HIF1_YEAST
ID HIF1_YEAST Reviewed; 385 AA.
AC Q12373; D6VXY2;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=HAT1-interacting factor 1;
GN Name=HIF1; OrderedLocusNames=YLL022C; ORFNames=L1205;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9046100;
RX DOI=10.1002/(sici)1097-0061(199702)13:2<183::aid-yea65>3.0.co;2-v;
RA Purnelle B., Goffeau A.;
RT "The sequence of 32kb on the left arm of yeast chromosome XII reveals six
RT known genes, a new member of the seripauperins family and a new ABC
RT transporter homologous to the human multidrug resistance protein.";
RL Yeast 13:183-188(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
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 [6]
RP IDENTIFICATION IN THE NUCLEAR HAT-B COMPLEX, FUNCTION OF THE HAT-B COMPLEX,
RP INTERACTION WITH HISTONE H4, AND SUBCELLULAR LOCATION.
RX PubMed=14761951; DOI=10.1074/jbc.m314228200;
RA Poveda A., Pamblanco M., Tafrov S., Tordera V., Sternglanz R., Sendra R.;
RT "Hif1 is a component of yeast histone acetyltransferase B, a complex mainly
RT localized in the nucleus.";
RL J. Biol. Chem. 279:16033-16043(2004).
RN [7]
RP FUNCTION, IDENTIFICATION IN THE NUCLEAR HAT-B COMPLEX, INTERACTION WITH
RP HISTONES H3 AND H4, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15099519; DOI=10.1016/s1097-2765(04)00184-4;
RA Ai X., Parthun M.R.;
RT "The nuclear Hat1p/Hat2p complex: a molecular link between type B histone
RT acetyltransferases and chromatin assembly.";
RL Mol. Cell 14:195-205(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174, AND IDENTIFICATION BY
RP 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-174, AND IDENTIFICATION BY
RP 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 X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), SUBUNIT, INTERACTION WITH HISTONE
RP H2A; H2B; H3 AND H4, DOMAIN, AND MUTAGENESIS OF 85-ASP--PHE-198 AND
RP 135-LEU--VAL-158.
RX PubMed=24946827; DOI=10.1042/bj20131640;
RA Liu H., Zhang M., He W., Zhu Z., Teng M., Gao Y., Niu L.;
RT "Structural insights into yeast histone chaperone Hif1: a scaffold protein
RT recruiting protein complexes to core histones.";
RL Biochem. J. 462:465-473(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS), SUBUNIT, INTERACTION WITH HISTONE
RP H2A; H2B; H3 AND H4, DOMAIN, AND MUTAGENESIS OF 80-GLY--VAL-158;
RP 85-ASP--GLU-198; 95-GLY--VAL-158; 135-LEU--VAL-158; GLU-248; GLU-250;
RP ASP-288; ARG-291 AND 332-GLN--GLU-342.
RX PubMed=27618665; DOI=10.1016/j.str.2016.08.001;
RA Zhang M., Liu H., Gao Y., Zhu Z., Chen Z., Zheng P., Xue L., Li J.,
RA Teng M., Niu L.;
RT "Structural Insights into the Association of Hif1 with Histones H2A-H2B
RT Dimer and H3-H4 Tetramer.";
RL Structure 24:1810-1820(2016).
CC -!- FUNCTION: Histone H3 and H4 specific chaperone component of the nuclear
CC histone acetyltransferase B (HAT-B) complex. Involved in chromatin
CC assembly and telomere silencing. {ECO:0000269|PubMed:14761951,
CC ECO:0000269|PubMed:15099519}.
CC -!- SUBUNIT: Homodimer (PubMed:27618665). The homodimer interacts with a
CC histone tetramer containing H3 and H4; the interaction is direct
CC (PubMed:24946827, PubMed:27618665). The homodimer interacts with
CC heterodimeric histone H2A and H2B; the interaction is direct
CC (PubMed:24946827, PubMed:27618665). Component of the nuclear histone
CC acetyltransferase B (HAT-B) complex composed of at least HAT1, HAT2 and
CC HIF1 (PubMed:14761951, PubMed:15099519). Does not interact with HAT1 in
CC the absence of HAT2 (PubMed:14761951, PubMed:24946827). Interacts with
CC histones H3 and H4 in a HAT1/HAT2 dependent manner (PubMed:14761951,
CC PubMed:15099519). Interaction with heterotetrameric histone H3 and H4
CC precludes interaction with dimeric histone H2A and H2B, irrespective of
CC the fact that their binding involves non-identical regions of the
CC protein (PubMed:24946827, PubMed:27618665).
CC {ECO:0000269|PubMed:14761951, ECO:0000269|PubMed:15099519,
CC ECO:0000269|PubMed:24946827, ECO:0000269|PubMed:27618665}.
CC -!- INTERACTION:
CC Q12373; P39984: HAT2; NbExp=4; IntAct=EBI-31911, EBI-8185;
CC Q12373; P02309: HHF2; NbExp=5; IntAct=EBI-31911, EBI-8113;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14761951, ECO:0000269|PubMed:15099519}.
CC -!- DOMAIN: The N-terminal TPR repeat region contains an acidic patch that
CC is important for interaction with histones (PubMed:24946827,
CC PubMed:27618665). A C-terminal, highly polar region mediates
CC interaction with dimeric histone H2A and H2B, but is not involved in
CC interaction with heterotetrameric histone H3 and H4 (PubMed:27618665).
CC {ECO:0000269|PubMed:24946827, ECO:0000269|PubMed:27618665}.
CC -!- MISCELLANEOUS: Present with 4550 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NASP family. {ECO:0000305}.
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DR EMBL; X97560; CAA66169.1; -; Genomic_DNA.
DR EMBL; Z73127; CAA97470.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09298.1; -; Genomic_DNA.
DR PIR; S64770; S64770.
DR RefSeq; NP_013078.1; NM_001181842.1.
DR PDB; 4NQ0; X-ray; 2.10 A; A=1-385.
DR PDB; 5BT1; X-ray; 2.62 A; A/B=1-385.
DR PDBsum; 4NQ0; -.
DR PDBsum; 5BT1; -.
DR AlphaFoldDB; Q12373; -.
DR SMR; Q12373; -.
DR BioGRID; 31231; 58.
DR ComplexPortal; CPX-1682; Histone acetyltransferase B.
DR DIP; DIP-6442N; -.
DR IntAct; Q12373; 6.
DR MINT; Q12373; -.
DR STRING; 4932.YLL022C; -.
DR iPTMnet; Q12373; -.
DR MaxQB; Q12373; -.
DR PaxDb; Q12373; -.
DR PRIDE; Q12373; -.
DR EnsemblFungi; YLL022C_mRNA; YLL022C; YLL022C.
DR GeneID; 850638; -.
DR KEGG; sce:YLL022C; -.
DR SGD; S000003945; HIF1.
DR VEuPathDB; FungiDB:YLL022C; -.
DR eggNOG; KOG4563; Eukaryota.
DR HOGENOM; CLU_797425_0_0_1; -.
DR InParanoid; Q12373; -.
DR OMA; TIFAQAV; -.
DR BioCyc; YEAST:G3O-32126-MON; -.
DR PRO; PR:Q12373; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12373; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0000123; C:histone acetyltransferase complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0016573; P:histone acetylation; IDA:SGD.
DR GO; GO:0006334; P:nucleosome assembly; IDA:SGD.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IGI:SGD.
DR Gene3D; 1.25.40.10; -; 2.
DR IDEAL; IID50290; -.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..385
FT /note="HAT1-interacting factor 1"
FT /id="PRO_0000227731"
FT REPEAT 186..220
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 229..262
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 289..322
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT REGION 80..199
FT /note="Important for interaction with heterotetrameric
FT histone H3 and H4 and for interaction with dimeric histone
FT H2A and H2B"
FT /evidence="ECO:0000269|PubMed:24946827,
FT ECO:0000269|PubMed:27618665"
FT REGION 85..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..332
FT /note="Interaction with dimeric histone H2A and H2B"
FT /evidence="ECO:0000269|PubMed:27618665"
FT REGION 340..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..160
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 80..158
FT /note="Missing: Abolishes interaction with heterotetrameric
FT histone H3 and H4 and with dimeric histone H2A and H2B."
FT /evidence="ECO:0000269|PubMed:27618665"
FT MUTAGEN 85..198
FT /note="Missing: Abolishes interaction with histones H2A,
FT H2B, H3 and H4."
FT /evidence="ECO:0000269|PubMed:24946827,
FT ECO:0000269|PubMed:27618665"
FT MUTAGEN 95..158
FT /note="Missing: Mildly decreases interaction with
FT heterotetrameric histone H3 and H4 and abolishes
FT interaction with dimeric histone H2A and H2B."
FT /evidence="ECO:0000269|PubMed:27618665"
FT MUTAGEN 135..158
FT /note="Missing: Minimal decrease of interaction with
FT heterotetrameric histone H3 and H4 and with dimeric histone
FT H2A and H2B."
FT /evidence="ECO:0000269|PubMed:24946827,
FT ECO:0000269|PubMed:27618665"
FT MUTAGEN 248
FT /note="E->A: Strongly reduces affinity for dimeric histone
FT H2A and H2B; when associated with A-250; A-288; A-291 and
FT 332-A--A-342."
FT /evidence="ECO:0000269|PubMed:27618665"
FT MUTAGEN 250
FT /note="E->A: Strongly reduces affinity for dimeric histone
FT H2A and H2B; when associated with A-248; A-288; A-291 and
FT 332-A--A-342."
FT /evidence="ECO:0000269|PubMed:27618665"
FT MUTAGEN 288
FT /note="D->A: Strongly reduces affinity for dimeric histone
FT H2A and H2B; when associated with A-248; A-250; A-291 and
FT 332-A--A-342."
FT /evidence="ECO:0000269|PubMed:27618665"
FT MUTAGEN 291
FT /note="R->A: Strongly reduces affinity for dimeric histone
FT H2A and H2B; when associated with A-248; A-250; A-288 and
FT 332-A--A-342."
FT /evidence="ECO:0000269|PubMed:27618665"
FT MUTAGEN 332..342
FT /note="QIQDDIDEVQE->AIQAAIDAVQA: Strongly reduces affinity
FT for dimeric histone H2A and H2B; when associated with A-
FT 248; A-250; A-288 and A-291."
FT /evidence="ECO:0000269|PubMed:27618665"
FT HELIX 14..34
FT /evidence="ECO:0007829|PDB:4NQ0"
FT HELIX 38..51
FT /evidence="ECO:0007829|PDB:4NQ0"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:4NQ0"
FT HELIX 61..77
FT /evidence="ECO:0007829|PDB:4NQ0"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:4NQ0"
FT HELIX 167..171
FT /evidence="ECO:0007829|PDB:4NQ0"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:5BT1"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:4NQ0"
FT HELIX 194..198
FT /evidence="ECO:0007829|PDB:4NQ0"
FT HELIX 202..218
FT /evidence="ECO:0007829|PDB:4NQ0"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:5BT1"
FT HELIX 229..248
FT /evidence="ECO:0007829|PDB:4NQ0"
FT HELIX 252..266
FT /evidence="ECO:0007829|PDB:4NQ0"
FT HELIX 273..290
FT /evidence="ECO:0007829|PDB:4NQ0"
FT HELIX 298..316
FT /evidence="ECO:0007829|PDB:4NQ0"
FT HELIX 323..342
FT /evidence="ECO:0007829|PDB:4NQ0"
SQ SEQUENCE 385 AA; 43428 MW; B280CFCCB6896506 CRC64;
MKLRAEDVLA NGTSRHKVQI DMERQVQIAK DLLAQKKFLE AAKRCQQTLD SLPKDGLLPD
PELFTIFAQA VYNMEVQNSG NLFGDALLAG DDGSGSESES EPESDVSNGE EGNENGQTEI
PNSRMFQFDQ EEEDLTGDVD SGDSEDSGEG SEEEEENVEK EEERLALHEL ANFSPANEHD
DEIEDVSQLR KSGFHIYFEN DLYENALDLL AQALMLLGRP TADGQSLTEN SRLRIGDVYI
LMGDIEREAE MFSRAIHHYL KALGYYKTLK PAEQVTEKVI QAEFLVCDAL RWVDQVPAKD
KLKRFKHAKA LLEKHMTTRP KDSELQQARL AQIQDDIDEV QENQQHGSKR PLSQPTTSIG
FPALEKPLGD FNDLSQLVKK KPRRH
