Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 146 (23 Feb 2022)
Sequence version 1 (01 Jul 1993)
Previous versions | rss
Add a publicationFeedback
Protein

Cohesin subunit rad21

Gene

rad21

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

Cleavable component of the cohesin complex, involved in chromosome cohesion during cell cycle. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At metaphase-anaphase transition, this protein is cleaved by cut1 and dissociates from chromatin, allowing sister chromatids to segregate. Also involved in the DNA double-strand-break (DSB) repair system.

2 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

  • chromatin binding Source: GO_Central

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

Biological processCell cycle, Cell division, Chromosome partition, DNA damage, DNA repair, Mitosis

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SPO-2470946, Cohesin Loading onto Chromatin
R-SPO-2500257, Resolution of Sister Chromatid Cohesion
R-SPO-3108214, SUMOylation of DNA damage response and repair proteins

<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:
Cohesin subunit rad21
Alternative name(s):
Double-strand-break repair protein rad21
SCC1 homolog
<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:rad21
ORF Names:SPCC338.17c
<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 III

Organism-specific databases

Schizosaccharomyces pombe database

More...
PomBasei
SPCC338.17c, rad21

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:SPCC338.17c

<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

Centromere, Chromosome, 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%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>Mutagenesisi179R → E: Sister chromatid separation blocked; when associated with E-231. 1 Publication1
Mutagenesisi231R → E: Sister chromatid separation blocked; when associated with E-179. 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000978711 – 628Cohesin subunit rad21Add BLAST628

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei219Phosphoserine1 Publication1
Modified residuei547Phosphoserine1 Publication1
Modified residuei553Phosphoserine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Hyperphosphorylated during S and G2 phases.
Proteolytic cleavage of a fraction of hyperphosphorylated form at the onset of anaphase may be essential for the proper progression of anaphase and sister chromatid separation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei179 – 180CleavageCurated2
Sitei231 – 232CleavageCurated2

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P30776

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

More...
PaxDbi
P30776

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P30776

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Cohesin complexes are composed of the psm1/smc1 and psm3/smc3 heterodimer attached via their hinge domain, rad21/scc1 which link them, and psc3/scc3, which interacts with rad21.

Interacts with ssl3.

2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
276010, 34 interactors

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
P30776

Protein interaction database and analysis system

More...
IntActi
P30776, 3 interactors

STRING: functional protein association networks

More...
STRINGi
4896.SPCC338.17c.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

3D structure databases

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

More...
SMRi
P30776

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

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>Regioni439 – 466DisorderedSequence analysisAdd BLAST28

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 biasi439 – 460Basic and acidic residuesSequence analysisAdd BLAST22

<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 rad21 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1213, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_015775_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P30776

Identification of Orthologs from Complete Genome Data

More...
OMAi
PLCLNTN

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P30776

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.10.580, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR039781, Rad21/Rec8-like
IPR006909, Rad21/Rec8_C_eu
IPR006910, Rad21_Rec8_N
IPR023093, ScpA-like_C
IPR036390, WH_DNA-bd_sf

The PANTHER Classification System

More...
PANTHERi
PTHR12585, PTHR12585, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF04824, Rad21_Rec8, 1 hit
PF04825, Rad21_Rec8_N, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF46785, SSF46785, 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.

P30776-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFYSEAILSK KGPLAKVWLA AHWEKKLSKV QTLHTSIEQS VHAIVTEETA
60 70 80 90 100
PMALRLSGQL MLGVVRIYSR KARYLLEDCT EALMRLKMSF QPGQVDMIEP
110 120 130 140 150
ATALQSLKGK DAVTQSANLT LPETITEFDL LVPDSTFDFQ WSQLLRTPSR
160 170 180 190 200
SSNTLELHSL PISSSPSFPS SQLSIEAGRN AQVESGFSLG ESFAHVGNDM
210 220 230 240 250
QFHLPISNSG AATPRSVHSD NQSQISIEVG RDAPAAAATD LSGIIGPQMT
260 270 280 290 300
KSPASSVTHF STPSMLPIGG TSLDDELLAP VDDLNLDLGL DDLLGDEQGA
310 320 330 340 350
NAPAIEADEQ AETSSIHLPS DIMEDDSSRP AAAGVEEGQV VESATAPQQE
360 370 380 390 400
KINPQKTVRR QRAIIDPVTE LSSKQMKKQL ADTSSITSPL CLNTSSIVFN
410 420 430 440 450
ATVNFTRNGK FNTSIFSSNL NPKVNELLQA DFKQAILRKR KNESPEEVEP
460 470 480 490 500
AKHQRTDTST ENQETAEVLD PEEIAAAELA NITEAAIATL PQETVVQPEG
510 520 530 540 550
EAPELGSPMG FPVTALESAD DSLFDAPPVM LDEADLLGSE RLDSSVSEAL
560 570 580 590 600
PSSQTAKDSL RNKWDPYTEG EKVSFQTLSA GCNREEAVQL FFDVLVLATK
610 620
DVISVKQDVA IQNEITLTAK RGMLLSSL
Length:628
Mass (Da):67,854
Last modified:July 1, 1993 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iDB60FF893AE0C9DE
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
M96437 Genomic DNA Translation: AAA35330.1
CU329672 Genomic DNA Translation: CAA19348.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S35547

NCBI Reference Sequences

More...
RefSeqi
NP_588151.1, NM_001023140.2

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
SPCC338.17c.1; SPCC338.17c.1:pep; SPCC338.17c

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
2539447

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
spo:SPCC338.17c

<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
M96437 Genomic DNA Translation: AAA35330.1
CU329672 Genomic DNA Translation: CAA19348.1
PIRiS35547
RefSeqiNP_588151.1, NM_001023140.2

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
6YUFelectron microscopy3.94B1-628[»]
SMRiP30776
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi276010, 34 interactors
ELMiP30776
IntActiP30776, 3 interactors
STRINGi4896.SPCC338.17c.1

PTM databases

iPTMnetiP30776

Proteomic databases

MaxQBiP30776
PaxDbiP30776

Genome annotation databases

EnsemblFungiiSPCC338.17c.1; SPCC338.17c.1:pep; SPCC338.17c
GeneIDi2539447
KEGGispo:SPCC338.17c

Organism-specific databases

PomBaseiSPCC338.17c, rad21
VEuPathDBiFungiDB:SPCC338.17c

Phylogenomic databases

eggNOGiKOG1213, Eukaryota
HOGENOMiCLU_015775_0_0_1
InParanoidiP30776
OMAiPLCLNTN
PhylomeDBiP30776

Enzyme and pathway databases

ReactomeiR-SPO-2470946, Cohesin Loading onto Chromatin
R-SPO-2500257, Resolution of Sister Chromatid Cohesion
R-SPO-3108214, SUMOylation of DNA damage response and repair proteins

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P30776

Family and domain databases

Gene3Di1.10.10.580, 1 hit
InterProiView protein in InterPro
IPR039781, Rad21/Rec8-like
IPR006909, Rad21/Rec8_C_eu
IPR006910, Rad21_Rec8_N
IPR023093, ScpA-like_C
IPR036390, WH_DNA-bd_sf
PANTHERiPTHR12585, PTHR12585, 1 hit
PfamiView protein in Pfam
PF04824, Rad21_Rec8, 1 hit
PF04825, Rad21_Rec8_N, 1 hit
SUPFAMiSSF46785, SSF46785, 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 nameiRAD21_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: P30776
<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: July 1, 1993
Last sequence update: July 1, 1993
Last modified: February 23, 2022
This is version 146 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

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

Keywords - Technical termi

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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again