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Description:
Actin-like protein ARP4.
Molecular weight: 54832
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-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
07-MAR-2006, entry version 44.
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 ARP4_YEAST:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | X75317 | CAA53066.1 | - |
| EMBL | X83502 | CAA58489.1 | - |
| EMBL | Z49356 | CAA89374.1 | - |
| PIR | S47608 | S47608. | |
| HSSP | P02577 | 1NMD | |
| IntAct | P80428 | -.1 | |
| GermOnline | 141695 | -.1 | |
| Ensembl | YJL081C | Saccharomyces cerevisiae.1 | |
| GenomeReviews | Y13136_GR | YJL081C.1 | |
| SGD | S000003617 | ARP4. | |
| BioCyc | SCER-S28-01:SCER-S28-01-003163-MONOMER | -.1 | |
| LinkHub | P80428 | -.1 | |
| GO | GO:0000123 | C:histone acetyltransferase complex | IDA. |
| GO | GO:0031011 | C:INO80 complex | IPI. |
| GO | GO:0000790 | C:nuclear chromatin | IDA. |
| GO | GO:0005634 | C:nucleus | IDA. |
| GO | GO:0000812 | C:SWR1 complex | IPI. |
| GO | GO:0003682 | F:chromatin binding | IDA. |
| GO | GO:0004402 | F:histone acetyltransferase activity | IDA. |
| GO | GO:0005515 | F:protein binding | IPI. |
| GO | GO:0006338 | P:chromatin remodeling | IDA. |
| GO | GO:0006325 | P:establishment and/or maintenance of chromat... | IMP. |
| GO | GO:0016573 | P:histone acetylation | IDA. |
| GO | GO:0006357 | P:regulation of transcription from RNA polyme... | IDA. |
| InterPro | IPR004000 | Actin_like. | |
| PANTHER | PTHR11937 | Actin_like.1 | 3. |
| Pfam | PF00022 | Actin | 2. |
| PRINTS | PR00190 | ACTIN. | |
| SMART | SM00268 | ACTIN | 1. |
| PROSITE | PS00406 | ACTINS_1 | FALSE_NEG. |
| PROSITE | PS00432 | ACTINS_2 | FALSE_NEG. |
| PROSITE | PS01132 | ACTINS_ACT_LIKE | 1. |
Keywords:
Activator; Chromatin regulator; Complete proteome; Direct protein sequencing; DNA damage; DNA repair; Nuclear protein; Repeat; Transcription; Transcription regulation.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX MEDLINE=94336725; PubMed=8058791;
RA Harata M., Karwan A., Wintersberger U.;
RT "An essential gene of Saccharomyces cerevisiae coding for an actin-
RT related protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:8258-8262(1994).
RN [2]
RP ERRATUM.
RA Harata M., Karwan A., Wintersberger U.;
RL Proc. Natl. Acad. Sci. U.S.A. 91:10757-10757(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S288c;
RX MEDLINE=96093911; PubMed=7483841;
RA Miosga T., Schaaff-Gerstenschlaeger I., Chalwatzis N., Baur A.,
RA Boles E., Fournier C., Schmitt S., Velten C., Wilhelm N.,
RA Zimmermann F.K.;
RT "Sequence analysis of a 33.1 kb fragment from the left arm of
RT Saccharomyces cerevisiae chromosome X, including putative proteins
RT with leucine zippers, a fungal Zn(II)2-Cys6 binuclear cluster domain
RT and a putative alpha 2-SCB-alpha 2 binding site.";
RL Yeast 11:681-689(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S288c / FY1679;
RX MEDLINE=96208490; PubMed=8641269;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N.,
RA Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H.,
RA Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A.,
RA Hennemann A., Herbert C.J., Heumann K., Hilger F., Hollenberg C.P.,
RA Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L.,
RA Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V.,
RA Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M.,
RA Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W.,
RA Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M.,
RA Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A.,
RA Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M.,
RA Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT X.";
RL EMBO J. 15:2031-2049(1996).
RN [5]
RP PROTEIN SEQUENCE OF 55-66; 202-210; 220-243; 269-296; 317-323; 378-430
RP AND 448-482, IDENTIFICATION IN THE NUA4 COMPLEX, INTERACTIONS WITH
RP HISTONES H2A; H3 AND H4, MUTAGENESIS OF CYS-155 AND GLY-455, AND
RP FUNCTION.
RX PubMed=10911987; DOI=10.1016/S1097-2765(00)80258-0;
RA Galarneau L., Nourani A., Boudreault A.A., Zhang Y., Heliot L.,
RA Allard S., Savard J., Lane W.S., Stillman D.J., Cote J.;
RT "Multiple links between the NuA4 histone acetyltransferase complex and
RT epigenetic control of transcription.";
RL Mol. Cell 5:927-937(2000).
RN [6]
RP SUBCELLULAR LOCATION.
RA Weber V., Harata M., Hauser H., Wintersberger U.;
RT "The actin-related protein Act3p of Saccharomyces cerevisiae is
RT located in the nucleus.";
RL Mol. Biol. Cell 6:1263-1270(1995).
RN [7]
RP IDENTIFICATION IN THE INO80 COMPLEX, FUNCTION OF THE INO80 COMPLEX,
RP AND MASS SPECTROMETRY.
RX PubMed=10952318; DOI=10.1038/35020123;
RA Shen X., Mizuguchi G., Hamiche A., Wu C.;
RT "A chromatin remodelling complex involved in transcription and DNA
RT processing.";
RL Nature 406:541-544(2000).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF GLY-187 AND GLY-455.
RX PubMed=11937627; DOI=10.1093/nar/30.8.1743;
RA Harata M., Zhang Y., Stillman D.J., Matsui D., Oma Y., Nishimori K.,
RA Mochizuki R.;
RT "Correlation between chromatin association and transcriptional
RT regulation for the Act3p/Arp4 nuclear actin-related protein of
RT Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 30:1743-1750(2002).
RN [9]
RP NOMENCLATURE.
RX MEDLINE=97435478; PubMed=9290209;
RX DOI=10.1002/(SICI)1097-0061(19970915)13:11<1053::AID-YEA164>3.3.CO;2-W;
RA Poch O., Winsor B.;
RT "Who's who among the Saccharomyces cerevisiae actin-related proteins?
RT A classification and nomenclature proposal for a large family.";
RL Yeast 13:1053-1058(1997).
RN [10]
RP FUNCTION.
RX PubMed=12353039; DOI=10.1038/nature01035;
RA Bird A.W., Yu D.Y., Pray-Grant M.G., Qiu Q., Harmon K.E., Megee P.C.,
RA Grant P.A., Smith M.M., Christman M.F.;
RT "Acetylation of histone H4 by Esa1 is required for DNA double-strand
RT break repair.";
RL Nature 419:411-415(2002).
RN [11]
RP IDENTIFICATION IN THE INO80 COMPLEX, AND MASS SPECTROMETRY.
RX MEDLINE=22770682; PubMed=12887900; DOI=10.1016/S1097-2765(03)00264-8;
RA Shen X., Ranallo R., Choi E., Wu C.;
RT "Involvement of actin-related proteins in ATP-dependent chromatin
RT remodeling.";
RL Mol. Cell 12:147-155(2003).
RN [12]
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 [13]
RP FUNCTION, IDENTIFICATION IN THE SWR1 COMPLEX, AND 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 [14]
RP FUNCTION.
RX PubMed=15610740; DOI=10.1016/j.molcel.2004.12.003;
RA Downs J.A., Allard S., Jobin-Robitaille O., Javaheri A., Auger A.,
RA Bouchard N., Kron S.J., Jackson S.P., Cote J.;
RT "Binding of chromatin-modifying activities to phosphorylated histone
RT H2A at DNA damage sites.";
RL Mol. Cell 16:979-990(2004).
RN [15]
RP FUNCTION, AND MUTAGENESIS OF SER-23; ASP-159 AND GLY-161.
RX PubMed=14622406; DOI=10.1046/j.1365-2958.2003.03759.x;
RA Goerzer I., Schueller C., Heidenreich E., Krupanska L., Kuchler K.,
RA Wintersberger U.;
RT "The nuclear actin-related protein Act3p/Arp4p of Saccharomyces
RT cerevisiae is involved in transcription regulation of stress genes.";
RL Mol. Microbiol. 50:1155-1171(2003).
RN [16]
RP FUNCTION, IDENTIFICATION IN THE SWR1 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 [17]
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 1 489 Actin-like protein ARP4.
/FTId=PRO_0000089103.
MUTAGEN 23 23 S->A: Lethal; when associated with D-161.
Formamide-, hydroxyurea and UV-
hypersensitivity, suppressor of TY
phenotype; when associated with A-159.
MUTAGEN 155 155 C->Y: No histone acetyltransferase
activity at 37 degrees celcius.
MUTAGEN 159 159 D->A: Formamide-, hydroxyurea and UV-
hypersensitivity, suppressor of TY
phenotype; when associated with S-23.
MUTAGEN 161 161 G->D: Formamide-, hydroxyurea and UV-
hypersensitivity, destabilization of
ARP4, suppressor of TY phenotype and
elevated levels of MSN2/MSN4-regulated
genes. Lethal; when associated with A-23.
MUTAGEN 187 187 G->R: Defect in promoter association and
change in chromatin structure.
MUTAGEN 455 455 G->S: No histone acetyltransferase
activity at 37 degrees celcius. Defect in
promoter association and change in
chromatin structure.
Comments:
-!- FUNCTION: Chromatin interaction component of the NuA4 histone
acetyltransferase complex which is involved in transcriptional
activation of selected genes principally by acetylation of
nucleosomal histone H4 and H2A. The NuA4 complex is also involved
in DNA repair. ARP4 recognizes the phosphorylated Ser-159 of
histones H2A and is required for NuA4 complex integrity. 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 INO80 complex which remodels chromatin by shifting
nucleosomes. Its ability to induce transcription of some
phosphate-responsive genes is modulated by inositol
polyphosphates. The INO80 complex is involved in DNA repair by
associating to Ser-129 phosphorylated H2A histones as a response
to DNA damage.
-!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex
composed of at least ACT1, ARP4, EAF3, EAF5, EAF6, EAF7, EPL1,
ESA1, SWC4, TRA1, VID21, YAF9 and YNG2. Compoment of the chromatin
remodeling INO80 complex, at least composed of ARP4, ARP5, ARP8,
IES1, IES3, NHP10, RVB1, RVB2 and TAF14. 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. Interacts with histones H4 (HHF1 and
HHF2), H3 (HHT1 and HHT2) and H2A (HTA1 and HTA2).
-!- INTERACTION:
Q08649:ESA1; NbExp=1; IntAct=EBI-2939, EBI-6648;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- MISCELLANEOUS: Present with 1070 molecules/cell.
-!- SIMILARITY: Belongs to the actin family. ARP4 subfamily.
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Sequence length: 489
MSNAALQVYG GDEVSAVVID PGSYTTNIGY SGSDFPQSIL PSVYGKYTAD EGNKKIFSEQ
SIGIPRKDYE LKPIIENGLV IDWDTAQEQW QWALQNELYL NSNSGIPALL TEPVWNSTEN
RKKSLEVLLE GMQFEACYLA PTSTCVSFAA GRPNCLVVDI GHDTCSVSPI VDGMTLSKST
RRNFIAGKFI NHLIKKALEP KEIIPLFAIK QRKPEFIKKT FDYEVDKSLY DYANNRGFFQ
ECKETLCHIC PTKTLEETKT ELSSTAKRSI ESPWNEEIVF DNETRYGFAE ELFLPKEDDI
PANWPRSNSG VVKTWRNDYV PLKRTKPSGV NKSDKKVTPT EEKEQEAVSK STSPAANSAD
TPNETGKRPL EEEKPPKENN ELIGLADLVY SSIMSSDVDL RATLAHNVVL TGGTSSIPGL
SDRLMTELNK ILPSLKFRIL TTGHTIERQY QSWLGGSILT SLGTFHQLWV GKKEYEEVGV
ERLLNDRFR