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Description:
Probable histone-binding protein Caf1 (Chromatin assembly factor 1 p55subunit) (CAF-1 p55 subunit) (dCAF-1) (Nucleosome remodeling factor 55kDa subunit) (NURF-55).
Molecular weight: 48635
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:
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
07-MAR-2006, entry version 55.
Phylogenetic order:
Eukaryota Metazoa Arthropoda Hexapoda Insecta Pterygota Neoptera Endopterygota Diptera Brachycera Muscomorpha Ephydroidea Drosophilidae Drosophila.
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 CAF1_DROME:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | U62388 | AAB37257.1 | - |
| EMBL | AE003708 | AAF55146.1 | - |
| EMBL | AY061408 | AAL28956.1 | - |
| IntAct | Q24572 | -.1 | |
| Ensembl | CG4236 | Drosophila melanogaster.1 | |
| FlyBase | FBgn0015610 | Caf1. | |
| BioCyc | DMEL-XXX-02:DMEL-XXX-02-011699-MONOMER | -.1 | |
| GO | GO:0035098 | C:ESC/E(Z) complex | IDA. |
| GO | GO:0031523 | C:Myb complex | IDA. |
| GO | GO:0005634 | C:nucleus | IDA. |
| GO | GO:0016589 | C:NURF complex | IPI. |
| GO | GO:0005700 | C:polytene chromosome | IDA. |
| GO | GO:0005667 | C:transcription factor complex | IPI. |
| GO | GO:0035035 | F:histone acetyltransferase binding | IPI. |
| GO | GO:0042393 | F:histone binding | TAS. |
| GO | GO:0042826 | F:histone deacetylase binding | IPI. |
| GO | GO:0046974 | F:histone lysine N-methyltransferase activity... | IC. |
| GO | GO:0046976 | F:histone lysine N-methyltransferase activity... | IC. |
| GO | GO:0007307 | P:chorion gene amplification | IC. |
| GO | GO:0006342 | P:chromatin silencing | IPI. |
| GO | GO:0006281 | P:DNA repair | TAS. |
| GO | GO:0016573 | P:histone acetylation | IDA. |
| GO | GO:0016571 | P:histone methylation | IDA. |
| GO | GO:0000122 | P:negative regulation of transcription from R... | IMP. |
| GO | GO:0006334 | P:nucleosome assembly | IDA. |
| GO | GO:0042766 | P:nucleosome mobilization | IDA. |
| GO | GO:0016584 | P:nucleosome spacing | IDA. |
| GO | GO:0006350 | P:transcription | IDA. |
| InterPro | IPR001680 | WD40. | |
| Pfam | PF00400 | WD40 | 5. |
| PRINTS | PR00320 | GPROTEINBRPT. | |
| ProDom | PD000018 | WD40 | 4. |
| SMART | SM00320 | WD40 | 5. |
| PROSITE | PS00678 | WD_REPEATS_1 | 3. |
| PROSITE | PS50082 | WD_REPEATS_2 | 5. |
| PROSITE | PS50294 | WD_REPEATS_REGION | 1. |
Keywords:
Chromatin regulator; Complete proteome; Direct protein sequencing; Nuclear protein; Repeat; Repressor; Transcription; Transcription regulation; WD repeat.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 256-268; 301-313;
RP 322-334 AND 354-376, FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=Canton-S;
RX MEDLINE=97042445; PubMed=8887645;
RA Tyler J.K., Bulger M., Kamakaka R.T., Kobayashi R., Kadonaga J.T.;
RT "The p55 subunit of Drosophila chromatin assembly factor 1 is
RT homologous to a histone deacetylase-associated protein.";
RL Mol. Cell. Biol. 16:6149-6159(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z.,
RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O.,
RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RX MEDLINE=22426069; PubMed=12537572;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a
RT systematic review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RX MEDLINE=22426066; PubMed=12537569;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA Rubin G.M., Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP PROTEIN SEQUENCE OF 64-80; 256-269; 301-310; 314-339 AND 354-368,
RP FUNCTION, IDENTIFICATION IN THE NURF COMPLEX, ASSOCIATION WITH
RP CHROMATIN, AND SUBCELLULAR LOCATION.
RA Martinez-Balbas M.A., Tsukiyama T., Gdula D., Wu C.;
RT "Drosophila NURF-55, a WD repeat protein involved in histone
RT metabolism.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:132-137(1998).
RN [6]
RP CHARACTERIZATION OF THE CAF-1 COMPLEX.
RA Bulger M., Ito T., Kamakaka R.T., Kadonaga J.T.;
RT "Assembly of regularly spaced nucleosome arrays by Drosophila
RT chromatin assembly factor 1 and a 56-kDa histone-binding protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:11726-11730(1995).
RN [7]
RP CHARACTERIZATION OF THE CAF-1 COMPLEX.
RA Kamakaka R.T., Bulger M., Kaufman P.D., Stillman B., Kadonaga J.T.;
RT "Postreplicative chromatin assembly by Drosophila and human chromatin
RT assembly factor 1.";
RL Mol. Cell. Biol. 16:810-817(1996).
RN [8]
RP FUNCTION, AND INTERACTIONS WITH ISWI AND NURF-38.
RX MEDLINE=99003073; PubMed=9784495;
RA Gdula D.A., Sandaltzopoulos R., Tsukiyama T., Ossipow V., Wu C.;
RT "Inorganic pyrophosphatase is a component of the Drosophila nucleosome
RT remodeling factor complex.";
RL Genes Dev. 12:3206-3216(1998).
RN [9]
RP IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH ESC; E(Z) AND RPD3.
RX MEDLINE=21064443; PubMed=11124122;
RA Tie F., Furuyama T., Prasad-Sinha J., Jane E., Harte P.J.;
RT "The Drosophila polycomb group proteins ESC and E(Z) are present in a
RT complex containing the histone-binding protein p55 and the histone
RT deacetylase RPD3.";
RL Development 128:275-286(2001).
RN [10]
RP INTERACTIONS WITH CAF1-105 AND CAF1-180.
RX PubMed=11533245; DOI=10.1128/MCB.21.19.6574-6584.2001;
RA Tyler J.K., Collins K.A., Prasad-Sinha J., Amiott E., Bulger M.,
RA Harte P.J., Kobayashi R., Kadonaga J.T.;
RT "Interaction between the Drosophila CAF-1 and ASF1 chromatin assembly
RT factors.";
RL Mol. Cell. Biol. 21:6574-6584(2001).
RN [11]
RP IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH ESC; E(Z); RPD3 AND
RP SU(Z)12.
RX MEDLINE=22296673; PubMed=12408863; DOI=10.1016/S0092-8674(02)00975-3;
RA Czermin B., Melfi R., McCabe D., Seitz V., Imhof A., Pirrotta V.;
RT "Drosophila Enhancer of zeste/ESC complexes have a histone H3
RT methyltransferase activity that marks chromosomal Polycomb sites.";
RL Cell 111:185-196(2002).
RN [12]
RP IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH ESC; E(Z) AND SU(Z)12.
RX MEDLINE=22296674; PubMed=12408864; DOI=10.1016/S0092-8674(02)00976-5;
RA Mueller J., Hart C.M., Francis N.J., Vargas M.L., Sengupta A.,
RA Wild B., Miller E.L., O'Connor M.B., Kingston R.E., Simon J.A.;
RT "Histone methyltransferase activity of a Drosophila Polycomb group
RT repressor complex.";
RL Cell 111:197-208(2002).
RN [13]
RP IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH ESC; E(Z) AND RPD3.
RX PubMed=12533794; DOI=10.1002/gene.10173;
RA Furuyama T., Tie F., Harte P.J.;
RT "Polycomb group proteins ESC and E(Z) are present in multiple distinct
RT complexes that undergo dynamic changes during development.";
RL Genesis 35:114-124(2003).
RN [14]
RP IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH ESC; E(Z); PCL; RPD3 AND
RP SU(Z)12.
RX PubMed=12697833; DOI=10.1128/MCB.23.9.3352-3362.2003;
RA Tie F., Prasad-Sinha J., Birve A., Rasmuson-Lestander A., Harte P.J.;
RT "A 1-megadalton ESC/E(Z) complex from Drosophila that contains
RT polycomblike and RPD3.";
RL Mol. Cell. Biol. 23:3352-3362(2003).
RN [15]
RP IDENTIFICATION IN THE NURD COMPLEX, AND SELF-ASSOCIATION.
RX PubMed=15516265; DOI=10.1186/1471-2199-5-20;
RA Marhold J., Brehm A., Kramer K.;
RT "The Drosophila methyl-DNA binding protein MBD2/3 interacts with the
RT NuRD complex via p55 and MI-2.";
RL BMC Mol. Biol. 5:20-20(2004).
RN [16]
RP FUNCTION, AND INTERACTIONS WITH RBF AND RBF2.
RX PubMed=15456884; DOI=10.1128/MCB.24.20.9124-9136.2004;
RA Taylor-Harding B., Binne U.K., Korenjak M., Brehm A., Dyson N.J.;
RT "p55, the Drosophila ortholog of RbAp46/RbAp48, is required for the
RT repression of dE2F2/RBF-regulated genes.";
RL Mol. Cell. Biol. 24:9124-9136(2004).
Feature:
CHAIN 1 430 Probable histone-binding protein Caf1.
/FTId=PRO_0000050895.
REPEAT 126 159 WD 1.
REPEAT 179 210 WD 2.
REPEAT 229 260 WD 3.
REPEAT 275 306 WD 4.
REPEAT 319 350 WD 5.
REPEAT 376 407 WD 6.
Comments:
-!- FUNCTION: Core histone-binding subunit that may target chromatin
assembly factors, chromatin remodeling factors and histone
deacetylases to their histone substrates in a manner that is
regulated by nucleosomal DNA. Component of several complexes which
regulate chromatin metabolism. These include the chromatin
assembly factor 1 (CAF-1) complex, which is required for chromatin
assembly following DNA replication and DNA repair; the nucleosome
remodeling and deacetylase complex (the NuRD complex), which
promotes transcriptional repression by histone deacetylation and
nucleosome remodeling; the nucleosome remodeling factor complex
(the NURF complex), which facilitates the perturbation of
chromatin structure in an ATP-dependent manner; and the polycomb
group (PcG) repressor complex ESC-E(Z), which promotes repression
of homeotic genes during development. Also required for
transcriptional repression of E2F target genes by E2f2 and Rbf or
Rbf2.
-!- SUBUNIT: Probably binds directly to helix 1 of the histone fold of
histone H4, a region that is not accessible when H4 is in
chromatin. Self associates. Associates with chromatin. Component
of the CAF-1 complex, composed of Caf1, Caf1-105 and Caf1-180.
Within the CAF-1 complex, Caf1-180 interacts directly with both
Caf1 and Caf1-105. Component of the NuRD complex, composed of at
least Caf1, Mi-2, MTA1-like and Rpd3. Within the NuRD complex,
Caf1 may interact directly with Mi-2, MTA1-like and Rpd3. The NuRD
complex may also associate with the methyl-DNA binding protein
MBD-like via Caf1 and Mi-2. Component of the NURF complex,
composed of Caf1, E(bx), Nurf-38 and Iswi. Component of the
Esc/E(z) complex, composed of Caf1, esc, E(z), Su(z)1, and
possibly Pho1. The Esc/E(z) complex may also associate with Pcl
and Rpd3 during early embryogenesis. Interacts with Rbf and Rbf2.
-!- INTERACTION:
Q9VPV7:CG4415; NbExp=1; IntAct=EBI-75924, EBI-134881;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- DEVELOPMENTAL STAGE: Highest level during early embryogenesis and
then decreases in larvae, pupae and adults.
-!- SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.
-!- SIMILARITY: Contains 6 WD repeats.
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Sequence length: 430
MVDRSDNAAE SFDDAVEERV INEEYKIWKK NTPFLYDLVM THALEWPSLT AQWLPDVTKQ
DGKDYSVHRL ILGTHTSDEQ NHLLIASVQL PSEDAQFDGS HYDNEKGEFG GFGSVCGKIE
IEIKINHEGE VNRARYMPQN ACVIATKTPS SDVLVFDYTK HPSKPEPSGE CQPDLRLRGH
QKEGYGLSWN PNLNGYLLSA SDDHTICLWD INATPKEHRV IDAKNIFTGH TAVVEDVAWH
LLHESLFGSV ADDQKLMIWD TRNNNTSKPS HTVDAHTAEV NCLSFNPYSE FILATGSADK
TVALWDLRNL KLKLHSFESH KDEIFQVQWS PHNETILASS GTDRRLHVWD LSKIGEEQST
EDAEDGPPEL LFIHGGHTAK ISDFSWNPNE PWIICSVSED NIMQVWQMAE NVYNDEEPEI
PASELETNTA