CNBP_MOUSE
ID CNBP_MOUSE Reviewed; 178 AA.
AC P53996; Q80Y06; Q8BP23;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=CCHC-type zinc finger nucleic acid binding protein {ECO:0000305};
DE AltName: Full=Cellular nucleic acid-binding protein {ECO:0000312|MGI:MGI:88431};
DE Short=CNBP {ECO:0000305};
DE AltName: Full=Zinc finger protein 9;
GN Name=Cnbp {ECO:0000312|MGI:MGI:88431}; Synonyms=Cnbp1, Znf9;
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 [MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J X CBA/J; TISSUE=Liver;
RX PubMed=7896269; DOI=10.1006/geno.1994.1576;
RA Warden C.H., Krisans S.K., Purcell-Huynh D., Leete L.M., Daluiski A.,
RA Diep A., Taylor B.A., Lusis A.J.;
RT "Mouse cellular nucleic acid binding proteins: a highly conserved family
RT identified by genetic mapping and sequencing.";
RL Genomics 24:14-19(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1), AND SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6J;
RA Kingsley P.D., Palis J.;
RT "Primary structure and developmental regulation of murine CNBP, a zinc
RT finger-containing protein whose general structure is present in
RT evolutionarily diverse eukaryotes.";
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=12706888; DOI=10.1016/s0378-1119(03)00406-2;
RA Shimizu K., Chen W., Ashique A.M., Moroi R., Li Y.P.;
RT "Molecular cloning, developmental expression, promoter analysis and
RT functional characterization of the mouse CNBP gene.";
RL Gene 307:51-62(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND LYS-8, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-32; ARG-34 AND ARG-72 (ISOFORM
RP 2), METHYLATION [LARGE SCALE ANALYSIS] AT ARG-79 (ISOFORM 3), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Single-stranded DNA-binding protein that preferentially binds
CC to the sterol regulatory element (SRE) sequence 5'-GTGCGGTG-3', and
CC thereby mediates transcriptional repression (By similarity). Has a role
CC as transactivator of the Myc promoter (PubMed:12706888). Binds single-
CC stranded RNA in a sequence-specific manner (By similarity). Binds G-
CC rich elements in target mRNA coding sequences (By similarity). Prevents
CC G-quadruplex structure formation in vitro, suggesting a role in
CC supporting translation by resolving stable structures on mRNAs (By
CC similarity). {ECO:0000250|UniProtKB:P62633,
CC ECO:0000250|UniProtKB:P62634, ECO:0000269|PubMed:12706888}.
CC -!- SUBUNIT: Associates with the 40S ribosomal subunit, the 80S ribosome
CC and with polysomes. {ECO:0000250|UniProtKB:P62633}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12706888}. Cytoplasm
CC {ECO:0000269|Ref.2}. Endoplasmic reticulum {ECO:0000269|Ref.2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P53996-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P53996-2; Sequence=VSP_010983, VSP_010984;
CC Name=3;
CC IsoId=P53996-3; Sequence=VSP_010984;
CC -!- DEVELOPMENTAL STAGE: Expressed from pre-gastrulation to organogenesis
CC stages (at protein level) (PubMed:12706888). At this stage 7.5 dpc,
CC expression becomes asymmetrical and localizes to all three germ layer
CC regions of the anterior conceptus, suggesting a possible role in
CC anterior-posterior axis patterning (at protein level)
CC (PubMed:12706888). Later expressed in the forebrain (9 dpc and 10 dpc)
CC and in the midbrain (11.5 dpc) (at protein level) (PubMed:12706888).
CC From 9 dpc to 11.5 dpc, expressed in the early craniofacial structures,
CC limb buds and somites (at protein level) (PubMed:12706888). Highest
CC expression is in the face and includes the cranial and caudal regions
CC of the mandibular prominences, the budding maxillary prominences and
CC the roof of the stomodeum (at protein level) (PubMed:12706888). Before
CC gastrulation, 5.5 dpc, expression is initially symmetric and uniform in
CC the epiblast and in the extra-embryonic visceral endoderm
CC (PubMed:7896269). {ECO:0000269|PubMed:12706888,
CC ECO:0000269|PubMed:7896269}.
CC -!- PTM: Arginine methylation by PRMT1 in the Arg/Gly-rich region impedes
CC RNA binding. {ECO:0000250|UniProtKB:P62633}.
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DR EMBL; L12693; AAA89198.1; -; mRNA.
DR EMBL; Z11870; CAA77896.1; -; mRNA.
DR EMBL; X63866; CAA45345.1; -; mRNA.
DR EMBL; Z11871; CAA77897.1; -; mRNA.
DR EMBL; U20326; AAB60490.1; -; mRNA.
DR EMBL; AY176064; AAO31613.1; -; Genomic_DNA.
DR EMBL; AK075760; BAC35938.1; -; mRNA.
DR EMBL; AK078427; BAC37269.1; -; mRNA.
DR EMBL; BC058723; AAH58723.1; -; mRNA.
DR CCDS; CCDS51841.1; -. [P53996-1]
DR CCDS; CCDS85091.1; -. [P53996-3]
DR CCDS; CCDS85092.1; -. [P53996-2]
DR PIR; I48297; I48297.
DR PIR; I48298; I48298.
DR PIR; I49259; I49259.
DR RefSeq; NP_001103215.1; NM_001109745.1.
DR RefSeq; NP_001334254.1; NM_001347325.1. [P53996-3]
DR RefSeq; NP_038521.1; NM_013493.3. [P53996-1]
DR AlphaFoldDB; P53996; -.
DR BioGRID; 198782; 16.
DR IntAct; P53996; 3.
DR MINT; P53996; -.
DR STRING; 10090.ENSMUSP00000032138; -.
DR iPTMnet; P53996; -.
DR PhosphoSitePlus; P53996; -.
DR SwissPalm; P53996; -.
DR EPD; P53996; -.
DR jPOST; P53996; -.
DR PaxDb; P53996; -.
DR PeptideAtlas; P53996; -.
DR PRIDE; P53996; -.
DR ProteomicsDB; 283393; -. [P53996-1]
DR ProteomicsDB; 283394; -. [P53996-2]
DR ProteomicsDB; 283395; -. [P53996-3]
DR Antibodypedia; 33233; 338 antibodies from 32 providers.
DR DNASU; 12785; -.
DR Ensembl; ENSMUST00000032138; ENSMUSP00000032138; ENSMUSG00000030057. [P53996-1]
DR Ensembl; ENSMUST00000113617; ENSMUSP00000109247; ENSMUSG00000030057. [P53996-3]
DR Ensembl; ENSMUST00000113619; ENSMUSP00000109249; ENSMUSG00000030057. [P53996-2]
DR Ensembl; ENSMUST00000204653; ENSMUSP00000145274; ENSMUSG00000030057. [P53996-3]
DR GeneID; 12785; -.
DR KEGG; mmu:12785; -.
DR UCSC; uc009cuc.2; mouse. [P53996-1]
DR CTD; 7555; -.
DR MGI; MGI:88431; Cnbp.
DR VEuPathDB; HostDB:ENSMUSG00000030057; -.
DR eggNOG; KOG4400; Eukaryota.
DR GeneTree; ENSGT00950000183041; -.
DR HOGENOM; CLU_058879_4_0_1; -.
DR InParanoid; P53996; -.
DR OMA; SHQARDC; -.
DR PhylomeDB; P53996; -.
DR TreeFam; TF316974; -.
DR BioGRID-ORCS; 12785; 6 hits in 44 CRISPR screens.
DR ChiTaRS; Cnbp; mouse.
DR PRO; PR:P53996; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P53996; protein.
DR Bgee; ENSMUSG00000030057; Expressed in otic placode and 292 other tissues.
DR ExpressionAtlas; P53996; baseline and differential.
DR Genevisible; P53996; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0051880; F:G-quadruplex DNA binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; ISO:MGI.
DR GO; GO:0003727; F:single-stranded RNA binding; ISO:MGI.
DR GO; GO:0045182; F:translation regulator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071919; P:G-quadruplex DNA formation; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:MGI.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00098; zf-CCHC; 7.
DR SMART; SM00343; ZnF_C2HC; 7.
DR SUPFAM; SSF57756; SSF57756; 4.
DR PROSITE; PS50158; ZF_CCHC; 7.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; DNA-binding;
KW Endoplasmic reticulum; Metal-binding; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CHAIN 2..178
FT /note="CCHC-type zinc finger nucleic acid binding protein"
FT /id="PRO_0000089966"
FT ZN_FING 4..21
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 52..69
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 72..90
FT /note="CCHC-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 97..114
FT /note="CCHC-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 118..135
FT /note="CCHC-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 136..153
FT /note="CCHC-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 157..174
FT /note="CCHC-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 25..38
FT /note="RNA-binding Arg/Gly-rich region (RGG-box)"
FT /evidence="ECO:0000250|UniProtKB:P62633"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 25
FT /note="Omega-N-methylarginine; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:P62633"
FT MOD_RES 27
FT /note="Omega-N-methylarginine; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:P62633"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 80
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P62633"
FT VAR_SEQ 36..42
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:7896269"
FT /id="VSP_010983"
FT VAR_SEQ 73
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:7896269"
FT /id="VSP_010984"
FT CONFLICT 2
FT /note="S -> R (in Ref. 1; CAA45345/CAA77896)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="S -> P (in Ref. 4; BAC37269)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="G -> D (in Ref. 1; CAA77897)"
FT /evidence="ECO:0000305"
FT MOD_RES P53996-2:32
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES P53996-2:34
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES P53996-2:72
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES P53996-3:79
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
SQ SEQUENCE 178 AA; 19592 MW; DF0CDAB9BF3D96BB CRC64;
MSSNECFKCG RSGHWARECP TGGGRGRGMR SRGRGGFTSD RGFQFVSSSL PDICYRCGES
GHLAKDCDLQ EDEACYNCGR GGHIAKDCKE PKREREQCCY NCGKPGHLAR DCDHADEQKC
YSCGEFGHIQ KDCTKVKCYR CGETGHVAIN CSKTSEVNCY RCGESGHLAR ECTIEATA
