CNBP_HUMAN
ID CNBP_HUMAN Reviewed; 177 AA.
AC P62633; A8K7V4; B2RAV9; B4DP17; D3DNB9; D3DNC0; D3DNC1; E9PDR7; P20694;
AC Q4JGY0; Q4JGY1; Q5QJR0; Q5U0E9; Q6PJI7; Q96NV3;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=CCHC-type zinc finger nucleic acid binding protein {ECO:0000312|HGNC:HGNC:13164};
DE AltName: Full=Cellular nucleic acid-binding protein {ECO:0000305};
DE Short=CNBP {ECO:0000305};
DE AltName: Full=Zinc finger protein 9;
GN Name=CNBP {ECO:0000312|HGNC:HGNC:13164}; Synonyms=RNF163, ZNF9;
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), FUNCTION, TISSUE SPECIFICITY, AND
RP INDUCTION BY STEROL.
RX PubMed=2562787; DOI=10.1126/science.2562787;
RA Rajavashisth T.B., Taylor A.K., Andalibi A., Svenson K.L., Lusis A.J.;
RT "Identification of a zinc finger protein that binds to the sterol
RT regulatory element.";
RL Science 245:640-643(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=7590281; DOI=10.1016/0378-1119(95)00421-2;
RA Flink I.L., Morkin E.;
RT "Organization of the gene encoding cellular nucleic acid-binding protein.";
RL Gene 163:279-282(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISEASE.
RX PubMed=11486088; DOI=10.1126/science.1062125;
RA Liquori C.L., Ricker K., Moseley M.L., Jacobsen J.F., Kress W.,
RA Naylor S.L., Day J.W., Ranum L.P.;
RT "Myotonic dystrophy type 2 caused by a CCTG expansion in intron 1 of
RT ZNF9.";
RL Science 293:864-867(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5 AND 8).
RA Yang F., Yan H., Zhang S.;
RT "Cloning of novel transcript variants of human cellular nucleic acid
RT binding protein.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 6 AND 7).
RC TISSUE=Placenta, and Synovium;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Lung, and Uterus;
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 [10]
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP METHYLATION AT ARG-25 AND ARG-27, AND MUTAGENESIS OF ARG-25 AND ARG-27.
RX PubMed=24726729; DOI=10.1016/j.febslet.2014.03.052;
RA Wei H.M., Hu H.H., Chang G.Y., Lee Y.J., Li Y.C., Chang H.H., Li C.;
RT "Arginine methylation of the cellular nucleic acid binding protein does not
RT affect its subcellular localization but impedes RNA binding.";
RL FEBS Lett. 588:1542-1548(2014).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-79, METHYLATION [LARGE SCALE
RP ANALYSIS] AT ARG-32 AND ARG-34 (ISOFORMS 2; 5 AND 8), METHYLATION [LARGE
RP SCALE ANALYSIS] AT ARG-80 (ISOFORM 4), METHYLATION [LARGE SCALE ANALYSIS]
RP AT ARG-73 (ISOFORM 8), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Colon carcinoma;
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).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [16]
RP FUNCTION (ISOFORMS 1; 2; 4; 5; 6 AND 8), ASSOCIATION WITH RIBOSOMES AND
RP POLYSOMES, AND SUBCELLULAR LOCATION (ISOFORMS 1; 2; 4; 5; 6 AND 8).
RX PubMed=28329689; DOI=10.1016/j.celrep.2017.02.080;
RA Benhalevy D., Gupta S.K., Danan C.H., Ghosal S., Sun H.W., Kazemier H.G.,
RA Paeschke K., Hafner M., Juranek S.A.;
RT "The Human CCHC-type Zinc Finger Nucleic Acid-Binding Protein Binds G-Rich
RT Elements in Target mRNA Coding Sequences and Promotes Translation.";
RL Cell Rep. 18:2979-2990(2017).
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 (PubMed:2562787). Has a
CC role as transactivator of the Myc promoter (By similarity). Binds
CC single-stranded RNA in a sequence-specific manner (By similarity).
CC {ECO:0000250|UniProtKB:P53996, ECO:0000250|UniProtKB:P62634,
CC ECO:0000269|PubMed:2562787}.
CC -!- FUNCTION: [Isoform 1]: Binds G-rich elements in target mRNA coding
CC sequences (PubMed:28329689). Prevents G-quadruplex structure formation
CC in vitro, suggesting a role in supporting translation by resolving
CC stable structures on mRNAs (PubMed:28329689).
CC {ECO:0000269|PubMed:28329689}.
CC -!- FUNCTION: [Isoform 2]: Binds to RNA. {ECO:0000269|PubMed:28329689}.
CC -!- FUNCTION: [Isoform 4]: Binds to RNA. {ECO:0000269|PubMed:28329689}.
CC -!- FUNCTION: [Isoform 5]: Binds to RNA. {ECO:0000269|PubMed:28329689}.
CC -!- FUNCTION: [Isoform 6]: Binds to RNA. {ECO:0000269|PubMed:28329689}.
CC -!- FUNCTION: [Isoform 8]: Binds to RNA. {ECO:0000269|PubMed:28329689}.
CC -!- SUBUNIT: Associates with the 40S ribosomal subunit, the 80S ribosome
CC and with polysomes. {ECO:0000269|PubMed:28329689}.
CC -!- INTERACTION:
CC P62633; Q63009: Prmt1; Xeno; NbExp=2; IntAct=EBI-1047529, EBI-78708;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P53996}. Cytoplasm
CC {ECO:0000269|PubMed:28329689}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P53996}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000269|PubMed:28329689}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:28329689}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm
CC {ECO:0000269|PubMed:28329689}.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm
CC {ECO:0000269|PubMed:28329689}.
CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm
CC {ECO:0000269|PubMed:28329689}.
CC -!- SUBCELLULAR LOCATION: [Isoform 8]: Cytoplasm
CC {ECO:0000269|PubMed:28329689}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1;
CC IsoId=P62633-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P62633-2; Sequence=VSP_010981;
CC Name=3;
CC IsoId=P62633-3; Sequence=VSP_010982;
CC Name=4;
CC IsoId=P62633-4; Sequence=VSP_043304;
CC Name=5;
CC IsoId=P62633-5; Sequence=VSP_010981, VSP_043424;
CC Name=6;
CC IsoId=P62633-6; Sequence=VSP_043424;
CC Name=7;
CC IsoId=P62633-7; Sequence=VSP_055084;
CC Name=8;
CC IsoId=P62633-8; Sequence=VSP_010981, VSP_043304;
CC -!- TISSUE SPECIFICITY: Expressed in the liver, kidney, spleen, testis,
CC lung, muscle and adrenal glands. {ECO:0000269|PubMed:2562787}.
CC -!- INDUCTION: Transcriptionally up-regulated by sterol treatment.
CC {ECO:0000269|PubMed:2562787}.
CC -!- PTM: Arginine methylation by PRMT1 in the Arg/Gly-rich region impedes
CC RNA binding. {ECO:0000269|PubMed:24726729}.
CC -!- DISEASE: Dystrophia myotonica 2 (DM2) [MIM:602668]: A multisystem
CC disease characterized by the association of proximal muscle weakness
CC with myotonia, cardiac manifestations and cataract. Additional features
CC can include hyperhidrosis, testicular atrophy, insulin resistance and
CC diabetes and central nervous system anomalies in rare cases. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry. The causative mutation is a CCTG expansion (mean approximately
CC 5000 repeats) located in intron 1 of the CNBP gene.
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DR EMBL; M28372; AAA61975.1; -; mRNA.
DR EMBL; U19765; AAA91782.1; -; Genomic_DNA.
DR EMBL; AY329622; AAR89462.1; -; Genomic_DNA.
DR EMBL; DQ092366; AAY96754.1; -; mRNA.
DR EMBL; DQ092367; AAY96755.1; -; mRNA.
DR EMBL; DQ091187; AAY89856.1; -; mRNA.
DR EMBL; AK054592; BAB70769.1; -; mRNA.
DR EMBL; AK298154; BAG60429.1; -; mRNA.
DR EMBL; AK292119; BAF84808.1; -; mRNA.
DR EMBL; AK314380; BAG37006.1; -; mRNA.
DR EMBL; BT019613; AAV38419.1; -; mRNA.
DR EMBL; AC108673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC135587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79271.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79272.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79273.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79274.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79275.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79277.1; -; Genomic_DNA.
DR EMBL; BC000288; AAH00288.1; -; mRNA.
DR EMBL; BC014911; AAH14911.1; -; mRNA.
DR EMBL; BC093058; AAH93058.1; -; mRNA.
DR CCDS; CCDS3056.1; -. [P62633-1]
DR CCDS; CCDS46906.1; -. [P62633-6]
DR CCDS; CCDS46907.1; -. [P62633-4]
DR CCDS; CCDS46908.1; -. [P62633-5]
DR CCDS; CCDS54637.1; -. [P62633-2]
DR PIR; A32760; A32760.
DR RefSeq; NP_001120664.1; NM_001127192.1. [P62633-6]
DR RefSeq; NP_001120665.1; NM_001127193.1. [P62633-4]
DR RefSeq; NP_001120666.1; NM_001127194.1. [P62633-5]
DR RefSeq; NP_001120667.1; NM_001127195.1. [P62633-8]
DR RefSeq; NP_001120668.1; NM_001127196.1. [P62633-2]
DR RefSeq; NP_003409.1; NM_003418.4. [P62633-1]
DR AlphaFoldDB; P62633; -.
DR SASBDB; P62633; -.
DR BioGRID; 113387; 231.
DR IntAct; P62633; 124.
DR MINT; P62633; -.
DR STRING; 9606.ENSP00000410769; -.
DR GlyGen; P62633; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62633; -.
DR PhosphoSitePlus; P62633; -.
DR SwissPalm; P62633; -.
DR BioMuta; CNBP; -.
DR DMDM; 50401852; -.
DR CPTAC; CPTAC-480; -.
DR CPTAC; CPTAC-481; -.
DR EPD; P62633; -.
DR jPOST; P62633; -.
DR MassIVE; P62633; -.
DR MaxQB; P62633; -.
DR PaxDb; P62633; -.
DR PeptideAtlas; P62633; -.
DR PRIDE; P62633; -.
DR ProteomicsDB; 19732; -.
DR ProteomicsDB; 4742; -.
DR ProteomicsDB; 57408; -. [P62633-1]
DR ProteomicsDB; 57409; -. [P62633-2]
DR ProteomicsDB; 57410; -. [P62633-3]
DR ProteomicsDB; 57411; -. [P62633-4]
DR ProteomicsDB; 57412; -. [P62633-5]
DR Antibodypedia; 33233; 338 antibodies from 32 providers.
DR DNASU; 7555; -.
DR Ensembl; ENST00000422453.7; ENSP00000410619.3; ENSG00000169714.17. [P62633-1]
DR Ensembl; ENST00000441626.6; ENSP00000410769.2; ENSG00000169714.17. [P62633-6]
DR Ensembl; ENST00000446936.6; ENSP00000400444.2; ENSG00000169714.17. [P62633-5]
DR Ensembl; ENST00000451728.6; ENSP00000399488.2; ENSG00000169714.17. [P62633-4]
DR Ensembl; ENST00000500450.6; ENSP00000426223.1; ENSG00000169714.17. [P62633-7]
DR Ensembl; ENST00000502976.5; ENSP00000421323.1; ENSG00000169714.17. [P62633-2]
DR Ensembl; ENST00000504813.5; ENSP00000422110.1; ENSG00000169714.17. [P62633-3]
DR GeneID; 7555; -.
DR KEGG; hsa:7555; -.
DR MANE-Select; ENST00000422453.7; ENSP00000410619.3; NM_003418.5; NP_003409.1.
DR UCSC; uc003elq.5; human. [P62633-1]
DR CTD; 7555; -.
DR DisGeNET; 7555; -.
DR GeneCards; CNBP; -.
DR GeneReviews; CNBP; -.
DR HGNC; HGNC:13164; CNBP.
DR HPA; ENSG00000169714; Low tissue specificity.
DR MalaCards; CNBP; -.
DR MIM; 116955; gene.
DR MIM; 602668; phenotype.
DR neXtProt; NX_P62633; -.
DR OpenTargets; ENSG00000169714; -.
DR Orphanet; 606; Proximal myotonic myopathy.
DR PharmGKB; PA37737; -.
DR VEuPathDB; HostDB:ENSG00000169714; -.
DR eggNOG; KOG4400; Eukaryota.
DR GeneTree; ENSGT00950000183041; -.
DR HOGENOM; CLU_058879_4_0_1; -.
DR InParanoid; P62633; -.
DR OMA; SHQARDC; -.
DR OrthoDB; 1535084at2759; -.
DR PhylomeDB; P62633; -.
DR TreeFam; TF316974; -.
DR PathwayCommons; P62633; -.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR SignaLink; P62633; -.
DR SIGNOR; P62633; -.
DR BioGRID-ORCS; 7555; 38 hits in 1088 CRISPR screens.
DR ChiTaRS; CNBP; human.
DR GeneWiki; CNBP; -.
DR GenomeRNAi; 7555; -.
DR Pharos; P62633; Tbio.
DR PRO; PR:P62633; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P62633; protein.
DR Bgee; ENSG00000169714; Expressed in skeletal muscle tissue of rectus abdominis and 205 other tissues.
DR ExpressionAtlas; P62633; baseline and differential.
DR Genevisible; P62633; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0051880; F:G-quadruplex DNA binding; IDA:ARUK-UCL.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:Ensembl.
DR GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0045182; F:translation regulator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0042632; P:cholesterol homeostasis; TAS:GO_Central.
DR GO; GO:0071919; P:G-quadruplex DNA formation; IDA:ARUK-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:ProtInc.
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:22814378"
FT CHAIN 2..177
FT /note="CCHC-type zinc finger nucleic acid binding protein"
FT /id="PRO_0000089965"
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..89
FT /note="CCHC-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 96..113
FT /note="CCHC-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 117..134
FT /note="CCHC-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 135..152
FT /note="CCHC-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 156..173
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:0000269|PubMed:28329689"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P53996"
FT MOD_RES 25
FT /note="Omega-N-methylarginine; by PRMT1"
FT /evidence="ECO:0000269|PubMed:24726729"
FT MOD_RES 27
FT /note="Omega-N-methylarginine; by PRMT1"
FT /evidence="ECO:0000269|PubMed:24726729"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53996"
FT MOD_RES 79
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 35..51
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055084"
FT VAR_SEQ 36..42
FT /note="Missing (in isoform 2, isoform 5 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_010981"
FT VAR_SEQ 42..51
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_010982"
FT VAR_SEQ 72
FT /note="D -> DE (in isoform 4 and isoform 8)"
FT /evidence="ECO:0000303|Ref.4, ECO:0000303|Ref.6"
FT /id="VSP_043304"
FT VAR_SEQ 72
FT /note="D -> DVE (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.4"
FT /id="VSP_043424"
FT MUTAGEN 25
FT /note="R->K: Significantly reduces methylation; when
FT associated with K-27."
FT /evidence="ECO:0000269|PubMed:24726729"
FT MUTAGEN 27
FT /note="R->K: Significantly reduces methylation; when
FT associated with K-25."
FT /evidence="ECO:0000269|PubMed:24726729"
FT CONFLICT 6
FT /note="C -> R (in Ref. 5; BAF84808)"
FT /evidence="ECO:0000305"
FT MOD_RES P62633-2:32
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES P62633-2:34
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES P62633-4:80
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES P62633-5:32
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES P62633-5:34
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES P62633-8:32
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES P62633-8:34
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES P62633-8:73
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
SQ SEQUENCE 177 AA; 19463 MW; 996F398285F52618 CRC64;
MSSNECFKCG RSGHWARECP TGGGRGRGMR SRGRGGFTSD RGFQFVSSSL PDICYRCGES
GHLAKDCDLQ EDACYNCGRG GHIAKDCKEP KREREQCCYN CGKPGHLARD CDHADEQKCY
SCGEFGHIQK DCTKVKCYRC GETGHVAINC SKTSEVNCYR CGESGHLARE CTIEATA
