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Protein

Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit stt3

Gene

stt3

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score:

Annotation score:4 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>
-Protein inferred from homologyi <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

<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 ‘Function’ 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 bindingi55ManganeseBy similarity1
<p>This subsection of the ‘Function’ 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 sitei55Target 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>Sitei166Important for catalytic activityBy similarity1
Metal bindingi173ManganeseBy similarity1
Metal bindingi175ManganeseBy similarity1
Binding sitei357Target acceptor peptideBy similarity1
Binding sitei411Lipid-linked oligosaccharideBy similarity1
Binding sitei555Lipid-linked oligosaccharideBy similarity1
Binding sitei620Target 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

  • dolichyl-diphosphooligosaccharide-protein glycotransferase activity Source: GO_Central
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • post-translational protein modification Source: GO_Central
  • protein N-linked glycosylation Source: PomBase
  • protein N-linked glycosylation via asparagine Source: GO_Central

<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 stt3 (EC:2.4.99.18)
Short name:
Oligosaccharyl transferase subunit stt3
<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:stt3
ORF Names:SPBC1271.02
<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>OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
<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 identifieri284812 [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 lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
<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
  • UP000002485 <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 II

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:SPBC1271.02

Schizosaccharomyces pombe database

More...
PomBasei
SPBC1271.02 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; 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 – 21CytoplasmicCuratedAdd BLAST21
<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>Transmembranei22 – 42HelicalSequence analysisAdd BLAST21
Topological domaini43 – 125LumenalCuratedAdd BLAST83
Transmembranei126 – 144HelicalBy similarityAdd BLAST19
Topological domaini145 – 146CytoplasmicCurated2
Transmembranei147 – 164HelicalBy similarityAdd BLAST18
Topological domaini165 – 175LumenalCuratedAdd BLAST11
Transmembranei176 – 195HelicalBy similarityAdd BLAST20
Topological domaini196 – 197CytoplasmicCurated2
Transmembranei198 – 212HelicalBy similarityAdd BLAST15
Topological domaini213 – 217LumenalCurated5
Transmembranei218 – 234HelicalBy similarityAdd BLAST17
Topological domaini235 – 239CytoplasmicCurated5
Transmembranei240 – 265HelicalBy similarityAdd BLAST26
Topological domaini266 – 273LumenalCurated8
Transmembranei274 – 293HelicalBy similarityAdd BLAST20
Topological domaini294 – 302CytoplasmicCurated9
Transmembranei303 – 323HelicalSequence analysisAdd BLAST21
Topological domaini324 – 362LumenalCuratedAdd BLAST39
Transmembranei363 – 385HelicalBy similarityAdd BLAST23
Topological domaini386 – 391CytoplasmicCurated6
Transmembranei392 – 408HelicalBy similarityAdd BLAST17
Topological domaini409 – 412LumenalCurated4
Transmembranei413 – 434HelicalBy similarityAdd BLAST22
Topological domaini435 – 482CytoplasmicCuratedAdd BLAST48
Transmembranei483 – 503HelicalSequence analysisAdd BLAST21
Topological domaini504 – 752LumenalCuratedAdd BLAST249

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_00000722921 – 752Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit stt3Add BLAST752

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>Glycosylationi569N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi573N-linked (GlcNAc...) (high mannose) asparagineBy similarity1

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
O94335

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

More...
PaxDbi
O94335

PRoteomics IDEntifications database

More...
PRIDEi
O94335

<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.By similarity

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
276723, 1 interactor

STRING: functional protein association networks

More...
STRINGi
4896.SPBC1271.02.1

<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>Regioni550 – 552Target 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>Motifi53 – 55DXD motif 1By similarity3
Motifi173 – 175DXD motif 2By similarity3
Motifi354 – 357SVSE motifBy similarity4
Motifi550 – 554WWDYG motifBy similarity5
Motifi617 – 624DK 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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000157471

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O94335

KEGG Orthology (KO)

More...
KOi
K07151

Identification of Orthologs from Complete Genome Data

More...
OMAi
NYRATAY

Database of Orthologous Groups

More...
OrthoDBi
EOG092C0UC6

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O94335

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>.<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_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.

O94335-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MANSATITSK KGVKSHQKDW KIPLKVLILI CIAVASVSSR LFSVIRYESI
60 70 80 90 100
IHEFDPWFNF RASKILVEQG FYNFLNWFDE RSWYPLGRVA GGTLYPGLMV
110 120 130 140 150
TSGIIFKVLH LLRINVNIRD VCVLLAPAFS GITAIATYYL ARELKSDACG
160 170 180 190 200
LLAAAFMGIA PGYTSRSVAG SYDNEAIAIT LLMSTFALWI KAVKSGSSFW
210 220 230 240 250
GACTGLLYFY MVTAWGGYVF ITNMIPLHVF VLLLMGRYTS KLYIAYTTYY
260 270 280 290 300
VIGTLASMQV PFVGFQPVST SEHMSALGVF GLLQLFAFYN YVKGLVSSKQ
310 320 330 340 350
FQILIRFALV CLVGLATVVL FALSSTGVIA PWTGRFYSLW DTNYAKIHIP
360 370 380 390 400
IIASVSEHQP PTWSSLFFDL QFLIWLLPVG VYLCFKELRN EHVFIIIYSV
410 420 430 440 450
LGTYFCGVMV RLVLTLTPCV CIAAAVAIST LLDTYMGPEV EEDKVSEEAA
460 470 480 490 500
SAKSKNKKGI FSILSFFTSG SKNIGIYSLL SRVLVISSTA YFLIMFVYHS
510 520 530 540 550
SWVTSNAYSS PTVVLSTVLN DGSLMYIDDF REAYDWLRRN TPYDTKVMSW
560 570 580 590 600
WDYGYQIAGM ADRITLVDNN TWNNTHIATV GKAMSSPEEK AYPILRKHDV
610 620 630 640 650
DYILIIYGGT LGYSSDDMNK FLWMIRISQG LWPDEIVERN FFTPNGEYRT
660 670 680 690 700
DDAATPTMRE SLLYKMSYHG AWKLFPPNQG YDRARNQKLP SKDPQLFTIE
710 720 730 740 750
EAFTTVHHLV RLYKVKKPDT LGRDLKQVTL FEEGKRKKLR RPAKTNEIPL

RV
Length:752
Mass (Da):84,974
Last modified:May 1, 1999 - 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:i2ACB97DFE82B10B8
GO

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 conflicti399S → P in BAA76479 (PubMed:10234787).Curated1
Sequence conflicti461F → S in BAA76479 (PubMed:10234787).Curated1
Sequence conflicti739 – 752LRRPA…IPLRV → SAVLQKLTKFL in BAA76479 (PubMed:10234787).CuratedAdd BLAST14

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
AB015232 Genomic DNA Translation: BAA76479.1
CU329671 Genomic DNA Translation: CAA22192.1

Protein sequence database of the Protein Information Resource

More...
PIRi
T39338
T43370

NCBI Reference Sequences

More...
RefSeqi
NP_595148.1, NM_001021056.2

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
SPBC1271.02.1; SPBC1271.02.1:pep; SPBC1271.02

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
2540190

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
spo:SPBC1271.02

<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
AB015232 Genomic DNA Translation: BAA76479.1
CU329671 Genomic DNA Translation: CAA22192.1
PIRiT39338
T43370
RefSeqiNP_595148.1, NM_001021056.2

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Protein-protein interaction databases

BioGridi276723, 1 interactor
STRINGi4896.SPBC1271.02.1

Protein family/group databases

CAZyiGT66 Glycosyltransferase Family 66

Proteomic databases

MaxQBiO94335
PaxDbiO94335
PRIDEiO94335

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC1271.02.1; SPBC1271.02.1:pep; SPBC1271.02
GeneIDi2540190
KEGGispo:SPBC1271.02

Organism-specific databases

EuPathDBiFungiDB:SPBC1271.02
PomBaseiSPBC1271.02 stt3

Phylogenomic databases

HOGENOMiHOG000157471
InParanoidiO94335
KOiK07151
OMAiNYRATAY
OrthoDBiEOG092C0UC6
PhylomeDBiO94335

Enzyme and pathway databases

UniPathwayi
UPA00378

Miscellaneous databases

Protein Ontology

More...
PROi
PR:O94335

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...

<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_SCHPO
<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: O94335
Secondary accession number(s): Q8WZK7
<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: August 31, 2004
Last sequence update: May 1, 1999
Last modified: December 5, 2018
This is version 115 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 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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