HAP5_YEAST
ID HAP5_YEAST Reviewed; 242 AA.
AC Q02516; D6W353; Q08827;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Transcriptional activator HAP5;
GN Name=HAP5; OrderedLocusNames=YOR358W;
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] OF 27-242.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7828851; DOI=10.1101/gad.9.1.47;
RA McNabb D.S., Xing Y., Guarente L.;
RT "Cloning of yeast HAP5: a novel subunit of a heterotrimeric complex
RT required for CCAAT binding.";
RL Genes Dev. 9:47-58(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RA McNabb D.S.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
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 [5]
RP IDENTIFICATION IN THE CCAT-BINDING FACTOR.
RX PubMed=9372932; DOI=10.1128/mcb.17.12.7008;
RA McNabb D.S., Tseng K.A.-S., Guarente L.;
RT "The Saccharomyces cerevisiae Hap5p homolog from fission yeast reveals two
RT conserved domains that are essential for assembly of heterotetrameric
RT CCAAT-binding factor.";
RL Mol. Cell. Biol. 17:7008-7018(1997).
RN [6]
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 [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP ASSEMBLY OF THE 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS
RP 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).
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'. HAP5 is essential for DNA-binding activity. It
CC may be the linchpin that binds to the subunit association domains (SAD)
CC of HAP2 and HAP3 to bring these proteins together.
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 ECO:0000269|PubMed:9372932}.
CC -!- INTERACTION:
CC Q02516; P06774: HAP2; NbExp=7; IntAct=EBI-8165, EBI-8152;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 450 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NFYC/HAP5 subunit family. {ECO:0000305}.
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DR EMBL; U19932; AAC49610.1; -; Genomic_DNA.
DR EMBL; Z75266; CAA99687.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11119.1; -; Genomic_DNA.
DR PIR; S67270; S67270.
DR RefSeq; NP_015003.1; NM_001183778.1.
DR AlphaFoldDB; Q02516; -.
DR SMR; Q02516; -.
DR BioGRID; 34743; 433.
DR ComplexPortal; CPX-1830; CCAAT-binding factor complex.
DR DIP; DIP-1363N; -.
DR IntAct; Q02516; 10.
DR MINT; Q02516; -.
DR STRING; 4932.YOR358W; -.
DR iPTMnet; Q02516; -.
DR MaxQB; Q02516; -.
DR PaxDb; Q02516; -.
DR PRIDE; Q02516; -.
DR EnsemblFungi; YOR358W_mRNA; YOR358W; YOR358W.
DR GeneID; 854540; -.
DR KEGG; sce:YOR358W; -.
DR SGD; S000005885; HAP5.
DR VEuPathDB; FungiDB:YOR358W; -.
DR eggNOG; KOG1657; Eukaryota.
DR GeneTree; ENSGT00940000155689; -.
DR HOGENOM; CLU_1134110_0_0_1; -.
DR InParanoid; Q02516; -.
DR BioCyc; YEAST:G3O-33829-MON; -.
DR PRO; PR:Q02516; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q02516; protein.
DR GO; GO:0016602; C:CCAAT-binding factor complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0000436; P:carbon catabolite activation of transcription from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0006109; P:regulation of carbohydrate metabolic process; IC:ComplexPortal.
DR GO; GO:0043457; P:regulation of cellular respiration; IGI:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR027170; HAP5_su.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR PANTHER; PTHR10252:SF8; PTHR10252:SF8; 1.
DR Pfam; PF00125; Histone; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..242
FT /note="Transcriptional activator HAP5"
FT /id="PRO_0000218260"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 242 AA; 27676 MW; 4104058BF48A4319 CRC64;
MTDRNFSPQQ GQGPQESLPE GPQPSTMIQR EEMNMPRQYS EQQQLQENEG EGENTRLPVS
EEEFRMVQEL QAIQAGHDQA NLPPSGRGSL EGEDNGNSDG ADGEMDEDDE EYDVFRNVGQ
GLVGHYKEIM IRYWQELINE IESTNEPGSE HQDDFKSHSL PFARIRKVMK TDEDVKMISA
EAPIIFAKAC EIFITELTMR AWCVAERNKR RTLQKADIAE ALQKSDMFDF LIDVVPRRPL
PQ
