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   27-MAR-2024, entry version 180.
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,
RC   Pancreas, 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; 17.
DR   IntAct; P53996; 3.
DR   MINT; P53996; -.
DR   STRING; 10090.ENSMUSP00000032138; -.
DR   GlyGen; P53996; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P53996; -.
DR   PhosphoSitePlus; P53996; -.
DR   SwissPalm; P53996; -.
DR   EPD; P53996; -.
DR   jPOST; P53996; -.
DR   PaxDb; 10090-ENSMUSP00000032138; -.
DR   PeptideAtlas; P53996; -.
DR   ProteomicsDB; 283393; -. [P53996-1]
DR   ProteomicsDB; 283394; -. [P53996-2]
DR   ProteomicsDB; 283395; -. [P53996-3]
DR   Pumba; P53996; -.
DR   Antibodypedia; 33233; 365 antibodies from 32 providers.
DR   DNASU; 12785; -.
DR   Ensembl; ENSMUST00000032138.15; ENSMUSP00000032138.9; ENSMUSG00000030057.16. [P53996-1]
DR   Ensembl; ENSMUST00000113617.3; ENSMUSP00000109247.3; ENSMUSG00000030057.16. [P53996-3]
DR   Ensembl; ENSMUST00000113619.8; ENSMUSP00000109249.3; ENSMUSG00000030057.16. [P53996-2]
DR   Ensembl; ENSMUST00000204653.3; ENSMUSP00000145274.2; ENSMUSG00000030057.16. [P53996-3]
DR   GeneID; 12785; -.
DR   KEGG; mmu:12785; -.
DR   UCSC; uc009cuc.2; mouse. [P53996-1]
DR   AGR; MGI:88431; -.
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; KGNPTCY; -.
DR   OrthoDB; 147033at2759; -.
DR   PhylomeDB; P53996; -.
DR   TreeFam; TF316974; -.
DR   BioGRID-ORCS; 12785; 7 hits in 49 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 296 other cell types or tissues.
DR   ExpressionAtlas; P53996; baseline and differential.
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:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 5.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   PANTHER; PTHR23002:SF117; CCHC-TYPE ZINC FINGER NUCLEIC ACID BINDING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR23002; ZINC FINGER CCHC DOMAIN CONTAINING PROTEIN; 1.
DR   Pfam; PF00098; zf-CCHC; 7.
DR   SMART; SM00343; ZnF_C2HC; 7.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 4.
DR   PROSITE; PS50158; ZF_CCHC; 7.
DR   Genevisible; P53996; MM.
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
//