ZNF24_MOUSE
ID ZNF24_MOUSE Reviewed; 368 AA.
AC Q91VN1; Q5MDG8; Q9WUQ0;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Zinc finger protein 24 {ECO:0000312|MGI:MGI:1929704};
DE AltName: Full=Hypomyelinated CNS protein {ECO:0000303|PubMed:20080941};
DE AltName: Full=Zinc finger protein 191 {ECO:0000250|UniProtKB:P17028};
DE AltName: Full=Zinc finger protein ZF-12 {ECO:0000303|PubMed:10542327};
GN Name=Znf24 {ECO:0000250|UniProtKB:P17028};
GN Synonyms=Hmcns {ECO:0000303|PubMed:20080941},
GN Zfp191 {ECO:0000250|UniProtKB:P17028}, Zfp24 {ECO:0000312|MGI:MGI:1929704};
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=CD-1; TISSUE=Cartilage chondrocyte;
RX PubMed=10542327; DOI=10.1016/s0167-4781(99)00157-8;
RA Prost J.-P., Negre D., Cornet-Javaux F., Cortay J.-C., Cozzone A.J.,
RA Herbage D., Mallein-Gerin F.;
RT "Isolation, cloning, and expression of a new murine zinc finger encoding
RT gene.";
RL Biochim. Biophys. Acta 1447:278-283(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=12812053;
RA Li J.-Z., Chen X., Wang S.L., Sun X., Zhang Y.Z., Yu L., Fu J.-L.;
RT "Cloning, genomic organization and promoter activity of the mouse zinc
RT finger protein gene ZF-12.";
RL Yi Chuan Xue Bao 30:311-316(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland, and Retina;
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 DISRUPTION PHENOTYPE.
RX PubMed=17064688; DOI=10.1016/j.yexcr.2006.08.020;
RA Li J., Chen X., Yang H., Wang S., Guo B., Yu L., Wang Z., Fu J.;
RT "The zinc finger transcription factor 191 is required for early embryonic
RT development and cell proliferation.";
RL Exp. Cell Res. 312:3990-3998(2006).
RN [7]
RP DNA-BINDING.
RX PubMed=18685786; DOI=10.1093/abbs/40.8.704;
RA Wang H., Sun R., Liu G., Yao M., Fei J., Shen H.;
RT "Characterization of the target DNA sequence for the DNA-binding domain of
RT zinc finger protein 191.";
RL Acta Biochim. Biophys. Sin. 40:704-710(2008).
RN [8]
RP DEVELOPMENTAL STAGE.
RX PubMed=18096443; DOI=10.1016/j.gep.2007.11.002;
RA Khalfallah O., Faucon-Biguet N., Nardelli J., Meloni R., Mallet J.;
RT "Expression of the transcription factor Zfp191 during embryonic development
RT in the mouse.";
RL Gene Expr. Patterns 8:148-154(2008).
RN [9]
RP FUNCTION.
RX PubMed=19544452; DOI=10.1002/stem.88;
RA Khalfallah O., Ravassard P., Lagache C.S., Fligny C., Serre A., Bayard E.,
RA Faucon-Biguet N., Mallet J., Meloni R., Nardelli J.;
RT "Zinc finger protein 191 (ZNF191/Zfp191) is necessary to maintain neural
RT cells as cycling progenitors.";
RL Stem Cells 27:1643-1653(2009).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20080941; DOI=10.1101/gad.1864510;
RA Howng S.Y., Avila R.L., Emery B., Traka M., Lin W., Watkins T., Cook S.,
RA Bronson R., Davisson M., Barres B.A., Popko B.;
RT "ZFP191 is required by oligodendrocytes for CNS myelination.";
RL Genes Dev. 24:301-311(2010).
CC -!- FUNCTION: Transcription factor required for myelination of
CC differentiated oligodendrocytes. Required for the conversion of
CC oligodendrocytes from the premyelinating to the myelinating state. In
CC the developing central nervous system (CNS), involved in the
CC maintenance in the progenitor stage by promoting the cell cycle.
CC Specifically binds to the 5'-TCAT-3' DNA sequence. Has transcription
CC repressor activity in vitro. {ECO:0000269|PubMed:19544452,
CC ECO:0000269|PubMed:20080941}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187,
CC ECO:0000269|PubMed:20080941}.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in heart,
CC brain, liver, skeletal muscle, kidney and testis and very low levels in
CC spleen and lung. {ECO:0000269|PubMed:10542327,
CC ECO:0000269|PubMed:20080941}.
CC -!- DEVELOPMENTAL STAGE: In the embryo, barely detectable at day 17, peaks
CC at day 11 and remains constant thereafter. Detected early during
CC embryogenesis in ectodermal, endodermal, mesodermal and extraembryonic
CC tissues. Expressed in the developing central nervous system. In the
CC developing central nervous system (CNS), mainly expressed in
CC progenitors. {ECO:0000269|PubMed:10542327,
CC ECO:0000269|PubMed:18096443}.
CC -!- PTM: Sumoylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: According to PubMed:20080941, most mice die by
CC postnatal day 25 (P25) due to myelination defects. Brains and spinal
CC cords isolated from P14 mice appear to be smaller than those from wild-
CC type mice and to lack white matter. Mutant oligodendrocytes arrest at a
CC late stage of differentiation. Expression of genes expressed
CC specifically in mature myelinating oligodendrocytes is down-regulated.
CC According to PubMed:17064688, embryos are severely retarded in
CC development and die at approximately 7.5 dpc. One possible explanation
CC for the different phenotypes described is that the two null alleles are
CC not identical. In the mutants described by PubMed:20080941, the PGK-neo
CC cassette used for positive selection of embryonic stem (ES) cells has
CC been removed, whereas it remains in the allele described by
CC PubMed:17064688. {ECO:0000269|PubMed:17064688,
CC ECO:0000269|PubMed:20080941}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AF149093; AAD37421.1; -; mRNA.
DR EMBL; AY052495; AAL13429.1; -; Genomic_DNA.
DR EMBL; AY832930; AAV91152.1; -; mRNA.
DR EMBL; AK146726; BAE27389.1; -; mRNA.
DR EMBL; CH466557; EDK96990.1; -; Genomic_DNA.
DR EMBL; CH466557; EDK96991.1; -; Genomic_DNA.
DR EMBL; BC011345; AAH11345.1; -; mRNA.
DR EMBL; BC054832; AAH54832.1; -; mRNA.
DR CCDS; CCDS29098.1; -.
DR RefSeq; NP_067534.2; NM_021559.2.
DR RefSeq; XP_006526199.1; XM_006526136.3.
DR RefSeq; XP_006526200.1; XM_006526137.3.
DR AlphaFoldDB; Q91VN1; -.
DR SMR; Q91VN1; -.
DR BioGRID; 208519; 24.
DR IntAct; Q91VN1; 2.
DR STRING; 10090.ENSMUSP00000064637; -.
DR iPTMnet; Q91VN1; -.
DR PhosphoSitePlus; Q91VN1; -.
DR EPD; Q91VN1; -.
DR MaxQB; Q91VN1; -.
DR PaxDb; Q91VN1; -.
DR PeptideAtlas; Q91VN1; -.
DR PRIDE; Q91VN1; -.
DR ProteomicsDB; 275041; -.
DR Antibodypedia; 8576; 271 antibodies from 32 providers.
DR DNASU; 59057; -.
DR Ensembl; ENSMUST00000066497; ENSMUSP00000064637; ENSMUSG00000051469.
DR Ensembl; ENSMUST00000153337; ENSMUSP00000122579; ENSMUSG00000051469.
DR GeneID; 59057; -.
DR KEGG; mmu:59057; -.
DR UCSC; uc008egm.1; mouse.
DR CTD; 59057; -.
DR MGI; MGI:1929704; Zfp24.
DR VEuPathDB; HostDB:ENSMUSG00000051469; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161396; -.
DR HOGENOM; CLU_002678_49_3_1; -.
DR InParanoid; Q91VN1; -.
DR OMA; VAQIFKY; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q91VN1; -.
DR TreeFam; TF338304; -.
DR BioGRID-ORCS; 59057; 2 hits in 38 CRISPR screens.
DR ChiTaRS; Zfp24; mouse.
DR PRO; PR:Q91VN1; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q91VN1; protein.
DR Bgee; ENSMUSG00000051469; Expressed in medial ganglionic eminence and 306 other tissues.
DR ExpressionAtlas; Q91VN1; baseline and differential.
DR Genevisible; Q91VN1; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0042552; P:myelination; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 1.10.4020.10; -; 1.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..368
FT /note="Zinc finger protein 24"
FT /id="PRO_0000047353"
FT DOMAIN 52..134
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT ZN_FING 251..273
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 279..301
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 307..329
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 335..357
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 251..301
FT /note="Necessary and sufficient for nuclear localization"
FT /evidence="ECO:0000250"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17028"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17028"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17028"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17028"
FT MOD_RES 335
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P17028"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17028"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P17028"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P17028"
FT CROSSLNK 147
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17028"
FT CROSSLNK 177
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17028"
FT CROSSLNK 236
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17028"
FT CROSSLNK 277
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17028"
FT CROSSLNK 286
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17028"
FT CROSSLNK 361
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17028"
FT CROSSLNK 367
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17028"
FT CONFLICT 91
FT /note="I -> M (in Ref. 1; AAD37421)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="Missing (in Ref. 1; AAD37421)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 368 AA; 41919 MW; 344974009D2A5469 CRC64;
MSAQSVEEDS ILIIPNPDEE EKILRVKLEE DPDGEEGSSI SWNHLPDPEV FRQRFRQFGY
QDSPGPREAV SQLRELCRLW LRPETHTKEQ ILELVVLEQF VAILPKELQT WVREHHPENG
EEAVAVLEDL ESELDDPGQP VSLRRQKREV LVEEITSQED AQGLPSSELD AVENQLKWAS
WELHSLRHCD DDATTENGAL APKQEMASAG ESHEGPGTLN IGVPQLFKYG ETCFPKGRFE
RKRNPSRKKQ HICDECGKHF SQGSALILHQ RIHSGEKPYG CVECGKAFSR SSILVQHQRV
HTGEKPYKCL ECGKAFSQNS GLINHQRIHT GEKPYECVQC GKSYSQSSNL FRHQRRHNAE
KLLNVVKV
