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Entry version 61 (26 Feb 2020)
Sequence version 1 (28 Jun 2011)
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Protein

Mating-type protein ALPHA2

Gene

MATALPHA2

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

Mating type proteins are sequence specific DNA-binding proteins that act as master switches in yeast differentiation by controlling gene expression in a cell type-specific fashion. Transcriptional corepressor that binds cooperatively with MCM1 to a 31-basepair DNA sequence termed the a-specific gene (asg) operator, to repress the transcription of a-cell-specific genes. Additionally, in a/alpha diploid cells, binds cooperatively with the A1 protein to a 21-basepair DNA sequence termed the haploid-specific gene (hsg) operator, to repress transcription of haploid-specific genes and of MATALPHA1.1 Publication

Miscellaneous

There are three genetic loci for mating type genes in S.cerevisiae. MAT is the expression locus that determines the mating type of the cell, whereas HML (containing HMLALPHA1 and HMLALPHA2) and HMR (containing HMRA1 and HMRA2) represent silenced repositories of mating type information. The mating type is determined by the MAT locus, which contains either a copy of HML or of HMR. Diploid cells are usually heterozygous for the MAT locus.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi129 – 191Homeobox; TALE-typePROSITE-ProRule annotationAdd BLAST63

<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 functionDNA-binding, Repressor
Biological processTranscription, Transcription regulation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-29351-MONOMER

<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:
Mating-type protein ALPHA2
Short name:
MATalpha2 protein
Alternative name(s):
Alpha-2 repressor
<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:MATALPHA2
Synonyms:ALPHA-2, MAT2A, MATAL2
Ordered Locus Names:YCR039C
ORF Names:YCR39C
<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>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's 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 identifieri559292 [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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<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
  • UP000002311 <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

Saccharomyces Genome Database

More...
SGDi
S000000635 MATALPHA2

<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

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>Mutagenesisi4I → T: Reduces the ability of ALPHA2 to repress transcription, but binds normally to DNA and MCM1. 1 Publication1
Mutagenesisi9L → F: Reduces the ability of ALPHA2 to repress transcription, but binds normally to DNA and MCM1. 1 Publication1
Mutagenesisi10L → S: Reduces the ability of ALPHA2 to repress transcription, but binds normally to DNA and MCM1. Disrupts interaction with TUP1. 1 Publication1
Mutagenesisi71E → K: Reduces the ability of alpha2 to repress transcription, but binds normally to DNA and MCM1. 1 Publication1
Mutagenesisi114L → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. 1 Publication1
Mutagenesisi115V → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. 1 Publication1
Mutagenesisi116F → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. 1 Publication1
Mutagenesisi117N → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. 1 Publication1
Mutagenesisi118V → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. 1 Publication1
Mutagenesisi119V → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. 1 Publication1
Mutagenesisi120T → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. 1 Publication1
Mutagenesisi173R → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. Disrupts interaction with SSN6. 1 Publication1
Mutagenesisi181S → A in ALPHA2-3A; defective in binding DNA alone or in complex with MCM1, but binds DNA normally in complex with A1; when associated with A-182 and A-185. 1 Publication1
Mutagenesisi182N → A in ALPHA2-3A; defective in binding DNA alone or in complex with MCM1, but binds DNA normally in complex with A1; when associated with A-181 and A-185. 1 Publication1
Mutagenesisi185R → A in ALPHA2-3A; defective in binding DNA alone or in complex with MCM1, but binds DNA normally in complex with A1; when associated with A-181 and A-182. 1 Publication1
Mutagenesisi192I → A: Disrupts the ability of A1/ALPHA2 to repress haploid-specific genes. 1 Publication1
Mutagenesisi196L → A or S: Disrupts the ability of A1/ALPHA2 to repress haploid-specific genes. 2 Publications1
Mutagenesisi199L → A: Disrupts the ability of A1/ALPHA2 to repress haploid-specific genes. 1 Publication1
Mutagenesisi200L → A: Disrupts the ability of A1/ALPHA2 to repress haploid-specific genes. 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_00000491861 – 210Mating-type protein ALPHA2Add BLAST210

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 residuei1N-acetylmethionine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P0CY08

PRoteomics IDEntifications database

More...
PRIDEi
P0CY08

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P0CY08

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Only present in alpha-cells and in a/alpha diploid cells.

<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

Binds DNA with a high specificity as a heterotetramer consisting of an ALPHA2 dimer and an MCM1 dimer. Also binds DNA with a high specificity as a heterodimer of A1 and ALPHA2 in a/alpha diploid cells.

Interacts with the general transcription repressor complex SSN6/TUP1.

8 Publications

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

WithEntry#Exp.IntActNotes
P117462EBI-10443,EBI-10528

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
30922, 7 interactors
31022, 22 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-684 Mating-type MATalpha2-MATa1 complex
CPX-692 Mating-type MATalpha2-MCM1 complex

Protein interaction database and analysis system

More...
IntActi
P0CY08, 3 interactors

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P0CY08 protein

<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

1210
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

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SMRi
P0CY08

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
P0CY08

<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>Regioni1 – 102N-terminal domainAdd BLAST102
Regioni103 – 128Flexible linkerAdd BLAST26
Regioni190 – 210C-terminal tailAdd BLAST21

<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 N-terminal domain is required for the interaction with the WD repeats of TUP1 and for dimerization.1 Publication
The homeobox domain binds to DNA and interacts with the TPR repeats of SSN6.1 Publication
The unstructured, flexible linker domain contains eight residues (Leu-114 to Gln-121), which, in the presence of MCM1, adopt a beta-fold and mediate the cooperative interaction to MCM1.1 Publication
The C-terminal tail domain is disordered in the monomer, even when bound to DNA. In the ternary complex with A1 and DNA, 16 residues (Ile-190 to Leu-205) of the C-terminal tail undergo a conformational change, becoming ordered and contacting the A1 homeodomain.1 Publication

<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 TALE/M-ATYP homeobox family.Curated

Keywords - Domaini

Homeobox

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_091806_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0CY08

KEGG Orthology (KO)

More...
KOi
K09359

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00086 homeodomain, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR009057 Homeobox-like_sf
IPR001356 Homeobox_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00046 Homeodomain, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00389 HOX, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF46689 SSF46689, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50071 HOMEOBOX_2, 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.

P0CY08-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNKIPIKDLL NPQITDEFKS SILDINKKLF SICCNLPKLP ESVTTEEEVE
60 70 80 90 100
LRDILGFLSR ANKNRKISDE EKKLLQTTSQ LTTTITVLLK EMRSIENDRS
110 120 130 140 150
NYQLTQKNKS ADGLVFNVVT QDMINKSTKP YRGHRFTKEN VRILESWFAK
160 170 180 190 200
NIENPYLDTK GLENLMKNTS LSRIQIKNWV SNRRRKEKTI TIAPELADLL
210
SGEPLAKKKE
Length:210
Mass (Da):24,282
Last modified:June 28, 2011 - 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:i30CD6A486D7D76CE
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 conflicti56G → L in AAA34762 (PubMed:7021055).Curated1
Sequence conflicti150K → KK in AAA34762 (PubMed:7021055).Curated1
Sequence conflicti154N → S in AAT92829 (PubMed:17322287).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
L00060 Genomic DNA Translation: AAA34762.1
X63853 Genomic DNA Translation: CAA45335.1
X59720 Genomic DNA Translation: CAA42306.1
AY692810 Genomic DNA Translation: AAT92829.1
BK006937 Genomic DNA Translation: DAA07518.1

Protein sequence database of the Protein Information Resource

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PIRi
S19398 JFBYA2

NCBI Reference Sequences

More...
RefSeqi
NP_009866.1, NM_001178708.1
NP_009868.3, NM_001178753.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YCL067C_mRNA; YCL067C; YCL067C
YCR039C_mRNA; YCR039C; YCR039C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
850292
850406

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YCL067C
sce:YCR039C

<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
L00060 Genomic DNA Translation: AAA34762.1
X63853 Genomic DNA Translation: CAA45335.1
X59720 Genomic DNA Translation: CAA42306.1
AY692810 Genomic DNA Translation: AAT92829.1
BK006937 Genomic DNA Translation: DAA07518.1
PIRiS19398 JFBYA2
RefSeqiNP_009866.1, NM_001178708.1
NP_009868.3, NM_001178753.1

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
1AKHX-ray2.50B128-210[»]
1APLX-ray2.70C/D128-210[»]
1K61X-ray2.10A/B/C/D132-191[»]
1LE8X-ray2.30B128-210[»]
1MNMX-ray2.25C/D103-189[»]
1YRNX-ray2.50B128-210[»]
SMRiP0CY08
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi30922, 7 interactors
31022, 22 interactors
ComplexPortaliCPX-684 Mating-type MATalpha2-MATa1 complex
CPX-692 Mating-type MATalpha2-MCM1 complex
IntActiP0CY08, 3 interactors

PTM databases

iPTMnetiP0CY08

Proteomic databases

MaxQBiP0CY08
PRIDEiP0CY08

Genome annotation databases

EnsemblFungiiYCL067C_mRNA; YCL067C; YCL067C
YCR039C_mRNA; YCR039C; YCR039C
GeneIDi850292
850406
KEGGisce:YCL067C
sce:YCR039C

Organism-specific databases

SGDiS000000635 MATALPHA2

Phylogenomic databases

HOGENOMiCLU_091806_1_0_1
InParanoidiP0CY08
KOiK09359

Enzyme and pathway databases

BioCyciYEAST:G3O-29351-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0CY08

Protein Ontology

More...
PROi
PR:P0CY08
RNActiP0CY08 protein

Family and domain databases

CDDicd00086 homeodomain, 1 hit
InterProiView protein in InterPro
IPR009057 Homeobox-like_sf
IPR001356 Homeobox_dom
PfamiView protein in Pfam
PF00046 Homeodomain, 1 hit
SMARTiView protein in SMART
SM00389 HOX, 1 hit
SUPFAMiSSF46689 SSF46689, 1 hit
PROSITEiView protein in PROSITE
PS50071 HOMEOBOX_2, 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 nameiMTAL2_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: P0CY08
Secondary accession number(s): D6VQV2
, P01367, P01368, Q6B2C0
<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: June 28, 2011
Last sequence update: June 28, 2011
Last modified: February 26, 2020
This is version 61 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, Direct protein sequencing, Reference proteome

Documents

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