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P0CY08

- MTAL2_YEAST

UniProt

P0CY08 - MTAL2_YEAST

Protein

Mating-type protein ALPHA2

Gene

MATALPHA2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 27 (01 Oct 2014)
      Sequence version 1 (28 Jun 2011)
      Previous versions | rss
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    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

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi129 – 19163Homeobox; TALE-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: SGD
    2. sequence-specific DNA binding Source: SGD

    GO - Biological processi

    1. negative regulation of mating-type specific transcription from RNA polymerase II promoter Source: SGD
    2. negative regulation of transcription from RNA polymerase II promoter Source: GOC

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29351-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mating-type protein ALPHA2
    Short name:
    MATalpha2 protein
    Alternative name(s):
    Alpha-2 repressor
    Gene namesi
    Name:MATALPHA2
    Synonyms:ALPHA-2, MAT2A, MATAL2
    Ordered Locus Names:YCR039C
    ORF Names:YCR39C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome III

    Organism-specific databases

    CYGDiYCR039c.
    SGDiS000000635. MATALPHA2.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: SGD

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi4 – 41I → T: Reduces the ability of ALPHA2 to repress transcription, but binds normally to DNA and MCM1. 1 Publication
    Mutagenesisi9 – 91L → F: Reduces the ability of ALPHA2 to repress transcription, but binds normally to DNA and MCM1. 1 Publication
    Mutagenesisi10 – 101L → S: Reduces the ability of ALPHA2 to repress transcription, but binds normally to DNA and MCM1. Disrupts interaction with TUP1. 1 Publication
    Mutagenesisi71 – 711E → K: Reduces the ability of alpha2 to repress transcription, but binds normally to DNA and MCM1. 1 Publication
    Mutagenesisi114 – 1141L → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes.
    Mutagenesisi115 – 1151V → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes.
    Mutagenesisi116 – 1161F → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes.
    Mutagenesisi117 – 1171N → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes.
    Mutagenesisi118 – 1181V → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes.
    Mutagenesisi119 – 1191V → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes.
    Mutagenesisi120 – 1201T → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes.
    Mutagenesisi173 – 1731R → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. Disrupts interaction with SSN6. 1 Publication
    Mutagenesisi181 – 1811S → 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 Publication
    Mutagenesisi182 – 1821N → 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 Publication
    Mutagenesisi185 – 1851R → 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 Publication
    Mutagenesisi192 – 1921I → A: Disrupts the ability of A1/ALPHA2 to repress haploid-specific genes. 1 Publication
    Mutagenesisi196 – 1961L → A or S: Disrupts the ability of A1/ALPHA2 to repress haploid-specific genes. 2 Publications
    Mutagenesisi199 – 1991L → A: Disrupts the ability of A1/ALPHA2 to repress haploid-specific genes. 1 Publication
    Mutagenesisi200 – 2001L → A: Disrupts the ability of A1/ALPHA2 to repress haploid-specific genes. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 210210Mating-type protein ALPHA2PRO_0000049186Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP0CY08.

    Expressioni

    Developmental stagei

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

    Interactioni

    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

    Protein-protein interaction databases

    BioGridi30922. 7 interactions.
    31022. 10 interactions.
    MINTiMINT-2735547.

    Structurei

    Secondary structure

    1
    210
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi116 – 1205
    Beta strandi125 – 1295
    Helixi138 – 15013
    Turni151 – 1533
    Helixi159 – 16911
    Helixi173 – 18816
    Helixi194 – 1974
    Beta strandi200 – 2023

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP0CY08.
    SMRiP0CY08. Positions 128-205.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0CY08.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 102102N-terminal domainAdd
    BLAST
    Regioni103 – 12826Flexible linkerAdd
    BLAST
    Regioni190 – 21021C-terminal tailAdd
    BLAST

    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

    Sequence similaritiesi

    Belongs to the TALE/M-ATYP homeobox family.Curated
    Contains 1 homeobox DNA-binding domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Homeobox

    Phylogenomic databases

    HOGENOMiHOG000000902.
    KOiK09359.
    OrthoDBiEOG7W41QS.

    Family and domain databases

    Gene3Di1.10.10.60. 1 hit.
    InterProiIPR001356. Homeobox_dom.
    IPR009057. Homeodomain-like.
    [Graphical view]
    PfamiPF00046. Homeobox. 1 hit.
    [Graphical view]
    SMARTiSM00389. HOX. 1 hit.
    [Graphical view]
    SUPFAMiSSF46689. SSF46689. 1 hit.
    PROSITEiPS50071. HOMEOBOX_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0CY08-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNKIPIKDLL NPQITDEFKS SILDINKKLF SICCNLPKLP ESVTTEEEVE    50
    LRDILGFLSR ANKNRKISDE EKKLLQTTSQ LTTTITVLLK EMRSIENDRS 100
    NYQLTQKNKS ADGLVFNVVT QDMINKSTKP YRGHRFTKEN VRILESWFAK 150
    NIENPYLDTK GLENLMKNTS LSRIQIKNWV SNRRRKEKTI TIAPELADLL 200
    SGEPLAKKKE 210
    Length:210
    Mass (Da):24,282
    Last modified:June 28, 2011 - v1
    Checksum:i30CD6A486D7D76CE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti56 – 561G → L in AAA34762. (PubMed:7021055)Curated
    Sequence conflicti150 – 1501K → KK in AAA34762. (PubMed:7021055)Curated
    Sequence conflicti154 – 1541N → S in AAT92829. (PubMed:17322287)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    Genome annotation databases

    EnsemblFungiiYCL067C; YCL067C; YCL067C.
    YCR039C; YCR039C; YCR039C.
    GeneIDi850292.
    850406.
    KEGGisce:YCL067C.
    sce:YCR039C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi S19398. JFBYA2.
    RefSeqi NP_009866.1. NM_001178708.1.
    NP_009868.3. NM_001178753.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AKH X-ray 2.50 B 128-210 [» ]
    1APL X-ray 2.70 C/D 128-210 [» ]
    1K61 X-ray 2.10 A/B/C/D 132-191 [» ]
    1LE8 X-ray 2.30 B 128-210 [» ]
    1MNM X-ray 2.25 C/D 103-189 [» ]
    1YRN X-ray 2.50 B 128-210 [» ]
    ProteinModelPortali P0CY08.
    SMRi P0CY08. Positions 128-205.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 30922. 7 interactions.
    31022. 10 interactions.
    MINTi MINT-2735547.

    Proteomic databases

    MaxQBi P0CY08.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YCL067C ; YCL067C ; YCL067C .
    YCR039C ; YCR039C ; YCR039C .
    GeneIDi 850292.
    850406.
    KEGGi sce:YCL067C.
    sce:YCR039C.

    Organism-specific databases

    CYGDi YCR039c.
    SGDi S000000635. MATALPHA2.

    Phylogenomic databases

    HOGENOMi HOG000000902.
    KOi K09359.
    OrthoDBi EOG7W41QS.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29351-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0CY08.
    NextBioi 965658.

    Family and domain databases

    Gene3Di 1.10.10.60. 1 hit.
    InterProi IPR001356. Homeobox_dom.
    IPR009057. Homeodomain-like.
    [Graphical view ]
    Pfami PF00046. Homeobox. 1 hit.
    [Graphical view ]
    SMARTi SM00389. HOX. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46689. SSF46689. 1 hit.
    PROSITEi PS50071. HOMEOBOX_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Physical analysis of mating-type loci in Saccharomyces cerevisiae."
      Nasmyth K.A., Tatchell K., Hall B.D., Astell C., Smith M.
      Cold Spring Harb. Symp. Quant. Biol. 45:961-981(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The MAT locus revisited within a 9.8 kb fragment of chromosome III containing BUD5 and two new open reading frames."
      Jacquet M., Buhler J.-M., Iborra F., Francingues-Gaillard M.-C., Soustelle C.
      Yeast 7:881-888(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The complete DNA sequence of yeast chromosome III."
      Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
      , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
      Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. "A repressor (MAT alpha 2 Product) and its operator control expression of a set of cell type specific genes in yeast."
      Johnson A.D., Herskowitz I.
      Cell 42:237-247(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING SPECIFICITY.
    7. "Homeo domain of the yeast repressor alpha 2 is a sequence-specific DNA-binding domain but is not sufficient for repression."
      Hall M.N., Johnson A.D.
      Science 237:1007-1012(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS BY DOMAIN DELETION.
    8. "Flexibility of the yeast alpha 2 repressor enables it to occupy the ends of its operator, leaving the center free."
      Sauer R.T., Smith D.L., Johnson A.D.
      Genes Dev. 2:807-816(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAINS, DIMERIZATION.
    9. "a/Alpha-specific repression by MAT alpha 2."
      Strathern J., Shafer B., Hicks J., McGill C.
      Genetics 120:75-81(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LEU-196.
    10. "N-terminal acetylation of cellular proteins creates specific degradation signals."
      Hwang C.S., Shemorry A., Varshavsky A.
      Science 327:973-977(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-7, ACETYLATION AT MET-1.
    11. "Fly and frog homoeo domains show homologies with yeast mating type regulatory proteins."
      Shepherd J.C.W., McGinnis W., Carrasco A.E., De Robertis E.M., Gehring W.J.
      Nature 310:70-71(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: SIMILARITY TO HOMEOBOX PROTEINS.
    12. "The WD repeats of Tup1 interact with the homeo domain protein alpha 2."
      Komachi K., Redd M.J., Johnson A.D.
      Genes Dev. 8:2857-2867(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TUP1, MUTAGENESIS OF ILE-4; LEU-9; LEU-10 AND GLU-71.
    13. "Molecular mechanisms of cell-type determination in budding yeast."
      Johnson A.D.
      Curr. Opin. Genet. Dev. 5:552-558(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MATING-TYPE REGULATION.
    14. "The tetratricopeptide repeats of Ssn6 interact with the homeo domain of alpha 2."
      Smith R.L., Redd M.J., Johnson A.D.
      Genes Dev. 9:2903-2910(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SSN6.
    15. "The yeast alpha2 and Mcm1 proteins interact through a region similar to a motif found in homeodomain proteins of higher eukaryotes."
      Mead J., Zhong H., Acton T.B., Vershon A.K.
      Mol. Cell. Biol. 16:2135-2143(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MCM1, MUTAGENESIS OF 114-LEU--THR-120.
    16. "A sequence resembling a peroxisomal targeting sequence directs the interaction between the tetratricopeptide repeats of Ssn6 and the homeodomain of alpha 2."
      Smith R.L., Johnson A.D.
      Proc. Natl. Acad. Sci. U.S.A. 97:3901-3906(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SSN6, MUTAGENESIS OF ARG-173.
    17. "Crystal structure of a MAT alpha 2 homeodomain-operator complex suggests a general model for homeodomain-DNA interactions."
      Wolberger C., Vershon A.K., Liu B., Johnson A.D., Pabo C.O.
      Cell 67:517-528(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF HOMEOBOX.
    18. "Secondary structure of the homeo domain of yeast alpha 2 repressor determined by NMR spectroscopy."
      Phillips C.L., Vershon A.K., Johnson A.D., Dahlquist F.W.
      Genes Dev. 5:764-772(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF HOMEOBOX.
    19. "Crystal structure of the MATa1/MAT alpha 2 homeodomain heterodimer bound to DNA."
      Li T., Stark M.R., Johnson A.D., Wolberger C.
      Science 270:262-269(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF HOMEOBOX IN COMPLEX WITH A1, MUTAGENESIS OF ILE-192; LEU-196; LEU-199 AND LEU-200.
    20. "Crystal structure of the yeast MATalpha2/MCM1/DNA ternary complex."
      Tan S., Richmond T.J.
      Nature 391:660-666(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF HOMEOBOX IN COMPLEX WITH MCM1.
    21. "Crystal structure of the MATa1/MATalpha2 homeodomain heterodimer in complex with DNA containing an A-tract."
      Li T., Jin Y., Vershon A.K., Wolberger C.
      Nucleic Acids Res. 26:5707-5718(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF HOMEOBOX IN COMPLEX WITH A1.
    22. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF HOMEOBOX.
    23. "Structural and thermodynamic characterization of the DNA binding properties of a triple alanine mutant of MATalpha2."
      Ke A., Mathias J.R., Vershon A.K., Wolberger C.
      Structure 10:961-971(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF HOMEOBOX IN COMPLEX WITH A1, MUTAGENESIS OF SER-181; ASN-182 AND ARG-185.

    Entry informationi

    Entry nameiMTAL2_YEAST
    AccessioniPrimary (citable) accession number: P0CY08
    Secondary accession number(s): D6VQV2
    , P01367, P01368, Q6B2C0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 28, 2011
    Last sequence update: June 28, 2011
    Last modified: October 1, 2014
    This is version 27 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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.

    Keywords - Technical termi

    3D-structure, Complete proteome, 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

    External Data

    Dasty 3