ZBT39_HUMAN
ID ZBT39_HUMAN Reviewed; 712 AA.
AC O15060; A7MD38; Q9UD98;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Zinc finger and BTB domain-containing protein 39;
GN Name=ZBTB39; Synonyms=KIAA0352;
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=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-82.
RC TISSUE=Brain;
RX PubMed=8358434; DOI=10.1038/ng0793-256;
RA Adams M.D., Kerlavage A.R., Fields C., Venter J.C.;
RT "3,400 new expressed sequence tags identify diversity of transcripts in
RT human brain.";
RL Nat. Genet. 4:256-267(1993).
RN [6]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-183 AND LYS-439, 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: May be involved in transcriptional regulation.
CC -!- INTERACTION:
CC O15060; P29972: AQP1; NbExp=3; IntAct=EBI-9995672, EBI-745213;
CC O15060; O95995: GAS8; NbExp=3; IntAct=EBI-9995672, EBI-1052570;
CC O15060; Q14005-2: IL16; NbExp=3; IntAct=EBI-9995672, EBI-17178971;
CC O15060; O60341: KDM1A; NbExp=3; IntAct=EBI-9995672, EBI-710124;
CC O15060; O00444: PLK4; NbExp=3; IntAct=EBI-9995672, EBI-746202;
CC O15060; Q13200: PSMD2; NbExp=3; IntAct=EBI-9995672, EBI-357648;
CC O15060; P61956: SUMO2; NbExp=3; IntAct=EBI-9995672, EBI-473220;
CC O15060; P55854: SUMO3; NbExp=3; IntAct=EBI-9995672, EBI-474067;
CC O15060; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-9995672, EBI-11955057;
CC O15060; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-9995672, EBI-725997;
CC O15060; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-9995672, EBI-744794;
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=BAA20809.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB002350; BAA20809.2; ALT_INIT; mRNA.
DR EMBL; AK292468; BAF85157.1; -; mRNA.
DR EMBL; CH471054; EAW96971.1; -; Genomic_DNA.
DR EMBL; BC140890; AAI40891.1; -; mRNA.
DR EMBL; BC146867; AAI46868.1; -; mRNA.
DR EMBL; BC152461; AAI52462.1; -; mRNA.
DR CCDS; CCDS31839.1; -.
DR RefSeq; NP_055645.1; NM_014830.2.
DR AlphaFoldDB; O15060; -.
DR SMR; O15060; -.
DR BioGRID; 115211; 25.
DR IntAct; O15060; 15.
DR STRING; 9606.ENSP00000300101; -.
DR iPTMnet; O15060; -.
DR PhosphoSitePlus; O15060; -.
DR BioMuta; ZBTB39; -.
DR EPD; O15060; -.
DR jPOST; O15060; -.
DR MassIVE; O15060; -.
DR MaxQB; O15060; -.
DR PaxDb; O15060; -.
DR PeptideAtlas; O15060; -.
DR PRIDE; O15060; -.
DR ProteomicsDB; 48410; -.
DR ABCD; O15060; 7 sequenced antibodies.
DR Antibodypedia; 28418; 117 antibodies from 17 providers.
DR DNASU; 9880; -.
DR Ensembl; ENST00000300101.3; ENSP00000300101.2; ENSG00000166860.3.
DR GeneID; 9880; -.
DR KEGG; hsa:9880; -.
DR MANE-Select; ENST00000300101.3; ENSP00000300101.2; NM_014830.3; NP_055645.1.
DR UCSC; uc001sml.3; human.
DR CTD; 9880; -.
DR DisGeNET; 9880; -.
DR GeneCards; ZBTB39; -.
DR HGNC; HGNC:29014; ZBTB39.
DR HPA; ENSG00000166860; Low tissue specificity.
DR MIM; 619384; gene.
DR neXtProt; NX_O15060; -.
DR OpenTargets; ENSG00000166860; -.
DR PharmGKB; PA142670543; -.
DR VEuPathDB; HostDB:ENSG00000166860; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000160722; -.
DR HOGENOM; CLU_391778_0_0_1; -.
DR InParanoid; O15060; -.
DR OMA; RACHATF; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; O15060; -.
DR TreeFam; TF350825; -.
DR PathwayCommons; O15060; -.
DR SignaLink; O15060; -.
DR BioGRID-ORCS; 9880; 51 hits in 1120 CRISPR screens.
DR GenomeRNAi; 9880; -.
DR Pharos; O15060; Tdark.
DR PRO; PR:O15060; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O15060; protein.
DR Bgee; ENSG00000166860; Expressed in oocyte and 130 other tissues.
DR Genevisible; O15060; HS.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
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; 2.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 5.
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 DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..712
FT /note="Zinc finger and BTB domain-containing protein 39"
FT /id="PRO_0000047744"
FT DOMAIN 30..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; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 480..502
FT /note="C2H2-type 3; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 508..530
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 538..560
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 605..627
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 633..655
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 661..683
FT /note="C2H2-type 8; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 129..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..212
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 183
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 439
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 689
FT /note="P -> A (in dbSNP:rs3741576)"
FT /id="VAR_019985"
SQ SEQUENCE 712 AA; 79001 MW; E09D2E2AEE35EF1A CRC64;
MGMRIKLQST NHPNNLLKEL NKCRLSETMC DVTIVVGSRS FPAHKAVLAC AAGYFQNLFL
NTGLDAARTY VVDFITPANF EKVLSFVYTS ELFTDLINVG VIYEVAERLG MEDLLQACHS
TFPDLESTAR AKPLTSTSES HSGTLSCPSA EPAHPLGELR GGGDYLGADR NYVLPSDAGG
SYKEEEKNVA SDANHSLHLP QPPPPPPKTE DHDTPAPFTS IPSMMTQPLL GTVSTGIQTS
TSSCQPYKVQ SNGDFSKNSF LTPDNAVDIT TGTNSCLSNS EHSKDPGFGQ MDELQLEDLG
DDDLQFEDPA EDIGTTEEVI ELSDDSEDEL AFGENDNREN KAMPCQVCKK VLEPNIQLIR
QHARDHVDLL TGNCKVCETH FQDRNSRVTH VLSHIGIFLF SCDMCETKFF TQWQLTLHRR
DGIFENNIIV HPNDPLPGKL GLFSGAASPE LKCAACGKVL AKDFHVVRGH ILDHLNLKGQ
ACSVCDQRHL NLCSLMWHTL SHLGISVFSC SVCANSFVDW HLLEKHMAVH QSLEDALFHC
RLCSQSFKSE AAYRYHVSQH KCNSGLDARP GFGLQHPALQ KRKLPAEEFL GEELALQGQP
GNSKYSCKVC GKRFAHTSEF NYHRRIHTGE KPYQCKVCHK FFRGRSTIKC HLKTHSGALM
YRCTVCGHYS STLNLMSKHV GVHKGSLPPD FTIEQTFMYI IHSKEADKNP DS
