ZNF23_HUMAN
ID ZNF23_HUMAN Reviewed; 643 AA.
AC P17027; Q8NDP5; Q96IT3; Q9UG42;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2003, sequence version 3.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Zinc finger protein 23;
DE AltName: Full=Zinc finger protein 359;
DE AltName: Full=Zinc finger protein 612;
DE AltName: Full=Zinc finger protein KOX16;
GN Name=ZNF23; Synonyms=KOX16, ZNF359, ZNF612;
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).
RX PubMed=12127974; DOI=10.1016/s0006-291x(02)00759-3;
RA Zhou L., Zhu C., Luo K., Li Y., Pi H., Yuan W., Wang Y., Huang C., Liu M.,
RA Wu X.;
RT "Identification and characterization of two novel zinc finger genes, ZNF359
RT and ZFP28, in human development.";
RL Biochem. Biophys. Res. Commun. 295:862-868(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 50-643 (ISOFORM 1).
RC TISSUE=Hippocampus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Muscle;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 476-531 (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 [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-157, 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).
CC -!- FUNCTION: May be involved in transcriptional regulation. May have a
CC role in embryonic development.
CC -!- INTERACTION:
CC P17027; Q8N5M1: ATPAF2; NbExp=3; IntAct=EBI-5657766, EBI-1166928;
CC P17027; Q8IYF1: ELOA2; NbExp=3; IntAct=EBI-5657766, EBI-741705;
CC P17027; Q14192: FHL2; NbExp=3; IntAct=EBI-5657766, EBI-701903;
CC P17027; Q5TD97: FHL5; NbExp=3; IntAct=EBI-5657766, EBI-750641;
CC P17027; Q96IK5: GMCL1; NbExp=3; IntAct=EBI-5657766, EBI-2548508;
CC P17027; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-5657766, EBI-10171774;
CC P17027; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-5657766, EBI-348259;
CC P17027; Q99750: MDFI; NbExp=3; IntAct=EBI-5657766, EBI-724076;
CC P17027; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-5657766, EBI-16439278;
CC P17027; Q13875-3: MOBP; NbExp=3; IntAct=EBI-5657766, EBI-12013470;
CC P17027; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-5657766, EBI-11522433;
CC P17027; Q9Y5B8: NME7; NbExp=3; IntAct=EBI-5657766, EBI-744782;
CC P17027; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-5657766, EBI-5235340;
CC P17027; O43609: SPRY1; NbExp=4; IntAct=EBI-5657766, EBI-3866665;
CC P17027; Q13077: TRAF1; NbExp=3; IntAct=EBI-5657766, EBI-359224;
CC P17027; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-5657766, EBI-744794;
CC P17027; Q9Y3S2: ZNF330; NbExp=3; IntAct=EBI-5657766, EBI-373456;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P17027-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P17027-2; Sequence=VSP_055936;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AF507946; AAM33359.1; -; mRNA.
DR EMBL; BT007400; AAP36064.1; -; mRNA.
DR EMBL; AL080123; CAB45722.1; -; mRNA.
DR EMBL; AL833815; CAD38678.1; -; mRNA.
DR EMBL; AC010547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007256; AAH07256.1; -; mRNA.
DR EMBL; BC048974; AAH48974.1; -; mRNA.
DR EMBL; X52347; CAA36573.1; -; mRNA.
DR CCDS; CCDS10900.1; -. [P17027-1]
DR CCDS; CCDS76895.1; -. [P17027-2]
DR PIR; T12488; T12488.
DR RefSeq; NP_001291421.1; NM_001304492.1. [P17027-1]
DR RefSeq; NP_001291422.1; NM_001304493.1. [P17027-2]
DR RefSeq; NP_001291423.1; NM_001304494.1. [P17027-2]
DR RefSeq; NP_666016.1; NM_145911.2. [P17027-1]
DR AlphaFoldDB; P17027; -.
DR SMR; P17027; -.
DR BioGRID; 113402; 32.
DR IntAct; P17027; 25.
DR MINT; P17027; -.
DR STRING; 9606.ENSP00000377171; -.
DR iPTMnet; P17027; -.
DR PhosphoSitePlus; P17027; -.
DR BioMuta; ZNF23; -.
DR DMDM; 29840831; -.
DR EPD; P17027; -.
DR jPOST; P17027; -.
DR MassIVE; P17027; -.
DR MaxQB; P17027; -.
DR PaxDb; P17027; -.
DR PeptideAtlas; P17027; -.
DR PRIDE; P17027; -.
DR ProteomicsDB; 53428; -. [P17027-1]
DR ProteomicsDB; 73048; -.
DR Antibodypedia; 16582; 164 antibodies from 30 providers.
DR DNASU; 7571; -.
DR Ensembl; ENST00000357254.8; ENSP00000349796.4; ENSG00000167377.19. [P17027-1]
DR Ensembl; ENST00000393539.6; ENSP00000377171.2; ENSG00000167377.19. [P17027-1]
DR Ensembl; ENST00000428724.5; ENSP00000387673.3; ENSG00000167377.19. [P17027-1]
DR Ensembl; ENST00000564528.1; ENSP00000462429.1; ENSG00000167377.19. [P17027-2]
DR GeneID; 7571; -.
DR KEGG; hsa:7571; -.
DR UCSC; uc002fad.4; human. [P17027-1]
DR CTD; 7571; -.
DR DisGeNET; 7571; -.
DR GeneCards; ZNF23; -.
DR HGNC; HGNC:13023; ZNF23.
DR HPA; ENSG00000167377; Low tissue specificity.
DR MIM; 194527; gene.
DR neXtProt; NX_P17027; -.
DR OpenTargets; ENSG00000167377; -.
DR PharmGKB; PA37602; -.
DR VEuPathDB; HostDB:ENSG00000167377; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162377; -.
DR HOGENOM; CLU_002678_44_7_1; -.
DR InParanoid; P17027; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P17027; -.
DR TreeFam; TF350833; -.
DR PathwayCommons; P17027; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; P17027; -.
DR BioGRID-ORCS; 7571; 9 hits in 1104 CRISPR screens.
DR ChiTaRS; ZNF23; human.
DR GeneWiki; ZNF23; -.
DR GenomeRNAi; 7571; -.
DR Pharos; P17027; Tbio.
DR PRO; PR:P17027; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P17027; protein.
DR Bgee; ENSG00000167377; Expressed in cortical plate and 93 other tissues.
DR ExpressionAtlas; P17027; baseline and differential.
DR Genevisible; P17027; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
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:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 14.
DR SMART; SM00355; ZnF_C2H2; 16.
DR SUPFAM; SSF57667; SSF57667; 11.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 16.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 17.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..643
FT /note="Zinc finger protein 23"
FT /id="PRO_0000047351"
FT DOMAIN 1..43
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 168..190
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 196..218
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 224..246
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 252..274
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 280..302
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 308..330
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 336..358
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 364..386
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 392..414
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 420..442
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 448..470
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 476..498
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 504..526
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 532..554
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 560..582
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 588..610
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 616..638
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 157
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..58
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_055936"
FT VARIANT 28
FT /note="S -> G (in dbSNP:rs2070832)"
FT /id="VAR_024195"
FT CONFLICT 50
FT /note="Q -> E (in Ref. 5; CAB45722)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 643 AA; 73059 MW; A86682E8A75F5A45 CRC64;
MLENYGNVAS LGFPLLKPAV ISQLEGGSEL GGSSPLAAGT GLQGLQTDIQ TDNDLTKEMY
EGKENVSFEL QRDFSQETDF SEASLLEKQQ EVHSAGNIKK EKSNTIDGTV KDETSPVEEC
FFSQSSNSYQ CHTITGEQPS GCTGLGKSIS FDTKLVKHEI INSEERPFKC EELVEPFRCD
SQLIQHQENN TEEKPYQCSE CGKAFSINEK LIWHQRLHSG EKPFKCVECG KSFSYSSHYI
THQTIHSGEK PYQCKMCGKA FSVNGSLSRH QRIHTGEKPY QCKECGNGFS CSSAYITHQR
VHTGEKPYEC NDCGKAFNVN AKLIQHQRIH TGEKPYECNE CGKGFRCSSQ LRQHQSIHTG
EKPYQCKECG KGFNNNTKLI QHQRIHTGEK PYECTECGKA FSVKGKLIQH QRIHTGEKPY
ECNECGKAFR CNSQFRQHLR IHTGEKPYEC NECGKAFSVN GKLMRHQRIH TGEKPFECNE
CGRCFTSKRN LLDHHRIHTG EKPYQCKECG KAFSINAKLT RHQRIHTGEK PFKCMECEKA
FSCSSNYIVH QRIHTGEKPF QCKECGKAFH VNAHLIRHQR SHTGEKPFRC VECGKGFSFS
SDYIIHQTVH TWKKPYMCSV CGKAFRFSFQ LSQHQSVHSE GKS
