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UniProtKB - P18296 (CUT1_SCHPO)

Entry version 152 (18 Sep 2019)
Sequence version 3 (14 Aug 2001)
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Protein

Separin

Gene

cut1

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

Caspase-like protease, which plays a central role in the chromosome segregation by cleaving the rad21 subunit of the cohesin complex at the onset of anaphase. During most of the cell cycle, it is inactivated by securin/cut2 protein. It is also required for pointed nuclear formation.1 Publication

<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

  • All bonds known to be hydrolyzed by this endopeptidase have arginine in P1 and an acidic residue in P4. P6 is often occupied by an acidic residue or by a hydroxy-amino-acid residue, the phosphorylation of which enhances cleavage. EC:3.4.22.49

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

It is inactivated via its interaction with cut2, which probably covers its active site. Cut2 degradation at anaphase, liberates it and triggers rad21 cleavage.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei17301

<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

  • cysteine-type endopeptidase activity Source: GO_Central
  • endopeptidase activity Source: PomBase
Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionHydrolase, Protease, Thiol protease
Biological processCell cycle, Cell division, Chromosome partition

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-SPO-2467813 Separation of Sister Chromatids

<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:
Separin (EC:3.4.22.49)
Alternative name(s):
Cell untimely torn protein 1
Separase
<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:cut1
ORF Names:SPCC5E4.04
<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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces ›
<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 III

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		FungiDB:SPCC5E4.04

Schizosaccharomyces pombe database

More...PomBasei		SPCC5E4.04 cut1

<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>Mutagenesisi1767D → A: Affects the formation of the pointed nucleus; when associated with V-1779. 1 Publication1
Mutagenesisi1779E → V: Affects the formation of the pointed nucleus; when associated with A-1767. 1 Publication1
Mutagenesisi1816A → T in cut1-T693; reduced function; when transferred at 33 degrees Celsius. 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002059031 – 1828SeparinAdd BLAST1828

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P18296

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

More...PaxDbi		P18296

PRoteomics IDEntifications database

More...PRIDEi		P18296

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P18296

<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

Interacts with cut2.

Interacts with rad21.

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		276005, 52 interactors

Database of interacting proteins

More...DIPi		DIP-84N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P18296

STRING: functional protein association networks

More...STRINGi		4896.SPCC5E4.04.1

<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

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>Domaini1647 – 1741Peptidase C50Add BLAST95

Phylogenomic databases

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P18296

KEGG Orthology (KO)

More...KOi		K02365

Identification of Orthologs from Complete Genome Data

More...OMAi		IYEHMGQ

Database for complete collections of gene phylogenies

More...PhylomeDBi		P18296

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.25.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR005314 Peptidase_C50
IPR030397 SEPARIN_core_dom
IPR011990 TPR-like_helical_dom_sf

The PANTHER Classification System

More...PANTHERi		PTHR12792 PTHR12792, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51700 SEPARIN, 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.

P18296-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSTRSIVTSK VSWTPEKFIS ALSYPEHCSI TLVKRLKASV KLKDLKQNIS 
        60         70         80         90        100
RDAPSWTFEH LFVAFKCAVS NLAKQWAELS TTDKEKTRRM FCTPSRLNTA 
       110        120        130        140        150
HRPEVFYLLE CCTYILEQMQ VVTKNTSHLY DCIRSGVSIC NRLLDMEIFE 
       160        170        180        190        200
PAISLLMKTH KNLIILLTYR DHDAIPTATL LNPTLDVSEI QLESCLFVPM 
       210        220        230        240        250
VPASYFLNIG TIVVTFQLNV LRCLSLSQIN GLSLNTINNL QSEDGPFQWI 
       260        270        280        290        300
ERSFPSQVQL ANSRREILAR LLTRFSMIQN NALQSFKLLI LSIALWLNIL 
       310        320        330        340        350
SSQRADDKEF DVNQLETRIL QLFSKVVQLC KSEDIEGSIL NKDMTQLHHL 
       360        370        380        390        400
LENLSKESRL HILLQLSQLY YKYNDFQLSA AYVIRGYSLS FEDISFKLKF 
       410        420        430        440        450
LLFSFRLSIH DNSICFPFNL IQELSSLQQL FVENALPYSE ALHLLDSIER 
       460        470        480        490        500
SFRLFNDSTV FDDTVFALNI SEILSWILSS VVRDILVEDE LLNLQLKIRK 
       510        520        530        540        550
FLMFTFHIIR SFSELTKFQS SLEGCLNLAA YYEDAEFPQK LSNHLYNLCV 
       560        570        580        590        600
KSSNVNYARE CISLSIKIAV SHKLTNDETY LLKILKNFQL RYHDSLQLQE 
       610        620        630        640        650
KCDVLHTTFN QLDLYVGTTS VGKSSVLDNI LKRIFNSLTS INDSNIEKLL 
       660        670        680        690        700
ESISYSLLKL FFKCANEGSR YNASAALSFK LSLMLHEKEE VLLLKTNVSC 
       710        720        730        740        750
VLANHGYNDI KFEEMVLCVI KGDQNLLEHN SNNNAKLALN ESLLCSWENL 
       760        770        780        790        800
LCYRRAEDDS RILTIIESWT IFISRFSSVI SRCSFTDFEI NSILNFFFCF 
       810        820        830        840        850
LHTVEPSGKL TFELAFLEIF YELFNCLLHL QFSKYLVIIG TLLSDKYMTL 
       860        870        880        890        900
GFSGKAHLFY TKCYSYLRQC KSSPFINFWN VSYGKYLILT GNTDKGILQL 
       910        920        930        940        950
KKYSLSSEED FNSNGLSRTV SLNLLLYERI QLSDALFQLG YTTVSLGFIM 
       960        970        980        990       1000
QNLKVIKGLF SKSSKEHFNG GKYITWRLFA VSAHSNVCAA RIYEHMGQAR 
      1010       1020       1030       1040       1050
EAEFFYRQAC SISEKMPFSC FSATFQLRLC SLLTRAGKLE KGEKILFDLT 
      1060       1070       1080       1090       1100
EAMKSTDTYH KLLWNYGAAE VCATKSELDG AICHYSECVK LLEIIKSEYY 
      1110       1120       1130       1140       1150
LFFNRNREKS LTKGIKRLSL SSQPTFVTES NTTEFDDWSI LQNTAANLLR 
      1160       1170       1180       1190       1200
LISMFELKRG NLEIAKALMT DSTKCSIASF FNIVSANILK SKLIVCEADS 
      1210       1220       1230       1240       1250
TLFGDPVLRT LPDSVISLPG ISHKFQKNQS KTKALGENTG FRKGSKRLDY 
      1260       1270       1280       1290       1300
LRERLKINLQ NVRLSCEIIF SNAYERSSVC VCREVNELIS YSTIMQSALT 
      1310       1320       1330       1340       1350
TIGETTDVDS SSASFFLEIP KALGFHRRRE AQKFRNQHKE LHFSSLEQIL 
      1360       1370       1380       1390       1400
NSRLSIPDVR TFQDNFIDSL PSIWNVVSIT INNSGEDLFI SKIRKGHSPL 
      1410       1420       1430       1440       1450
IFRLPLQRHN SRDADEEILV FTKAQTELFR IISKSNQMAQ NGKHYTRRED 
      1460       1470       1480       1490       1500
KETWWKERRH LDQCLQQLLE NIEISWLGGF KGIFNPHKID TSLFAKFSSQ 
      1510       1520       1530       1540       1550
FQNIIAKNFN MDKKTPVPTL SPEILELFIT LGKPGYEGYE QLLEDLIYFI 
      1560       1570       1580       1590       1600
LDIFQFRGLH FAYDEIDTDQ LSMDLQDALN AYFNNYVSEE NRSHTVLVLD 
      1610       1620       1630       1640       1650
KSVHQFPWES LPCLNRQSVS RVPSLSILRD ILSQSFVVNG EYVEVRKEAG 
      1660       1670       1680       1690       1700
SYILNPSLDL KHTQEMFEHK LVEGGWKGLI ASQPSNRDFI KMLSGNDFFL 
      1710       1720       1730       1740       1750
YFGHGGGEQY TTSYDLATLK RCAVTILMGC SSGALYECGS FEPWGTPLDY 
      1760       1770       1780       1790       1800
LSAGCPTLVA NLWDVTDKDI DRFSLKMLES WGLFENKAPF VNSTSICTAV 
      1810       1820 
SESRSCCHLR YLNGAAPVIY GIPAYIIP
Length:1,828
Mass (Da):209,434
Last modified:August 14, 2001 - v3
<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:iB6216CA28DA7CAE1
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 conflicti430 – 437LFVENALP → PLSKMLDR (PubMed:2203537).Curated8
Sequence conflicti430 – 437LFVENALP → PLSKMLDR (PubMed:8978688).Curated8
Sequence conflicti1125T → S (PubMed:2203537).Curated1
Sequence conflicti1125T → S (PubMed:8978688).Curated1
Sequence conflicti1131N → Y (PubMed:2203537).Curated1
Sequence conflicti1131N → Y (PubMed:8978688).Curated1

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
M36179 Genomic DNA Translation: AAB06192.1
CU329672 Genomic DNA Translation: CAA21959.1

Protein sequence database of the Protein Information Resource

More...PIRi		A35694
T41455

NCBI Reference Sequences

More...RefSeqi		NP_587903.1, NM_001022895.2

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		SPCC5E4.04.1; SPCC5E4.04.1:pep; SPCC5E4.04

Database of genes from NCBI RefSeq genomes

More...GeneIDi		2539442

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		spo:SPCC5E4.04

<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
M36179 Genomic DNA Translation: AAB06192.1
CU329672 Genomic DNA Translation: CAA21959.1
PIRiA35694
T41455
RefSeqiNP_587903.1, NM_001022895.2

3D structure databases

Database of comparative protein structure models

More...ModBasei		Search...

SWISS-MODEL Interactive Workspace

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

Protein-protein interaction databases

BioGridi276005, 52 interactors
DIPiDIP-84N
ELMiP18296
STRINGi4896.SPCC5E4.04.1

PTM databases

iPTMnetiP18296

Proteomic databases

MaxQBiP18296
PaxDbiP18296
PRIDEiP18296

Genome annotation databases

EnsemblFungiiSPCC5E4.04.1; SPCC5E4.04.1:pep; SPCC5E4.04
GeneIDi2539442
KEGGispo:SPCC5E4.04

Organism-specific databases

EuPathDBiFungiDB:SPCC5E4.04
PomBaseiSPCC5E4.04 cut1

Phylogenomic databases

InParanoidiP18296
KOiK02365
OMAiIYEHMGQ
PhylomeDBiP18296

Enzyme and pathway databases

ReactomeiR-SPO-2467813 Separation of Sister Chromatids

Miscellaneous databases

Protein Ontology

More...PROi		PR:P18296

Family and domain databases

Gene3Di1.25.40.10, 1 hit
InterProiView protein in InterPro
IPR005314 Peptidase_C50
IPR030397 SEPARIN_core_dom
IPR011990 TPR-like_helical_dom_sf
PANTHERiPTHR12792 PTHR12792, 1 hit
PROSITEiView protein in PROSITE
PS51700 SEPARIN, 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 nameiCUT1_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: P18296
Secondary accession number(s): O94304
<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: November 1, 1990
Last sequence update: August 14, 2001
Last modified: September 18, 2019
This is version 152 of the entry and version 3 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. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
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