CXXC1_HUMAN
ID CXXC1_HUMAN Reviewed; 656 AA.
AC Q9P0U4; B2RC03; Q8N2W4; Q96BC8; Q9P2V7;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=CXXC-type zinc finger protein 1;
DE AltName: Full=CpG-binding protein;
DE AltName: Full=PHD finger and CXXC domain-containing protein 1;
GN Name=CXXC1; Synonyms=CFP1, CGBP, PCCX1, PHF18;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10688657; DOI=10.1128/mcb.20.6.2108-2121.2000;
RA Voo K.S., Carlone D.L., Jacobsen B.M., Flodin A., Skalnik D.G.;
RT "Cloning of a mammalian transcriptional activator that binds unmethylated
RT CpG motifs and shares a CXXC domain with DNA methyltransferase, human
RT trithorax, and methyl-CpG binding domain protein 1.";
RL Mol. Cell. Biol. 20:2108-2121(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DNA-BINDING.
RX PubMed=10799292; DOI=10.1006/bbrc.2000.2614;
RA Fujino T., Hasegawa M., Shibata S., Kishimoto T., Imai S., Takano T.;
RT "PCCX1, a novel DNA-binding protein with PHD finger and CXXC domain, is
RT regulated by proteolysis.";
RL Biochem. Biophys. Res. Commun. 271:305-310(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cervix, Colon, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP DNA-BINDING DOMAIN, AND MUTAGENESIS OF CYS-169 AND CYS-208.
RX PubMed=11572867; DOI=10.1074/jbc.m107179200;
RA Lee J.-H., Voo K.S., Skalnik D.G.;
RT "Identification and characterization of the DNA binding domain of CpG-
RT binding protein.";
RL J. Biol. Chem. 276:44669-44676(2001).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=12200428; DOI=10.1074/jbc.m205054200;
RA Lee J.-H., Skalnik D.G.;
RT "CpG-binding protein is a nuclear matrix- and euchromatin-associated
RT protein localized to nuclear speckles containing human trithorax.
RT Identification of nuclear matrix targeting signals.";
RL J. Biol. Chem. 277:42259-42267(2002).
RN [9]
RP IDENTIFICATION IN THE SET1 COMPLEX.
RX PubMed=16253997; DOI=10.1074/jbc.m508312200;
RA Lee J.-H., Skalnik D.G.;
RT "CpG-binding protein (CXXC finger protein 1) is a component of the
RT mammalian Set1 histone H3-Lys4 methyltransferase complex, the analogue of
RT the yeast Set1/COMPASS complex.";
RL J. Biol. Chem. 280:41725-41731(2005).
RN [10]
RP IDENTIFICATION IN THE SET1 COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=17355966; DOI=10.1074/jbc.m609809200;
RA Lee J.-H., Tate C.M., You J.-S., Skalnik D.G.;
RT "Identification and characterization of the human Set1B histone H3-Lys4
RT methyltransferase complex.";
RL J. Biol. Chem. 282:13419-13428(2007).
RN [11]
RP IDENTIFICATION IN SET1 COMPLEX, AND INTERACTION WITH SETD1A.
RX PubMed=17998332; DOI=10.1128/mcb.01356-07;
RA Lee J.H., Skalnik D.G.;
RT "Wdr82 is a C-terminal domain-binding protein that recruits the Setd1A
RT Histone H3-Lys4 methyltransferase complex to transcription start sites of
RT transcribed human genes.";
RL Mol. Cell. Biol. 28:609-618(2008).
RN [12]
RP IDENTIFICATION IN SET1 COMPLEX.
RX PubMed=18838538; DOI=10.1128/mcb.00976-08;
RA Wu M., Wang P.F., Lee J.S., Martin-Brown S., Florens L., Washburn M.,
RA Shilatifard A.;
RT "Molecular regulation of H3K4 trimethylation by Wdr82, a component of human
RT Set1/COMPASS.";
RL Mol. Cell. Biol. 28:7337-7344(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-227, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-6 AND SER-19, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP INTERACTION WITH ZNF335.
RX PubMed=23178126; DOI=10.1016/j.cell.2012.10.043;
RA Yang Y.J., Baltus A.E., Mathew R.S., Murphy E.A., Evrony G.D.,
RA Gonzalez D.M., Wang E.P., Marshall-Walker C.A., Barry B.J., Murn J.,
RA Tatarakis A., Mahajan M.A., Samuels H.H., Shi Y., Golden J.A., Mahajnah M.,
RA Shenhav R., Walsh C.A.;
RT "Microcephaly gene links trithorax and REST/NRSF to control neural stem
RT cell proliferation and differentiation.";
RL Cell 151:1097-1112(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-224, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-250, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-250, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 161-222 IN COMPLEX WITH DNA, AND
RP FUNCTION.
RX PubMed=21407193; DOI=10.1038/ncomms1237;
RA Xu C., Bian C., Lam R., Dong A., Min J.;
RT "The structural basis for selective binding of non-methylated CpG islands
RT by the CFP1 CXXC domain.";
RL Nat. Commun. 2:227-227(2011).
CC -!- FUNCTION: Transcriptional activator that exhibits a unique DNA binding
CC specificity for CpG unmethylated motifs with a preference for CpGG.
CC {ECO:0000269|PubMed:21407193}.
CC -!- SUBUNIT: Component of the SET1 complex, at least composed of the
CC catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2,
CC CXXC1/CFP1 HCFC1 and DPY30. Interacts with SETD1A. Interacts with
CC ZNF335. Interacts with PRDM9; this interaction does not link PRDM9-
CC activated recombination hotspot sites with DSB machinery and is not
CC required for the hotspot recognition pathway. Interacts with histone
CC H3K4me3 (By similarity). {ECO:0000250|UniProtKB:Q9CWW7,
CC ECO:0000269|PubMed:16253997, ECO:0000269|PubMed:17355966,
CC ECO:0000269|PubMed:17998332, ECO:0000269|PubMed:18838538,
CC ECO:0000269|PubMed:21407193, ECO:0000269|PubMed:23178126}.
CC -!- INTERACTION:
CC Q9P0U4; P50222: MEOX2; NbExp=3; IntAct=EBI-949911, EBI-748397;
CC Q9P0U4; P60484: PTEN; NbExp=2; IntAct=EBI-949911, EBI-696162;
CC Q9P0U4; Q15291: RBBP5; NbExp=6; IntAct=EBI-949911, EBI-592823;
CC Q9P0U4; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-949911, EBI-529518;
CC Q9P0U4; P04637: TP53; NbExp=7; IntAct=EBI-949911, EBI-366083;
CC Q9P0U4-2; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-12743307, EBI-529518;
CC Q9P0U4-2; Q8N4U5: TCP11L2; NbExp=3; IntAct=EBI-12743307, EBI-11897462;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:12200428,
CC ECO:0000269|PubMed:17355966}. Nucleus {ECO:0000250|UniProtKB:Q9CWW7}.
CC Note=Associated with euchromatin. During mitosis, excluded from
CC condensed chromosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P0U4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P0U4-2; Sequence=VSP_040132;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The acidic domain carries the potential to activate
CC transcription.
CC -!- PTM: May be regulated by proteolysis.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF149758; AAF37799.1; -; mRNA.
DR EMBL; AB031069; BAA96307.1; -; mRNA.
DR EMBL; AL136862; CAB66796.1; -; mRNA.
DR EMBL; AK314886; BAG37400.1; -; mRNA.
DR EMBL; AC090246; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014940; AAH14940.1; -; mRNA.
DR EMBL; BC015733; AAH15733.1; -; mRNA.
DR EMBL; BC029922; AAH29922.1; -; mRNA.
DR CCDS; CCDS11945.1; -. [Q9P0U4-1]
DR CCDS; CCDS45866.1; -. [Q9P0U4-2]
DR RefSeq; NP_001095124.1; NM_001101654.1. [Q9P0U4-2]
DR RefSeq; NP_055408.2; NM_014593.3. [Q9P0U4-1]
DR RefSeq; XP_011524242.1; XM_011525940.2. [Q9P0U4-2]
DR RefSeq; XP_016881207.1; XM_017025718.1. [Q9P0U4-1]
DR PDB; 3QMB; X-ray; 2.06 A; A=161-222.
DR PDB; 3QMC; X-ray; 2.10 A; A=161-222.
DR PDB; 3QMD; X-ray; 1.90 A; A=161-222.
DR PDB; 3QMG; X-ray; 2.30 A; A=161-222.
DR PDB; 3QMH; X-ray; 2.50 A; A=161-222.
DR PDB; 3QMI; X-ray; 2.10 A; A=161-222.
DR PDBsum; 3QMB; -.
DR PDBsum; 3QMC; -.
DR PDBsum; 3QMD; -.
DR PDBsum; 3QMG; -.
DR PDBsum; 3QMH; -.
DR PDBsum; 3QMI; -.
DR AlphaFoldDB; Q9P0U4; -.
DR SMR; Q9P0U4; -.
DR BioGRID; 119045; 125.
DR ComplexPortal; CPX-7110; Histone-lysine N-methyltransferase complex, SET1A variant.
DR ComplexPortal; CPX-7111; Histone-lysine N-methyltransferase complex, SET1B variant.
DR CORUM; Q9P0U4; -.
DR DIP; DIP-50001N; -.
DR IntAct; Q9P0U4; 56.
DR MINT; Q9P0U4; -.
DR STRING; 9606.ENSP00000390475; -.
DR iPTMnet; Q9P0U4; -.
DR MetOSite; Q9P0U4; -.
DR PhosphoSitePlus; Q9P0U4; -.
DR BioMuta; CXXC1; -.
DR DMDM; 20138037; -.
DR EPD; Q9P0U4; -.
DR jPOST; Q9P0U4; -.
DR MassIVE; Q9P0U4; -.
DR MaxQB; Q9P0U4; -.
DR PaxDb; Q9P0U4; -.
DR PeptideAtlas; Q9P0U4; -.
DR PRIDE; Q9P0U4; -.
DR ProteomicsDB; 83600; -. [Q9P0U4-1]
DR ProteomicsDB; 83601; -. [Q9P0U4-2]
DR Antibodypedia; 9406; 282 antibodies from 29 providers.
DR DNASU; 30827; -.
DR Ensembl; ENST00000285106.11; ENSP00000285106.6; ENSG00000154832.16. [Q9P0U4-1]
DR Ensembl; ENST00000412036.6; ENSP00000390475.1; ENSG00000154832.16. [Q9P0U4-2]
DR GeneID; 30827; -.
DR KEGG; hsa:30827; -.
DR MANE-Select; ENST00000285106.11; ENSP00000285106.6; NM_014593.4; NP_055408.2.
DR UCSC; uc002leq.5; human. [Q9P0U4-1]
DR CTD; 30827; -.
DR DisGeNET; 30827; -.
DR GeneCards; CXXC1; -.
DR HGNC; HGNC:24343; CXXC1.
DR HPA; ENSG00000154832; Low tissue specificity.
DR MIM; 609150; gene.
DR neXtProt; NX_Q9P0U4; -.
DR OpenTargets; ENSG00000154832; -.
DR PharmGKB; PA134908762; -.
DR VEuPathDB; HostDB:ENSG00000154832; -.
DR eggNOG; KOG1632; Eukaryota.
DR GeneTree; ENSGT00730000111044; -.
DR HOGENOM; CLU_025011_2_0_1; -.
DR InParanoid; Q9P0U4; -.
DR OMA; VLPQRIQ; -.
DR OrthoDB; 463371at2759; -.
DR PhylomeDB; Q9P0U4; -.
DR TreeFam; TF320326; -.
DR PathwayCommons; Q9P0U4; -.
DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
DR SignaLink; Q9P0U4; -.
DR BioGRID-ORCS; 30827; 349 hits in 1088 CRISPR screens.
DR ChiTaRS; CXXC1; human.
DR EvolutionaryTrace; Q9P0U4; -.
DR GeneWiki; CXXC1; -.
DR GenomeRNAi; 30827; -.
DR Pharos; Q9P0U4; Tbio.
DR PRO; PR:Q9P0U4; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q9P0U4; protein.
DR Bgee; ENSG00000154832; Expressed in right hemisphere of cerebellum and 196 other tissues.
DR ExpressionAtlas; Q9P0U4; baseline and differential.
DR Genevisible; Q9P0U4; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0035097; C:histone methyltransferase complex; IDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IDA:LIFEdb.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IDA:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:0045322; F:unmethylated CpG binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051568; P:histone H3-K4 methylation; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
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 Pfam; PF02008; zf-CXXC; 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 3D-structure; Acetylation; Activator; Alternative splicing; Coiled coil;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..656
FT /note="CXXC-type zinc finger protein 1"
FT /id="PRO_0000079743"
FT ZN_FING 28..76
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 160..209
FT /note="CXXC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 422..474
FT /evidence="ECO:0000255"
FT COMPBIAS 84..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..357
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 187
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 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 227
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 250
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 340
FT /note="K -> KVMER (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040132"
FT MUTAGEN 169
FT /note="C->A: Complete loss of DNA binding activity. No
FT effect on localization in nuclear speckles."
FT /evidence="ECO:0000269|PubMed:11572867"
FT MUTAGEN 208
FT /note="C->A: Complete loss of DNA binding activity. No
FT effect on localization in nuclear speckles."
FT /evidence="ECO:0000269|PubMed:11572867"
FT CONFLICT 117
FT /note="D -> N (in Ref. 1; AAF37799)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="C -> R (in Ref. 4; BAG37400)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="P -> S (in Ref. 4; BAG37400)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="H -> N (in Ref. 1; AAF37799)"
FT /evidence="ECO:0000305"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:3QMD"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:3QMD"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:3QMB"
FT HELIX 185..189
FT /evidence="ECO:0007829|PDB:3QMD"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:3QMD"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:3QMD"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:3QMD"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:3QMD"
SQ SEQUENCE 656 AA; 75712 MW; 6D2376E449905A18 CRC64;
MEGDGSDPEP PDAGEDSKSE NGENAPIYCI CRKPDINCFM IGCDNCNEWF HGDCIRITEK
MAKAIREWYC RECREKDPKL EIRYRHKKSR ERDGNERDSS EPRDEGGGRK RPVPDPDLQR
RAGSGTGVGA MLARGSASPH KSSPQPLVAT PSQHHQQQQQ QIKRSARMCG ECEACRRTED
CGHCDFCRDM KKFGGPNKIR QKCRLRQCQL RARESYKYFP SSLSPVTPSE SLPRPRRPLP
TQQQPQPSQK LGRIREDEGA VASSTVKEPP EATATPEPLS DEDLPLDPDL YQDFCAGAFD
DHGLPWMSDT EESPFLDPAL RKRAVKVKHV KRREKKSEKK KEERYKRHRQ KQKHKDKWKH
PERADAKDPA SLPQCLGPGC VRPAQPSSKY CSDDCGMKLA ANRIYEILPQ RIQQWQQSPC
IAEEHGKKLL ERIRREQQSA RTRLQEMERR FHELEAIILR AKQQAVREDE ESNEGDSDDT
DLQIFCVSCG HPINPRVALR HMERCYAKYE SQTSFGSMYP TRIEGATRLF CDVYNPQSKT
YCKRLQVLCP EHSRDPKVPA DEVCGCPLVR DVFELTGDFC RLPKRQCNRH YCWEKLRRAE
VDLERVRVWY KLDELFEQER NVRTAMTNRA GLLALMLHQT IQHDPLTTDL RSSADR
