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Entry version 168 (18 Sep 2019)
Sequence version 2 (14 Aug 2001)
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Protein

AP-1-like transcription factor

Gene

pap1

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

Annotation score:5 out of 5

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

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

Transcription activator involved in multidrug resistance, oxidative stress response, and redox homeostasis. Regulates the transcription of genes encoding antioxidant enzymes like catalase ctt1 and components of the cellular thiol-reducing pathways, including the thioredoxin system (trx2, trr1), ABC tansporters involved in multidrug resistance like bfr1/hba2 and pmd1 as well as the gene obr1/apt1. Preferentially binds to promoters with the core binding site 5'-TTA[CG]TAA-3'. Activity of the transcription factor is controlled through oxidation of specific cysteine residues resulting in the alteration of its subcellular location. Oxidative stress induces nuclear accumulation and as a result pap1 transcriptional activity. Required for sty1/spc1-confered staurosporine resistance.5 Publications

<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 functionActivator, DNA-binding
Biological processTranscription, Transcription regulation

<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:
AP-1-like transcription factor
Alternative name(s):
Caffeine resistance protein 3
<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:pap1
Synonyms:caf3
ORF Names:SPAC1783.07c
<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 I

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:SPAC1783.07c

Schizosaccharomyces pombe database

More...
PomBasei
SPAC1783.07c pap1

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

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi259C → S: No effect. 1 Publication1
Mutagenesisi278C → A: Constitutively cytoplasmic. 2 Publications1
Mutagenesisi285C → S: Constitutively cytoplasmic. 1 Publication1
Mutagenesisi501C → A: Constitutively cytoplasmic. 2 Publications1
Mutagenesisi517F → A: Impairs nuclear export; when associated with A-519. 1 Publication1
Mutagenesisi519I → A: Weakens nuclear export. Impairs nuclear export; when associated with A-517. 1 Publication1
Mutagenesisi522L → A: Impairs nuclear export. 1 Publication1
Mutagenesisi523C → A: No effect. 1 Publication1
Mutagenesisi523C → S: Impairs nuclear export; when associated with S-532. 1 Publication1
Mutagenesisi526L → A: Impairs nuclear export. 1 Publication1
Mutagenesisi532C → S: Weakens nuclear export. Impairs nuclear export; when associated with S-523. 1 Publication1
Mutagenesisi532C → T: Constitutively cytoplasmic. 1 Publication1

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000765321 – 552AP-1-like transcription factorAdd BLAST552

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi278 ↔ 501In nuclear retained form2 Publications
Disulfide bondi285 ↔ 532In nuclear retained formBy similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Depending on the oxidative stress inducing agent, pap1 can undergo two distinct conformational changes, both masking the nuclear export signal, thus abolishing nuclear export by crm1/exportin 1. The glutathione-depleting agent diethylmaleate (DEM) leads to the non-reversible modification of at least 2 cysteine residues in the c-CRD. Peroxide stress induces the formation of a tpx1-dependent interdomain disulfide bond between Cys-278 and Cys-501.3 Publications

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q01663

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

More...
PaxDbi
Q01663

PRoteomics IDEntifications database

More...
PRIDEi
Q01663

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q01663

<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

Homodimer (PubMed:11017199). The reduced form of pap1 interacts in the nucleus with the nuclear export protein crm1, and in the cytoplasm with the peroxiredoxin tpx1 (PubMed:12100563, PubMed:24316080).

3 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
278616, 72 interactors

Protein interaction database and analysis system

More...
IntActi
Q01663, 1 interactor

Molecular INTeraction database

More...
MINTi
Q01663

STRING: functional protein association networks

More...
STRINGi
4896.SPAC1783.07c.1

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

Secondary structure

1552
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
Q01663

Database of comparative protein structure models

More...
ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q01663

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini76 – 139bZIPPROSITE-ProRule annotationAdd BLAST64

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>Regioni81 – 102Basic motifPROSITE-ProRule annotationAdd BLAST22
Regioni104 – 111Leucine-zipperPROSITE-ProRule annotation8
Regioni259 – 290n-CRD1 PublicationAdd BLAST32
Regioni501 – 532c-CRD1 PublicationAdd BLAST32

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>Motifi81 – 88Nuclear localization signalPROSITE-ProRule annotation8
Motifi515 – 533Nuclear export signal1 PublicationAdd BLAST19

<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

Contains two cysteine rich domains (CRD), referred to as the N- and C-terminal CRD's, n-CRD (Cys-259, Cys-278, Cys-285 and Cys-290) and c-CRD (Cys-501, Cys-523 and Cys-532), respectively. Cys-259 and Cys-290 are not conserved in orthologs in other yeast species. A nuclear export signal is embedded in the c-CRD, with which the nuclear export protein crm1/exportin 1 interacts only in the absence of disulfide bonds (or otherwise oxidized cysteines) within the c-CRD or between the c-CRD and the n-CRD.2 Publications

<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 bZIP family. YAP subfamily.Curated

Phylogenomic databases

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q01663

KEGG Orthology (KO)

More...
KOi
K09043

Identification of Orthologs from Complete Genome Data

More...
OMAi
QFDPVLF

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q01663

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.238.100, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR004827 bZIP
IPR013910 TF_PAP1
IPR023167 Yap1_redox_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00170 bZIP_1, 1 hit
PF08601 PAP1, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00338 BRLZ, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF111430 SSF111430, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50217 BZIP, 1 hit
PS00036 BZIP_BASIC, 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>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.

Q01663-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSGQTETLSS TSNIPIAKAE PEQSADFSAS HKKRGPVSDR SSRRTSSEEV
60 70 80 90 100
DLMPNVDDEV DGDVKPKKIG RKNSDQEPSS KRKAQNRAAQ RAFRKRKEDH
110 120 130 140 150
LKALETQVVT LKELHSSTTL ENDQLRQKVR QLEEELRILK DGSFTFEMSL
160 170 180 190 200
PHRNPSLSSL PTTGFSSNFA HMKDGISPQS NLHLSPNSIE KPNMHQNVLH
210 220 230 240 250
NDRSADNLNH RYQVPPTLVD SNSAQGTLSP ETPSSSDSPS NLYLNYPKRK
260 270 280 290 300
SITHLHHDCS ALSNGENGED VADGKQFCQK LSTACGSIAC SMLTKTTPHR
310 320 330 340 350
ASVDILSNLH ESTVSPPMAD ESVQRSSEVS KSIPNVELSL NVNQQFVSPF
360 370 380 390 400
GGTDSFPLPT DTGLDSLFEP DSAIENSHLK NVVMEPELFQ AWREPAESLD
410 420 430 440 450
KEFFNDEGEI DDVFHNYFHN SNENGDLITN SLHGLDFLEN ANESFPEQMY
460 470 480 490 500
PFIKHNKDYI SNHPDEVPPD GLPQKGKHDT SSQMPSENEI VPAKERAYLS
510 520 530 540 550
CPKVWSKIIN HPRFESFDID DLCSKLKNKA KCSSSGVLLD ERDVEAALNQ

FN
Length:552
Mass (Da):61,532
Last modified:August 14, 2001 - 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:iD9E7FEA0A286B4BE
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 conflicti166S → P in CAA40363 (PubMed:1899230).Curated1
Sequence conflicti280 – 281KL → NV in CAA40363 (PubMed:1899230).Curated2
Sequence conflicti543 – 552DVEAALNQFN → RC in CAA40363 (PubMed:1899230).Curated10

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X57078 Genomic DNA Translation: CAA40363.1
CU329670 Genomic DNA Translation: CAB66170.1
AB027778 Genomic DNA Translation: BAA87082.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S15664
T50109

NCBI Reference Sequences

More...
RefSeqi
NP_593662.1, NM_001019094.2

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
SPAC1783.07c.1; SPAC1783.07c.1:pep; SPAC1783.07c

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
2542140

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
spo:SPAC1783.07c

<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
X57078 Genomic DNA Translation: CAA40363.1
CU329670 Genomic DNA Translation: CAB66170.1
AB027778 Genomic DNA Translation: BAA87082.1
PIRiS15664
T50109
RefSeqiNP_593662.1, NM_001019094.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GD2X-ray2.00E/F/G/H/I/J71-140[»]
SMRiQ01663
ModBaseiSearch...

Protein-protein interaction databases

BioGridi278616, 72 interactors
IntActiQ01663, 1 interactor
MINTiQ01663
STRINGi4896.SPAC1783.07c.1

PTM databases

iPTMnetiQ01663

Proteomic databases

MaxQBiQ01663
PaxDbiQ01663
PRIDEiQ01663

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC1783.07c.1; SPAC1783.07c.1:pep; SPAC1783.07c
GeneIDi2542140
KEGGispo:SPAC1783.07c

Organism-specific databases

EuPathDBiFungiDB:SPAC1783.07c
PomBaseiSPAC1783.07c pap1

Phylogenomic databases

InParanoidiQ01663
KOiK09043
OMAiQFDPVLF
PhylomeDBiQ01663

Miscellaneous databases

EvolutionaryTraceiQ01663

Protein Ontology

More...
PROi
PR:Q01663

Family and domain databases

Gene3Di1.10.238.100, 1 hit
InterProiView protein in InterPro
IPR004827 bZIP
IPR013910 TF_PAP1
IPR023167 Yap1_redox_dom_sf
PfamiView protein in Pfam
PF00170 bZIP_1, 1 hit
PF08601 PAP1, 1 hit
SMARTiView protein in SMART
SM00338 BRLZ, 1 hit
SUPFAMiSSF111430 SSF111430, 1 hit
PROSITEiView protein in PROSITE
PS50217 BZIP, 1 hit
PS00036 BZIP_BASIC, 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 nameiAP1_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: Q01663
Secondary accession number(s): Q9US23, Q9UU69
<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 1, 1993
Last sequence update: August 14, 2001
Last modified: September 18, 2019
This is version 168 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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