Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 112 (18 Sep 2019)
Sequence version 2 (11 Jul 2006)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B

Gene

Stt3b

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). 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 post-translational 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 (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 bindingi100ManganeseBy 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 sitei100Target 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>Sitei211Important for catalytic activityBy similarity1
Metal bindingi218ManganeseBy similarity1
Metal bindingi220ManganeseBy similarity1
Binding sitei402Target acceptor peptideBy similarity1
Binding sitei456Lipid-linked oligosaccharideBy similarity1
Binding sitei606Lipid-linked oligosaccharideBy similarity1
Binding sitei671Target 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 STT3B (EC:2.4.99.18)
Short name:
Oligosaccharyl transferase subunit STT3B
Short name:
STT3-B
Alternative name(s):
B6dom1 antigen
Source of immunodominant MHC-associated peptides
<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:Stt3b
Synonyms:Simp
<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: Unplaced

Organism-specific databases

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

More...
MGIi
MGI:1915542 Stt3b

<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 domaini2 – 41CytoplasmicCuratedAdd BLAST40
<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>Transmembranei42 – 83HelicalBy similarityAdd BLAST42
Topological domaini84 – 170LumenalCuratedAdd BLAST87
Transmembranei171 – 189HelicalBy similarityAdd BLAST19
Topological domaini190 – 191CytoplasmicCurated2
Transmembranei192 – 209HelicalBy similarityAdd BLAST18
Topological domaini210 – 220LumenalCuratedAdd BLAST11
Transmembranei221 – 240HelicalBy similarityAdd BLAST20
Topological domaini241 – 242CytoplasmicCurated2
Transmembranei243 – 257HelicalBy similarityAdd BLAST15
Topological domaini258 – 262LumenalCurated5
Transmembranei263 – 279HelicalBy similarityAdd BLAST17
Topological domaini280 – 284CytoplasmicCurated5
Transmembranei285 – 310HelicalBy similarityAdd BLAST26
Topological domaini311 – 318LumenalCurated8
Transmembranei319 – 338HelicalBy similarityAdd BLAST20
Topological domaini339 – 347CytoplasmicCurated9
Transmembranei348 – 368HelicalSequence analysisAdd BLAST21
Topological domaini369 – 407LumenalCuratedAdd BLAST39
Transmembranei408 – 430HelicalBy similarityAdd BLAST23
Topological domaini431 – 436CytoplasmicCurated6
Transmembranei437 – 453HelicalBy similarityAdd BLAST17
Topological domaini454 – 457LumenalCurated4
Transmembranei458 – 479HelicalBy similarityAdd BLAST22
Topological domaini480 – 523CytoplasmicCuratedAdd BLAST44
Transmembranei524 – 549HelicalBy similarityAdd BLAST26
Topological domaini550 – 823LumenalCuratedAdd BLAST274

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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<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_00002460022 – 823Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3BAdd BLAST822

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineBy similarity1
Modified residuei13PhosphoserineCombined sources1
Modified residuei18PhosphoserineBy similarity1
Modified residuei29PhosphoserineCombined sources1
Modified residuei495PhosphoserineCombined sources1
Modified residuei496PhosphoserineCombined sources1
<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>Glycosylationi613N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi620N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi624N-linked (GlcNAc...) (high mannose) asparagine1 Publication1
Glycosylationi638N-linked (GlcNAc...) asparagine1 Publication1

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q3TDQ1

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q3TDQ1

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q3TDQ1

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

More...
PaxDbi
Q3TDQ1

PeptideAtlas

More...
PeptideAtlasi
Q3TDQ1

PRoteomics IDEntifications database

More...
PRIDEi
Q3TDQ1

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
2265

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q3TDQ1

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

More...
PhosphoSitePlusi
Q3TDQ1

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q3TDQ1

<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. OST can form stable complexes with the Sec61 complex or with both the Sec61 and TRAP complexes (By similarity).

By similarity

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
212788, 2 interactors

Protein interaction database and analysis system

More...
IntActi
Q3TDQ1, 3 interactors

Molecular INTeraction database

More...
MINTi
Q3TDQ1

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000035010

<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>Regioni601 – 603Target 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>Motifi98 – 100DXD motif 1By similarity3
Motifi218 – 220DXD motif 2By similarity3
Motifi399 – 402SVSE motifBy similarity4
Motifi601 – 605WWDYG motifBy similarity5
Motifi668 – 675DK 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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000157471

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q3TDQ1

KEGG Orthology (KO)

More...
KOi
K07151

Database of Orthologous Groups

More...
OrthoDBi
187775at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q3TDQ1

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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q3TDQ1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAEPSAPESK HKSSLNSSPW SGLMALGNSR HGHHGPGTQS ASSAAAPKPG
60 70 80 90 100
PPAGLSGGLS QPAGWQSLLS FTILFLAWLA GFSSRLFAVI RFESIIHEFD
110 120 130 140 150
PWFNYRSTHH LASHGFYEFL NWFDERAWYP LGRIVGGTVY PGLMITAGLI
160 170 180 190 200
HWILNTLNIT VHIRDVCVFL APTFSGLTSI STFLLTRELW NQGAGLLAAC
210 220 230 240 250
FIAIVPGYIS RSVAGSFDNE GIAIFALQFT YYLWVKSVKT GSVFWTMCCC
260 270 280 290 300
LSYFYMVSAW GGYVFIINLI PLHVFVLLLM QRYSKRVYIA YSTFYIVGLI
310 320 330 340 350
LSMQIPFVGF QPIRTSEHMA AAGVFALLQA YAFLQYLRDR LTKQEFQTLF
360 370 380 390 400
FLGVSLAAGA VFLSVIYLTY TGYIAPWSGR FYSLWDTGYA KIHIPIIASV
410 420 430 440 450
SEHQPTTWVS FFFDLHILVC TFPAGLWFCI KNINDERVFV ALYAISAVYF
460 470 480 490 500
AGVMVRLMLT LTPVVCMLSA IAFSNVFEHY LGDDMKRENP PVEDSSDEDD
510 520 530 540 550
KRNPGNLYDK AGKVRKHVTE QEKPEEGLGP NIKSIVTMLM LMLLMMFAVH
560 570 580 590 600
CTWVTSNAYS SPSVVLASYN HDGTRNILDD FREAYFWLRQ NTDEHARVMS
610 620 630 640 650
WWDYGYQIAG MANRTTLVDN NTWNNSHIAL VGKAMSSNET AAYKIMRSLD
660 670 680 690 700
VDYVLVIFGG VIGYSGDDIN KFLWMVRIAE GEHPKDIREG DYFTQQGEFR
710 720 730 740 750
VDKAGSPTLL NCLMYKMSYY RFGEMQLDFR TPPGFDRTRN AEIGNKDIKF
760 770 780 790 800
KHLEEAFTSE HWLVRIYKVK APDNRETLGH KPRVTNIVPK QKYLSKKTTK
810 820
RKRGYVKNKL VFKKGKKTSK KTV
Length:823
Mass (Da):93,246
Last modified:July 11, 2006 - 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:iBBC27DB07EE609D1
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0R4J0D3A0A0R4J0D3_MOUSE
Dolichyl-diphosphooligosaccharide--...
Stt3b
823Annotation score:

Annotation score:2 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAH13054 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti43S → R in BAE41550 (PubMed:16141072).Curated1
Sequence conflicti43S → R in AAH03206 (PubMed:15489334).Curated1
Sequence conflicti240T → I in BAE41550 (PubMed:16141072).Curated1
Sequence conflicti294F → L in BAB31390 (PubMed:16141072).Curated1

<p>This subsection of the ‘Sequence’ section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement_in_disease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

In strains 129, C57BL/10, C57BL/6 and LP Glu-776 correlates with a B6dom1-positive phenotype, Asp-776 is found in resistant strains. The B6dom1 minor histocompatibility antigen (MiHA) is used as a model antigen in studying immunodominance.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti776E → D in strain: A.BY, B10.H7 and C3H.SW; correlated with B6dom1-negative phenotype. 1 Publication1

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
AK018758 mRNA Translation: BAB31390.1
AK145674 mRNA Translation: BAE26582.1
AK154979 mRNA Translation: BAE32968.1
AK152899 mRNA Translation: BAE31580.1
AK170079 mRNA Translation: BAE41550.1
BC003206 mRNA Translation: AAH03206.1
BC013054 mRNA Translation: AAH13054.2 Different initiation.
BC052433 mRNA Translation: AAH52433.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS23599.1

NCBI Reference Sequences

More...
RefSeqi
NP_077184.2, NM_024222.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
68292

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:68292

UCSC genome browser

More...
UCSCi
uc009ryp.1 mouse

Keywords - Coding sequence diversityi

Polymorphism

<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
AK018758 mRNA Translation: BAB31390.1
AK145674 mRNA Translation: BAE26582.1
AK154979 mRNA Translation: BAE32968.1
AK152899 mRNA Translation: BAE31580.1
AK170079 mRNA Translation: BAE41550.1
BC003206 mRNA Translation: AAH03206.1
BC013054 mRNA Translation: AAH13054.2 Different initiation.
BC052433 mRNA Translation: AAH52433.1
CCDSiCCDS23599.1
RefSeqiNP_077184.2, NM_024222.2

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

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

Protein-protein interaction databases

BioGridi212788, 2 interactors
IntActiQ3TDQ1, 3 interactors
MINTiQ3TDQ1
STRINGi10090.ENSMUSP00000035010

Protein family/group databases

CAZyiGT66 Glycosyltransferase Family 66

PTM databases

GlyConnecti2265
iPTMnetiQ3TDQ1
PhosphoSitePlusiQ3TDQ1
SwissPalmiQ3TDQ1

Proteomic databases

EPDiQ3TDQ1
jPOSTiQ3TDQ1
MaxQBiQ3TDQ1
PaxDbiQ3TDQ1
PeptideAtlasiQ3TDQ1
PRIDEiQ3TDQ1

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi68292
KEGGimmu:68292
UCSCiuc009ryp.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
201595
MGIiMGI:1915542 Stt3b

Phylogenomic databases

eggNOGiKOG2292 Eukaryota
COG1287 LUCA
HOGENOMiHOG000157471
InParanoidiQ3TDQ1
KOiK07151
OrthoDBi187775at2759
PhylomeDBiQ3TDQ1
TreeFamiTF300822

Enzyme and pathway databases

UniPathwayiUPA00378

Miscellaneous databases

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

More...
ChiTaRSi
Stt3b mouse

Protein Ontology

More...
PROi
PR:Q3TDQ1

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

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

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 nameiSTT3B_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: Q3TDQ1
Secondary accession number(s): Q7TT24
, Q921E3, Q99LL0, Q9D2V2
<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: July 11, 2006
Last sequence update: July 11, 2006
Last modified: September 18, 2019
This is version 112 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 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again