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Description:
Chromatin modification-related protein eaf3 (Altered polarity protein13) (ESA1-associated factor 3).
Molecular weight: 39138
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:
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
07-FEB-2006, entry version 39.
Phylogenetic order:
Eukaryota Fungi Ascomycota Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces.
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 EAF3_SCHPO:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AB015294 | BAA28826.1 | - |
| EMBL | Z98977 | CAB11666.1 | - |
| PIR | T43372 | T43372. | |
| GeneDB_Spombe | SPAC23H4.12 | -.1 | |
| BioCyc | SPOM-XXX-01:SPOM-XXX-01-001081-MONOMER | -.1 | |
| GO | GO:0000118 | C:histone deacetylase complex | IDA. |
| GO | GO:0005634 | C:nucleus | IDA. |
| GO | GO:0005515 | F:protein binding | IPI. |
| GO | GO:0030467 | P:establishment and/or maintenance of cell po... | IMP. |
| GO | GO:0016575 | P:histone deacetylation | IMP. |
| InterPro | IPR000953 | Chromo. | |
| InterPro | IPR008676 | MRG. | |
| PANTHER | PTHR10880 | MRG.1 | 1. |
| Pfam | PF05712 | MRG | 1. |
| SMART | SM00298 | CHROMO | 1. |
Keywords:
Chromatin regulator; Complete proteome; Direct protein sequencing; DNA damage; DNA repair; Nuclear protein; Transcription; Transcription regulation.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=972;
RA Radcliffe P.A., Toda T.;
RT "Chromo domain protein required for cell polarity.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972;
RX MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP PROTEIN SEQUENCE OF 105-123; 129-138; 147-169 AND 311-332, FUNCTION,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX MEDLINE=22658054; PubMed=12773392; DOI=10.1093/emboj/cdg248;
RA Nakayama J., Xiao G., Noma K., Malikzay A., Bjerling P., Ekwall K.,
RA Kobayashi R., Grewal S.I.S.;
RT "Alp13, an MRG family protein, is a component of fission yeast Clr6
RT histone deacetylase required for genomic integrity.";
RL EMBO J. 22:2776-2787(2003).
Feature:
CHAIN 1 337 Chromatin modification-related protein
eaf3.
/FTId=PRO_0000088780.
Comments:
-!- FUNCTION: 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 (By similarity). Also
involved in deacetylation of histones, chromatin assembly and
chromosome segregation. May act as a transcriptional oscillator,
directing histone deacetylases to specific chromosomal domains.
-!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex
(By similarity). Heterotetramer of alp13, clr6, prw1 and pst2.
-!- SUBCELLULAR LOCATION: Nucleus.
-!- SIMILARITY: Belongs to the MRG family.
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Sequence length: 337
MAVSYKVNER VLCFHGPLLY EAKIVDTEMK GDVTTYLIHY KGWKNSWDEW VEQDRILQWT
EENLKTQKEL KNAAISTRQK PTSKKSASST SKHDSTGVKT SGKRSRESST VTVDGDSHEL
PSRIKTQKSE SPIPQQVKRD GTTDAKNEET TKPENNEKDD FEEEPPLPKH KISVPDVLKL
WLVDDWENIT KNQQLIAIPR NPTVRAAIAA FRESKISHLN NEIDVDVFEQ AMAGLVIYFN
KCLGNMLLYR FERQQYLEIR QQYPDTEMCD LYGVEHLIRL FVSLPELIDR TNMDSQSIEC
LLNYIEEFLK YLVLHKDEYF IKEYQNAPPN YRSLVGV