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Entry version 173 (17 Jun 2020)
Sequence version 2 (01 Oct 1996)
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Protein

Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3

Gene

STT3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalytic subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc3Man9GlcNAc2 in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. 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). All subunits are required for a maximal enzyme activity (PubMed:12359722). This subunit contains the active site and the acceptor peptide and donor lipid-linked oligosaccharide (LLO) binding pockets (PubMed:29301962).2 Publications

Miscellaneous

Present with 3000 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+By similarity, Mn2+By similarity

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Glycosylates at a rate of 3.5 peptides per minute per OST.1 Publication
  1. KM=21.3 µM for an Asn-Tyr-Thr tripeptide1 Publication
  2. KM=0.094 µM for Glc3Man9GlcNAc2-PP-Dol1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein glycosylation

    This protein is involved in the pathway protein glycosylation, which is part of Protein modification.1 Publication
    View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi47ManganeseBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei47Target acceptor peptideBy similarity1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei159Important for catalytic activityBy similarity1
    Metal bindingi166ManganeseBy similarity1
    Metal bindingi168ManganeseBy similarity1
    Binding sitei350Target acceptor peptideBy similarity1
    Binding sitei404Lipid-linked oligosaccharideBy similarity1
    Binding sitei521Lipid-linked oligosaccharideBy similarity1
    Binding sitei586Target acceptor peptideBy similarity1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionGlycosyltransferase, Transferase
    LigandMagnesium, Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:YGL022W-MONOMER
    YEAST:YGL022W-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.4.99.18 984

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00378

    Protein family/group databases

    Carbohydrate-Active enZymes

    More...
    CAZyi
    GT66 Glycosyltransferase Family 66

    Transport Classification Database

    More...
    TCDBi
    9.B.142.3.14 the integral membrane glycosyltransferase family 39 (gt39) family

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3 (EC:2.4.99.18)
    Short name:
    Oligosaccharyl transferase subunit STT3
    Alternative name(s):
    Staurosporine and temperature sensitivity protein 3
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:STT3
    Ordered Locus Names:YGL022W
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome VII

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    FungiDB:YGL022W

    Saccharomyces Genome Database

    More...
    SGDi
    S000002990 STT3

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 8Cytoplasmic1 Publication8
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei9 – 30Helical1 PublicationAdd BLAST22
    Topological domaini31 – 118Lumenal1 PublicationAdd BLAST88
    Transmembranei119 – 137Helical1 PublicationAdd BLAST19
    Topological domaini138 – 139Cytoplasmic1 Publication2
    Transmembranei140 – 157Helical1 PublicationAdd BLAST18
    Topological domaini158 – 168Lumenal1 PublicationAdd BLAST11
    Transmembranei169 – 188Helical1 PublicationAdd BLAST20
    Topological domaini189 – 190Cytoplasmic1 Publication2
    Transmembranei191 – 205Helical1 PublicationAdd BLAST15
    Topological domaini206 – 210Lumenal1 Publication5
    Transmembranei211 – 227Helical1 PublicationAdd BLAST17
    Topological domaini228 – 232Cytoplasmic1 Publication5
    Transmembranei233 – 258Helical1 PublicationAdd BLAST26
    Topological domaini259 – 266Lumenal1 Publication8
    Transmembranei267 – 286Helical1 PublicationAdd BLAST20
    Topological domaini287 – 300Cytoplasmic1 PublicationAdd BLAST14
    Transmembranei301 – 322HelicalSequence analysisAdd BLAST22
    Topological domaini323 – 355Lumenal1 PublicationAdd BLAST33
    Transmembranei356 – 378Helical1 PublicationAdd BLAST23
    Topological domaini379 – 384Cytoplasmic1 Publication6
    Transmembranei385 – 401Helical1 PublicationAdd BLAST17
    Topological domaini402 – 405Lumenal1 Publication4
    Transmembranei406 – 427Helical1 PublicationAdd BLAST22
    Topological domaini428 – 441Cytoplasmic1 PublicationAdd BLAST14
    Transmembranei442 – 464Helical1 PublicationAdd BLAST23
    Topological domaini465 – 718Lumenal1 PublicationAdd BLAST254

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi47D → A: Lethal; impairs the catalytic activity. 1 Publication1
    Mutagenesisi159R → A: Temperature sensitive and staurosporine sensitive. 1 Publication1
    Mutagenesisi160S → A: Temperature sensitive and staurosporine sensitive. 1 Publication1
    Mutagenesisi163G → R: Temperature sensitive and staurosporine sensitive. 1
    Mutagenesisi164S → A: Temperature sensitive and staurosporine sensitive. 1 Publication1
    Mutagenesisi166D → A: Lethal; impairs the catalytic activity. 1 Publication1
    Mutagenesisi168E → Q: Lethal; impairs the catalytic activity. 1 Publication1
    Mutagenesisi208W → A: Lethal; abolishes interaction with OST1 and WBP1. 1 Publication1
    Mutagenesisi210G → D: Temperature sensitive and staurosporine sensitive. 1 Publication1
    Mutagenesisi350E → A: Lethal; impairs the catalytic activity. 1 Publication1
    Mutagenesisi393V → I: Staurosporine sensitive. 1 Publication1
    Mutagenesisi404R → A: Lethal; abolishes interaction with OST1 and WBP1. 2 Publications1
    Mutagenesisi516 – 519WWDY → AAAA: Lethal; greatly reduces amount of OST1 in complex. 4
    Mutagenesisi516W → A: Temperature-sensitive. 1 Publication1
    Mutagenesisi517W → A: Lethal. 1 Publication1
    Mutagenesisi518D → A: Lethal. 1 Publication1
    Mutagenesisi519Y → A: Temperature-sensitive. 1 Publication1
    Mutagenesisi520G → D: Temperature-sensitive. 1 Publication1
    Mutagenesisi554 – 556EEK → AAA: Temperature-sensitive; reduces amount of OST1 in complex. 3
    Mutagenesisi586K → A: Temperature sensitive. 1 Publication1
    Mutagenesisi592 – 594RIS → AAA: Lethal; reduces glycosylation; greatly reduces amount of OST1 in complex. 3
    Mutagenesisi593I → D: Temperature-sensitive. 1 Publication1

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000722931 – 718Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3Add BLAST718

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi60N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
    Glycosylationi535N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
    Glycosylationi539N-linked (GlcNAc...) (high mannose) asparagine1 Publication1

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P39007

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P39007

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P39007

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P39007

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Component of the oligosaccharyltransferase (OST) complex, which appears to exist in two assemblies comprising OST1, OST2, OST4, OST5, STT3, SWP1, WPB1, and either OST3 or OST6 (PubMed:10677492, PubMed:16297388, PubMed:16096345, PubMed:15831493, PubMed:15886282, PubMed:9405463, PubMed:9435788, PubMed:29301962). OST assembly occurs through the formation of 3 subcomplexes. Subcomplex 1 contains OST1 and OST5, subcomplex 2 contains STT3, OST3, and OST4, and subcomplex 3 contains OST2, WBP1, and SWP1 (PubMed:29301962).

    Interacts with SEC61 (PubMed:15831493).

    8 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Hide details

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    33224, 642 interactors

    ComplexPortal: manually curated resource of macromolecular complexes

    More...
    ComplexPortali
    CPX-1638 Oligosaccharyl transferase complex variant 1
    CPX-1639 Oligosaccharyl transferase complex variant 2

    Database of interacting proteins

    More...
    DIPi
    DIP-2459N

    Protein interaction database and analysis system

    More...
    IntActi
    P39007, 8 interactors

    Molecular INTeraction database

    More...
    MINTi
    P39007

    STRING: functional protein association networks

    More...
    STRINGi
    4932.YGL022W

    Miscellaneous databases

    RNAct, Protein-RNA interaction predictions for model organisms.

    More...
    RNActi
    P39007 protein

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1718
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P39007

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni516 – 518Target acceptor peptide bindingBy similarity3

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi45 – 47DXD motif 1By similarity3
    Motifi166 – 168DXD motif 21 Publication3
    Motifi347 – 350SVSE motifBy similarity4
    Motifi516 – 520WWDYG motif1 Publication5
    Motifi583 – 590DK motif1 Publication8

    <p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    Despite low primary sequence conservation between eukaryotic catalytic subunits and bacterial and archaeal single subunit OSTs (ssOST), structural comparison revealed several common motifs at spatially equivalent positions, like the DXD motif 1 on the external loop 1 and the DXD motif 2 on the external loop 2 involved in binding of the metal ion cofactor and the carboxamide group of the acceptor asparagine, the conserved Glu residue of the TIXE/SVSE motif on the external loop 5 involved in catalysis, as well as the WWDYG and the DK/MI motifs in the globular domain that define the binding pocket for the +2 Ser/Thr of the acceptor sequon. In bacterial ssOSTs, an Arg residue was found to interact with a negatively charged side chain at the -2 position of the sequon. This Arg is conserved in bacterial enzymes and correlates with an extended sequon requirement (Asp-X-Asn-X-Ser/Thr) for bacterial N-glycosylation.1 Publication

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the STT3 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000155488

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_009279_1_0_1

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P39007

    KEGG Orthology (KO)

    More...
    KOi
    K07151

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    NYRATAY

    Family and domain databases

    Database of protein disorder

    More...
    DisProti
    DP01195

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR003674 Oligo_trans_STT3

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02516 STT3, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    P39007-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MGSDRSCVLS VFQTILKLVI FVAIFGAAIS SRLFAVIKFE SIIHEFDPWF
    60 70 80 90 100
    NYRATKYLVN NSFYKFLNWF DDRTWYPLGR VTGGTLYPGL MTTSAFIWHA
    110 120 130 140 150
    LRNWLGLPID IRNVCVLFAP LFSGVTAWAT YEFTKEIKDA SAGLLAAGFI
    160 170 180 190 200
    AIVPGYISRS VAGSYDNEAI AITLLMVTFM FWIKAQKTGS IMHATCAALF
    210 220 230 240 250
    YFYMVSAWGG YVFITNLIPL HVFLLILMGR YSSKLYSAYT TWYAIGTVAS
    260 270 280 290 300
    MQIPFVGFLP IRSNDHMAAL GVFGLIQIVA FGDFVKGQIS TAKFKVIMMV
    310 320 330 340 350
    SLFLILVLGV VGLSALTYMG LIAPWTGRFY SLWDTNYAKI HIPIIASVSE
    360 370 380 390 400
    HQPVSWPAFF FDTHFLIWLF PAGVFLLFLD LKDEHVFVIA YSVLCSYFAG
    410 420 430 440 450
    VMVRLMLTLT PVICVSAAVA LSKIFDIYLD FKTSDRKYAI KPAALLAKLI
    460 470 480 490 500
    VSGSFIFYLY LFVFHSTWVT RTAYSSPSVV LPSQTPDGKL ALIDDFREAY
    510 520 530 540 550
    YWLRMNSDED SKVAAWWDYG YQIGGMADRT TLVDNNTWNN THIAIVGKAM
    560 570 580 590 600
    ASPEEKSYEI LKEHDVDYVL VIFGGLIGFG GDDINKFLWM IRISEGIWPE
    610 620 630 640 650
    EIKERDFYTA EGEYRVDARA SETMRNSLLY KMSYKDFPQL FNGGQATDRV
    660 670 680 690 700
    RQQMITPLDV PPLDYFDEVF TSENWMVRIY QLKKDDAQGR TLRDVGELTR
    710
    SSTKTRRSIK RPELGLRV
    Length:718
    Mass (Da):81,529
    Last modified:October 1, 1996 - v2
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD00B8FF7B2B11B9F
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    D28952 Genomic DNA Translation: BAA06079.1
    Z72544 Genomic DNA Translation: CAA96722.1
    BK006941 Genomic DNA Translation: DAA08076.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S64024

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_011493.1, NM_001180887.1

    Genome annotation databases

    Ensembl fungal genome annotation project

    More...
    EnsemblFungii
    YGL022W_mRNA; YGL022W; YGL022W

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    852862

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    sce:YGL022W

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D28952 Genomic DNA Translation: BAA06079.1
    Z72544 Genomic DNA Translation: CAA96722.1
    BK006941 Genomic DNA Translation: DAA08076.1
    PIRiS64024
    RefSeqiNP_011493.1, NM_001180887.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2LGZNMR-A465-718[»]
    6C26electron microscopy3.50A1-718[»]
    6EZNelectron microscopy3.30F1-718[»]
    SMRiP39007
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi33224, 642 interactors
    ComplexPortaliCPX-1638 Oligosaccharyl transferase complex variant 1
    CPX-1639 Oligosaccharyl transferase complex variant 2
    DIPiDIP-2459N
    IntActiP39007, 8 interactors
    MINTiP39007
    STRINGi4932.YGL022W

    Protein family/group databases

    CAZyiGT66 Glycosyltransferase Family 66
    TCDBi9.B.142.3.14 the integral membrane glycosyltransferase family 39 (gt39) family

    PTM databases

    iPTMnetiP39007

    Proteomic databases

    MaxQBiP39007
    PaxDbiP39007
    PRIDEiP39007

    Genome annotation databases

    EnsemblFungiiYGL022W_mRNA; YGL022W; YGL022W
    GeneIDi852862
    KEGGisce:YGL022W

    Organism-specific databases

    EuPathDBiFungiDB:YGL022W
    SGDiS000002990 STT3

    Phylogenomic databases

    GeneTreeiENSGT00940000155488
    HOGENOMiCLU_009279_1_0_1
    InParanoidiP39007
    KOiK07151
    OMAiNYRATAY

    Enzyme and pathway databases

    UniPathwayiUPA00378
    BioCyciMetaCyc:YGL022W-MONOMER
    YEAST:YGL022W-MONOMER
    BRENDAi2.4.99.18 984

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P39007
    RNActiP39007 protein

    Family and domain databases

    DisProtiDP01195
    InterProiView protein in InterPro
    IPR003674 Oligo_trans_STT3
    PfamiView protein in Pfam
    PF02516 STT3, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSTT3_YEAST
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P39007
    Secondary accession number(s): D6VUB5
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: October 1, 1996
    Last modified: June 17, 2020
    This is version 173 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    4. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    5. Yeast chromosome VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names
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