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Q8TCJ2

- STT3B_HUMAN

UniProt

Q8TCJ2 - STT3B_HUMAN

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
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      Previous versions | rss
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    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

    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

    GO - Cellular componenti

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

    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...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 6463CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini86 – 16883LumenalSequence AnalysisAdd
    BLAST
    Topological domaini190 – 22334CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini245 – 26218LumenalSequence AnalysisAdd
    BLAST
    Topological domaini284 – 2918CytoplasmicSequence Analysis
    Topological domaini313 – 3197LumenalSequence Analysis
    Topological domaini341 – 35111CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini373 – 41038LumenalSequence AnalysisAdd
    BLAST
    Topological domaini432 – 4409CytoplasmicSequence Analysis
    Topological domaini462 – 4632LumenalSequence Analysis
    Topological domaini485 – 53753CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini559 – 826268LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei65 – 8521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei169 – 18921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei224 – 24421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei263 – 28321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei292 – 31221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei320 – 34021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei352 – 37221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei411 – 43121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei441 – 46121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei464 – 48421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei538 – 55821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the STT3 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1287.
    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

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    MAEPSAPESK HKSSLNSSPW SGLMALGNSR HGHHGPGAQC AHKAAGGAAP    50
    PKPAPAGLSG GLSQPAGWQS LLSFTILFLA WLAGFSSRLF AVIRFESIIH 100
    EFDPWFNYRS THHLASHGFY EFLNWFDERA WYPLGRIVGG TVYPGLMITA 150
    GLIHWILNTL NITVHIRDVC VFLAPTFSGL TSISTFLLTR ELWNQGAGLL 200
    AACFIAIVPG YISRSVAGSF DNEGIAIFAL QFTYYLWVKS VKTGSVFWTM 250
    CCCLSYFYMV SAWGGYVFII NLIPLHVFVL LLMQRYSKRV YIAYSTFYIV 300
    GLILSMQIPF VGFQPIRTSE HMAAAGVFAL LQAYAFLQYL RDRLTKQEFQ 350
    TLFFLGVSLA AGAVFLSVIY LTYTGYIAPW SGRFYSLWDT GYAKIHIPII 400
    ASVSEHQPTT WVSFFFDLHI LVCTFPAGLW FCIKNINDER VFVALYAISA 450
    VYFAGVMVRL MLTLTPVVCM LSAIAFSNVF EHYLGDDMKR ENPPVEDSSD 500
    EDDKRNQGNL YDKAGKVRKH ATEQEKTEEG LGPNIKSIVT MLMLMLLMMF 550
    AVHCTWVTSN AYSSPSVVLA SYNHDGTRNI LDDFREAYFW LRQNTDEHAR 600
    VMSWWDYGYQ IAGMANRTTL VDNNTWNNSH IALVGKAMSS NETAAYKIMR 650
    TLDVDYVLVI FGGVIGYSGD DINKFLWMVR IAEGEHPKDI RESDYFTPQG 700
    EFRVDKAGSP TLLNCLMYKM SYYRFGEMQL DFRTPPGFDR TRNAEIGNKD 750
    IKFKHLEEAF TSEHWLVRIY KVKAPDNRET LDHKPRVTNI FPKQKYLSKK 800
    TTKRKRGYIK NKLVFKKGKK ISKKTV 826
    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.
    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.

    Experimental Info

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_178862.1.
    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:
    EMBL
    GenBank
    DDBJ
    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_178862.1.
    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.
    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

    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 1, 2014
    This is version 94 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