ZBT42_HUMAN
ID ZBT42_HUMAN Reviewed; 422 AA.
AC B2RXF5; B7ZW21;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Zinc finger and BTB domain-containing protein 42;
GN Name=ZBTB42;
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 GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Brain cortex;
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 [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21193930; DOI=10.1007/s00439-010-0940-2;
RA Devaney S.A., Mate S.E., Devaney J.M., Hoffman E.P.;
RT "Characterization of the ZBTB42 gene in humans and mice.";
RL Hum. Genet. 129:433-441(2011).
RN [4]
RP INVOLVEMENT IN LCCS6, VARIANT LCCS6 HIS-397, AND CHARACTERIZATION OF
RP VARIANT LCCS6 HIS-397.
RX PubMed=25055871; DOI=10.1093/hmg/ddu384;
RA Patel N., Smith L.L., Faqeih E., Mohamed J., Gupta V.A., Alkuraya F.S.;
RT "ZBTB42 mutation defines a novel lethal congenital contracture syndrome
RT (LCCS6).";
RL Hum. Mol. Genet. 23:6584-6593(2014).
CC -!- FUNCTION: Transcriptional repressor. Specifically binds DNA and
CC probably acts by recruiting chromatin remodeling multiprotein
CC complexes. {ECO:0000250|UniProtKB:Q811H0}.
CC -!- INTERACTION:
CC B2RXF5; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-12287587, EBI-11954519;
CC B2RXF5; Q9NWX5: ASB6; NbExp=3; IntAct=EBI-12287587, EBI-6425205;
CC B2RXF5; Q7Z3C6-3: ATG9A; NbExp=3; IntAct=EBI-12287587, EBI-12006308;
CC B2RXF5; P51451: BLK; NbExp=3; IntAct=EBI-12287587, EBI-2105445;
CC B2RXF5; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-12287587, EBI-8643161;
CC B2RXF5; Q9NP86: CABP5; NbExp=3; IntAct=EBI-12287587, EBI-10311131;
CC B2RXF5; Q8NEC5: CATSPER1; NbExp=3; IntAct=EBI-12287587, EBI-744545;
CC B2RXF5; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-12287587, EBI-10171570;
CC B2RXF5; Q86X02: CDR2L; NbExp=3; IntAct=EBI-12287587, EBI-11063830;
CC B2RXF5; Q96AQ7: CIDEC; NbExp=3; IntAct=EBI-12287587, EBI-14151404;
CC B2RXF5; Q9BW66: CINP; NbExp=3; IntAct=EBI-12287587, EBI-739784;
CC B2RXF5; O95833: CLIC3; NbExp=3; IntAct=EBI-12287587, EBI-10192241;
CC B2RXF5; Q49AN0: CRY2; NbExp=3; IntAct=EBI-12287587, EBI-2212355;
CC B2RXF5; P56545-3: CTBP2; NbExp=3; IntAct=EBI-12287587, EBI-10171902;
CC B2RXF5; Q8IXW7: FMR1; NbExp=6; IntAct=EBI-12287587, EBI-11976595;
CC B2RXF5; P55040: GEM; NbExp=3; IntAct=EBI-12287587, EBI-744104;
CC B2RXF5; Q08379: GOLGA2; NbExp=3; IntAct=EBI-12287587, EBI-618309;
CC B2RXF5; Q96NT3-2: GUCD1; NbExp=3; IntAct=EBI-12287587, EBI-11978177;
CC B2RXF5; Q9H2F3: HSD3B7; NbExp=3; IntAct=EBI-12287587, EBI-3918847;
CC B2RXF5; O75031: HSF2BP; NbExp=3; IntAct=EBI-12287587, EBI-7116203;
CC B2RXF5; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-12287587, EBI-2556193;
CC B2RXF5; Q7L273: KCTD9; NbExp=3; IntAct=EBI-12287587, EBI-4397613;
CC B2RXF5; Q6A162: KRT40; NbExp=3; IntAct=EBI-12287587, EBI-10171697;
CC B2RXF5; Q96A72: MAGOHB; NbExp=3; IntAct=EBI-12287587, EBI-746778;
CC B2RXF5; P28482: MAPK1; NbExp=3; IntAct=EBI-12287587, EBI-959949;
CC B2RXF5; Q99750: MDFI; NbExp=3; IntAct=EBI-12287587, EBI-724076;
CC B2RXF5; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-12287587, EBI-10172526;
CC B2RXF5; Q13064: MKRN3; NbExp=3; IntAct=EBI-12287587, EBI-2340269;
CC B2RXF5; Q8WY64: MYLIP; NbExp=3; IntAct=EBI-12287587, EBI-6952711;
CC B2RXF5; O43639: NCK2; NbExp=3; IntAct=EBI-12287587, EBI-713635;
CC B2RXF5; Q9UHB4: NDOR1; NbExp=5; IntAct=EBI-12287587, EBI-10249760;
CC B2RXF5; Q9BVI4: NOC4L; NbExp=3; IntAct=EBI-12287587, EBI-395927;
CC B2RXF5; Q9UMX2-2: OAZ3; NbExp=3; IntAct=EBI-12287587, EBI-12049527;
CC B2RXF5; Q9UJX0: OSGIN1; NbExp=3; IntAct=EBI-12287587, EBI-9057006;
CC B2RXF5; P32242: OTX1; NbExp=3; IntAct=EBI-12287587, EBI-740446;
CC B2RXF5; Q13526: PIN1; NbExp=3; IntAct=EBI-12287587, EBI-714158;
CC B2RXF5; O60733: PLA2G6; NbExp=3; IntAct=EBI-12287587, EBI-12089905;
CC B2RXF5; O15160: POLR1C; NbExp=3; IntAct=EBI-12287587, EBI-1055079;
CC B2RXF5; O75771: RAD51D; NbExp=3; IntAct=EBI-12287587, EBI-1055693;
CC B2RXF5; Q96RF0: SNX18; NbExp=3; IntAct=EBI-12287587, EBI-298169;
CC B2RXF5; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-12287587, EBI-742688;
CC B2RXF5; Q9UL33-2: TRAPPC2L; NbExp=3; IntAct=EBI-12287587, EBI-11119202;
CC B2RXF5; Q6AZZ1: TRIM68; NbExp=3; IntAct=EBI-12287587, EBI-2130449;
CC B2RXF5; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-12287587, EBI-9090990;
CC B2RXF5; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-12287587, EBI-7353612;
CC B2RXF5; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-12287587, EBI-739895;
CC B2RXF5; Q05516: ZBTB16; NbExp=3; IntAct=EBI-12287587, EBI-711925;
CC B2RXF5; O15156-2: ZBTB7B; NbExp=3; IntAct=EBI-12287587, EBI-11522250;
CC B2RXF5; Q9Y3S2: ZNF330; NbExp=3; IntAct=EBI-12287587, EBI-373456;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q811H0}. Nucleus
CC {ECO:0000269|PubMed:21193930}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q811H0}. Note=In skeletal myofibers, highly
CC enriched in subsynaptic nuclei at the neuromuscular junctions.
CC {ECO:0000250|UniProtKB:Q811H0}.
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle (at protein level).
CC {ECO:0000269|PubMed:21193930}.
CC -!- DISEASE: Lethal congenital contracture syndrome 6 (LCCS6) [MIM:616248]:
CC A form of lethal congenital contracture syndrome, an autosomal
CC recessive disorder characterized by degeneration of anterior horn
CC neurons, extreme skeletal muscle atrophy and congenital non-progressive
CC joint contractures. The contractures can involve the upper or lower
CC limbs and/or the vertebral column, leading to various degrees of
CC flexion or extension limitations evident at birth. LCCS6 features
CC include severe polyhydramnios and absent stomach, in addition to
CC multiple contracture deformities. {ECO:0000269|PubMed:25055871}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. ZBTB18 subfamily. {ECO:0000305}.
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DR EMBL; AL590327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC157833; AAI57834.1; -; mRNA.
DR EMBL; BC171822; AAI71822.1; -; mRNA.
DR CCDS; CCDS45174.1; -.
DR RefSeq; NP_001131073.1; NM_001137601.2.
DR RefSeq; XP_016876400.1; XM_017020911.1.
DR AlphaFoldDB; B2RXF5; -.
DR SMR; B2RXF5; -.
DR BioGRID; 612563; 65.
DR IntAct; B2RXF5; 58.
DR STRING; 9606.ENSP00000409107; -.
DR iPTMnet; B2RXF5; -.
DR PhosphoSitePlus; B2RXF5; -.
DR BioMuta; ZBTB42; -.
DR jPOST; B2RXF5; -.
DR MassIVE; B2RXF5; -.
DR PaxDb; B2RXF5; -.
DR PeptideAtlas; B2RXF5; -.
DR PRIDE; B2RXF5; -.
DR ProteomicsDB; 3461; -.
DR Antibodypedia; 58775; 72 antibodies from 11 providers.
DR DNASU; 100128927; -.
DR Ensembl; ENST00000342537.8; ENSP00000409107.2; ENSG00000179627.10.
DR Ensembl; ENST00000555360.1; ENSP00000450673.1; ENSG00000179627.10.
DR GeneID; 100128927; -.
DR KEGG; hsa:100128927; -.
DR MANE-Select; ENST00000342537.8; ENSP00000409107.2; NM_001137601.3; NP_001131073.1.
DR UCSC; uc001ypp.4; human.
DR CTD; 100128927; -.
DR DisGeNET; 100128927; -.
DR GeneCards; ZBTB42; -.
DR HGNC; HGNC:32550; ZBTB42.
DR HPA; ENSG00000179627; Low tissue specificity.
DR MalaCards; ZBTB42; -.
DR MIM; 613915; gene.
DR MIM; 616248; phenotype.
DR neXtProt; NX_B2RXF5; -.
DR OpenTargets; ENSG00000179627; -.
DR PharmGKB; PA144596242; -.
DR VEuPathDB; HostDB:ENSG00000179627; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000163959; -.
DR HOGENOM; CLU_034521_0_0_1; -.
DR InParanoid; B2RXF5; -.
DR OMA; PCILQTP; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; B2RXF5; -.
DR TreeFam; TF337437; -.
DR PathwayCommons; B2RXF5; -.
DR SignaLink; B2RXF5; -.
DR BioGRID-ORCS; 100128927; 14 hits in 1079 CRISPR screens.
DR ChiTaRS; ZBTB42; human.
DR GenomeRNAi; 100128927; -.
DR Pharos; B2RXF5; Tbio.
DR PRO; PR:B2RXF5; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; B2RXF5; protein.
DR Bgee; ENSG00000179627; Expressed in parotid gland and 109 other tissues.
DR Genevisible; B2RXF5; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
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:0007517; P:muscle organ development; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
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; 2.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW Cytoplasm; Disease variant; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..422
FT /note="Zinc finger and BTB domain-containing protein 42"
FT /id="PRO_0000343711"
FT DOMAIN 24..92
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 294..316
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 334..356
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 362..384
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 390..413
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 121..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 397
FT /note="R -> H (in LCCS6; loss of function mutation;
FT dbSNP:rs730882163)"
FT /evidence="ECO:0000269|PubMed:25055871"
FT /id="VAR_073265"
FT CONFLICT 232
FT /note="E -> K (in Ref. 2; AAI57834/AAI71822)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 422 AA; 46491 MW; CA057072A5C67DE8 CRC64;
MEFPEHGGRL LGRLRQQREL GFLCDCTVLV GDARFPAHRA VLAACSVYFH LFYRDRPAGS
RDTVRLNGDI VTAPAFGRLL DFMYEGRLDL RSLPVEDVLA AASYLHMYDI VKVCKGRLQE
KDRSLDPGNP APGAEPAQPP CPWPVWTADL CPAARKAKLP PFGVKAALPP RASGPPPCQV
PEESDQALDL SLKSGPRQER VHPPCVLQTP LCSQRQPGAQ PLVKDERDSL SEQEESSSSR
SPHSPPKPPP VPAAKGLVVG LQPLPLSGEG SRELELGAGR LASEDELGPG GPLCICPLCS
KLFPSSHVLQ LHLSAHFRER DSTRARLSPD GVAPTCPLCG KTFSCTYTLK RHERTHSGEK
PYTCVQCGKS FQYSHNLSRH TVVHTREKPH ACRWCERRFT QSGDLYRHVR KFHCGLVKSL
LV
