ZBT25_HUMAN
ID ZBT25_HUMAN Reviewed; 435 AA.
AC P24278; B3KUX6; Q8IYH9;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Zinc finger and BTB domain-containing protein 25;
DE AltName: Full=Zinc finger protein 46;
DE AltName: Full=Zinc finger protein KUP;
GN Name=ZBTB25; Synonyms=C14orf51, KUP, ZNF46;
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].
RX PubMed=2027750; DOI=10.1093/nar/19.7.1431;
RA Chardin P., Courtois G., Mattei M.-G., Gisselbrecht S.;
RT "The KUP gene, located on human chromosome 14, encodes a protein with two
RT distant zinc fingers.";
RL Nucleic Acids Res. 19:1431-1436(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
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=Blood;
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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-204, AND IDENTIFICATION BY MASS
RP 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 [6]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-142; LYS-148; LYS-198; LYS-204;
RP LYS-303; LYS-330 AND LYS-405, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 P24278; Q96GX9: APIP; NbExp=3; IntAct=EBI-739899, EBI-359248;
CC P24278; Q8N4Y2-3: CRACR2B; NbExp=3; IntAct=EBI-739899, EBI-11982645;
CC P24278; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-739899, EBI-3867333;
CC P24278; P35638-2: DDIT3; NbExp=3; IntAct=EBI-739899, EBI-10173632;
CC P24278; O75506: HSBP1; NbExp=3; IntAct=EBI-739899, EBI-748664;
CC P24278; O43464: HTRA2; NbExp=3; IntAct=EBI-739899, EBI-517086;
CC P24278; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-739899, EBI-1055254;
CC P24278; Q719H9: KCTD1; NbExp=3; IntAct=EBI-739899, EBI-9027502;
CC P24278; Q7L273: KCTD9; NbExp=3; IntAct=EBI-739899, EBI-4397613;
CC P24278; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-739899, EBI-10171774;
CC P24278; Q9BYP8: KRTAP17-1; NbExp=3; IntAct=EBI-739899, EBI-11988175;
CC P24278; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-739899, EBI-741037;
CC P24278; Q99750: MDFI; NbExp=2; IntAct=EBI-739899, EBI-724076;
CC P24278; Q96PV4: PNMA5; NbExp=4; IntAct=EBI-739899, EBI-10171633;
CC P24278; P49903: SEPHS1; NbExp=7; IntAct=EBI-739899, EBI-714091;
CC P24278; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-739899, EBI-5235340;
CC P24278; Q13148: TARDBP; NbExp=3; IntAct=EBI-739899, EBI-372899;
CC P24278; Q92609: TBC1D5; NbExp=3; IntAct=EBI-739899, EBI-742381;
CC P24278; Q15025: TNIP1; NbExp=6; IntAct=EBI-739899, EBI-357849;
CC P24278; Q12933: TRAF2; NbExp=4; IntAct=EBI-739899, EBI-355744;
CC P24278; Q9Y4K3: TRAF6; NbExp=3; IntAct=EBI-739899, EBI-359276;
CC P24278; Q96PN8: TSSK3; NbExp=3; IntAct=EBI-739899, EBI-3918381;
CC P24278; P55072: VCP; NbExp=3; IntAct=EBI-739899, EBI-355164;
CC P24278; Q2NL98: VMAC; NbExp=3; IntAct=EBI-739899, EBI-2803134;
CC P24278; Q9Y2K1: ZBTB1; NbExp=4; IntAct=EBI-739899, EBI-2682961;
CC P24278; Q8N680: ZBTB2; NbExp=3; IntAct=EBI-739899, EBI-2515601;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Expressed mainly in hematopoietic cells and testis.
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DR EMBL; X16576; CAA34595.1; -; mRNA.
DR EMBL; AK098181; BAG53588.1; -; mRNA.
DR EMBL; CH471061; EAW80861.1; -; Genomic_DNA.
DR EMBL; BC035804; AAH35804.1; -; mRNA.
DR CCDS; CCDS9765.1; -.
DR PIR; S15647; S15647.
DR RefSeq; NP_001291436.1; NM_001304507.1.
DR RefSeq; NP_008908.2; NM_006977.3.
DR RefSeq; XP_006720314.1; XM_006720251.3.
DR RefSeq; XP_006720315.1; XM_006720252.3.
DR RefSeq; XP_011535445.1; XM_011537143.2.
DR RefSeq; XP_016877121.1; XM_017021632.1.
DR RefSeq; XP_016877122.1; XM_017021633.1.
DR RefSeq; XP_016877123.1; XM_017021634.1.
DR RefSeq; XP_016877124.1; XM_017021635.1.
DR AlphaFoldDB; P24278; -.
DR SMR; P24278; -.
DR BioGRID; 113422; 60.
DR IntAct; P24278; 48.
DR MINT; P24278; -.
DR STRING; 9606.ENSP00000476746; -.
DR MoonDB; P24278; Predicted.
DR iPTMnet; P24278; -.
DR PhosphoSitePlus; P24278; -.
DR BioMuta; ZBTB25; -.
DR DMDM; 116242849; -.
DR EPD; P24278; -.
DR jPOST; P24278; -.
DR MassIVE; P24278; -.
DR MaxQB; P24278; -.
DR PaxDb; P24278; -.
DR PeptideAtlas; P24278; -.
DR PRIDE; P24278; -.
DR ProteomicsDB; 54193; -.
DR Antibodypedia; 11914; 203 antibodies from 25 providers.
DR DNASU; 7597; -.
DR Ensembl; ENST00000394715.1; ENSP00000378204.1; ENSG00000089775.12.
DR Ensembl; ENST00000608382.6; ENSP00000476746.1; ENSG00000089775.12.
DR GeneID; 7597; -.
DR KEGG; hsa:7597; -.
DR MANE-Select; ENST00000608382.6; ENSP00000476746.1; NM_006977.5; NP_008908.2.
DR UCSC; uc001xhf.4; human.
DR CTD; 7597; -.
DR DisGeNET; 7597; -.
DR GeneCards; ZBTB25; -.
DR HGNC; HGNC:13112; ZBTB25.
DR HPA; ENSG00000089775; Low tissue specificity.
DR MIM; 194541; gene.
DR neXtProt; NX_P24278; -.
DR OpenTargets; ENSG00000089775; -.
DR PharmGKB; PA37687; -.
DR VEuPathDB; HostDB:ENSG00000089775; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000159887; -.
DR HOGENOM; CLU_025271_0_0_1; -.
DR InParanoid; P24278; -.
DR OMA; PDHSNRG; -.
DR OrthoDB; 567120at2759; -.
DR PhylomeDB; P24278; -.
DR TreeFam; TF332229; -.
DR PathwayCommons; P24278; -.
DR SignaLink; P24278; -.
DR BioGRID-ORCS; 7597; 13 hits in 1140 CRISPR screens.
DR ChiTaRS; ZBTB25; human.
DR GenomeRNAi; 7597; -.
DR Pharos; P24278; Tbio.
DR PRO; PR:P24278; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P24278; protein.
DR Bgee; ENSG00000089775; Expressed in apex of heart and 113 other tissues.
DR ExpressionAtlas; P24278; baseline and differential.
DR Genevisible; P24278; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
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; 2.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
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..435
FT /note="Zinc finger and BTB domain-containing protein 25"
FT /id="PRO_0000047738"
FT DOMAIN 1..107
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 238..260
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 349..371
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 142
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 148
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 198
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 204
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 303
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 330
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 405
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 165
FT /note="H -> L (in Ref. 1; CAA34595)"
FT /evidence="ECO:0000305"
FT CONFLICT 169..170
FT /note="Missing (in Ref. 1; CAA34595)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 435 AA; 48990 MW; 5994E14B735AA0AE CRC64;
MDTASHSLVL LQQLNMQREF GFLCDCTVAI GDVYFKAHRA VLAAFSNYFK MIFIHQTSEC
IKIQPTDIQP DIFSYLLHIM YTGKGPKQIV DHSRLEEGIR FLHADYLSHI ATEMNQVFSP
ETVQSSNLYG IQISTTQKTV VKQGLEVKEA PSSNSGNRAA VQGDHPQLQL SLAIGLDDGT
ADQQRACPAT QALEEHQKPP VSIKQERCDP ESVISQSHPS PSSEVTGPTF TENSVKIHLC
HYCGERFDSR SNLRQHLHTH VSGSLPFGVP ASILESNDLG EVHPLNENSE ALECRRLSSF
IVKENEQQPD HTNRGTTEPL QISQVSLISK DTEPVELNCN FSFSRKRKMS CTICGHKFPR
KSQLLEHMYT HKGKSYRYNR CQRFGNALAQ RFQPYCDSWS DVSLKSSRLS QEHLDLPCAL
ESELTQENVD TILVE
