HPA2_YEAST
ID HPA2_YEAST Reviewed; 156 AA.
AC Q06592; D6W4J3;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Histone acetyltransferase HPA2 {ECO:0000303|PubMed:10600387};
DE EC=2.3.1.48 {ECO:0000269|PubMed:10600387, ECO:0000269|PubMed:23775086};
GN Name=HPA2 {ECO:0000303|PubMed:10600387};
GN OrderedLocusNames=YPR193C {ECO:0000312|SGD:S000006397}; ORFNames=P9677.12;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, AND SUBSTRATE SPECIFICITY.
RX PubMed=23775086; DOI=10.1074/jbc.m113.486274;
RA Sampath V., Liu B., Tafrov S., Srinivasan M., Rieger R., Chen E.I.,
RA Sternglanz R.;
RT "Biochemical characterization of Hpa2 and Hpa3, two small closely related
RT acetyltransferases from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 288:21506-21513(2013).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 7-156 WITH ACETYL-COA, AND
RP SUBUNIT.
RX PubMed=10600387; DOI=10.1006/jmbi.1999.3338;
RA Angus-Hill M.L., Dutnall R.N., Tafrov S.T., Sternglanz R., Ramakrishnan V.;
RT "Crystal structure of the histone acetyltransferase Hpa2: a tetrameric
RT member of the Gcn5-related N-acetyltransferase superfamily.";
RL J. Mol. Biol. 294:1311-1325(1999).
CC -!- FUNCTION: N-acetyltransferase that acetylates histone H3 at 'Lys-14'
CC and histone H4 at 'Lys-5' and 'Lys-12'. Also acetylates polyamines like
CC putrescine, spermidine and spermine, and certain other small basic
CC proteins like nuclear HMG proteins. {ECO:0000269|PubMed:23775086}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000269|PubMed:10600387, ECO:0000269|PubMed:23775086};
CC -!- SUBUNIT: Forms homodimers in the absence, and homotetramers in the
CC presence of acetyl-CoA. {ECO:0000269|PubMed:10600387}.
CC -!- INTERACTION:
CC Q06592; Q06592: HPA2; NbExp=3; IntAct=EBI-34205, EBI-34205;
CC -!- PTM: Autoacetylates in an intermolecular reaction.
CC {ECO:0000305|PubMed:10600387}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GNAT subfamily.
CC {ECO:0000305}.
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DR EMBL; U25841; AAB64622.1; -; Genomic_DNA.
DR EMBL; AY558056; AAS56382.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11609.1; -; Genomic_DNA.
DR PIR; S58823; S58823.
DR RefSeq; NP_015519.1; NM_001184290.1.
DR PDB; 1QSM; X-ray; 2.40 A; A/B/C/D=5-156.
DR PDB; 1QSO; X-ray; 2.90 A; A/B/C/D=8-156.
DR PDBsum; 1QSM; -.
DR PDBsum; 1QSO; -.
DR AlphaFoldDB; Q06592; -.
DR SMR; Q06592; -.
DR BioGRID; 36365; 108.
DR ComplexPortal; CPX-2143; Hpa2 acetyltransferase.
DR DIP; DIP-2953N; -.
DR IntAct; Q06592; 4.
DR MINT; Q06592; -.
DR STRING; 4932.YPR193C; -.
DR PaxDb; Q06592; -.
DR EnsemblFungi; YPR193C_mRNA; YPR193C; YPR193C.
DR GeneID; 856323; -.
DR KEGG; sce:YPR193C; -.
DR SGD; S000006397; HPA2.
DR VEuPathDB; FungiDB:YPR193C; -.
DR eggNOG; KOG3216; Eukaryota.
DR GeneTree; ENSGT00950000183121; -.
DR HOGENOM; CLU_013985_32_1_1; -.
DR InParanoid; Q06592; -.
DR OMA; DGHIRYR; -.
DR BioCyc; YEAST:G3O-34315-MON; -.
DR BRENDA; 2.3.1.48; 984.
DR Reactome; R-SCE-351200; Interconversion of polyamines.
DR EvolutionaryTrace; Q06592; -.
DR PRO; PR:Q06592; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06592; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:1990331; C:Hpa2 acetyltransferase complex; IPI:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008080; F:N-acetyltransferase activity; IDA:SGD.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:ComplexPortal.
DR GO; GO:0043967; P:histone H4 acetylation; IDA:ComplexPortal.
DR GO; GO:0032917; P:polyamine acetylation; IDA:ComplexPortal.
DR GO; GO:0006473; P:protein acetylation; IDA:SGD.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR032962; HPA2/HPA3.
DR PANTHER; PTHR10545:SF42; PTHR10545:SF42; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Chromatin regulator; Reference proteome;
KW Transferase.
FT CHAIN 1..156
FT /note="Histone acetyltransferase HPA2"
FT /id="PRO_0000074633"
FT DOMAIN 9..156
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 93..106
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:10600387"
FT SITE 139
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000305|PubMed:10600387"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:1QSM"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:1QSM"
FT HELIX 19..32
FT /evidence="ECO:0007829|PDB:1QSM"
FT HELIX 39..50
FT /evidence="ECO:0007829|PDB:1QSM"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:1QSO"
FT STRAND 56..66
FT /evidence="ECO:0007829|PDB:1QSM"
FT STRAND 69..78
FT /evidence="ECO:0007829|PDB:1QSM"
FT STRAND 87..95
FT /evidence="ECO:0007829|PDB:1QSM"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:1QSM"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1QSM"
FT HELIX 104..118
FT /evidence="ECO:0007829|PDB:1QSM"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:1QSM"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:1QSM"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:1QSM"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:1QSM"
SQ SEQUENCE 156 AA; 18334 MW; 707C6EA8B8ED73A7 CRC64;
MSNTSEDNIT VRFVTENDKE GWQRLWKSYQ DFYEVSFPDD LDDFNFGRFL DPNIKMWAAV
AVESSSEKII GMINFFNHMT TWDFKDKIYI NDLYVDENSR VKGAGGKLIQ FVYDEADKLG
TPSVYWCTDE SNHRAQLLYV KVGYKAPKIL YKRKGY
