CXXC1_DROME
ID CXXC1_DROME Reviewed; 663 AA.
AC Q9W352;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=CXXC-type zinc finger protein 1;
DE AltName: Full=PHD finger and CXXC domain-containing protein 1;
GN Name=Cfp1; ORFNames=CG17446;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX 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., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., 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., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
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., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [4]
RP FUNCTION, IDENTIFICATION IN THE SET1 COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=21694722; DOI=10.1038/emboj.2011.194;
RA Ardehali M.B., Mei A., Zobeck K.L., Caron M., Lis J.T., Kusch T.;
RT "Drosophila Set1 is the major histone H3 lysine 4 trimethyltransferase with
RT role in transcription.";
RL EMBO J. 30:2817-2828(2011).
RN [5]
RP IDENTIFICATION IN THE SET1 COMPLEX.
RX PubMed=21875999; DOI=10.1128/mcb.06092-11;
RA Mohan M., Herz H.M., Smith E.R., Zhang Y., Jackson J., Washburn M.P.,
RA Florens L., Eissenberg J.C., Shilatifard A.;
RT "The COMPASS family of H3K4 methylases in Drosophila.";
RL Mol. Cell. Biol. 31:4310-4318(2011).
CC -!- FUNCTION: Component of the SET1 complex that specifically di- and
CC trimethylates 'Lys-4' of histone H3. Essential for Set1 association
CC with chromatin and trimethylation of histone H3 at 'Lys-4' at
CC transcription puffs. Additionally, is critical for general chromosomal
CC association of Set1. {ECO:0000269|PubMed:21694722}.
CC -!- SUBUNIT: Component of the SET1 complex, composed at least of the
CC catalytic subunit Set1, wds/WDR5, Wdr82, Rbbp5, ash2, Cfp1/CXXC1, hcf
CC and Dpy-30L1. {ECO:0000269|PubMed:21694722,
CC ECO:0000269|PubMed:21875999}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21694722}.
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DR EMBL; AE014298; AAF46483.1; -; Genomic_DNA.
DR RefSeq; NP_572556.1; NM_132328.3.
DR AlphaFoldDB; Q9W352; -.
DR BioGRID; 58329; 17.
DR IntAct; Q9W352; 9.
DR MINT; Q9W352; -.
DR STRING; 7227.FBpp0071262; -.
DR iPTMnet; Q9W352; -.
DR PaxDb; Q9W352; -.
DR PRIDE; Q9W352; -.
DR EnsemblMetazoa; FBtr0071327; FBpp0071262; FBgn0030121.
DR GeneID; 31880; -.
DR KEGG; dme:Dmel_CG17446; -.
DR UCSC; CG17446-RA; d. melanogaster.
DR CTD; 104320; -.
DR FlyBase; FBgn0030121; Cfp1.
DR VEuPathDB; VectorBase:FBgn0030121; -.
DR eggNOG; KOG1632; Eukaryota.
DR GeneTree; ENSGT00940000169358; -.
DR InParanoid; Q9W352; -.
DR OrthoDB; 463371at2759; -.
DR PhylomeDB; Q9W352; -.
DR SignaLink; Q9W352; -.
DR BioGRID-ORCS; 31880; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 31880; -.
DR PRO; PR:Q9W352; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030121; Expressed in egg cell and 20 other tissues.
DR ExpressionAtlas; Q9W352; baseline and differential.
DR Genevisible; Q9W352; DM.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051568; P:histone H3-K4 methylation; IDA:FlyBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR022056; CpG-bd_C.
DR InterPro; IPR037869; Spp1/CFP1.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR002857; Znf_CXXC.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46174; PTHR46174; 1.
DR Pfam; PF12269; CpG_bind_C; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51058; ZF_CXXC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..663
FT /note="CXXC-type zinc finger protein 1"
FT /id="PRO_0000372848"
FT ZN_FING 60..110
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 175..219
FT /note="CXXC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT REGION 134..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
SQ SEQUENCE 663 AA; 76696 MW; 8573CD209AE28157 CRC64;
MTDKRKYKKT VSFTRCTAII FLTTKEVSKQ KEEIRREIAR EFDLPERKSK IATILKQEDQ
AYCICRSSDC SRFMIGCDGC EEWYHGDCIG ITEKEAKHIK QYYCRRCKKE NPELQTIFRL
VATERAAASN AASTSLNAPG VGPSGAAPAA APVASATTSQ QAPPPTTAAA KRKNSSAREP
KMGKRCGTCE GCRRPNCNQC DACRVRVGHK PRCIFRTCVV QAATVLKESQ ATQAGPSRKR
EKAAPKSRNV QVGPRAASPE IFLNPELQGI RQCYGPNCCS HARPQSKYCS DKCGFNLATK
RIFQVLPQRL QEWNLTPSRA AEETRKHLDN IRHKQSLVRF ALAELEKRSE ELNMVVERAK
RSSIDTLGSQ DTADMEDEQS MYCITCGHEI HSRTAIKHME KCFNKYESQA SFGSIFKTRM
EGNNMFCDFY NPASKTYCKR LRVLCPEHSK DPKVNDTDVC GSPLVNNVFN PTGEFCRAPK
KNCFKHYAWE KIRRAEIDLE RVRQWLKMDD LMEQERVMRQ QLTSRANLLG LMLHSTYNHE
VMDELVRKQQ EHLVEFEKQR RRLAHQQQIQ TQQKQYQEKQ KLMLQQQQQQ QQQQQQQQQQ
QQQQQLQQPQ QQQQQQQQQQ QEQQQLQLKP HHLQQLQLQL LQQQQKKAQI PQKTQIIYLQ
KKT
