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P46977

- STT3A_HUMAN

UniProt

P46977 - STT3A_HUMAN

Protein

Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A

Gene

STT3A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (08 Apr 2008)
      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). SST3A seems to be involved in complex substrate specificity. STT3A is present in the majority of OST complexes and mediates cotranslational N-glycosylation of most sites on target proteins, while STT3B-containing complexes are required for efficient cotranslational glycosylation and mediate glycosylation of sites that have been skipped by STT3A.1 Publication

    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
    2. protein binding Source: IntAct

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. co-translational protein modification Source: UniProtKB
    3. post-translational protein modification Source: Reactome
    4. protein N-linked glycosylation via asparagine Source: UniProtKB

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    ReactomeiREACT_22426. Asparagine N-linked glycosylation.
    SignaLinkiP46977.
    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiGT66. Glycosyltransferase Family 66.
    TCDBi9.B.142.3.4. the integral membrane glycosyltransferase family 39 (gt39) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A (EC:2.4.99.18)
    Short name:
    Oligosaccharyl transferase subunit STT3A
    Short name:
    STT3-A
    Alternative name(s):
    B5
    Integral membrane protein 1
    Transmembrane protein TMC
    Gene namesi
    Name:STT3A
    Synonyms:ITM1, TMC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:6172. STT3A.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: Reactome
    2. integral component of membrane Source: UniProtKB-KW
    3. membrane Source: UniProtKB
    4. oligosaccharyltransferase complex Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Congenital disorder of glycosylation 1W (CDG1W) [MIM:615596]: 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.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti626 – 6261V → A in CDG1W; affects activity resulting in hypoglycosylation of STT3A-specific substrates. 1 Publication
    VAR_070944

    Keywords - Diseasei

    Congenital disorder of glycosylation, Disease mutation

    Organism-specific databases

    MIMi615596. phenotype.
    Orphaneti370921. STT3A-CDG.
    PharmGKBiPA29969.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 705705Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3APRO_0000072290Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi537 – 5371N-linked (GlcNAc...)1 Publication
    Glycosylationi544 – 5441N-linked (GlcNAc...)1 Publication
    Glycosylationi548 – 5481N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiP46977.
    PaxDbiP46977.
    PRIDEiP46977.

    PTM databases

    PhosphoSiteiP46977.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiP46977.
    BgeeiP46977.
    CleanExiHS_STT3A.
    GenevestigatoriP46977.

    Organism-specific databases

    HPAiHPA030735.

    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. Also identified as part of a complex which includes CANX, DERL1, DERL2, DDOST/OST48, RPN1, RPN2, SELK, VIMP, STT3A AND VCP. This contains known members of the OST complex and may be a form of this complex.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IRAK2O431872EBI-719212,EBI-447733
    Sarm1Q6PDS32EBI-719212,EBI-6117196From a different organism.
    TMEM173Q86WV62EBI-719212,EBI-2800345

    Protein-protein interaction databases

    BioGridi109908. 10 interactions.
    IntActiP46977. 14 interactions.
    MINTiMINT-1407187.
    STRINGi9606.ENSP00000376472.

    Structurei

    3D structure databases

    ProteinModelPortaliP46977.
    SMRiP46977. Positions 20-183, 474-701.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1717CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini39 – 11476LumenalSequence AnalysisAdd
    BLAST
    Topological domaini136 – 16934CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini191 – 20818LumenalSequence AnalysisAdd
    BLAST
    Topological domaini230 – 2356CytoplasmicSequence Analysis
    Topological domaini260 – 2656LumenalSequence Analysis
    Topological domaini287 – 30014CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini322 – 35938LumenalSequence AnalysisAdd
    BLAST
    Topological domaini381 – 3833CytoplasmicSequence Analysis
    Topological domaini405 – 4051LumenalSequence Analysis
    Topological domaini427 – 45327CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini475 – 705231LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei18 – 3821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei115 – 13521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei170 – 19021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei209 – 22921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei236 – 25924HelicalSequence AnalysisAdd
    BLAST
    Transmembranei266 – 28621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei301 – 32121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei360 – 38021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei384 – 40421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei406 – 42621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei454 – 47421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the STT3 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1287.
    HOGENOMiHOG000157471.
    HOVERGENiHBG010606.
    InParanoidiP46977.
    KOiK07151.
    OMAiSAVLYHV.
    OrthoDBiEOG7VHSWP.
    PhylomeDBiP46977.
    TreeFamiTF300822.

    Family and domain databases

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

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P46977-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MTKFGFLRLS YEKQDTLLKL LILSMAAVLS FSTRLFAVLR FESVIHEFDP    50
    YFNYRTTRFL AEEGFYKFHN WFDDRAWYPL GRIIGGTIYP GLMITSAAIY 100
    HVLHFFHITI DIRNVCVFLA PLFSSFTTIV TYHLTKELKD AGAGLLAAAM 150
    IAVVPGYISR SVAGSYDNEG IAIFCMLLTY YMWIKAVKTG SICWAAKCAL 200
    AYFYMVSSWG GYVFLINLIP LHVLVLMLTG RFSHRIYVAY CTVYCLGTIL 250
    SMQISFVGFQ PVLSSEHMAA FGVFGLCQIH AFVDYLRSKL NPQQFEVLFR 300
    SVISLVGFVL LTVGALLMLT GKISPWTGRF YSLLDPSYAK NNIPIIASVS 350
    EHQPTTWSSY YFDLQLLVFM FPVGLYYCFS NLSDARIFII MYGVTSMYFS 400
    AVMVRLMLVL APVMCILSGI GVSQVLSTYM KNLDISRPDK KSKKQQDSTY 450
    PIKNEVASGM ILVMAFFLIT YTFHSTWVTS EAYSSPSIVL SARGGDGSRI 500
    IFDDFREAYY WLRHNTPEDA KVMSWWDYGY QITAMANRTI LVDNNTWNNT 550
    HISRVGQAMA STEEKAYEIM RELDVSYVLV IFGGLTGYSS DDINKFLWMV 600
    RIGGSTDTGK HIKENDYYTP TGEFRVDREG SPVLLNCLMY KMCYYRFGQV 650
    YTEAKRPPGF DRVRNAEIGN KDFELDVLEE AYTTEHWLVR IYKVKDLDNR 700
    GLSRT 705
    Length:705
    Mass (Da):80,530
    Last modified:April 8, 2008 - v2
    Checksum:i71426CA5598B51C4
    GO
    Isoform 2 (identifier: P46977-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-92: Missing.

    Show »
    Length:613
    Mass (Da):69,589
    Checksum:iB37EB58A0D0776FC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti61 – 611A → S in AAL77539. (PubMed:8634329)Curated
    Sequence conflicti117 – 1171V → M in BAG58686. (PubMed:14702039)Curated
    Sequence conflicti128 – 1281T → S in AAB05994. (PubMed:8838310)Curated
    Sequence conflicti133 – 1331H → L in AAB05994. (PubMed:8838310)Curated
    Sequence conflicti252 – 2521M → R in AAB05994. (PubMed:8838310)Curated
    Sequence conflicti270 – 2701A → G in AAB05994. (PubMed:8838310)Curated
    Sequence conflicti415 – 4151C → S in AAB05994. (PubMed:8838310)Curated
    Sequence conflicti454 – 4541N → I in AAB05994. (PubMed:8838310)Curated
    Sequence conflicti494 – 4941G → D in AAL77539. (PubMed:8634329)Curated
    Sequence conflicti681 – 6811A → G in AAB05994. (PubMed:8838310)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti626 – 6261V → A in CDG1W; affects activity resulting in hypoglycosylation of STT3A-specific substrates. 1 Publication
    VAR_070944

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9292Missing in isoform 2. 1 PublicationVSP_055106Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L38961 mRNA. Translation: AAB05994.1.
    L47337 mRNA. Translation: AAL77539.1.
    AK290040 mRNA. Translation: BAF82729.1.
    AK290657 mRNA. Translation: BAF83346.1.
    AK295892 mRNA. Translation: BAG58686.1.
    BT007100 mRNA. Translation: AAP35764.1.
    AP001132 Genomic DNA. No translation available.
    AP001494 Genomic DNA. No translation available.
    CH471065 Genomic DNA. Translation: EAW67647.1.
    BC020965 mRNA. Translation: AAH20965.1.
    BC048348 mRNA. Translation: AAH48348.2.
    CCDSiCCDS60998.1. [P46977-2]
    CCDS8458.1. [P46977-1]
    PIRiS70029.
    RefSeqiNP_001265432.1. NM_001278503.1.
    NP_001265433.1. NM_001278504.1.
    NP_689926.1. NM_152713.4.
    UniGeneiHs.504237.
    Hs.659244.

    Genome annotation databases

    EnsembliENST00000392708; ENSP00000376472; ENSG00000134910. [P46977-1]
    ENST00000529196; ENSP00000436962; ENSG00000134910. [P46977-1]
    ENST00000531491; ENSP00000432820; ENSG00000134910. [P46977-2]
    GeneIDi3703.
    KEGGihsa:3703.
    UCSCiuc001qcd.2. human. [P46977-1]

    Polymorphism databases

    DMDMi182676409.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L38961 mRNA. Translation: AAB05994.1 .
    L47337 mRNA. Translation: AAL77539.1 .
    AK290040 mRNA. Translation: BAF82729.1 .
    AK290657 mRNA. Translation: BAF83346.1 .
    AK295892 mRNA. Translation: BAG58686.1 .
    BT007100 mRNA. Translation: AAP35764.1 .
    AP001132 Genomic DNA. No translation available.
    AP001494 Genomic DNA. No translation available.
    CH471065 Genomic DNA. Translation: EAW67647.1 .
    BC020965 mRNA. Translation: AAH20965.1 .
    BC048348 mRNA. Translation: AAH48348.2 .
    CCDSi CCDS60998.1. [P46977-2 ]
    CCDS8458.1. [P46977-1 ]
    PIRi S70029.
    RefSeqi NP_001265432.1. NM_001278503.1.
    NP_001265433.1. NM_001278504.1.
    NP_689926.1. NM_152713.4.
    UniGenei Hs.504237.
    Hs.659244.

    3D structure databases

    ProteinModelPortali P46977.
    SMRi P46977. Positions 20-183, 474-701.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109908. 10 interactions.
    IntActi P46977. 14 interactions.
    MINTi MINT-1407187.
    STRINGi 9606.ENSP00000376472.

    Protein family/group databases

    CAZyi GT66. Glycosyltransferase Family 66.
    TCDBi 9.B.142.3.4. the integral membrane glycosyltransferase family 39 (gt39) family.

    PTM databases

    PhosphoSitei P46977.

    Polymorphism databases

    DMDMi 182676409.

    Proteomic databases

    MaxQBi P46977.
    PaxDbi P46977.
    PRIDEi P46977.

    Protocols and materials databases

    DNASUi 3703.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000392708 ; ENSP00000376472 ; ENSG00000134910 . [P46977-1 ]
    ENST00000529196 ; ENSP00000436962 ; ENSG00000134910 . [P46977-1 ]
    ENST00000531491 ; ENSP00000432820 ; ENSG00000134910 . [P46977-2 ]
    GeneIDi 3703.
    KEGGi hsa:3703.
    UCSCi uc001qcd.2. human. [P46977-1 ]

    Organism-specific databases

    CTDi 3703.
    GeneCardsi GC11P125462.
    HGNCi HGNC:6172. STT3A.
    HPAi HPA030735.
    MIMi 601134. gene.
    615596. phenotype.
    neXtProti NX_P46977.
    Orphaneti 370921. STT3A-CDG.
    PharmGKBi PA29969.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1287.
    HOGENOMi HOG000157471.
    HOVERGENi HBG010606.
    InParanoidi P46977.
    KOi K07151.
    OMAi SAVLYHV.
    OrthoDBi EOG7VHSWP.
    PhylomeDBi P46977.
    TreeFami TF300822.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    Reactomei REACT_22426. Asparagine N-linked glycosylation.
    SignaLinki P46977.

    Miscellaneous databases

    ChiTaRSi STT3A. human.
    GenomeRNAii 3703.
    NextBioi 14511.
    PROi P46977.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P46977.
    Bgeei P46977.
    CleanExi HS_STT3A.
    Genevestigatori P46977.

    Family and domain databases

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

    Publicationsi

    1. "Molecular cloning of a highly conserved mouse and human integral membrane protein (Itm1) and genetic mapping to mouse chromosome 9."
      Hong G., Deleersnjider W., Kozak C.A., van Marck E., Tylzanowski P., Merregaert J.
      Genomics 31:295-300(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Isolation, characterization, and mapping to human chromosome 11q24-25 of a cDNA encoding a highly conserved putative transmembrane protein, TMC."
      Lissy N.A., Bellacosa A., Sonoda G., Miller P.D., Jhanwar S.C., Testa J.R.
      Biochim. Biophys. Acta 1306:137-141(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] (ISOFORMS 1 AND 2).
      Tissue: Hippocampus.
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1).
      Tissue: Duodenum and Lung.
    8. "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.
    9. "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.
    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-537; ASN-544 AND ASN-548.
      Tissue: Liver.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Selenoprotein K binds multiprotein complexes and is involved in the regulation of endoplasmic reticulum homeostasis."
      Shchedrina V.A., Everley R.A., Zhang Y., Gygi S.P., Hatfield D.L., Gladyshev V.N.
      J. Biol. Chem. 286:42937-42948(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH CANX; DERL1; DERL2; DDOST; RPN1; RPN2; SELK; VCP AND VIMP.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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: VARIANT CDG1W ALA-626, CHARACTERIZATION OF VARIANT CDG1W ALA-626.

    Entry informationi

    Entry nameiSTT3A_HUMAN
    AccessioniPrimary (citable) accession number: P46977
    Secondary accession number(s): B4DJ24
    , E9PNQ1, Q86XU9, Q8TE35, Q8WUB4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: April 8, 2008
    Last modified: October 1, 2014
    This is version 123 of the entry and version 2 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 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3