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UniProtKB - Q12158 (SCC1_YEAST)

Entry version 171 (16 Oct 2019)
Sequence version 1 (01 Nov 1996)
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Protein

Sister chromatid cohesion protein 1

Gene

MCD1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's 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 ESP1 and dissociates from chromatin, allowing sister chromatids to segregate.4 Publications

Miscellaneous

Present with 1040 molecules/cell in log phase SD medium.1 Publication

<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

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

Biological processCell cycle, Cell division, Chromosome partition, Mitosis

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		YEAST:G3O-29434-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-SCE-2468052 Establishment of Sister Chromatid Cohesion
R-SCE-2500257 Resolution of Sister Chromatid Cohesion
R-SCE-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_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:
Sister chromatid cohesion protein 1
<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:MCD1
Synonyms:PDS3, RHC21, SCC1
Ordered Locus Names:YDL003W
ORF Names:YD8119.04
<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>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's 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 identifieri559292 [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 › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<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
  • UP000002311 <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 IV

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		FungiDB:YDL003W

Saccharomyces Genome Database

More...SGDi		S000002161 MCD1

<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

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_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>Mutagenesisi175S → A: Reduces phosphorylation. Abolishes phosphorylation; when associated with A-263. 1 Publication1
Mutagenesisi180R → D: Abolishes cleavage by ESP1; when associated with D-268. 1 Publication1
Mutagenesisi210K → R: Loss of acetylation by ECO1. 1 Publication1
Mutagenesisi252K → R: No effect on acetylation by ECO1. 1 Publication1
Mutagenesisi263S → A: Reduces phosphorylation. Abolishes phosphorylation; when associated with A-175. 1 Publication1
Mutagenesisi268R → D: Abolishes first cleavage by ESP1. Abolishes all cleavage by ESP1; when associated with D-180. 1 Publication1
Mutagenesisi290K → R: No effect on acetylation by ECO1. 1 Publication1
Mutagenesisi310K → R: No effect on acetylation by ECO1. 1 Publication1
Mutagenesisi319K → R: No effect on acetylation by ECO1. 1 Publication1
Mutagenesisi324K → R: No effect on acetylation by ECO1. 1 Publication1

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000978811 – 566Sister chromatid cohesion protein 1Add BLAST566

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 residuei161PhosphoserineCombined sources1
Modified residuei175Phosphoserine; by CDC51 Publication1
Modified residuei210N6-acetyllysine; by ECO11 Publication1
Modified residuei263Phosphoserine; by CDC51 Publication1
Modified residuei307PhosphoserineCombined sources1
Modified residuei354PhosphothreonineCombined sources1

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

Cleaved by ESP1 at the onset of anaphase.
Phosphorylated by CDC5/Polo-like kinase at the onset of anaphase. Phosphorylation takes places at proximity to cleavage sites and is required for an efficient cleavage by ESP1.2 Publications
Acetylated by ECO1.1 Publication

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>Sitei180 – 181Cleavage; by ESP12
Sitei268 – 269Cleavage; by ESP12

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q12158

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

More...PaxDbi		Q12158

PRoteomics IDEntifications database

More...PRIDEi		Q12158

Consortium for Top Down Proteomics

More...TopDownProteomicsi		Q12158

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q12158

Miscellaneous databases

CutDB - Proteolytic event database

More...PMAP-CutDBi		Q12158

<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 directly with IRR1/SCC3 in cohesin complex. Cohesin complexes are composed of the SMC1 and SMC3 heterodimer attached via their hinge domain, MCD1/SCC1 which link them, and IRR1, which interacts with MCD1. The cohesin complex also interacts with SCC2, which is required for its association with chromosomes.

2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		32051, 342 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-1867 Nuclear mitotic cohesin complex

Database of interacting proteins

More...DIPi		DIP-5812N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		Q12158

Protein interaction database and analysis system

More...IntActi		Q12158, 36 interactors

Molecular INTeraction database

More...MINTi		Q12158

STRING: functional protein association networks

More...STRINGi		4932.YDL003W

<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

1566
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		Q12158

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q12158

<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

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 amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi258 – 261Poly-Asp4

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The C-terminal part associates with the head of SMC1, while the N-terminal part binds to the head of SMC3.

<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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000141751

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q12158

KEGG Orthology (KO)

More...KOi		K06670

Identification of Orthologs from Complete Genome Data

More...OMAi		GPLAQIW

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_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.

Q12158-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVTENPQRLT VLRLATNKGP LAQIWLASNM SNIPRGSVIQ THIAESAKEI 
        60         70         80         90        100
AKASGCDDES GDNEYITLRT SGELLQGIVR VYSKQATFLL TDIKDTLTKI 
       110        120        130        140        150
SMLFKTSQKM TSTVNRLNTV TRVHQLMLED AVTEREVLVT PGLEFLDDTT 
       160        170        180        190        200
IPVGLMAQEN SMERKVQGAA PWDTSLEVGR RFSPDEDFEH NNLSSMNLDF 
       210        220        230        240        250
DIEEGPITSK SWEEGTRQSS RNFDTHENYI QDDDFPLDDA GTIGWDLGIT 
       260        270        280        290        300
EKNDQNNDDD DNSVEQGRRL GESIMSEEPT DFGFDLDIEK EAPAGNIDTI 
       310        320        330        340        350
TDAMTESQPK QTGTRRNSKL LNTKSIQIDE ETENSESIAS SNTYKEERSN 
       360        370        380        390        400
NLLTPQPTNF TTKRLWSEIT ESMSYLPDPI LKNFLSYESL KKRKIHNGRE 
       410        420        430        440        450
GSIEEPELNV SLNLTDDVIS NAGTNDNSFN ELTDNMSDFV PIDAGLNEAP 
       460        470        480        490        500
FPEENIIDAK TRNEQTTIQT EKVRPTPGEV ASKAIVQMAK ILRKELSEEK 
       510        520        530        540        550
EVIFTDVLKS QANTEPENIT KREASRGFFD ILSLATEGCI GLSQTEAFGN 
       560 
IKIDAKPALF ERFINA
Length:566
Mass (Da):63,290
Last modified:November 1, 1996 - 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:iEB6C7CA33BAC208F
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
Y14280 Genomic DNA Translation: CAA74657.1
U23759 Genomic DNA Translation: AAB38803.1
Z48008 Genomic DNA Translation: CAA88058.1
Z48432 Genomic DNA Translation: CAA88356.1
Z74051 Genomic DNA Translation: CAA98559.1
BK006938 Genomic DNA Translation: DAA11845.1

Protein sequence database of the Protein Information Resource

More...PIRi		S50979

NCBI Reference Sequences

More...RefSeqi		NP_010281.1, NM_001180062.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YDL003W_mRNA; YDL003W; YDL003W

Database of genes from NCBI RefSeq genomes

More...GeneIDi		851561

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YDL003W

<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
Y14280 Genomic DNA Translation: CAA74657.1
U23759 Genomic DNA Translation: AAB38803.1
Z48008 Genomic DNA Translation: CAA88058.1
Z48432 Genomic DNA Translation: CAA88356.1
Z74051 Genomic DNA Translation: CAA98559.1
BK006938 Genomic DNA Translation: DAA11845.1
PIRiS50979
RefSeqiNP_010281.1, NM_001180062.1

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
1W1WX-ray2.90E/F/G/H451-564[»]
4UX3X-ray3.30B1-115[»]
5FRPX-ray2.90C/D116-159[»]
5FRSX-ray4.07C126-142[»]
6H8QX-ray3.63G/H301-400[»]
SMRiQ12158
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi32051, 342 interactors
ComplexPortaliCPX-1867 Nuclear mitotic cohesin complex
DIPiDIP-5812N
ELMiQ12158
IntActiQ12158, 36 interactors
MINTiQ12158
STRINGi4932.YDL003W

PTM databases

iPTMnetiQ12158

Proteomic databases

MaxQBiQ12158
PaxDbiQ12158
PRIDEiQ12158
TopDownProteomicsiQ12158

Genome annotation databases

EnsemblFungiiYDL003W_mRNA; YDL003W; YDL003W
GeneIDi851561
KEGGisce:YDL003W

Organism-specific databases

EuPathDBiFungiDB:YDL003W
SGDiS000002161 MCD1

Phylogenomic databases

HOGENOMiHOG000141751
InParanoidiQ12158
KOiK06670
OMAiGPLAQIW

Enzyme and pathway databases

BioCyciYEAST:G3O-29434-MONOMER
ReactomeiR-SCE-2468052 Establishment of Sister Chromatid Cohesion
R-SCE-2500257 Resolution of Sister Chromatid Cohesion
R-SCE-3108214 SUMOylation of DNA damage response and repair proteins

Miscellaneous databases

EvolutionaryTraceiQ12158
PMAP-CutDBiQ12158

Protein Ontology

More...PROi		PR:Q12158

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

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 nameiSCC1_YEAST
<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: Q12158
Secondary accession number(s): D6VRY5, Q05325
<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: May 9, 2003
Last sequence update: November 1, 1996
Last modified: October 16, 2019
This is version 171 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, Complete proteome, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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