AF9_YEAST
ID AF9_YEAST Reviewed; 226 AA.
AC P53930; D6W173; Q6B1N1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Protein AF-9 homolog;
GN Name=YAF9; OrderedLocusNames=YNL107W; ORFNames=N1966;
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].
RX PubMed=9090055;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<261::aid-yea64>3.0.co;2-l;
RA de Antoni A., D'Angelo M., Dal Pero F., Sartorello F., Pandolfo D.,
RA Pallavicini A., Lanfranchi G., Valle G.;
RT "The DNA sequence of cosmid 14-13b from chromosome XIV of Saccharomyces
RT cerevisiae reveals an unusually high number of overlapping open reading
RT frames.";
RL Yeast 13:261-266(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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [6]
RP IDENTIFICATION IN THE SWR1 COMPLEX, FUNCTION OF THE SWR1 COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690608; DOI=10.1016/s1097-2765(03)00497-0;
RA Krogan N.J., Keogh M.-C., Datta N., Sawa C., Ryan O.W., Ding H., Haw R.A.,
RA Pootoolal J., Tong A., Canadien V., Richards D.P., Wu X., Emili A.,
RA Hughes T.R., Buratowski S., Greenblatt J.F.;
RT "A Snf2 family ATPase complex required for recruitment of the histone H2A
RT variant Htz1.";
RL Mol. Cell 12:1565-1576(2003).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE NUA4 COMPLEX.
RX PubMed=12917332; DOI=10.1128/mcb.23.17.6086-6102.2003;
RA Le Masson I., Yu D.Y., Jensen K., Chevalier A., Courbeyrette R.,
RA Boulard Y., Smith M.M., Mann C.;
RT "Yaf9, a novel NuA4 histone acetyltransferase subunit, is required for the
RT cellular response to spindle stress in yeast.";
RL Mol. Cell. Biol. 23:6086-6102(2003).
RN [8]
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 [9]
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 [10]
RP INTERACTION WITH SWC4.
RX PubMed=15302830; DOI=10.1128/ec.3.4.976-983.2004;
RA Bittner C.B., Zeisig D.T., Zeisig B.B., Slany R.K.;
RT "Direct physical and functional interaction of the NuA4 complex components
RT Yaf9p and Swc4p.";
RL Eukaryot. Cell 3:976-983(2004).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE NUA4 COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15485911; DOI=10.1128/mcb.24.21.9424-9436.2004;
RA Zhang H., Richardson D.O., Roberts D.N., Utley R.T., Erdjument-Bromage H.,
RA Tempst P., Cote J., Cairns B.R.;
RT "The Yaf9 component of the SWR1 and NuA4 complexes is required for proper
RT gene expression, histone H4 acetylation, and Htz1 replacement near
RT telomeres.";
RL Mol. Cell. Biol. 24:9424-9436(2004).
RN [12]
RP FUNCTION, IDENTIFICATION IN THE SWR1 COMPLEX, IDENTIFICATION IN THE NUA4
RP COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15045029; DOI=10.1371/journal.pbio.0020131;
RA Kobor M.S., Venkatasubrahmanyam S., Meneghini M.D., Gin J.W.,
RA Jennings J.L., Link A.J., Madhani H.D., Rine J.;
RT "A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p
RT deposits histone variant H2A.Z into euchromatin.";
RL PLoS Biol. 2:587-599(2004).
RN [13]
RP IDENTIFICATION IN THE NUA4 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15353583; DOI=10.1073/pnas.0405753101;
RA Krogan N.J., Baetz K., Keogh M.-C., Datta N., Sawa C., Kwok T.C.Y.,
RA Thompson N.J., Davey M.G., Pootoolal J., Hughes T.R., Emili A.,
RA Buratowski S., Hieter P., Greenblatt J.F.;
RT "Regulation of chromosome stability by the histone H2A variant Htz1, the
RT Swr1 chromatin remodeling complex, and the histone acetyltransferase
RT NuA4.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13513-13518(2004).
RN [14]
RP IDENTIFICATION IN THE SWR1 COMPLEX, FUNCTION OF THE SWR1 COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14645854; DOI=10.1126/science.1090701;
RA Mizuguchi G., Shen X., Landry J., Wu W.-H., Sen S., Wu C.;
RT "ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin
RT remodeling complex.";
RL Science 303:343-348(2004).
CC -!- FUNCTION: Component of the SWR1 complex which mediates the ATP-
CC dependent exchange of histone H2A for the H2A variant HZT1 leading to
CC transcriptional regulation of selected genes by chromatin remodeling.
CC Component of the NuA4 histone acetyltransferase complex which is
CC involved in transcriptional activation of selected genes principally by
CC acetylation of nucleosomal histones H4 and H2A. The NuA4 complex is
CC also involved in DNA repair. Yaf9 may also be required for viability in
CC conditions in which the structural integrity of the spindle is
CC compromised. {ECO:0000269|PubMed:12917332, ECO:0000269|PubMed:14645854,
CC ECO:0000269|PubMed:14690608, ECO:0000269|PubMed:15045029,
CC ECO:0000269|PubMed:15485911}.
CC -!- SUBUNIT: Component of the SWR1 chromatin-remodeling complex composed of
CC at least ACT1, ARP4, RVB1, RVB2, ARP6, YAF9, VPS71, VPS72, SWC3, SWC4,
CC SWC5, SWC7 and SWR1, and perhaps BDF1. Component of the NuA4 histone
CC acetyltransferase complex composed of at least ACT1, ARP4, YAF9, VID21,
CC SWC4, EAF3, EAF5, EAF6, EAF7, EPL1, ESA1, TRA1 and YNG2. Interacts with
CC SWC4. {ECO:0000269|PubMed:12917332, ECO:0000269|PubMed:14645854,
CC ECO:0000269|PubMed:14690608, ECO:0000269|PubMed:15045029,
CC ECO:0000269|PubMed:15302830, ECO:0000269|PubMed:15353583,
CC ECO:0000269|PubMed:15485911}.
CC -!- INTERACTION:
CC P53930; P35817: BDF1; NbExp=3; IntAct=EBI-28841, EBI-3493;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- DOMAIN: The coiled-coil domain is required for assembly into the NuA4
CC complex.
CC -!- MISCELLANEOUS: Present with 259 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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; Z69382; CAA93400.1; -; Genomic_DNA.
DR EMBL; Z71383; CAA95984.1; -; Genomic_DNA.
DR EMBL; AY693049; AAT93068.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10439.1; -; Genomic_DNA.
DR PIR; S63048; S63048.
DR RefSeq; NP_014292.3; NM_001182945.3.
DR PDB; 3FK3; X-ray; 2.30 A; A/B/C=8-169.
DR PDB; 3RLS; X-ray; 1.70 A; A/B=9-176.
DR PDB; 6AXJ; X-ray; 2.38 A; A/B/C/D=8-171.
DR PDBsum; 3FK3; -.
DR PDBsum; 3RLS; -.
DR PDBsum; 6AXJ; -.
DR AlphaFoldDB; P53930; -.
DR SMR; P53930; -.
DR BioGRID; 35717; 448.
DR ComplexPortal; CPX-2122; Swr1 chromatin remodelling complex.
DR ComplexPortal; CPX-3155; NuA4 histone acetyltransferase complex.
DR DIP; DIP-4347N; -.
DR IntAct; P53930; 31.
DR MINT; P53930; -.
DR STRING; 4932.YNL107W; -.
DR MaxQB; P53930; -.
DR PaxDb; P53930; -.
DR PRIDE; P53930; -.
DR EnsemblFungi; YNL107W_mRNA; YNL107W; YNL107W.
DR GeneID; 855616; -.
DR KEGG; sce:YNL107W; -.
DR SGD; S000005051; YAF9.
DR VEuPathDB; FungiDB:YNL107W; -.
DR eggNOG; KOG3149; Eukaryota.
DR HOGENOM; CLU_051385_2_1_1; -.
DR InParanoid; P53930; -.
DR OMA; PYHNEDM; -.
DR BioCyc; YEAST:G3O-33132-MON; -.
DR BRENDA; 2.3.1.48; 984.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-75955; RNA Polymerase II Transcription Elongation.
DR EvolutionaryTrace; P53930; -.
DR PRO; PR:P53930; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53930; protein.
DR GO; GO:0000785; C:chromatin; IDA:ComplexPortal.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0000812; C:Swr1 complex; IDA:SGD.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IDA:SGD.
DR GO; GO:0006281; P:DNA repair; IDA:SGD.
DR GO; GO:0016573; P:histone acetylation; IDA:ComplexPortal.
DR GO; GO:0043486; P:histone exchange; 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 GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR GO; GO:0006351; P:transcription, DNA-templated; IC:ComplexPortal.
DR Gene3D; 2.60.40.1970; -; 1.
DR InterPro; IPR037989; Yaf9.
DR InterPro; IPR038704; YEAST_sf.
DR InterPro; IPR005033; YEATS.
DR PANTHER; PTHR23195; PTHR23195; 1.
DR PANTHER; PTHR23195:SF15; PTHR23195:SF15; 1.
DR Pfam; PF03366; YEATS; 1.
DR PROSITE; PS51037; YEATS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Chromatin regulator; Coiled coil; Cytoplasm;
KW DNA damage; DNA repair; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..226
FT /note="Protein AF-9 homolog"
FT /id="PRO_0000215934"
FT DOMAIN 8..169
FT /note="YEATS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00376"
FT COILED 187..224
FT /evidence="ECO:0000255"
FT CONFLICT 65
FT /note="K -> R (in Ref. 4; AAT93068)"
FT /evidence="ECO:0000305"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:3FK3"
FT STRAND 14..26
FT /evidence="ECO:0007829|PDB:3RLS"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:3RLS"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:3RLS"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:3RLS"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:3RLS"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:3RLS"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:3RLS"
FT STRAND 79..90
FT /evidence="ECO:0007829|PDB:3RLS"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:3RLS"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:3RLS"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:3RLS"
FT STRAND 145..157
FT /evidence="ECO:0007829|PDB:3RLS"
FT HELIX 160..168
FT /evidence="ECO:0007829|PDB:3RLS"
SQ SEQUENCE 226 AA; 25981 MW; 1FE08F72942061D1 CRC64;
MAPTISKRIK TLSVSRPIIY GNTAKKMGSV KPPNAPAEHT HLWTIFVRGP QNEDISYFIK
KVVFKLHDTY PNPVRSIEAP PFELTETGWG EFDINIKVYF VEEANEKVLN FYHRLRLHPY
ANPVPNSDNG NEQNTTDHNS KDAEVSSVYF DEIVFNEPNE EFFKILMSRP GNLLPSNKTD
DCVYSKQLEQ EEIDRIEIGI EKVDKEIDEL KQKLENLVKQ EAINGS
