ZBT34_HUMAN
ID ZBT34_HUMAN Reviewed; 500 AA.
AC Q8NCN2; Q38IA7; Q5VYE9;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 4.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Zinc finger and BTB domain-containing protein 34;
GN Name=ZBTB34; Synonyms=KIAA1993;
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], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=16718364; DOI=10.1007/s11010-006-9183-x;
RA Qi J., Zhang X., Zhang H.-K., Yang H.-M., Zhou Y.-B., Han Z.-G.;
RT "ZBTB34, a novel human BTB/POZ zinc finger protein, is a potential
RT transcriptional repressor.";
RL Mol. Cell. Biochem. 290:159-167(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=12056414; DOI=10.1093/dnares/9.2.47;
RA Ohara O., Nagase T., Mitsui G., Kohga H., Kikuno R., Hiraoka S.,
RA Takahashi Y., Kitajima S., Saga Y., Koseki H.;
RT "Characterization of size-fractionated cDNA libraries generated by the in
RT vitro recombination-assisted method.";
RL DNA Res. 9:47-57(2002).
RN [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164 AND SER-463, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [5]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-235; LYS-237; LYS-426 AND
RP LYS-474, AND IDENTIFICATION BY MASS 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 a transcriptional repressor.
CC {ECO:0000269|PubMed:16718364}.
CC -!- INTERACTION:
CC Q8NCN2; Q9BYV9: BACH2; NbExp=3; IntAct=EBI-11317716, EBI-1642333;
CC Q8NCN2; Q8N2W9: PIAS4; NbExp=3; IntAct=EBI-11317716, EBI-473160;
CC Q8NCN2; P78317: RNF4; NbExp=3; IntAct=EBI-11317716, EBI-2340927;
CC Q8NCN2; Q9Y2W6: TDRKH; NbExp=3; IntAct=EBI-11317716, EBI-12842466;
CC Q8NCN2; Q9HCK0: ZBTB26; NbExp=3; IntAct=EBI-11317716, EBI-3918996;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16718364}.
CC -!- TISSUE SPECIFICITY: Expressed in several tissues, including heart,
CC brain, thymus, skeletal muscle, small intestine, testis, kidney,
CC placenta, peripheral blood cells and adult and fetal liver.
CC {ECO:0000269|PubMed:16718364}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABA86591.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC02702.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ227306; ABA86591.1; ALT_INIT; mRNA.
DR EMBL; AB082524; BAC02702.1; ALT_INIT; mRNA.
DR EMBL; AL354944; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001092740.1; NM_001099270.1.
DR RefSeq; XP_011517001.1; XM_011518699.2.
DR AlphaFoldDB; Q8NCN2; -.
DR SMR; Q8NCN2; -.
DR BioGRID; 135630; 29.
DR IntAct; Q8NCN2; 14.
DR MINT; Q8NCN2; -.
DR STRING; 9606.ENSP00000362551; -.
DR iPTMnet; Q8NCN2; -.
DR PhosphoSitePlus; Q8NCN2; -.
DR BioMuta; ZBTB34; -.
DR DMDM; 308153674; -.
DR EPD; Q8NCN2; -.
DR jPOST; Q8NCN2; -.
DR MassIVE; Q8NCN2; -.
DR MaxQB; Q8NCN2; -.
DR PaxDb; Q8NCN2; -.
DR PeptideAtlas; Q8NCN2; -.
DR PRIDE; Q8NCN2; -.
DR ProteomicsDB; 72912; -.
DR Antibodypedia; 7766; 46 antibodies from 13 providers.
DR DNASU; 403341; -.
DR Ensembl; ENST00000373452.2; ENSP00000362551.2; ENSG00000177125.5.
DR GeneID; 403341; -.
DR KEGG; hsa:403341; -.
DR UCSC; uc004bqm.5; human.
DR CTD; 403341; -.
DR GeneCards; ZBTB34; -.
DR HGNC; HGNC:31446; ZBTB34.
DR HPA; ENSG00000177125; Low tissue specificity.
DR MIM; 611692; gene.
DR neXtProt; NX_Q8NCN2; -.
DR OpenTargets; ENSG00000177125; -.
DR PharmGKB; PA134869916; -.
DR VEuPathDB; HostDB:ENSG00000177125; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000159944; -.
DR HOGENOM; CLU_029118_2_0_1; -.
DR InParanoid; Q8NCN2; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8NCN2; -.
DR TreeFam; TF331184; -.
DR PathwayCommons; Q8NCN2; -.
DR SignaLink; Q8NCN2; -.
DR BioGRID-ORCS; 403341; 15 hits in 1106 CRISPR screens.
DR GenomeRNAi; 403341; -.
DR Pharos; Q8NCN2; Tdark.
DR PRO; PR:Q8NCN2; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q8NCN2; protein.
DR Bgee; ENSG00000177125; Expressed in amniotic fluid and 180 other tissues.
DR ExpressionAtlas; Q8NCN2; baseline and differential.
DR Genevisible; Q8NCN2; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor 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: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; 3.
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; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..500
FT /note="Zinc finger and BTB domain-containing protein 34"
FT /id="PRO_0000047740"
FT DOMAIN 32..96
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 372..394
FT /note="C2H2-type 1"
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..451
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 164..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 235
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 237
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 426
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 474
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
SQ SEQUENCE 500 AA; 55534 MW; FCDB4408355F3F26 CRC64;
MDSSSFIQFD VPEYSSTVLS QLNELRLQGK LCDIIVHIQG QPFRAHKAVL AASSPYFRDH
SALSTMSGLS ISVIKNPNVF EQLLSFCYTG RMSLQLKDVV SFLTAASFLQ MQCVIDKCTQ
ILESIHSKIS VGDVDSVTVG AEENPESRNG VKDSSFFANP VEISPPYCSQ GRQPTASSDL
RMETTPSKAL RSRLQEEGHS DRGSSGSVSE YEIQIEGDHE QGDLLVRESQ ITEVKVKMEK
SDRPSCSDSS SLGDDGYHTE MVDGEQVVAV NVGSYGSVLQ HAYSYSQAAS QPTNVSEAFG
SLSNSSPSRS MLSCFRGGRA RQKRALSVHL HSDLQGLVQG SDSEAMMNNP GYESSPRERS
ARGHWYPYNE RLICIYCGKS FNQKGSLDRH MRLHMGITPF VCKFCGKKYT RKDQLEYHIR
GHTDDKPFRC EICGKCFPFQ GTLNQHLRKN HPGVAEVRSR IESPERTDVY VEQKLENDAS
ASEMGLDSRM EIHTVSDAPD
