HAP2_YEAST
ID HAP2_YEAST Reviewed; 265 AA.
AC P06774; D6VV97;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Transcriptional activator HAP2;
GN Name=HAP2; OrderedLocusNames=YGL237C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3547076; DOI=10.1128/mcb.7.2.578-585.1987;
RA Pinkham J.L., Olesen J.T., Guarente L.P.;
RT "Sequence and nuclear localization of the Saccharomyces cerevisiae HAP2
RT protein, a transcriptional activator.";
RL Mol. Cell. Biol. 7:578-585(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP MUTAGENESIS.
RX PubMed=8223474; DOI=10.1002/j.1460-2075.1993.tb06153.x;
RA Xing Y., Fikes J.D., Guarente L.;
RT "Mutations in yeast HAP2/HAP3 define a hybrid CCAAT box binding domain.";
RL EMBO J. 12:4647-4655(1993).
RN [5]
RP IDENTIFICATION IN THE CCAT-BINDING FACTOR.
RX PubMed=11390369; DOI=10.1074/jbc.c100274200;
RA Li Y., Takagi Y., Jiang Y., Tokunaga M., Erdjument-Bromage H., Tempst P.,
RA Kornberg R.D.;
RT "A multiprotein complex that interacts with RNA polymerase II elongator.";
RL J. Biol. Chem. 276:29628-29631(2001).
RN [6]
RP FUNCTION.
RX PubMed=15075264; DOI=10.1128/ec.3.2.339-347.2004;
RA Stebbins J.L., Triezenberg S.J.;
RT "Identification, mutational analysis, and coactivator requirements of two
RT distinct transcriptional activation domains of the Saccharomyces cerevisiae
RT Hap4 protein.";
RL Eukaryot. Cell 3:339-347(2004).
RN [7]
RP ASSOCIATION WITH THE HAP2-HAP3-HAP5 HETEROMER, AND ASSEMBLY OF THE
RP CCAT-BINDING FACTOR.
RX PubMed=16278450; DOI=10.1128/ec.4.11.1829-1839.2005;
RA McNabb D.S., Pinto I.;
RT "Assembly of the Hap2p/Hap3p/Hap4p/Hap5p-DNA complex in Saccharomyces
RT cerevisiae.";
RL Eukaryot. Cell 4:1829-1839(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND THR-265, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Acts a component of the CCAT-binding factor, which is a
CC transcriptional activator and binds to the upstream activation site
CC (UAS2) of the CYC1 gene and other genes involved in mitochondrial
CC electron transport and activates their expression. Recognizes the
CC sequence 5'-CCAAT-3'. HAP2 has primarily a structural role in the HAP
CC complexes I and II. {ECO:0000269|PubMed:15075264}.
CC -!- SUBUNIT: Component of the CCAT-binding factor (CBF or HAP complex II),
CC which consists of one copy each of HAP2, HAP3, HAP4 and HAP5. The
CC assembly of the HAP2-HAP3-HAP5 heteromer (HAP complex I) occurs in a
CC one-step pathway and its binding to DNA is a prerequisite for the
CC association of HAP4. {ECO:0000269|PubMed:11390369}.
CC -!- INTERACTION:
CC P06774; Q02516: HAP5; NbExp=7; IntAct=EBI-8152, EBI-8165;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the NFYA/HAP2 subunit family.
CC {ECO:0000255|PROSITE-ProRule:PRU00966}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M15243; AAA34663.1; -; Genomic_DNA.
DR EMBL; Z72759; CAA96955.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07881.1; -; Genomic_DNA.
DR PIR; A26771; A26771.
DR RefSeq; NP_011277.1; NM_001181103.1.
DR AlphaFoldDB; P06774; -.
DR SMR; P06774; -.
DR BioGRID; 33002; 173.
DR ComplexPortal; CPX-1830; CCAAT-binding factor complex.
DR DIP; DIP-1361N; -.
DR IntAct; P06774; 142.
DR MINT; P06774; -.
DR STRING; 4932.YGL237C; -.
DR iPTMnet; P06774; -.
DR MaxQB; P06774; -.
DR PaxDb; P06774; -.
DR PRIDE; P06774; -.
DR EnsemblFungi; YGL237C_mRNA; YGL237C; YGL237C.
DR GeneID; 852614; -.
DR KEGG; sce:YGL237C; -.
DR SGD; S000003206; HAP2.
DR VEuPathDB; FungiDB:YGL237C; -.
DR eggNOG; KOG1561; Eukaryota.
DR GeneTree; ENSGT00390000015714; -.
DR HOGENOM; CLU_1046461_0_0_1; -.
DR InParanoid; P06774; -.
DR OMA; QYHRIMV; -.
DR BioCyc; YEAST:G3O-30710-MON; -.
DR PRO; PR:P06774; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P06774; protein.
DR GO; GO:0016602; C:CCAAT-binding factor complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000436; P:carbon catabolite activation of transcription from RNA polymerase II promoter; IDA:SGD.
DR GO; GO:0006109; P:regulation of carbohydrate metabolic process; IC:ComplexPortal.
DR GO; GO:0043457; P:regulation of cellular respiration; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR InterPro; IPR018362; CCAAT-binding_factor_CS.
DR InterPro; IPR001289; NFYA.
DR PANTHER; PTHR12632; PTHR12632; 1.
DR Pfam; PF02045; CBFB_NFYA; 1.
DR PRINTS; PR00616; CCAATSUBUNTB.
DR SMART; SM00521; CBF; 1.
DR PROSITE; PS00686; NFYA_HAP2_1; 1.
DR PROSITE; PS51152; NFYA_HAP2_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..265
FT /note="Transcriptional activator HAP2"
FT /id="PRO_0000198781"
FT DNA_BIND 192..217
FT /note="NFYA/HAP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00966"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 23..180
FT /note="Interaction with the HAP2-HAP3-HAP5 heteromer"
FT REGION 78..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 162..185
FT /note="Subunit association domain (SAD)"
FT COMPBIAS 18..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 265
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 199
FT /note="R->L: Favors CCACC binding over CCAAT."
FT /evidence="ECO:0000269|PubMed:8223474"
SQ SEQUENCE 265 AA; 29867 MW; 282D8AC2BD6A4CB3 CRC64;
MSADETDAKF HPLETDLQSD TAAATSTAAA SRSPSLQEKP IEMPLDMGKA PSPRGEDQRV
TNEEDLFLFN RLRASQNRVM DSLEPQQQSQ YTSSSVSTME PSADFTSFSA VTTLPPPPHQ
QQQQQQQQQQ QQQLVVQAQY TQNQPNLQSD VLGTAIAEQP FYVNAKQYYR ILKRRYARAK
LEEKLRISRE RKPYLHESRH KHAMRRPRGE GGRFLTAAEI KAMKSKKSGA SDDPDDSHED
KKITTKIIQE QPHATSTAAA ADKKT
