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Entry version 132 (07 Oct 2020)
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%5Fsection">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%5Fsection">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%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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:SPAC19D5.03

    Schizosaccharomyces pombe database

    More...
    PomBasei
    SPAC19D5.03, cid1

    <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

    <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%5Fand%5Fbiotech%5Fsection">'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%5Fand%5Fdomains%5Fsection">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

    <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

    KEGG Orthology (KO)

    More...
    KOi
    K13291

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    PCTIPPY

    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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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

    EuPathDBiFungiDB:SPAC19D5.03
    PomBaseiSPAC19D5.03, cid1

    Phylogenomic databases

    eggNOGiKOG2277, Eukaryota
    HOGENOMiCLU_033943_0_2_1
    InParanoidiO13833
    KOiK13291
    OMAiPCTIPPY
    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

    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 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%5Fand%5Fisoforms">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: October 7, 2020
    This is version 132 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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