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Entry version 142 (16 Oct 2019)
Sequence version 1 (01 Nov 1995)
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Protein

Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A

Gene

Stt3a

Organism
Mus musculus (Mouse)
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. This subunit contains the active site and the acceptor peptide and donor lipid-linked oligosaccharide (LLO) binding pockets (By similarity). 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 post-translational glycosylation and mediate glycosylation of sites that have been skipped by STT3A (By similarity).By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 <a href="http://www.uniprot.org/help/function_section">'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.By similarity
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_section">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 bindingi49ManganeseBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei49Target 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>Sitei160Important for catalytic activityBy similarity1
Metal bindingi167ManganeseBy similarity1
Metal bindingi169ManganeseBy similarity1
Binding sitei351Target acceptor peptideBy similarity1
Binding sitei405Lipid-linked oligosaccharideBy similarity1
Binding sitei530Lipid-linked oligosaccharideBy similarity1
Binding sitei595Target 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, Metal-binding

Enzyme and pathway databases

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

<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_and_taxonomy_section">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 STT3A (EC:2.4.99.18)
Short name:
Oligosaccharyl transferase subunit STT3A
Short name:
STT3-A
Alternative name(s):
B5
Integral membrane protein 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:Stt3a
Synonyms:Itm1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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 9

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:105124 Stt3a

<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 Cytoskeleton Lysosome 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_location_section">'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 – 17CytoplasmicCuratedAdd BLAST17
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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>Transmembranei18 – 38HelicalSequence analysisAdd BLAST21
Topological domaini39 – 119LumenalCuratedAdd BLAST81
Transmembranei120 – 138HelicalBy similarityAdd BLAST19
Topological domaini139 – 140CytoplasmicCurated2
Transmembranei141 – 158HelicalBy similarityAdd BLAST18
Topological domaini159 – 169LumenalCuratedAdd BLAST11
Transmembranei170 – 189HelicalBy similarityAdd BLAST20
Topological domaini190 – 191CytoplasmicCurated2
Transmembranei192 – 206HelicalBy similarityAdd BLAST15
Topological domaini207 – 211LumenalCurated5
Transmembranei212 – 228HelicalBy similarityAdd BLAST17
Topological domaini229 – 233CytoplasmicCurated5
Transmembranei234 – 259HelicalBy similarityAdd BLAST26
Topological domaini260 – 267LumenalCurated8
Transmembranei268 – 287HelicalBy similarityAdd BLAST20
Topological domaini288 – 300CytoplasmicCuratedAdd BLAST13
Transmembranei301 – 321HelicalSequence analysisAdd BLAST21
Topological domaini322 – 356LumenalCuratedAdd BLAST35
Transmembranei357 – 379HelicalBy similarityAdd BLAST23
Topological domaini380 – 385CytoplasmicCurated6
Transmembranei386 – 402HelicalBy similarityAdd BLAST17
Topological domaini403 – 406LumenalCurated4
Transmembranei407 – 428HelicalBy similarityAdd BLAST22
Topological domaini429 – 453CytoplasmicCuratedAdd BLAST25
Transmembranei454 – 473HelicalBy similarityAdd BLAST20
Topological domaini474 – 705LumenalCuratedAdd BLAST232

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000722911 – 705Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3AAdd BLAST705

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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>Glycosylationi537N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi544N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi548N-linked (GlcNAc...) (high mannose) asparagine1 Publication1

Keywords - PTMi

Glycoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P46978

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P46978

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

More...
PaxDbi
P46978

PeptideAtlas

More...
PeptideAtlasi
P46978

PRoteomics IDEntifications database

More...
PRIDEi
P46978

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
2264

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P46978

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P46978

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P46978

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000032116 Expressed in 282 organ(s), highest expression level in cumulus cell

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P46978 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P46978 MM

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the oligosaccharyltransferase (OST) complex. OST exists in two different complex forms which contain common core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either STT3A or STT3B as catalytic subunits, and form-specific accessory subunits. STT3A complex assembly occurs through the formation of 3 subcomplexes. Subcomplex 1 contains RPN1 and TMEM258, subcomplex 2 contains the STT3A-specific subunits STT3A, DC2/OSTC, and KCP2 as well as the core subunit OST4, and subcomplex 3 contains RPN2, DAD1, and OST48. The STT3A complex can form stable complexes with the Sec61 complex or with both the Sec61 and TRAP complexes.

By similarity

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
200842, 1 interactor

Protein interaction database and analysis system

More...
IntActi
P46978, 2 interactors

Molecular INTeraction database

More...
MINTi
P46978

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000113116

<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>Regioni525 – 527Target 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>Motifi47 – 49DXD motif 1By similarity3
Motifi167 – 169DXD motif 2By similarity3
Motifi348 – 351SVSE motifBy similarity4
Motifi525 – 529WWDYG motifBy similarity5
Motifi592 – 599DK motifBy similarity8

<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.By similarity

<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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2292 Eukaryota
COG1287 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000156655

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000157471

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P46978

KEGG Orthology (KO)

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KOi
K07151

Identification of Orthologs from Complete Genome Data

More...
OMAi
SWSSFYF

Database of Orthologous Groups

More...
OrthoDBi
187775at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P46978

TreeFam database of animal gene trees

More...
TreeFami
TF300822

Family and domain databases

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_length">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>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

This entry has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

P46978-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTKLGFLRLS YEKQDTLLKL LILSMAAVLS FSTRLFAVLR FESVIHEFDP
60 70 80 90 100
YFNYRTTRFL AEEGFYKFHN WFDDRAWYPL GRIIGGTIYP GLMITSAAIY
110 120 130 140 150
HVLHFFHITI DIRNVCVFLA PLFSSFTTIV TYHLTKELKD AGAGLLAAAM
160 170 180 190 200
IAVVPGYISR SVAGSYDNEG IAIFCMLLTY YMWIKAVKTG SIYWAAKCAL
210 220 230 240 250
AYFYMVSSWG GYVFLINLIP LHVLVLMLTG RFSHRIYVAY CTVYCLGTIL
260 270 280 290 300
SMQISFVGFQ PVLSSEHMAA FGVFGLCQIH AFVDYLRSKL NPQQFEVLFR
310 320 330 340 350
SVISLVGFVL LTVGALLMLT GKISPWTGRF YSLLDPSYAK NNIPIIASVS
360 370 380 390 400
EHQPTTWSSY YFDLQLLVFM FPVGLYYCFS NLSDARIFII MYGVTSMYFS
410 420 430 440 450
AVMVRLMLVL APVMCILSGI GVSQVLSTYM KNLDISRPDK KSKKQQDSTY
460 470 480 490 500
PIKNEVASGM ILVMAFFLIT YTFHSTWVTS EAYSSPSIVL SARGGDGSRI
510 520 530 540 550
IFDDFREAYY WLRHNTPEDA KVMSWWDYGY QITAMANRTI LVDNNTWNNT
560 570 580 590 600
HISRVGQAMA STEEKAYEIM RELDVSYVLV IFGGLTGYSS DDINKFLWMV
610 620 630 640 650
RIGGSTETGR HIKENDYYTP TGEFRVDREG SPVLLNCLMY KMCYYRFGQV
660 670 680 690 700
YTEAKRPPGF DRVRNAEIGN KDFELDVLEE AYTTEHWLVR IYKVKDLDNR

GLSRT
Length:705
Mass (Da):80,598
Last modified:November 1, 1995 - v1
<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:iCD1D796D0479F321
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F6YHG5F6YHG5_MOUSE
Dolichyl-diphosphooligosaccharide--...
Stt3a
112Annotation score:

Annotation score:1 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>
D3YZN5D3YZN5_MOUSE
Dolichyl-diphosphooligosaccharide--...
Stt3a
90Annotation score:

Annotation score:1 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>
A0A1L1SSD1A0A1L1SSD1_MOUSE
Dolichyl-diphosphooligosaccharide--...
Stt3a
60Annotation score:

Annotation score:1 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>
D6RDS9D6RDS9_MOUSE
Dolichyl-diphosphooligosaccharide--...
Stt3a
69Annotation score:

Annotation score:1 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>

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
L34260 mRNA Translation: AAB47775.1
BC037612 mRNA Translation: AAH37612.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS52768.1

NCBI Reference Sequences

More...
RefSeqi
NP_032434.3, NM_008408.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000120381; ENSMUSP00000113116; ENSMUSG00000032116

Database of genes from NCBI RefSeq genomes

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GeneIDi
16430

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:16430

UCSC genome browser

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UCSCi
uc009oty.1 mouse

<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
L34260 mRNA Translation: AAB47775.1
BC037612 mRNA Translation: AAH37612.1
CCDSiCCDS52768.1
RefSeqiNP_032434.3, NM_008408.4

3D structure databases

Database of comparative protein structure models

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ModBasei
Search...

SWISS-MODEL Interactive Workspace

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SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

BioGridi200842, 1 interactor
IntActiP46978, 2 interactors
MINTiP46978
STRINGi10090.ENSMUSP00000113116

Protein family/group databases

CAZyiGT66 Glycosyltransferase Family 66

PTM databases

GlyConnecti2264
iPTMnetiP46978
PhosphoSitePlusiP46978
SwissPalmiP46978

Proteomic databases

EPDiP46978
jPOSTiP46978
PaxDbiP46978
PeptideAtlasiP46978
PRIDEiP46978

Genome annotation databases

EnsembliENSMUST00000120381; ENSMUSP00000113116; ENSMUSG00000032116
GeneIDi16430
KEGGimmu:16430
UCSCiuc009oty.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
3703
MGIiMGI:105124 Stt3a

Phylogenomic databases

eggNOGiKOG2292 Eukaryota
COG1287 LUCA
GeneTreeiENSGT00940000156655
HOGENOMiHOG000157471
InParanoidiP46978
KOiK07151
OMAiSWSSFYF
OrthoDBi187775at2759
PhylomeDBiP46978
TreeFamiTF300822

Enzyme and pathway databases

UniPathwayiUPA00378

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
Stt3a mouse

Protein Ontology

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PROi
PR:P46978

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSMUSG00000032116 Expressed in 282 organ(s), highest expression level in cumulus cell
ExpressionAtlasiP46978 baseline and differential
GenevisibleiP46978 MM

Family and domain databases

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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiSTT3A_MOUSE
<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: P46978
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 16, 2019
This is version 142 of the entry and version 1 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 programChordata 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
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