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Database: UniProt
Entry: Q12373
LinkDB: Q12373
Original site: Q12373 
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   07-APR-2021, entry version 155.
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   SMR; Q12373; -.
DR   BioGRID; 31231; 57.
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   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:0006348; P:chromatin silencing at telomere; IGI:SGD.
DR   GO; GO:0016573; P:histone acetylation; IDA:SGD.
DR   GO; GO:0006334; P:nucleosome assembly; IDA: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          248..332
FT                   /note="Interaction with dimeric histone H2A and H2B"
FT                   /evidence="ECO:0000269|PubMed:27618665"
FT   COMPBIAS        97..184
FT                   /note="Glu-rich"
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:0007744|PDB:4NQ0"
FT   HELIX           38..51
FT                   /evidence="ECO:0007744|PDB:4NQ0"
FT   STRAND          54..56
FT                   /evidence="ECO:0007744|PDB:4NQ0"
FT   HELIX           61..77
FT                   /evidence="ECO:0007744|PDB:4NQ0"
FT   HELIX           161..163
FT                   /evidence="ECO:0007744|PDB:4NQ0"
FT   HELIX           167..171
FT                   /evidence="ECO:0007744|PDB:4NQ0"
FT   TURN            175..177
FT                   /evidence="ECO:0007744|PDB:5BT1"
FT   HELIX           186..188
FT                   /evidence="ECO:0007744|PDB:4NQ0"
FT   HELIX           194..198
FT                   /evidence="ECO:0007744|PDB:4NQ0"
FT   HELIX           202..218
FT                   /evidence="ECO:0007744|PDB:4NQ0"
FT   STRAND          222..224
FT                   /evidence="ECO:0007744|PDB:5BT1"
FT   HELIX           229..248
FT                   /evidence="ECO:0007744|PDB:4NQ0"
FT   HELIX           252..266
FT                   /evidence="ECO:0007744|PDB:4NQ0"
FT   HELIX           273..290
FT                   /evidence="ECO:0007744|PDB:4NQ0"
FT   HELIX           298..316
FT                   /evidence="ECO:0007744|PDB:4NQ0"
FT   HELIX           323..342
FT                   /evidence="ECO:0007744|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
//
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