GlcNAc...)1 Publication
Glycosylationi641 – 6411N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ8TCJ2.
PaxDbiQ8TCJ2.
PeptideAtlasiQ8TCJ2.
PRIDEiQ8TCJ2.

PTM databases

PhosphoSiteiQ8TCJ2.

Expressioni

Tissue specificityi

Expressed in heart, brain, placenta, lung, liver, muscle, kidney and pancreas. Expressed in skin fibroblasts (at protein level).1 Publication

Gene expression databases

BgeeiQ8TCJ2.
CleanExiHS_STT3B.
GenevestigatoriQ8TCJ2.

Organism-specific databases

HPAiHPA036646.

Interactioni

Subunit structurei

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.By similarity2 Publications

Protein-protein interaction databases

BioGridi128394. 22 interactions.
IntActiQ8TCJ2. 7 interactions.
STRINGi9606.ENSP00000295770.

Structurei

3D structure databases

ProteinModelPortaliQ8TCJ2.
SMRiQ8TCJ2. Positions 103-272.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the STT3 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1287.
GeneTreeiENSGT00390000015238.
HOGENOMiHOG000157471.
HOVERGENiHBG010606.
InParanoidiQ8TCJ2.
KOiK07151.
OMAiTVPVDIR.
OrthoDBiEOG7VHSWP.
PhylomeDBiQ8TCJ2.
TreeFamiTF300822.

Family and domain databases

InterProiIPR003674. Oligo_trans_STT3.
[Graphical view]
PfamiPF02516. STT3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8TCJ2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEPSAPESK HKSSLNSSPW SGLMALGNSR HGHHGPGAQC AHKAAGGAAP
60 70 80 90 100
PKPAPAGLSG GLSQPAGWQS LLSFTILFLA WLAGFSSRLF AVIRFESIIH
110 120 130 140 150
EFDPWFNYRS THHLASHGFY EFLNWFDERA WYPLGRIVGG TVYPGLMITA
160 170 180 190 200
GLIHWILNTL NITVHIRDVC VFLAPTFSGL TSISTFLLTR ELWNQGAGLL
210 220 230 240 250
AACFIAIVPG YISRSVAGSF DNEGIAIFAL QFTYYLWVKS VKTGSVFWTM
260 270 280 290 300
CCCLSYFYMV SAWGGYVFII NLIPLHVFVL LLMQRYSKRV YIAYSTFYIV
310 320 330 340 350
GLILSMQIPF VGFQPIRTSE HMAAAGVFAL LQAYAFLQYL RDRLTKQEFQ
360 370 380 390 400
TLFFLGVSLA AGAVFLSVIY LTYTGYIAPW SGRFYSLWDT GYAKIHIPII
410 420 430 440 450
ASVSEHQPTT WVSFFFDLHI LVCTFPAGLW FCIKNINDER VFVALYAISA
460 470 480 490 500
VYFAGVMVRL MLTLTPVVCM LSAIAFSNVF EHYLGDDMKR ENPPVEDSSD
510 520 530 540 550
EDDKRNQGNL YDKAGKVRKH ATEQEKTEEG LGPNIKSIVT MLMLMLLMMF
560 570 580 590 600
AVHCTWVTSN AYSSPSVVLA SYNHDGTRNI LDDFREAYFW LRQNTDEHAR
610 620 630 640 650
VMSWWDYGYQ IAGMANRTTL VDNNTWNNSH IALVGKAMSS NETAAYKIMR
660 670 680 690 700
TLDVDYVLVI FGGVIGYSGD DINKFLWMVR IAEGEHPKDI RESDYFTPQG
710 720 730 740 750
EFRVDKAGSP TLLNCLMYKM SYYRFGEMQL DFRTPPGFDR TRNAEIGNKD
760 770 780 790 800
IKFKHLEEAF TSEHWLVRIY KVKAPDNRET LDHKPRVTNI FPKQKYLSKK
810 820
TTKRKRGYIK NKLVFKKGKK ISKKTV
Length:826
Mass (Da):93,674
Last modified:June 1, 2002 - v1
Checksum:iB70C221C7CBEB798
GO

Sequence cautioni

The sequence AAH15880.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB55370.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC11581.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti822 – 8221S → F in AAH15880. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2650.1.
RefSeqiNP_849193.1. NM_178862.2.
UniGeneiHs.475812.

Genome annotation databases

EnsembliENST00000295770; ENSP00000295770; ENSG00000163527.
GeneIDi201595.
KEGGihsa:201595.
UCSCiuc003cer.1. human.

Polymorphism databases

DMDMi74715800.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSi CCDS2650.1.
RefSeqi NP_849193.1. NM_178862.2.
UniGenei Hs.475812.

3D structure databases

ProteinModelPortali Q8TCJ2.
SMRi Q8TCJ2. Positions 103-272.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 128394. 22 interactions.
IntActi Q8TCJ2. 7 interactions.
STRINGi 9606.ENSP00000295770.

Protein family/group databases

CAZyi GT66. Glycosyltransferase Family 66.

PTM databases

PhosphoSitei Q8TCJ2.

Polymorphism databases

DMDMi 74715800.

Proteomic databases

MaxQBi Q8TCJ2.
PaxDbi Q8TCJ2.
PeptideAtlasi Q8TCJ2.
PRIDEi Q8TCJ2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000295770 ; ENSP00000295770 ; ENSG00000163527 .
GeneIDi 201595.
KEGGi hsa:201595.
UCSCi uc003cer.1. human.

Organism-specific databases

CTDi 201595.
GeneCardsi GC03P031550.
HGNCi HGNC:30611. STT3B.
HPAi HPA036646.
MIMi 608605. gene.
615597. phenotype.
neXtProti NX_Q8TCJ2.
Orphaneti 370924. STT3B-CDG.
PharmGKBi PA143485625.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1287.
GeneTreei ENSGT00390000015238.
HOGENOMi HOG000157471.
HOVERGENi HBG010606.
InParanoidi Q8TCJ2.
KOi K07151.
OMAi TVPVDIR.
OrthoDBi EOG7VHSWP.
PhylomeDBi Q8TCJ2.
TreeFami TF300822.

Enzyme and pathway databases

UniPathwayi UPA00378 .
SignaLinki Q8TCJ2.

Miscellaneous databases

GeneWikii STT3B.
GenomeRNAii 201595.
NextBioi 90168.
PROi Q8TCJ2.
SOURCEi Search...

Gene expression databases

Bgeei Q8TCJ2.
CleanExi HS_STT3B.
Genevestigatori Q8TCJ2.

Family and domain databases

InterProi IPR003674. Oligo_trans_STT3.
[Graphical view ]
Pfami PF02516. STT3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. 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. 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.
  17. "Mutations in STT3A and STT3B cause two congenital disorders of glycosylation."
    Shrimal S., Ng B.G., Losfeld M.E., Gilmore R., Freeze H.H.
    Hum. Mol. Genet. 22:4638-4645(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN CDG1X.

Entry informationi

Entry nameiSTT3B_HUMAN
AccessioniPrimary (citable) accession number: Q8TCJ2
Secondary accession number(s): Q96JZ4, Q96KY7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: June 1, 2002
Last modified: October 29, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3