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Description:
Protein AF-9 homolog.
Molecular weight: 25981
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 )
Important dates:
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
07-MAR-2006, entry version 39.
Phylogenetic order:
Eukaryota Fungi Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein AF9_YEAST:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | Z69382 | CAA93400.1 | - |
| EMBL | Z71383 | CAA95984.1 | - |
| EMBL | AY693049 | AAT93068.1 | - |
| PIR | S63048 | S63048. | |
| IntAct | P53930 | -.1 | |
| GermOnline | 143113 | -.1 | |
| Ensembl | YNL107W | Saccharomyces cerevisiae.1 | |
| GenomeReviews | Y13139_GR | YNL107W.1 | |
| SGD | S000005051 | YAF9. | |
| BioCyc | SCER-S28-01:SCER-S28-01-004963-MONOMER | -.1 | |
| LinkHub | P53930 | -.1 | |
| GO | GO:0005737 | C:cytoplasm | IDA. |
| GO | GO:0043189 | C:H4/H2A histone acetyltransferase complex | IPI. |
| GO | GO:0005634 | C:nucleus | IDA. |
| GO | GO:0000812 | C:SWR1 complex | IPI. |
| GO | GO:0006338 | P:chromatin remodeling | IDA. |
| GO | GO:0006348 | P:chromatin silencing at telomere | IMP. |
| InterPro | IPR005033 | YEATS. | |
| Pfam | PF03366 | YEATS | 1. |
| PROSITE | PS51037 | YEATS | 1. |
Keywords:
Activator; Chromatin regulator; Coiled coil; Complete proteome; DNA damage; DNA repair; Nuclear protein; Transcription; Transcription regulation.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX MEDLINE=97245296; 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
RT Saccharomyces cerevisiae reveals an unusually high number of
RT overlapping open reading frames.";
RL Yeast 13:261-266(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S288c / FY1679;
RX MEDLINE=97313269; 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.,
RA Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
RA Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
RA Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
RA Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
RA Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
RA Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
RA Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
RA Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
RA Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
RA Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
RA Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
RA Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
RA Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
RT and its evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c;
RA Marsischky G., Rolfs A., Richardson A., Kane M., Baqui M., Taycher E.,
RA Hu Y., Vannberg F., Weger J., Kramer J., Moreira D., Kelley F.,
RA Zuo D., Raphael J., Hogle C., Jepson D., Williamson J., Camargo A.,
RA Gonzaga L., Vasconcelos A.T., Simpson A., Kolodner R., Harlow E.,
RA LaBaer J.;
RT "Creation of the YFLEX clone resource: cloning of Saccharomyces
RT cerevisiae ORFs in the Gateway recombinational cloning system.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION IN THE SWR1 COMPLEX, FUNCTION OF THE SWR1 COMPLEX, AND
RP 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.,
RA Haw R.A., Pootoolal J., Tong A., Canadien V., Richards D.P., Wu X.,
RA Emili A., Hughes T.R., Buratowski S., Greenblatt J.F.;
RT "A Snf2 family ATPase complex required for recruitment of the histone
RT H2A variant Htz1.";
RL Mol. Cell 12:1565-1576(2003).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE NUA4
RP 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
RT the cellular response to spindle stress in yeast.";
RL Mol. Cell. Biol. 23:6086-6102(2003).
RN [6]
RP SUBCELLULAR LOCATION.
RX MEDLINE=22923954; 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 [7]
RP LEVEL OF PROTEIN EXPRESSION.
RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA Dephoure N., O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
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
RT components Yaf9p and Swc4p.";
RL Eukaryot. Cell 3:976-983(2004).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE NUA4 COMPLEX,
RP AND 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.,
RA Erdjument-Bromage H., Tempst P., Cote J., Cairns B.R.;
RT "The Yaf9 component of the SWR1 and NuA4 complexes is required for
RT proper gene expression, histone H4 acetylation, and Htz1 replacement
RT near telomeres.";
RL Mol. Cell. Biol. 24:9424-9436(2004).
RN [10]
RP FUNCTION, IDENTIFICATION IN THE SWR1 COMPLEX, IDENTIFICATION IN THE
RP NUA4 COMPLEX, AND 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
RT Swr1p deposits histone variant H2A.Z into euchromatin.";
RL PLoS Biol. 2:E131-E131(2004).
RN [11]
RP IDENTIFICATION IN THE NUA4 COMPLEX, AND MASS 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,
RT the Swr1 chromatin remodeling complex, and the histone
RT acetyltransferase NuA4.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13513-13518(2004).
RN [12]
RP IDENTIFICATION IN THE SWR1 COMPLEX, FUNCTION OF THE SWR1 COMPLEX, AND
RP 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
RT chromatin remodeling complex.";
RL Science 303:343-348(2004).
Feature:
CHAIN 1 226 Protein AF-9 homolog.
/FTId=PRO_0000215934.
DOMAIN 15 123 YEATS.
COILED 187 224 Potential.
CONFLICT 65 65 K -> R (in Ref. 3).
Comments:
-!- FUNCTION: Component of the SWR1 complex which mediates the ATP-
dependent exchange of histone H2A for the H2A variant HZT1 leading
to transcriptional regulation of selected genes by chromatin
remodeling. Component of the NuA4 histone acetyltransferase
complex which is involved in transcriptional activation of
selected genes principally by acetylation of nucleosomal histones
H4 and H2A. The NuA4 complex is also involved in DNA repair. Yaf9
may also be required for viability in conditions in which the
structural integrity of the spindle is compromised.
-!- SUBUNIT: Component of the SWR1 chromatin remodeling complex
composed of at least ACT1, ARP4, RVB1, RVB2, ARP6, YAF9, VPS71,
VPS72, SWC3, SWC4, SWC5, SWC7 and SWR1, and perhaps BDF1.
Component of the NuA4 histone acetyltransferase complex composed
of at least ACT1, ARP4, YAF9, VID21, SWC4, EAF3, EAF5, EAF6, EAF7,
EPL1, ESA1, TRA1 and YNG2. Interacts with SWC4.
-!- SUBCELLULAR LOCATION: Cytoplasmic and nuclear.
-!- DOMAIN: The coiled-coil domain is required for assembly into the
NuA4 complex.
-!- MISCELLANEOUS: Present with 259 molecules/cell.
-!- SIMILARITY: Contains 1 YEATS domain.
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Sequence length: 226
MAPTISKRIK TLSVSRPIIY GNTAKKMGSV KPPNAPAEHT HLWTIFVRGP QNEDISYFIK
KVVFKLHDTY PNPVRSIEAP PFELTETGWG EFDINIKVYF VEEANEKVLN FYHRLRLHPY
ANPVPNSDNG NEQNTTDHNS KDAEVSSVYF DEIVFNEPNE EFFKILMSRP GNLLPSNKTD
DCVYSKQLEQ EEIDRIEIGI EKVDKEIDEL KQKLENLVKQ EAINGS