ZNF24_HUMAN
ID ZNF24_HUMAN Reviewed; 368 AA.
AC P17028; O14754; Q53YE4; Q6ICR5; Q8IZN4;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 4.
DT 03-AUG-2022, entry version 230.
DE RecName: Full=Zinc finger protein 24;
DE AltName: Full=Retinoic acid suppression protein A;
DE Short=RSG-A;
DE AltName: Full=Zinc finger and SCAN domain-containing protein 3;
DE AltName: Full=Zinc finger protein 191;
DE AltName: Full=Zinc finger protein KOX17;
GN Name=ZNF24; Synonyms=KOX17, ZNF191, ZSCAN3;
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 [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP SER-220.
RC TISSUE=Liver;
RA Shi S., Yu L.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND VARIANT SER-220.
RC TISSUE=Bone marrow;
RX PubMed=10585455; DOI=10.1074/jbc.274.50.35741;
RA Han Z.-G., Zhang Q.-H., Ye M., Kan L.-X., Gu B.-W., He K.-L., Shi S.-L.,
RA Zhou J., Fu G., Mao M., Chen S.-J., Yu L., Chen Z.;
RT "Molecular cloning of six novel Kruppel-like zinc finger genes from
RT hematopoietic cells and identification of a novel transregulatory domain
RT KRNB.";
RL J. Biol. Chem. 274:35741-35748(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-220.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-220.
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 (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-220.
RC TISSUE=Lung, and Testis;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 319-362 (ISOFORM 1).
RC TISSUE=Lymphoid tissue;
RX PubMed=2288909;
RA Thiesen H.-J.;
RT "Multiple genes encoding zinc finger domains are expressed in human T
RT cells.";
RL New Biol. 2:363-374(1990).
RN [9]
RP SUMOYLATION.
RX PubMed=15561718; DOI=10.1074/jbc.m411718200;
RA Gocke C.B., Yu H., Kang J.;
RT "Systematic identification and analysis of mammalian small ubiquitin-like
RT modifier substrates.";
RL J. Biol. Chem. 280:5004-5012(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-335, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142 AND SER-274, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-286 AND ARG-290.
RX PubMed=24224020; DOI=10.1371/journal.pone.0079910;
RA Li J.Z., Chen X., Gong X.L., Hu H.Y., Shi D., Lu Y.M., Qiu L., Lu F.,
RA Hu Z.L., Zhang J.P.;
RT "Identification of a functional nuclear localization signal mediating
RT nuclear import of the zinc finger transcription factor ZNF24.";
RL PLoS ONE 8:E79910-E79910(2013).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-27, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-27, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-27, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-27 AND LYS-277, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-22; LYS-27; LYS-147; LYS-177;
RP LYS-236; LYS-277; LYS-286; LYS-361 AND LYS-367, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [22]
RP STRUCTURE BY NMR OF 272-330.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structures of the C2H2 type zinc finger domain of human zinc
RT finger protein 24.";
RL Submitted (NOV-2005) to the PDB data bank.
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 (By similarity). Has
CC transcription repressor activity in vitro. {ECO:0000250,
CC ECO:0000269|PubMed:10585455}.
CC -!- INTERACTION:
CC P17028; P51693: APLP1; NbExp=2; IntAct=EBI-707773, EBI-74648;
CC P17028; P02649: APOE; NbExp=3; IntAct=EBI-707773, EBI-1222467;
CC P17028; P05067: APP; NbExp=3; IntAct=EBI-707773, EBI-77613;
CC P17028; P26196: DDX6; NbExp=3; IntAct=EBI-707773, EBI-351257;
CC P17028; Q86Y13: DZIP3; NbExp=5; IntAct=EBI-707773, EBI-948630;
CC P17028; Q3B820: FAM161A; NbExp=3; IntAct=EBI-707773, EBI-719941;
CC P17028; P25800: LMO1; NbExp=5; IntAct=EBI-707773, EBI-8639312;
CC P17028; P25791: LMO2; NbExp=4; IntAct=EBI-707773, EBI-739696;
CC P17028; P25791-3: LMO2; NbExp=3; IntAct=EBI-707773, EBI-11959475;
CC P17028; Q9BXW4: MAP1LC3C; NbExp=3; IntAct=EBI-707773, EBI-2603996;
CC P17028; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-707773, EBI-10172526;
CC P17028; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-707773, EBI-11750983;
CC P17028; Q96JS3: PGBD1; NbExp=8; IntAct=EBI-707773, EBI-10290053;
CC P17028; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-707773, EBI-1567797;
CC P17028; P57086: SCAND1; NbExp=7; IntAct=EBI-707773, EBI-745846;
CC P17028; Q9Y4C2: TCAF1; NbExp=3; IntAct=EBI-707773, EBI-750484;
CC P17028; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-707773, EBI-10180829;
CC P17028; P13994: YJU2B; NbExp=7; IntAct=EBI-707773, EBI-716093;
CC P17028; Q8N5A5-2: ZGPAT; NbExp=3; IntAct=EBI-707773, EBI-10183064;
CC P17028; Q969J2: ZKSCAN4; NbExp=5; IntAct=EBI-707773, EBI-2818641;
CC P17028; P49910: ZNF165; NbExp=3; IntAct=EBI-707773, EBI-741694;
CC P17028; Q15697-2: ZNF174; NbExp=4; IntAct=EBI-707773, EBI-11158827;
CC P17028; Q9UNY5: ZNF232; NbExp=3; IntAct=EBI-707773, EBI-749023;
CC P17028; P17028: ZNF24; NbExp=4; IntAct=EBI-707773, EBI-707773;
CC P17028; Q96N95-3: ZNF396; NbExp=5; IntAct=EBI-707773, EBI-12328453;
CC P17028; Q86VK4-3: ZNF410; NbExp=3; IntAct=EBI-707773, EBI-11741890;
CC P17028; Q8N0Y2-2: ZNF444; NbExp=6; IntAct=EBI-707773, EBI-12010736;
CC P17028; Q9NWS9: ZNF446; NbExp=4; IntAct=EBI-707773, EBI-3925851;
CC P17028; Q9NWS9-2: ZNF446; NbExp=13; IntAct=EBI-707773, EBI-740232;
CC P17028; Q6P088: ZNF483; NbExp=3; IntAct=EBI-707773, EBI-10196963;
CC P17028; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-707773, EBI-4395669;
CC P17028; O43309: ZSCAN12; NbExp=3; IntAct=EBI-707773, EBI-1210440;
CC P17028; Q9H4T2: ZSCAN16; NbExp=3; IntAct=EBI-707773, EBI-723596;
CC P17028; Q9Y5A6: ZSCAN21; NbExp=6; IntAct=EBI-707773, EBI-10281938;
CC P17028; P10073: ZSCAN22; NbExp=6; IntAct=EBI-707773, EBI-10178224;
CC P17028; Q3MJ62: ZSCAN23; NbExp=3; IntAct=EBI-707773, EBI-5667532;
CC P17028; Q9NX65: ZSCAN32; NbExp=9; IntAct=EBI-707773, EBI-739949;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187,
CC ECO:0000269|PubMed:24224020}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P17028-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P17028-2; Sequence=VSP_039219, VSP_039220;
CC -!- TISSUE SPECIFICITY: Expressed in many tissues except in heart.
CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:15561718}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; U68536; AAB37275.1; -; mRNA.
DR EMBL; AF016052; AAB70216.1; -; Genomic_DNA.
DR EMBL; AF542097; AAN40767.1; -; mRNA.
DR EMBL; AF038964; AAD19827.1; -; mRNA.
DR EMBL; AK291246; BAF83935.1; -; mRNA.
DR EMBL; BT006658; AAP35304.1; -; mRNA.
DR EMBL; CR450328; CAG29324.1; -; mRNA.
DR EMBL; AC116447; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471088; EAX01348.1; -; Genomic_DNA.
DR EMBL; CH471088; EAX01349.1; -; Genomic_DNA.
DR EMBL; BC003566; AAH03566.1; -; mRNA.
DR EMBL; BC016801; AAH16801.1; -; mRNA.
DR EMBL; X52348; CAA36574.1; -; mRNA.
DR CCDS; CCDS11912.1; -. [P17028-1]
DR CCDS; CCDS77175.1; -. [P17028-2]
DR PIR; I37956; I37956.
DR RefSeq; NP_001295052.1; NM_001308123.1. [P17028-2]
DR RefSeq; NP_008896.2; NM_006965.3. [P17028-1]
DR RefSeq; XP_005258398.1; XM_005258341.3.
DR PDB; 1X6E; NMR; -; A=272-330.
DR PDB; 3LHR; X-ray; 1.90 A; A/B=46-136.
DR PDBsum; 1X6E; -.
DR PDBsum; 3LHR; -.
DR AlphaFoldDB; P17028; -.
DR SMR; P17028; -.
DR BioGRID; 113403; 139.
DR IntAct; P17028; 90.
DR MINT; P17028; -.
DR STRING; 9606.ENSP00000261332; -.
DR iPTMnet; P17028; -.
DR PhosphoSitePlus; P17028; -.
DR SwissPalm; P17028; -.
DR BioMuta; ZNF24; -.
DR DMDM; 160376173; -.
DR EPD; P17028; -.
DR jPOST; P17028; -.
DR MassIVE; P17028; -.
DR MaxQB; P17028; -.
DR PaxDb; P17028; -.
DR PeptideAtlas; P17028; -.
DR PRIDE; P17028; -.
DR ProteomicsDB; 53429; -. [P17028-1]
DR ProteomicsDB; 53430; -. [P17028-2]
DR Antibodypedia; 8576; 271 antibodies from 32 providers.
DR DNASU; 7572; -.
DR Ensembl; ENST00000261332.11; ENSP00000261332.5; ENSG00000172466.16. [P17028-1]
DR Ensembl; ENST00000399061.3; ENSP00000382015.2; ENSG00000172466.16. [P17028-1]
DR Ensembl; ENST00000589881.5; ENSP00000467655.1; ENSG00000172466.16. [P17028-2]
DR GeneID; 7572; -.
DR KEGG; hsa:7572; -.
DR MANE-Select; ENST00000261332.11; ENSP00000261332.5; NM_006965.4; NP_008896.2.
DR UCSC; uc002kys.3; human. [P17028-1]
DR CTD; 7572; -.
DR DisGeNET; 7572; -.
DR GeneCards; ZNF24; -.
DR HGNC; HGNC:13032; ZNF24.
DR HPA; ENSG00000172466; Low tissue specificity.
DR MIM; 194534; gene.
DR neXtProt; NX_P17028; -.
DR OpenTargets; ENSG00000172466; -.
DR PharmGKB; PA37610; -.
DR VEuPathDB; HostDB:ENSG00000172466; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161396; -.
DR HOGENOM; CLU_002678_49_3_1; -.
DR InParanoid; P17028; -.
DR OMA; VAQIFKY; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P17028; -.
DR TreeFam; TF338304; -.
DR PathwayCommons; P17028; -.
DR SignaLink; P17028; -.
DR BioGRID-ORCS; 7572; 80 hits in 1102 CRISPR screens.
DR ChiTaRS; ZNF24; human.
DR EvolutionaryTrace; P17028; -.
DR GeneWiki; ZNF24; -.
DR GenomeRNAi; 7572; -.
DR Pharos; P17028; Tbio.
DR PRO; PR:P17028; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; P17028; protein.
DR Bgee; ENSG00000172466; Expressed in medial globus pallidus and 213 other tissues.
DR ExpressionAtlas; P17028; baseline and differential.
DR Genevisible; P17028; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
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; IPI:IntAct.
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:NTNU_SB.
DR GO; GO:0042552; P:myelination; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
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 3D-structure; Alternative splicing; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..368
FT /note="Zinc finger protein 24"
FT /id="PRO_0000047352"
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 MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 335
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 147
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 177
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 236
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 277
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 286
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 361
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 367
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 190..193
FT /note="DDDG -> VIIP (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_039219"
FT VAR_SEQ 194..368
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_039220"
FT VARIANT 220
FT /note="N -> S (in dbSNP:rs2032729)"
FT /evidence="ECO:0000269|PubMed:10585455,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.1, ECO:0000269|Ref.4"
FT /id="VAR_012017"
FT VARIANT 331
FT /note="G -> W (in dbSNP:rs3568)"
FT /id="VAR_012018"
FT MUTAGEN 286
FT /note="K->A: Partial cytoplasmic accumulation."
FT /evidence="ECO:0000269|PubMed:24224020"
FT MUTAGEN 290
FT /note="R->A: Partial cytoplasmic accumulation."
FT /evidence="ECO:0000269|PubMed:24224020"
FT CONFLICT 367
FT /note="K -> E (in Ref. 1; AAB37275 and 4; CAG29324)"
FT /evidence="ECO:0000305"
FT HELIX 47..57
FT /evidence="ECO:0007829|PDB:3LHR"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:3LHR"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:3LHR"
FT HELIX 66..81
FT /evidence="ECO:0007829|PDB:3LHR"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:3LHR"
FT HELIX 88..102
FT /evidence="ECO:0007829|PDB:3LHR"
FT HELIX 106..114
FT /evidence="ECO:0007829|PDB:3LHR"
FT HELIX 120..134
FT /evidence="ECO:0007829|PDB:3LHR"
FT TURN 272..275
FT /evidence="ECO:0007829|PDB:1X6E"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:1X6E"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:1X6E"
FT HELIX 291..299
FT /evidence="ECO:0007829|PDB:1X6E"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:1X6E"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:1X6E"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:1X6E"
FT HELIX 319..330
FT /evidence="ECO:0007829|PDB:1X6E"
SQ SEQUENCE 368 AA; 42155 MW; B890EDC512493E0E CRC64;
MSAQSVEEDS ILIIPTPDEE EKILRVKLEE DPDGEEGSSI PWNHLPDPEI FRQRFRQFGY
QDSPGPREAV SQLRELCRLW LRPETHTKEQ ILELVVLEQF VAILPKELQT WVRDHHPENG
EEAVTVLEDL ESELDDPGQP VSLRRRKREV LVEDMVSQEE AQGLPSSELD AVENQLKWAS
WELHSLRHCD DDGRTENGAL APKQELPSAL ESHEVPGTLN MGVPQIFKYG ETCFPKGRFE
RKRNPSRKKQ HICDECGKHF SQGSALILHQ RIHSGEKPYG CVECGKAFSR SSILVQHQRV
HTGEKPYKCL ECGKAFSQNS GLINHQRIHT GEKPYECVQC GKSYSQSSNL FRHQRRHNAE
KLLNVVKV
