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P0CY08

- MTAL2_YEAST

UniProt

P0CY08 - MTAL2_YEAST

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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: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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. 1 Publication
Mutagenesisi115 – 1151V → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. 1 Publication
Mutagenesisi116 – 1161F → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. 1 Publication
Mutagenesisi117 – 1171N → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. 1 Publication
Mutagenesisi118 – 1181V → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. 1 Publication
Mutagenesisi119 – 1191V → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. 1 Publication
Mutagenesisi120 – 1201T → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. 1 Publication
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. 8 interactions.
31022. 11 interactions.
MINTiMINT-2735547.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP0CY08.
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

        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
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:
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.

Genome annotation databases

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

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 .
PIRi S19398. JFBYA2.
RefSeqi NP_009866.1. NM_001178708.1.
NP_009868.3. NM_001178753.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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. 8 interactions.
31022. 11 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.
InParanoidi P0CY08.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 29 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