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Mating-type protein ALPHA2 (MATalpha2 protein) (Alpha-2 repressor)

 MTAL2_YEAST             Reviewed;         210 AA.
P0CY08; D6VQV2; P01367; P01368; Q6B2C0;
28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
28-JUN-2011, sequence version 1.
22-NOV-2017, entry version 47.
RecName: Full=Mating-type protein ALPHA2;
Short=MATalpha2 protein;
AltName: Full=Alpha-2 repressor;
Name=MATALPHA2; Synonyms=ALPHA-2, MAT2A, MATAL2;
OrderedLocusNames=YCR039C; ORFNames=YCR39C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7021055;
Nasmyth K.A., Tatchell K., Hall B.D., Astell C., Smith M.;
"Physical analysis of mating-type loci in Saccharomyces cerevisiae.";
Cold Spring Harb. Symp. Quant. Biol. 45:961-981(1981).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1789011; DOI=10.1002/yea.320070815;
Jacquet M., Buhler J.-M., Iborra F., Francingues-Gaillard M.-C.,
Soustelle C.;
"The MAT locus revisited within a 9.8 kb fragment of chromosome III
containing BUD5 and two new open reading frames.";
Yeast 7:881-888(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=1574125; DOI=10.1038/357038a0;
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.;
"The complete DNA sequence of yeast chromosome III.";
Nature 357:38-46(1992).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[6]
DNA-BINDING SPECIFICITY.
PubMed=3893743; DOI=10.1016/S0092-8674(85)80119-7;
Johnson A.D., Herskowitz I.;
"A repressor (MAT alpha 2 Product) and its operator control expression
of a set of cell type specific genes in yeast.";
Cell 42:237-247(1985).
[7]
MUTAGENESIS BY DOMAIN DELETION.
PubMed=2887035; DOI=10.1126/science.2887035;
Hall M.N., Johnson A.D.;
"Homeo domain of the yeast repressor alpha 2 is a sequence-specific
DNA-binding domain but is not sufficient for repression.";
Science 237:1007-1012(1987).
[8]
DOMAINS, AND DIMERIZATION.
PubMed=3061876; DOI=10.1101/gad.2.7.807;
Sauer R.T., Smith D.L., Johnson A.D.;
"Flexibility of the yeast alpha 2 repressor enables it to occupy the
ends of its operator, leaving the center free.";
Genes Dev. 2:807-816(1988).
[9]
MUTAGENESIS OF LEU-196.
PubMed=2851482;
Strathern J., Shafer B., Hicks J., McGill C.;
"a/Alpha-specific repression by MAT alpha 2.";
Genetics 120:75-81(1988).
[10]
PROTEIN SEQUENCE OF 1-7, AND ACETYLATION AT MET-1.
PubMed=20110468; DOI=10.1126/science.1183147;
Hwang C.S., Shemorry A., Varshavsky A.;
"N-terminal acetylation of cellular proteins creates specific
degradation signals.";
Science 327:973-977(2010).
[11]
SIMILARITY TO HOMEOBOX PROTEINS.
PubMed=6429549; DOI=10.1038/310070a0;
Shepherd J.C.W., McGinnis W., Carrasco A.E., De Robertis E.M.,
Gehring W.J.;
"Fly and frog homoeo domains show homologies with yeast mating type
regulatory proteins.";
Nature 310:70-71(1984).
[12]
INTERACTION WITH TUP1, AND MUTAGENESIS OF ILE-4; LEU-9; LEU-10 AND
GLU-71.
PubMed=7995523; DOI=10.1101/gad.8.23.2857;
Komachi K., Redd M.J., Johnson A.D.;
"The WD repeats of Tup1 interact with the homeo domain protein alpha
2.";
Genes Dev. 8:2857-2867(1994).
[13]
FUNCTION IN MATING-TYPE REGULATION.
PubMed=8664541; DOI=10.1016/0959-437X(95)80022-0;
Johnson A.D.;
"Molecular mechanisms of cell-type determination in budding yeast.";
Curr. Opin. Genet. Dev. 5:552-558(1995).
[14]
INTERACTION WITH SSN6.
PubMed=7498787; DOI=10.1101/gad.9.23.2903;
Smith R.L., Redd M.J., Johnson A.D.;
"The tetratricopeptide repeats of Ssn6 interact with the homeo domain
of alpha 2.";
Genes Dev. 9:2903-2910(1995).
[15]
INTERACTION WITH MCM1, AND MUTAGENESIS OF 114-LEU--THR-120.
PubMed=8628280; DOI=10.1128/MCB.16.5.2135;
Mead J., Zhong H., Acton T.B., Vershon A.K.;
"The yeast alpha2 and Mcm1 proteins interact through a region similar
to a motif found in homeodomain proteins of higher eukaryotes.";
Mol. Cell. Biol. 16:2135-2143(1996).
[16]
INTERACTION WITH SSN6, AND MUTAGENESIS OF ARG-173.
PubMed=10759558; DOI=10.1073/pnas.070506797;
Smith R.L., Johnson A.D.;
"A sequence resembling a peroxisomal targeting sequence directs the
interaction between the tetratricopeptide repeats of Ssn6 and the
homeodomain of alpha 2.";
Proc. Natl. Acad. Sci. U.S.A. 97:3901-3906(2000).
[17]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF HOMEOBOX.
PubMed=1682054; DOI=10.1016/0092-8674(91)90526-5;
Wolberger C., Vershon A.K., Liu B., Johnson A.D., Pabo C.O.;
"Crystal structure of a MAT alpha 2 homeodomain-operator complex
suggests a general model for homeodomain-DNA interactions.";
Cell 67:517-528(1991).
[18]
STRUCTURE BY NMR OF HOMEOBOX.
PubMed=1673952; DOI=10.1101/gad.5.5.764;
Phillips C.L., Vershon A.K., Johnson A.D., Dahlquist F.W.;
"Secondary structure of the homeo domain of yeast alpha 2 repressor
determined by NMR spectroscopy.";
Genes Dev. 5:764-772(1991).
[19]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF HOMEOBOX IN COMPLEX WITH A1,
AND MUTAGENESIS OF ILE-192; LEU-196; LEU-199 AND LEU-200.
PubMed=7569974; DOI=10.1126/science.270.5234.262;
Li T., Stark M.R., Johnson A.D., Wolberger C.;
"Crystal structure of the MATa1/MAT alpha 2 homeodomain heterodimer
bound to DNA.";
Science 270:262-269(1995).
[20]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF HOMEOBOX IN COMPLEX WITH
MCM1.
PubMed=9490409; DOI=10.1038/35563;
Tan S., Richmond T.J.;
"Crystal structure of the yeast MATalpha2/MCM1/DNA ternary complex.";
Nature 391:660-666(1998).
[21]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF HOMEOBOX IN COMPLEX WITH A1.
PubMed=9838003; DOI=10.1093/nar/26.24.5707;
Li T., Jin Y., Vershon A.K., Wolberger C.;
"Crystal structure of the MATa1/MATalpha2 homeodomain heterodimer in
complex with DNA containing an A-tract.";
Nucleic Acids Res. 26:5707-5718(1998).
[22]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF HOMEOBOX.
PubMed=12466549; DOI=10.1093/nar/gkf661;
Aishima J., Gitti R.K., Noah J.E., Gan H.H., Schlick T., Wolberger C.;
"A Hoogsteen base pair embedded in undistorted B-DNA.";
Nucleic Acids Res. 30:5244-5252(2002).
[23]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF HOMEOBOX IN COMPLEX WITH A1,
AND MUTAGENESIS OF SER-181; ASN-182 AND ARG-185.
PubMed=12121651; DOI=10.1016/S0969-2126(02)00790-6;
Ke A., Mathias J.R., Vershon A.K., Wolberger C.;
"Structural and thermodynamic characterization of the DNA binding
properties of a triple alanine mutant of MATalpha2.";
Structure 10:961-971(2002).
-!- FUNCTION: 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. {ECO:0000269|PubMed:8664541}.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:10759558,
ECO:0000269|PubMed:12121651, ECO:0000269|PubMed:7498787,
ECO:0000269|PubMed:7569974, ECO:0000269|PubMed:7995523,
ECO:0000269|PubMed:8628280, ECO:0000269|PubMed:9490409,
ECO:0000269|PubMed:9838003}.
-!- INTERACTION:
P11746:MCM1; NbExp=2; IntAct=EBI-10443, EBI-10528;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- DEVELOPMENTAL STAGE: Only present in alpha-cells and in a/alpha
diploid cells.
-!- DOMAIN: The N-terminal domain is required for the interaction with
the WD repeats of TUP1 and for dimerization.
{ECO:0000269|PubMed:3061876}.
-!- DOMAIN: The homeobox domain binds to DNA and interacts with the
TPR repeats of SSN6. {ECO:0000269|PubMed:3061876}.
-!- DOMAIN: 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.
{ECO:0000269|PubMed:3061876}.
-!- DOMAIN: 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. {ECO:0000269|PubMed:3061876}.
-!- 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.
-!- SIMILARITY: Belongs to the TALE/M-ATYP homeobox family.
{ECO:0000305}.
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EMBL; L00060; AAA34762.1; -; Genomic_DNA.
EMBL; X63853; CAA45335.1; -; Genomic_DNA.
EMBL; X59720; CAA42306.1; -; Genomic_DNA.
EMBL; AY692810; AAT92829.1; -; Genomic_DNA.
EMBL; BK006937; DAA07518.1; -; Genomic_DNA.
PIR; S19398; JFBYA2.
RefSeq; NP_009866.1; NM_001178708.1.
RefSeq; NP_009868.3; NM_001178753.1.
PDB; 1AKH; X-ray; 2.50 A; B=128-210.
PDB; 1APL; X-ray; 2.70 A; C/D=128-210.
PDB; 1K61; X-ray; 2.10 A; A/B/C/D=132-191.
PDB; 1LE8; X-ray; 2.30 A; B=128-210.
PDB; 1MNM; X-ray; 2.25 A; C/D=103-189.
PDB; 1YRN; X-ray; 2.50 A; B=128-210.
PDBsum; 1AKH; -.
PDBsum; 1APL; -.
PDBsum; 1K61; -.
PDBsum; 1LE8; -.
PDBsum; 1MNM; -.
PDBsum; 1YRN; -.
ProteinModelPortal; P0CY08; -.
SMR; P0CY08; -.
BioGrid; 30922; 7.
BioGrid; 31022; 21.
IntAct; P0CY08; 3.
MINT; MINT-2735547; -.
iPTMnet; P0CY08; -.
MaxQB; P0CY08; -.
PRIDE; P0CY08; -.
EnsemblFungi; CAA42306; CAA42306; CAA42306.
EnsemblFungi; YCL067C; YCL067C; YCL067C.
EnsemblFungi; YCR039C; YCR039C; YCR039C.
GeneID; 850292; -.
GeneID; 850406; -.
KEGG; sce:YCL067C; -.
KEGG; sce:YCR039C; -.
SGD; S000000635; MATALPHA2.
HOGENOM; HOG000000902; -.
InParanoid; P0CY08; -.
KO; K09359; -.
OrthoDB; EOG092C2OFZ; -.
BioCyc; YEAST:G3O-29351-MONOMER; -.
EvolutionaryTrace; P0CY08; -.
PRO; PR:P0CY08; -.
Proteomes; UP000002311; Chromosome III.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0008301; F:DNA binding, bending; IDA:SGD.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:SGD.
GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding; IDA:SGD.
GO; GO:0001198; P:negative regulation of mating-type specific transcription from RNA polymerase II promoter; IDA:SGD.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00086; homeodomain; 1.
InterPro; IPR009057; Homeobox-like_sf.
InterPro; IPR001356; Homeobox_dom.
Pfam; PF00046; Homeobox; 1.
SMART; SM00389; HOX; 1.
SUPFAM; SSF46689; SSF46689; 1.
PROSITE; PS50071; HOMEOBOX_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; DNA-binding; Homeobox; Nucleus;
Reference proteome; Repressor; Transcription;
Transcription regulation.
CHAIN 1 210 Mating-type protein ALPHA2.
/FTId=PRO_0000049186.
DNA_BIND 129 191 Homeobox; TALE-type.
{ECO:0000255|PROSITE-ProRule:PRU00108}.
REGION 1 102 N-terminal domain.
REGION 103 128 Flexible linker.
REGION 190 210 C-terminal tail.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000269|PubMed:20110468}.
MUTAGEN 4 4 I->T: Reduces the ability of ALPHA2 to
repress transcription, but binds normally
to DNA and MCM1.
{ECO:0000269|PubMed:7995523}.
MUTAGEN 9 9 L->F: Reduces the ability of ALPHA2 to
repress transcription, but binds normally
to DNA and MCM1.
{ECO:0000269|PubMed:7995523}.
MUTAGEN 10 10 L->S: Reduces the ability of ALPHA2 to
repress transcription, but binds normally
to DNA and MCM1. Disrupts interaction
with TUP1. {ECO:0000269|PubMed:7995523}.
MUTAGEN 71 71 E->K: Reduces the ability of alpha2 to
repress transcription, but binds normally
to DNA and MCM1.
{ECO:0000269|PubMed:7995523}.
MUTAGEN 114 114 L->A: Reduces the ability of ALPHA2/MCM1
to repress a-specific genes.
{ECO:0000269|PubMed:2887035}.
MUTAGEN 115 115 V->A: Reduces the ability of ALPHA2/MCM1
to repress a-specific genes.
{ECO:0000269|PubMed:2887035}.
MUTAGEN 116 116 F->A: Reduces the ability of ALPHA2/MCM1
to repress a-specific genes.
{ECO:0000269|PubMed:2887035}.
MUTAGEN 117 117 N->A: Reduces the ability of ALPHA2/MCM1
to repress a-specific genes.
{ECO:0000269|PubMed:2887035}.
MUTAGEN 118 118 V->A: Reduces the ability of ALPHA2/MCM1
to repress a-specific genes.
{ECO:0000269|PubMed:2887035}.
MUTAGEN 119 119 V->A: Reduces the ability of ALPHA2/MCM1
to repress a-specific genes.
{ECO:0000269|PubMed:2887035}.
MUTAGEN 120 120 T->A: Reduces the ability of ALPHA2/MCM1
to repress a-specific genes.
{ECO:0000269|PubMed:2887035}.
MUTAGEN 173 173 R->A: Reduces the ability of ALPHA2/MCM1
to repress a-specific genes. Disrupts
interaction with SSN6.
{ECO:0000269|PubMed:10759558}.
MUTAGEN 181 181 S->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.
{ECO:0000269|PubMed:12121651}.
MUTAGEN 182 182 N->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.
{ECO:0000269|PubMed:12121651}.
MUTAGEN 185 185 R->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.
{ECO:0000269|PubMed:12121651}.
MUTAGEN 192 192 I->A: Disrupts the ability of A1/ALPHA2
to repress haploid-specific genes.
{ECO:0000269|PubMed:7569974}.
MUTAGEN 196 196 L->A,S: Disrupts the ability of A1/ALPHA2
to repress haploid-specific genes.
{ECO:0000269|PubMed:2851482,
ECO:0000269|PubMed:7569974}.
MUTAGEN 199 199 L->A: Disrupts the ability of A1/ALPHA2
to repress haploid-specific genes.
{ECO:0000269|PubMed:7569974}.
MUTAGEN 200 200 L->A: Disrupts the ability of A1/ALPHA2
to repress haploid-specific genes.
{ECO:0000269|PubMed:7569974}.
CONFLICT 56 56 G -> L (in Ref. 1; AAA34762).
{ECO:0000305}.
CONFLICT 150 150 K -> KK (in Ref. 1; AAA34762).
{ECO:0000305}.
CONFLICT 154 154 N -> S (in Ref. 5; AAT92829).
{ECO:0000305}.
STRAND 116 120 {ECO:0000244|PDB:1MNM}.
STRAND 125 129 {ECO:0000244|PDB:1MNM}.
HELIX 138 150 {ECO:0000244|PDB:1K61}.
TURN 151 153 {ECO:0000244|PDB:1K61}.
HELIX 159 169 {ECO:0000244|PDB:1K61}.
HELIX 173 188 {ECO:0000244|PDB:1K61}.
HELIX 194 197 {ECO:0000244|PDB:1LE8}.
STRAND 200 202 {ECO:0000244|PDB:1LE8}.
SEQUENCE 210 AA; 24282 MW; 30CD6A486D7D76CE CRC64;
MNKIPIKDLL NPQITDEFKS SILDINKKLF SICCNLPKLP ESVTTEEEVE LRDILGFLSR
ANKNRKISDE EKKLLQTTSQ LTTTITVLLK EMRSIENDRS NYQLTQKNKS ADGLVFNVVT
QDMINKSTKP YRGHRFTKEN VRILESWFAK NIENPYLDTK GLENLMKNTS LSRIQIKNWV
SNRRRKEKTI TIAPELADLL SGEPLAKKKE


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18-003-44012 Transcriptional repressor p66 alpha - GATA zinc finger domain-containing protein 2A Polyclonal 0.1 mg Protein A
15-288-21471 Liprin-alpha-1 - Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-1; PTPRF-interacting protein alpha-1; LAR-interacting protein 1; LIP.1 Polyclonal 0.05 mg
15-288-21470 Liprin-alpha-1 - Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-1; PTPRF-interacting protein alpha-1; LAR-interacting protein 1; LIP.1 Polyclonal 0.1 mg
15-288-21471 Liprin-alpha-1 - Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-1; PTPRF-interacting protein alpha-1; LAR-interacting protein 1; LIP.1 Polyclonal 0.1 mg
15-288-21470 Liprin-alpha-1 - Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-1; PTPRF-interacting protein alpha-1; LAR-interacting protein 1; LIP.1 Polyclonal 0.05 mg
orb70284 alpha Mating Factor (1-6) peptide This is alpha Mating Factor (1-6) peptide. For research use only. 1 mg
EIAAB29594 GATA zinc finger domain-containing protein 2A,Gatad2a,Mouse,Mus musculus,Transcriptional repressor p66 alpha
15-288-21472 Liprin-alpha-2 - Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-2; PTPRF-interacting protein alpha-2 Polyclonal 0.05 mg
15-288-21472 Liprin-alpha-2 - Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-2; PTPRF-interacting protein alpha-2 Polyclonal 0.1 mg
28-844 ZNF76 belongs to the krueppel C2H2-type zinc-finger protein family. ZNF76 is a general transcription repressor targeting TATA-binding protein (TBP), through a process regulated by sumoylation. ZNF76 i 0.1 mg
EIAAB29593 GATA zinc finger domain-containing protein 2A,GATAD2A,Homo sapiens,Hp66alpha,Human,Transcriptional repressor p66-alpha
EIAAB37584 HBSC II,Homo sapiens,Human,NAC2,SCN2A,SCN2A1,SCN2A2,Sodium channel protein brain II subunit alpha,Sodium channel protein type 2 subunit alpha,Sodium channel protein type II subunit alpha,Voltage-gated
25-495 HIF1AN is a co-repressor that interacts with hypoxia-inducible factor 1 (HIF-1) alpha and the von Hippel-Lindau tumor suppressor protein to mediate repression of HIF-1 transcriptional activity. 0.05 mg
27-739 HIF1AN is a co-repressor that interacts with hypoxia-inducible factor 1 (HIF-1) alpha and the von Hippel-Lindau tumor suppressor protein to mediate repression of HIF-1 transcriptional activity. 0.05 mg
27-738 HIF1AN is a co-repressor that interacts with hypoxia-inducible factor 1 (HIF-1) alpha and the von Hippel-Lindau tumor suppressor protein to mediate repression of HIF-1 transcriptional activity. 0.1 mg
29-041 HIF1AN is a co-repressor that interacts with hypoxia-inducible factor 1 (HIF-1) alpha and the von Hippel-Lindau tumor suppressor protein to mediate repression of HIF-1 transcriptional activity. 0.05 mg


 

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