ZBT43_HUMAN
ID ZBT43_HUMAN Reviewed; 467 AA.
AC O43298; Q5JU96;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Zinc finger and BTB domain-containing protein 43;
DE AltName: Full=Zinc finger and BTB domain-containing protein 22B;
DE AltName: Full=Zinc finger protein 297B;
DE AltName: Full=ZnF-x;
GN Name=ZBTB43; Synonyms=KIAA0414, ZBTB22B, ZNF297B;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=9455477; DOI=10.1093/dnares/4.5.307;
RA Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VIII. 78
RT new cDNA clones from brain which code for large proteins in vitro.";
RL DNA Res. 4:307-313(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang X., Liu C.-X., Lisitsina M.N., Musco S., Lisitsyn N.A.;
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [7]
RP INTERACTION WITH BDP1.
RX PubMed=16542149; DOI=10.1515/bc.2006.037;
RA Schoenen F., Wirth B.;
RT "The zinc finger protein ZNF297B interacts with BDP1, a subunit of
RT TFIIIB.";
RL Biol. Chem. 387:277-284(2006).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-423, 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 [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-182; LYS-247 AND LYS-458, AND
RP IDENTIFICATION BY MASS 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 [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-247 AND LYS-458, 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 [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-182; LYS-241; LYS-247; LYS-297;
RP LYS-358 AND LYS-458, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [13]
RP STRUCTURE BY NMR OF 370-466.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of tandem repeat of the ZF-C2H2 domains of human zinc
RT finger protein 297B.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBUNIT: Interacts with BDP1. {ECO:0000269|PubMed:16542149}.
CC -!- INTERACTION:
CC O43298; Q8WTP8: AEN; NbExp=3; IntAct=EBI-740718, EBI-8637627;
CC O43298; Q9BXS5: AP1M1; NbExp=6; IntAct=EBI-740718, EBI-541426;
CC O43298; P36575: ARR3; NbExp=3; IntAct=EBI-740718, EBI-718116;
CC O43298; P49407: ARRB1; NbExp=5; IntAct=EBI-740718, EBI-743313;
CC O43298; P54253: ATXN1; NbExp=7; IntAct=EBI-740718, EBI-930964;
CC O43298; Q8IYE1: CCDC13; NbExp=3; IntAct=EBI-740718, EBI-10961312;
CC O43298; Q8IVW4: CDKL3; NbExp=3; IntAct=EBI-740718, EBI-3919850;
CC O43298; Q96Q77: CIB3; NbExp=3; IntAct=EBI-740718, EBI-10292696;
CC O43298; P26196: DDX6; NbExp=3; IntAct=EBI-740718, EBI-351257;
CC O43298; Q14689-6: DIP2A; NbExp=3; IntAct=EBI-740718, EBI-10233719;
CC O43298; Q3B820: FAM161A; NbExp=3; IntAct=EBI-740718, EBI-719941;
CC O43298; P25800: LMO1; NbExp=7; IntAct=EBI-740718, EBI-8639312;
CC O43298; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-740718, EBI-11742507;
CC O43298; P61968: LMO4; NbExp=3; IntAct=EBI-740718, EBI-2798728;
CC O43298; Q8TBB1: LNX1; NbExp=5; IntAct=EBI-740718, EBI-739832;
CC O43298; Q9UBU8-2: MORF4L1; NbExp=3; IntAct=EBI-740718, EBI-10288852;
CC O43298; Q15014: MORF4L2; NbExp=4; IntAct=EBI-740718, EBI-399257;
CC O43298; O43242: PSMD3; NbExp=7; IntAct=EBI-740718, EBI-357622;
CC O43298; Q5T7P8-2: SYT6; NbExp=6; IntAct=EBI-740718, EBI-10246152;
CC O43298; Q15560: TCEA2; NbExp=3; IntAct=EBI-740718, EBI-710310;
CC O43298; O43167: ZBTB24; NbExp=3; IntAct=EBI-740718, EBI-744471;
CC O43298; P15622-3: ZNF250; NbExp=3; IntAct=EBI-740718, EBI-10177272;
CC O43298; Q8TAU3: ZNF417; NbExp=4; IntAct=EBI-740718, EBI-740727;
CC O43298; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-740718, EBI-6427977;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA24844.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB007874; BAA24844.2; ALT_INIT; mRNA.
DR EMBL; AF049907; AAC05500.1; -; mRNA.
DR EMBL; BT007194; AAP35858.1; -; mRNA.
DR EMBL; AL161731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87643.1; -; Genomic_DNA.
DR EMBL; BC008828; AAH08828.1; -; mRNA.
DR CCDS; CCDS6867.1; -.
DR RefSeq; NP_001129248.1; NM_001135776.1.
DR RefSeq; NP_054726.1; NM_014007.3.
DR RefSeq; XP_005251892.1; XM_005251835.3.
DR RefSeq; XP_011516711.1; XM_011518409.1.
DR RefSeq; XP_011516713.1; XM_011518411.2.
DR PDB; 2CSH; NMR; -; A=370-466.
DR PDBsum; 2CSH; -.
DR AlphaFoldDB; O43298; -.
DR SMR; O43298; -.
DR BioGRID; 116727; 51.
DR IntAct; O43298; 32.
DR MINT; O43298; -.
DR STRING; 9606.ENSP00000362563; -.
DR iPTMnet; O43298; -.
DR PhosphoSitePlus; O43298; -.
DR BioMuta; ZBTB43; -.
DR EPD; O43298; -.
DR jPOST; O43298; -.
DR MassIVE; O43298; -.
DR PaxDb; O43298; -.
DR PeptideAtlas; O43298; -.
DR PRIDE; O43298; -.
DR ProteomicsDB; 48871; -.
DR Antibodypedia; 16550; 141 antibodies from 18 providers.
DR DNASU; 23099; -.
DR Ensembl; ENST00000373457.1; ENSP00000362556.1; ENSG00000169155.10.
DR Ensembl; ENST00000373464.5; ENSP00000362563.4; ENSG00000169155.10.
DR Ensembl; ENST00000449886.5; ENSP00000390344.1; ENSG00000169155.10.
DR GeneID; 23099; -.
DR KEGG; hsa:23099; -.
DR MANE-Select; ENST00000373464.5; ENSP00000362563.4; NM_014007.4; NP_054726.1.
DR UCSC; uc004bql.4; human.
DR CTD; 23099; -.
DR GeneCards; ZBTB43; -.
DR HGNC; HGNC:17908; ZBTB43.
DR HPA; ENSG00000169155; Tissue enhanced (bone).
DR MIM; 618676; gene.
DR neXtProt; NX_O43298; -.
DR OpenTargets; ENSG00000169155; -.
DR PharmGKB; PA38257; -.
DR VEuPathDB; HostDB:ENSG00000169155; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000160616; -.
DR HOGENOM; CLU_029118_2_0_1; -.
DR InParanoid; O43298; -.
DR OMA; IEMVAGI; -.
DR OrthoDB; 830409at2759; -.
DR PhylomeDB; O43298; -.
DR TreeFam; TF333162; -.
DR PathwayCommons; O43298; -.
DR SignaLink; O43298; -.
DR SIGNOR; O43298; -.
DR BioGRID-ORCS; 23099; 9 hits in 1137 CRISPR screens.
DR ChiTaRS; ZBTB43; human.
DR EvolutionaryTrace; O43298; -.
DR GenomeRNAi; 23099; -.
DR Pharos; O43298; Tdark.
DR PRO; PR:O43298; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; O43298; protein.
DR Bgee; ENSG00000169155; Expressed in buccal mucosa cell and 201 other tissues.
DR ExpressionAtlas; O43298; baseline and differential.
DR Genevisible; O43298; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0001025; F:RNA polymerase III general transcription initiation factor binding; IPI:ARUK-UCL.
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 Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; DNA-binding; Isopeptide bond; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..467
FT /note="Zinc finger and BTB domain-containing protein 43"
FT /id="PRO_0000047519"
FT DOMAIN 33..97
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 373..394
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 400..422
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 428..450
FT /note="C2H2-type 3; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 134..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 423
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 182
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 241
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 247
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 358
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 458
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT STRAND 380..383
FT /evidence="ECO:0007829|PDB:2CSH"
FT HELIX 384..394
FT /evidence="ECO:0007829|PDB:2CSH"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:2CSH"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:2CSH"
FT STRAND 408..412
FT /evidence="ECO:0007829|PDB:2CSH"
FT HELIX 413..419
FT /evidence="ECO:0007829|PDB:2CSH"
FT TURN 420..422
FT /evidence="ECO:0007829|PDB:2CSH"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:2CSH"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:2CSH"
FT HELIX 440..458
FT /evidence="ECO:0007829|PDB:2CSH"
SQ SEQUENCE 467 AA; 52630 MW; 9DFB6CEEB8562425 CRC64;
MEPGTNSFRV EFPDFSSTIL QKLNQQRQQG QLCDVSIVVQ GHIFRAHKAV LAASSPYFCD
QVLLKNSRRI VLPDVMNPRV FENILLSSYT GRLVMPAPEI VSYLTAASFL QMWHVVDKCT
EVLEGNPTVL CQKLNHGSDH QSPSSSSYNG LVESFELGSG GHTDFPKAQE LRDGENEEES
TKDELSSQLT EHEYLPSNSS TEHDRLSTEM ASQDGEEGAS DSAEFHYTRP MYSKPSIMAH
KRWIHVKPER LEQACEGMDV HATYDEHQVT ESINTVQTEH TVQPSGVEED FHIGEKKVEA
EFDEQADESN YDEQVDFYGS SMEEFSGERS DGNLIGHRQE AALAAGYSEN IEMVTGIKEE
ASHLGFSATD KLYPCQCGKS FTHKSQRDRH MSMHLGLRPY GCGVCGKKFK MKHHLVGHMK
IHTGIKPYEC NICAKRFMWR DSFHRHVTSC TKSYEAAKAE QNTTEAN
