ID CXXC1_MOUSE Reviewed; 660 AA.
AC Q9CWW7;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 163.
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=Cgbp, Pccx1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [3]
RP INTERACTION WITH PRDM9.
RX PubMed=27932493; DOI=10.1091/mbc.e16-09-0686;
RA Parvanov E.D., Tian H., Billings T., Saxl R.L., Spruce C., Aithal R.,
RA Krejci L., Paigen K., Petkov P.M.;
RT "PRDM9 interactions with other proteins provide a link between
RT recombination hotspots and the chromosomal axis in meiosis.";
RL Mol. Biol. Cell 28:488-499(2017).
RN [4]
RP INTERACTION WITH PRDM9 AND METHYLATED HISTONE H3K4ME3, SUBCELLULAR
RP LOCATION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=30365547; DOI=10.1371/journal.pgen.1007657;
RA Tian H., Billings T., Petkov P.M.;
RT "CXXC1 is not essential for normal DNA double-strand break formation and
RT meiotic recombination in mouse.";
RL PLoS Genet. 14:E1007657-E1007657(2018).
CC -!- FUNCTION: Transcriptional activator that exhibits a unique DNA binding
CC specificity for CpG unmethylated motifs with a preference for CpGG.
CC {ECO:0000250}.
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 (By similarity).
CC Interacts with ZNF335 (By similarity). Interacts with PRDM9; this
CC interaction does not link PRDM9-activated recombination hotspot sites
CC with DSB machinery and is not required for the hotspot recognition
CC pathway (PubMed:27932493, PubMed:30365547). Interacts with histone
CC H3K4me3 (PubMed:30365547). {ECO:0000250, ECO:0000269|PubMed:27932493,
CC ECO:0000269|PubMed:30365547}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q9P0U4}.
CC Nucleus {ECO:0000269|PubMed:30365547}. Note=Associated with
CC euchromatin. During mitosis, excluded from condensed chromosomes (By
CC similarity). {ECO:0000250|UniProtKB:Q9P0U4}.
CC -!- TISSUE SPECIFICITY: Expressed in seminiferous tubules and in both germ
CC cells and Sertoli cells. Highly expressed in spermatogonia, weakly
CC expressed in leptonema and zygonema, and then again high expression in
CC pachynema and diplonema, decreasing to undetectable levels in
CC spermatids. {ECO:0000269|PubMed:30365547}.
CC -!- DISRUPTION PHENOTYPE: Cxxc1 knockout male mice are fertile. In contrast
CC Cxxc1 germ cell-specific knockout female mice are sterile.
CC {ECO:0000269|PubMed:30365547}.
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DR EMBL; AK010337; BAB26862.1; -; mRNA.
DR EMBL; AK083655; BAC38986.1; -; mRNA.
DR EMBL; BC030938; AAH30938.1; -; mRNA.
DR CCDS; CCDS50320.1; -.
DR RefSeq; NP_083144.1; NM_028868.3.
DR AlphaFoldDB; Q9CWW7; -.
DR SMR; Q9CWW7; -.
DR BioGRID; 216665; 32.
DR IntAct; Q9CWW7; 24.
DR MINT; Q9CWW7; -.
DR STRING; 10090.ENSMUSP00000025444; -.
DR GlyGen; Q9CWW7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9CWW7; -.
DR PhosphoSitePlus; Q9CWW7; -.
DR SwissPalm; Q9CWW7; -.
DR EPD; Q9CWW7; -.
DR jPOST; Q9CWW7; -.
DR MaxQB; Q9CWW7; -.
DR PaxDb; 10090-ENSMUSP00000025444; -.
DR ProteomicsDB; 279228; -.
DR Pumba; Q9CWW7; -.
DR Antibodypedia; 9406; 324 antibodies from 29 providers.
DR Ensembl; ENSMUST00000025444.8; ENSMUSP00000025444.7; ENSMUSG00000024560.8.
DR GeneID; 74322; -.
DR KEGG; mmu:74322; -.
DR UCSC; uc008fpg.1; mouse.
DR AGR; MGI:1921572; -.
DR CTD; 30827; -.
DR MGI; MGI:1921572; Cxxc1.
DR VEuPathDB; HostDB:ENSMUSG00000024560; -.
DR eggNOG; KOG1632; Eukaryota.
DR GeneTree; ENSGT00730000111044; -.
DR HOGENOM; CLU_025011_2_0_1; -.
DR InParanoid; Q9CWW7; -.
DR OMA; VRQWLKI; -.
DR OrthoDB; 124870at2759; -.
DR PhylomeDB; Q9CWW7; -.
DR TreeFam; TF320326; -.
DR Reactome; R-MMU-9772755; Formation of WDR5-containing histone-modifying complexes.
DR BioGRID-ORCS; 74322; 13 hits in 85 CRISPR screens.
DR ChiTaRS; Cxxc1; mouse.
DR PRO; PR:Q9CWW7; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9CWW7; Protein.
DR Bgee; ENSMUSG00000024560; Expressed in ileal epithelium and 271 other cell types or tissues.
DR ExpressionAtlas; Q9CWW7; baseline and differential.
DR Genevisible; Q9CWW7; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0035097; C:histone methyltransferase complex; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; IDA:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048188; C:Set1C/COMPASS complex; ISS:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0045322; F:unmethylated CpG binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:MGI.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:MGI.
DR CDD; cd15553; PHD_Cfp1; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; CXXC-TYPE ZINC FINGER PROTEIN 1; 1.
DR PANTHER; PTHR46174:SF1; CXXC-TYPE ZINC FINGER PROTEIN 1; 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; FYVE/PHD zinc finger; 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 Acetylation; Activator; Coiled coil; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..660
FT /note="CXXC-type zinc finger protein 1"
FT /id="PRO_0000079744"
FT ZN_FING 28..76
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 164..213
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 91..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 426..479
FT /evidence="ECO:0000255"
FT COMPBIAS 91..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..361
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 212
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:0000250|UniProtKB:Q9P0U4"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0U4"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0U4"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0U4"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0U4"
FT MOD_RES 231
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0U4"
FT CROSSLNK 254
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9P0U4"
SQ SEQUENCE 660 AA; 76167 MW; 9D92CB6DA82069EA CRC64;
MEGDGSDLEP PDAGDDSKSE NGENAPIYCI CRKPDINCFM IGCDNCNEWF HGDCIRITEK
MAKAIREWYC RECREKDPKL EIRYRHKKCR ERDGSERAGS EPRDEGGGRK RPASDPELQR
RAGSGTGVGA MLARGSASPH KSSPQPLVAT PSQHHHQQQQ QQQQQIKRSA RMCGECEACR
RTEDCGHCDF CRDMKKFGGP NKIRQKCRLR QCQLRARESY KYFPSSLSPV TPSEALPRPR
RPPPTQQQPQ QSQKLGRIRE DEGTVLSSVV KEPPEATATP EPLSDEDLAL DPDLYQDFCA
GAFDDHGLPW MSDAEESPFL DPALRKRAVK VKHVKRREKK SEKKKEERYK RHRQKQKHKD
KWKHPERADA KDPASLPQCL GPGCVRAAQP GSKYCSDDCG MKLAANRIYE ILPQRIQQWQ
QSPCIAEEHG KKLLERIRRE QQSARTRLQE MERRFHELEA IILRAKQQAV REDEENNEND
SDDTDLQIFC VSCGHPINPR VALRHMERCY AKYESQTSFG SMYPTRIEGA TRLFCDVYNP
QSKTYCKRLQ VLCPEHSRDP KVPADEVCGC PLVRDVFELT GDFCRLPKRQ CNRHYCWEKL
RRAEVDLERV RVWYKLDELF EQERNVRTAM TNRAGLLALM LHQTIQHDPL TTDLRSSADR
//
