ZBT14_HUMAN
ID ZBT14_HUMAN Reviewed; 449 AA.
AC O43829; O00403; Q2TB80;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Zinc finger and BTB domain-containing protein 14;
DE AltName: Full=Zinc finger protein 161 homolog;
DE Short=Zfp-161;
DE AltName: Full=Zinc finger protein 478;
DE AltName: Full=Zinc finger protein 5 homolog;
DE Short=ZF5;
DE Short=Zfp-5;
DE Short=hZF5;
GN Name=ZBTB14; Synonyms=ZFP161, ZNF478;
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].
RC TISSUE=Nasal polyp;
RX PubMed=9244432; DOI=10.1006/geno.1997.4784;
RA Sobek-Klocke I., Disque-Kochem C., Ronsiek M., Klocke R., Jockusch H.,
RA Breuning A., Ponstingl H., Rojas K., Overhauser J., Eichenlaub-Ritter U.;
RT "The human gene ZFP161 on 18p11.21-pter encodes a putative c-myc repressor
RT and is homologous to murine Zfp161 (Chr 17) and Zfp161-rs1 (X Chr).";
RL Genomics 43:156-164(1997).
RN [2]
RP ERRATUM OF PUBMED:9244432.
RA Sobek-Klocke I., Disque-Kochem C., Ronsiek M., Klocke R., Jockusch H.,
RA Breuning A., Ponstingl H., Rojas K., Overhauser J., Eichenlaub-Ritter U.;
RL Genomics 45:633-633(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cervix carcinoma;
RX PubMed=9177479; DOI=10.1016/s0167-4781(97)00045-6;
RA Sugiura K., Muro Y., Nagai Y., Kamimoto T., Wakabayashi T., Ohashi M.,
RA Hagiwara M.;
RT "Expression cloning and intracellular localization of a human ZF5
RT homologue.";
RL Biochim. Biophys. Acta 1352:23-26(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP FUNCTION.
RC TISSUE=Hepatoma;
RX PubMed=17714511; DOI=10.1111/j.1742-4658.2007.06006.x;
RA Orlov S.V., Kuteykin-Teplyakov K.B., Ignatovich I.A., Dizhe E.B.,
RA Mirgorodskaya O.A., Grishin A.V., Guzhova O.B., Prokhortchouk E.B.,
RA Guliy P.V., Perevozchikov A.P.;
RT "Novel repressor of the human FMR1 gene - identification of p56 human
RT (GCC)(n)-binding protein as a Kruppel-like transcription factor ZF5.";
RL FEBS J. 274:4848-4862(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 DOPAMINE TRANSPORTER ACTIVATION.
RX PubMed=14706637; DOI=10.1016/j.bbrc.2003.11.183;
RA Lee K.H., Kwak Y.D., Kim D.H., Chang M.Y., Lee Y.S., Lee Y.S.;
RT "Human zinc finger protein 161, a novel transcriptional activator of the
RT dopamine transporter.";
RL Biochem. Biophys. Res. Commun. 313:969-976(2004).
RN [7]
RP INTERACTION WITH ZBTB21, AND SUBCELLULAR LOCATION.
RC TISSUE=Fetal kidney, and Testis;
RX PubMed=15629158; DOI=10.1016/j.bbrc.2004.12.048;
RA Wang J., Kudoh J., Takayanagi A., Shimizu N.;
RT "Novel human BTB/POZ domain-containing zinc finger protein ZNF295 is
RT directly associated with ZFP161.";
RL Biochem. Biophys. Res. Commun. 327:615-627(2005).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-46; LYS-203 AND LYS-249, AND
RP 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: Transcriptional activator of the dopamine transporter (DAT),
CC binding it's promoter at the consensus sequence 5'-CCTGCACAGTTCACGGA-
CC 3'. Binds to 5'-d(GCC)(n)-3' trinucleotide repeats in promoter regions
CC and acts as a repressor of the FMR1 gene. Transcriptional repressor of
CC MYC and thymidine kinase promoters. {ECO:0000269|PubMed:17714511}.
CC -!- SUBUNIT: Interacts with ZBTB21. {ECO:0000269|PubMed:15629158}.
CC -!- INTERACTION:
CC O43829; Q9BXS5: AP1M1; NbExp=6; IntAct=EBI-10176632, EBI-541426;
CC O43829; P48047: ATP5PO; NbExp=3; IntAct=EBI-10176632, EBI-355815;
CC O43829; Q9UIF8-2: BAZ2B; NbExp=3; IntAct=EBI-10176632, EBI-10321972;
CC O43829; Q13895: BYSL; NbExp=8; IntAct=EBI-10176632, EBI-358049;
CC O43829; Q2NKX9: C2orf68; NbExp=3; IntAct=EBI-10176632, EBI-11603468;
CC O43829; Q9Y6Q1: CAPN6; NbExp=3; IntAct=EBI-10176632, EBI-7183095;
CC O43829; P55212: CASP6; NbExp=3; IntAct=EBI-10176632, EBI-718729;
CC O43829; Q9HC52: CBX8; NbExp=6; IntAct=EBI-10176632, EBI-712912;
CC O43829; Q00536: CDK16; NbExp=3; IntAct=EBI-10176632, EBI-726261;
CC O43829; Q00536-3: CDK16; NbExp=3; IntAct=EBI-10176632, EBI-12401765;
CC O43829; Q8IVW4: CDKL3; NbExp=3; IntAct=EBI-10176632, EBI-3919850;
CC O43829; Q96LK0: CEP19; NbExp=6; IntAct=EBI-10176632, EBI-741885;
CC O43829; P99999: CYCS; NbExp=3; IntAct=EBI-10176632, EBI-446479;
CC O43829; P26196: DDX6; NbExp=3; IntAct=EBI-10176632, EBI-351257;
CC O43829; Q96JC9: EAF1; NbExp=3; IntAct=EBI-10176632, EBI-769261;
CC O43829; Q8N9N8: EIF1AD; NbExp=3; IntAct=EBI-10176632, EBI-750700;
CC O43829; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-10176632, EBI-744099;
CC O43829; Q7L775: EPM2AIP1; NbExp=6; IntAct=EBI-10176632, EBI-6255981;
CC O43829; Q3B820: FAM161A; NbExp=3; IntAct=EBI-10176632, EBI-719941;
CC O43829; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-10176632, EBI-6658203;
CC O43829; P22607: FGFR3; NbExp=3; IntAct=EBI-10176632, EBI-348399;
CC O43829; Q9H8Y8: GORASP2; NbExp=4; IntAct=EBI-10176632, EBI-739467;
CC O43829; Q14957: GRIN2C; NbExp=3; IntAct=EBI-10176632, EBI-8285963;
CC O43829; P06396: GSN; NbExp=3; IntAct=EBI-10176632, EBI-351506;
CC O43829; O00291: HIP1; NbExp=3; IntAct=EBI-10176632, EBI-473886;
CC O43829; P01112: HRAS; NbExp=3; IntAct=EBI-10176632, EBI-350145;
CC O43829; Q68E01: INTS3; NbExp=3; IntAct=EBI-10176632, EBI-2680854;
CC O43829; Q92993: KAT5; NbExp=3; IntAct=EBI-10176632, EBI-399080;
CC O43829; O14901: KLF11; NbExp=3; IntAct=EBI-10176632, EBI-948266;
CC O43829; Q5T3J3: LRIF1; NbExp=3; IntAct=EBI-10176632, EBI-473196;
CC O43829; Q15013: MAD2L1BP; NbExp=6; IntAct=EBI-10176632, EBI-712181;
CC O43829; P55081: MFAP1; NbExp=3; IntAct=EBI-10176632, EBI-1048159;
CC O43829; Q15014: MORF4L2; NbExp=3; IntAct=EBI-10176632, EBI-399257;
CC O43829; Q9Y3B7: MRPL11; NbExp=3; IntAct=EBI-10176632, EBI-5453723;
CC O43829; P41227: NAA10; NbExp=6; IntAct=EBI-10176632, EBI-747693;
CC O43829; Q9BSU3: NAA11; NbExp=3; IntAct=EBI-10176632, EBI-2585120;
CC O43829; Q96CV9: OPTN; NbExp=3; IntAct=EBI-10176632, EBI-748974;
CC O43829; Q9BRL4: PCTK1; NbExp=3; IntAct=EBI-10176632, EBI-10296950;
CC O43829; Q13526: PIN1; NbExp=3; IntAct=EBI-10176632, EBI-714158;
CC O43829; Q96T60: PNKP; NbExp=6; IntAct=EBI-10176632, EBI-1045072;
CC O43829; P62875: POLR2L; NbExp=3; IntAct=EBI-10176632, EBI-359527;
CC O43829; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-10176632, EBI-5280197;
CC O43829; P62826: RAN; NbExp=3; IntAct=EBI-10176632, EBI-286642;
CC O43829; Q8N451: RNASEH2B; NbExp=3; IntAct=EBI-10176632, EBI-12177615;
CC O43829; D3DU92: RNPS1; NbExp=3; IntAct=EBI-10176632, EBI-10176640;
CC O43829; P32969: RPL9P9; NbExp=3; IntAct=EBI-10176632, EBI-358122;
CC O43829; P62851: RPS25; NbExp=3; IntAct=EBI-10176632, EBI-353054;
CC O43829; P62081: RPS7; NbExp=4; IntAct=EBI-10176632, EBI-354360;
CC O43829; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-10176632, EBI-748391;
CC O43829; O00560: SDCBP; NbExp=3; IntAct=EBI-10176632, EBI-727004;
CC O43829; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-10176632, EBI-2623095;
CC O43829; P08579: SNRPB2; NbExp=6; IntAct=EBI-10176632, EBI-1053651;
CC O43829; Q17RD7: SYT16; NbExp=3; IntAct=EBI-10176632, EBI-10238936;
CC O43829; Q8N8B7: TCEANC; NbExp=3; IntAct=EBI-10176632, EBI-954696;
CC O43829; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-10176632, EBI-11955057;
CC O43829; Q5T7W7: TSTD2; NbExp=3; IntAct=EBI-10176632, EBI-8994397;
CC O43829; Q99757: TXN2; NbExp=3; IntAct=EBI-10176632, EBI-2932492;
CC O43829; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-10176632, EBI-741480;
CC O43829; O14904: WNT9A; NbExp=3; IntAct=EBI-10176632, EBI-12053451;
CC O43829; Q8TBK6: ZCCHC10; NbExp=3; IntAct=EBI-10176632, EBI-597063;
CC O43829; Q96NC0: ZMAT2; NbExp=3; IntAct=EBI-10176632, EBI-2682299;
CC O43829; Q96BH6; NbExp=3; IntAct=EBI-10176632, EBI-25872486;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15629158}.
CC Note=Colocalizes with ZBTB21 in nucleus in HEK293 cells.
CC -!- DOMAIN: The BTB/POZ domain seems to direct the protein to discrete
CC regions in the nucleus.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; Y12726; CAA73258.1; -; mRNA.
DR EMBL; D89859; BAA20131.1; -; mRNA.
DR EMBL; BC110519; AAI10520.1; -; mRNA.
DR CCDS; CCDS11837.1; -.
DR RefSeq; NP_001137295.1; NM_001143823.2.
DR RefSeq; NP_001230631.1; NM_001243702.1.
DR RefSeq; NP_001230633.1; NM_001243704.1.
DR RefSeq; NP_003400.2; NM_003409.4.
DR AlphaFoldDB; O43829; -.
DR SMR; O43829; -.
DR BioGRID; 113373; 75.
DR IntAct; O43829; 74.
DR STRING; 9606.ENSP00000349503; -.
DR iPTMnet; O43829; -.
DR PhosphoSitePlus; O43829; -.
DR BioMuta; ZBTB14; -.
DR EPD; O43829; -.
DR jPOST; O43829; -.
DR MassIVE; O43829; -.
DR MaxQB; O43829; -.
DR PaxDb; O43829; -.
DR PeptideAtlas; O43829; -.
DR PRIDE; O43829; -.
DR ProteomicsDB; 49195; -.
DR Antibodypedia; 21919; 64 antibodies from 18 providers.
DR DNASU; 7541; -.
DR Ensembl; ENST00000357006.8; ENSP00000349503.4; ENSG00000198081.11.
DR Ensembl; ENST00000400143.7; ENSP00000383009.3; ENSG00000198081.11.
DR Ensembl; ENST00000614697.4; ENSP00000484129.1; ENSG00000198081.11.
DR Ensembl; ENST00000615385.4; ENSP00000478971.1; ENSG00000198081.11.
DR Ensembl; ENST00000651870.1; ENSP00000499212.1; ENSG00000198081.11.
DR GeneID; 7541; -.
DR KEGG; hsa:7541; -.
DR MANE-Select; ENST00000651870.1; ENSP00000499212.1; NM_001243702.2; NP_001230631.1.
DR UCSC; uc002kmq.4; human.
DR CTD; 7541; -.
DR DisGeNET; 7541; -.
DR GeneCards; ZBTB14; -.
DR HGNC; HGNC:12860; ZBTB14.
DR HPA; ENSG00000198081; Low tissue specificity.
DR MIM; 602126; gene.
DR neXtProt; NX_O43829; -.
DR OpenTargets; ENSG00000198081; -.
DR PharmGKB; PA37449; -.
DR VEuPathDB; HostDB:ENSG00000198081; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158052; -.
DR HOGENOM; CLU_697455_0_0_1; -.
DR InParanoid; O43829; -.
DR OMA; KMIEHMG; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; O43829; -.
DR TreeFam; TF333100; -.
DR PathwayCommons; O43829; -.
DR SignaLink; O43829; -.
DR SIGNOR; O43829; -.
DR BioGRID-ORCS; 7541; 30 hits in 1140 CRISPR screens.
DR ChiTaRS; ZBTB14; human.
DR GeneWiki; ZFP161; -.
DR GenomeRNAi; 7541; -.
DR Pharos; O43829; Tbio.
DR PRO; PR:O43829; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; O43829; protein.
DR Bgee; ENSG00000198081; Expressed in calcaneal tendon and 161 other tissues.
DR ExpressionAtlas; O43829; baseline and differential.
DR Genevisible; O43829; HS.
DR GO; GO:0016235; C:aggresome; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
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:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0003279; P:cardiac septum development; IEA:Ensembl.
DR GO; GO:0060976; P:coronary vasculature development; IEA:Ensembl.
DR GO; GO:0003170; P:heart valve development; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
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; 4.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..449
FT /note="Zinc finger and BTB domain-containing protein 14"
FT /id="PRO_0000047317"
FT DOMAIN 36..102
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 277..304
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 305..332
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 333..360
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 361..388
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 389..417
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 153..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 50..66
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 158..175
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 46
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 203
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 77
FT /note="E -> G (in dbSNP:rs7235740)"
FT /id="VAR_027810"
FT VARIANT 139
FT /note="Q -> R (in dbSNP:rs7235420)"
FT /id="VAR_027811"
FT CONFLICT 5
FT /note="I -> V (in Ref. 1; CAA73258)"
FT /evidence="ECO:0000305"
FT CONFLICT 160..161
FT /note="DD -> GC (in Ref. 1; CAA73258)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 449 AA; 50956 MW; B99F22E3B1D4E6CE CRC64;
MEFFISMSET IKYNDDDHKT LFLKTLNEQR LEGEFCDIAI VVEDVKFRAH RCVLAACSTY
FKKLFKKLEV DSSSVIEIDF LRSDIFEEVL NYMYTAKISV KKEDVNLMMS SGQILGIRFL
DKLCSQKRDV SSPDENNGQS KSKYCLKINR PIGDAADTQD DDVEEIGDQD DSPSDDTVEG
TPPSQEDGKS PTTTLRVQEA ILKELGSEEV RKVNCYGQEV ESMETPESKD LGSQTPQALT
FNDGMSEVKD EQTPGWTTAA SDMKFEYLLY GHHREQIACQ ACGKTFSDEG RLRKHEKLHT
ADRPFVCEMC TKGFTTQAHL KEHLKIHTGY KPYSCEVCGK SFIRAPDLKK HERVHSNERP
FACHMCDKAF KHKSHLKDHE RRHRGEKPFV CGSCTKAFAK ASDLKRHENN MHSERKQVTP
SAIQSETEQL QAAAMAAEAE QQLETIACS
