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Entry version 137 (29 Sep 2021)
Sequence version 2 (01 Nov 1999)
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Protein

Terminal uridylyltransferase cid1

Gene

cid1

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

Cytoplasmic uridylyltransferase that mediates the terminal uridylation of mRNAs with short poly(A) tails such as such as act1, hcn1 and urg1 mRNAs, hence facilitating global mRNA decay (PubMed:17353264, PubMed:17449726, PubMed:19430462, PubMed:22751018, PubMed:22885303).

Uridylates the 3' ends of actin mRNAs upon S-phase arrest (PubMed:17353264).

Has also a weak poly(A) polymerase (PAP) activity (PubMed:22751018, PubMed:22885303).

Residue His-336 is responsible for the specificity for UTP (PubMed:22751018, PubMed:22885303).

Involved in cell cycle arrest where in association with crb2/rhp9 and chk1 it inhibits unscheduled mitosis (PubMed:10757807).

5 Publications

Caution

Has been first identified as a cytoplasmic poly(A) polymerase (PAP) implicated in cell cycle checkpoint controls (PubMed:12218190). Further studies showed that cid1 had robust poly(U) polymerase activity in vitro and that is was rather an RNA uridylyltransferase (PubMed:17353264, PubMed:17449726).3 Publications

<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+2 Publications, Mn2+1 Publication

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

Mutation of His-336 to Asn decreases the Km for ATP to 65 µM and increases the Km for UTP to 45 µM.1 Publication
  1. KM=12 µM for UTP1 Publication
  2. KM=312 µM for ATP1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei90Substrate4 Publications1
<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 bindingi101Magnesium; catalytic1 Publication1
Binding sitei101Substrate1 Publication1
Metal bindingi103Magnesium; catalytic1 Publication1
Binding sitei103Substrate1 Publication1
Binding sitei171Substrate2 Publications1
Binding sitei193Substrate4 Publications1
Binding sitei197Substrate4 Publications1
Binding sitei211Substrate1 Publication1
Binding sitei336Substrate4 Publications1
Binding sitei340Substrate1 Publication1

<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 functionNucleotidyltransferase, Transferase
LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SPO-429947, Deadenylation of mRNA

<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:
Terminal uridylyltransferase cid1Curated (EC:2.7.7.195 Publications, EC:2.7.7.526 Publications)
Short name:
TUTase cid1Curated
Alternative name(s):
Caffeine-induced death protein 11 Publication
Poly(A) polymerase cid11 Publication
Short name:
PAP1 Publication
Poly(U) polymerase cid11 Publication
Short name:
PUP1 Publication
<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:cid11 Publication
ORF Names:SPAC19D5.03
<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

Schizosaccharomyces pombe database

More...
PomBasei
SPAC19D5.03, cid1

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:SPAC19D5.03

<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

Keywords - Cellular componenti

Cytoplasm

<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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Stabilizes urg1 transcripts (PubMed:19430462).1 Publication

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>Mutagenesisi88F → D: Impairs catalytic activity. 1 Publication1
Mutagenesisi101D → A: Abolishes catalytic activity but does not affect RNA binding; when associated with A-103. 2 Publications1
Mutagenesisi103D → A: Abolishes catalytic activity but does not affect RNA binding; when associated with A-101. 2 Publications1
Mutagenesisi133K → A: Impairs binding to RNA; when associated with A-137; A-321 and A-323. Impairs also binding to RNA; when associated with A-137; A-277 and A-282. 1 Publication1
Mutagenesisi137R → A: Impairs binding to RNA; when associated with A-133; A-321 and A-323. Impairs also binding to RNA; when associated with A-133; A-277 and A-282. 1 Publication1
Mutagenesisi144K → A: Reduces association with a 15-mer A stretch but does not affect association with a 15-mer U stretch. 1 Publication1
Mutagenesisi160D → A: Abolishes catalytic activity. 2 Publications1
Mutagenesisi164N → P: Predominantly performs monouridylation. 1 Publication1
Mutagenesisi165N → A or P: Abolishes catalytic activity. 2 Publications1
Mutagenesisi277R → A: Impairs binding to RNA; when associated with A-282; A-133 and A-137. Impairs also binding to RNA; when associated with A-282; A-321 and A-323. 1 Publication1
Mutagenesisi282K → A: Impairs binding to RNA; when associated with A-277; A-133 and A-137. Impairs also binding to RNA; when associated with A-277; A-321 and A-323. 1 Publication1
Mutagenesisi321K → A: Impairs binding to RNA; when associated with A-323; A-277 and A-282. Impairs also binding to RNA; when associated with A-323; A-133 and A-137. 1 Publication1
Mutagenesisi323R → A: Impairs binding to RNA; when associated with A-321; A-277 and A-282. Impairs also binding to RNA; when associated with A-321; A-133 and A-137. 1 Publication1
Mutagenesisi330D → A: Leads to diminished TUTase activity. 1 Publication1
Mutagenesisi332F → A: Reduces capacity for binding RNAs. 1 Publication1
Mutagenesisi333E → A: Leads to diminished TUTase activity. 1 Publication1
Mutagenesisi336H → A or N: Abolishes the UTP specificity and converts Cid1 from a TUTase into a poly(A) polymerase (PAP). 2 Publications1

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001203121 – 405Terminal uridylyltransferase cid1Add BLAST405

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
O13833

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

More...
PaxDbi
O13833

PRoteomics IDEntifications database

More...
PRIDEi
O13833

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O13833

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
278883, 30 interactors

STRING: functional protein association networks

More...
STRINGi
4896.SPAC19D5.03.1

<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

1405
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
O13833

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

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

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>Domaini267 – 336PAP-associatedSequence analysisAdd BLAST70

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>Regioni168 – 172Substrate binding3 Publications5
Regioni211 – 212Substrate binding4 Publications2
Regioni377 – 405DisorderedSequence analysisAdd BLAST29

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi378 – 405Basic and acidic residuesSequence analysisAdd BLAST28

<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 DNA polymerase type-B-like family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2277, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_033943_0_2_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O13833

Identification of Orthologs from Complete Genome Data

More...
OMAi
AYKFEPR

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O13833

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.460.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR043519, NT_sf
IPR002058, PAP_assoc

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03828, PAP_assoc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF81301, SSF81301, 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.

O13833-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNISSAQFIP GVHTVEEIEA EIHKNLHISK SCSYQKVPNS HKEFTKFCYE
60 70 80 90 100
VYNEIKISDK EFKEKRAALD TLRLCLKRIS PDAELVAFGS LESGLALKNS
110 120 130 140 150
DMDLCVLMDS RVQSDTIALQ FYEELIAEGF EGKFLQRARI PIIKLTSDTK
160 170 180 190 200
NGFGASFQCD IGFNNRLAIH NTLLLSSYTK LDARLKPMVL LVKHWAKRKQ
210 220 230 240 250
INSPYFGTLS SYGYVLMVLY YLIHVIKPPV FPNLLLSPLK QEKIVDGFDV
260 270 280 290 300
GFDDKLEDIP PSQNYSSLGS LLHGFFRFYA YKFEPREKVV TFRRPDGYLT
310 320 330 340 350
KQEKGWTSAT EHTGSADQII KDRYILAIED PFEISHNVGR TVSSSGLYRI
360 370 380 390 400
RGEFMAASRL LNSRSYPIPY DSLFEEAPIP PRRQKKTDEQ SNKKLLNETD

GDNSE
Length:405
Mass (Da):46,257
Last modified:November 1, 1999 - 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:i0AA24B4411B61027
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
CU329670 Genomic DNA Translation: CAB50789.1
AF105076 mRNA Translation: AAD16889.1

Protein sequence database of the Protein Information Resource

More...
PIRi
T37963

NCBI Reference Sequences

More...
RefSeqi
NP_594901.1, NM_001020330.2

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
SPAC19D5.03.1; SPAC19D5.03.1:pep; SPAC19D5.03

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
2542420

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
spo:SPAC19D5.03

<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
CU329670 Genomic DNA Translation: CAB50789.1
AF105076 mRNA Translation: AAD16889.1
PIRiT37963
RefSeqiNP_594901.1, NM_001020330.2

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
4E7XX-ray3.20A/B/C/D1-405[»]
4E80X-ray3.02A/B/C/D1-405[»]
4E8FX-ray2.60A/B1-405[»]
4EP7X-ray2.28A/B40-377[»]
4FH3X-ray2.00A33-377[»]
4FH5X-ray2.30A33-377[»]
4FHPX-ray2.50A33-377[»]
4FHVX-ray2.10A33-377[»]
4FHWX-ray2.50A33-377[»]
4FHXX-ray2.70A33-377[»]
4FHYX-ray2.70A33-377[»]
4NKTX-ray1.90A/B40-377[»]
4NKUX-ray1.94A/B40-377[»]
4UD4X-ray1.74A/B40-405[»]
4UD5X-ray2.52A/B40-405[»]
SMRiO13833
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi278883, 30 interactors
STRINGi4896.SPAC19D5.03.1

PTM databases

iPTMnetiO13833

Proteomic databases

MaxQBiO13833
PaxDbiO13833
PRIDEiO13833

Genome annotation databases

EnsemblFungiiSPAC19D5.03.1; SPAC19D5.03.1:pep; SPAC19D5.03
GeneIDi2542420
KEGGispo:SPAC19D5.03

Organism-specific databases

PomBaseiSPAC19D5.03, cid1
VEuPathDBiFungiDB:SPAC19D5.03

Phylogenomic databases

eggNOGiKOG2277, Eukaryota
HOGENOMiCLU_033943_0_2_1
InParanoidiO13833
OMAiAYKFEPR
PhylomeDBiO13833

Enzyme and pathway databases

ReactomeiR-SPO-429947, Deadenylation of mRNA

Miscellaneous databases

Protein Ontology

More...
PROi
PR:O13833

Family and domain databases

Gene3Di3.30.460.10, 1 hit
InterProiView protein in InterPro
IPR043519, NT_sf
IPR002058, PAP_assoc
PfamiView protein in Pfam
PF03828, PAP_assoc, 1 hit
SUPFAMiSSF81301, SSF81301, 1 hit

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 nameiCID1_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: O13833
Secondary accession number(s): O94608
<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 14, 2001
Last sequence update: November 1, 1999
Last modified: September 29, 2021
This is version 137 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

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

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. 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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