ZBT26_HUMAN
ID ZBT26_HUMAN Reviewed; 441 AA.
AC Q9HCK0; B3KQ53; Q8WTR1;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2002, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Zinc finger and BTB domain-containing protein 26;
DE AltName: Full=Zinc finger protein 481;
DE AltName: Full=Zinc finger protein Bioref;
GN Name=ZBTB26; Synonyms=KIAA1572, ZNF481;
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=Brain;
RA Alliel P.M., Goudou D., Seddiqi N., Rieger F., Perin J.-P.;
RT "Bioref, a novel bioregulating factor ubiquitously expressed.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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-184; LYS-255 AND LYS-329, 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 Q9HCK0; O15169: AXIN1; NbExp=3; IntAct=EBI-3918996, EBI-710484;
CC Q9HCK0; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-3918996, EBI-3866279;
CC Q9HCK0; Q16543: CDC37; NbExp=3; IntAct=EBI-3918996, EBI-295634;
CC Q9HCK0; O00311: CDC7; NbExp=3; IntAct=EBI-3918996, EBI-374980;
CC Q9HCK0; Q9UER7: DAXX; NbExp=3; IntAct=EBI-3918996, EBI-77321;
CC Q9HCK0; Q92997: DVL3; NbExp=3; IntAct=EBI-3918996, EBI-739789;
CC Q9HCK0; Q08426: EHHADH; NbExp=5; IntAct=EBI-3918996, EBI-2339219;
CC Q9HCK0; O95995: GAS8; NbExp=5; IntAct=EBI-3918996, EBI-1052570;
CC Q9HCK0; Q8TF65: GIPC2; NbExp=3; IntAct=EBI-3918996, EBI-712067;
CC Q9HCK0; V9HWH0: HEL164; NbExp=3; IntAct=EBI-3918996, EBI-10330301;
CC Q9HCK0; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-3918996, EBI-2549423;
CC Q9HCK0; Q969R5: L3MBTL2; NbExp=3; IntAct=EBI-3918996, EBI-739909;
CC Q9HCK0; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-3918996, EBI-739832;
CC Q9HCK0; Q9UBU8-2: MORF4L1; NbExp=3; IntAct=EBI-3918996, EBI-10288852;
CC Q9HCK0; Q15014: MORF4L2; NbExp=3; IntAct=EBI-3918996, EBI-399257;
CC Q9HCK0; O60437: PPL; NbExp=3; IntAct=EBI-3918996, EBI-368321;
CC Q9HCK0; P54725: RAD23A; NbExp=3; IntAct=EBI-3918996, EBI-746453;
CC Q9HCK0; Q9Y4B4: RAD54L2; NbExp=3; IntAct=EBI-3918996, EBI-948156;
CC Q9HCK0; P78317: RNF4; NbExp=3; IntAct=EBI-3918996, EBI-2340927;
CC Q9HCK0; P35711-4: SOX5; NbExp=3; IntAct=EBI-3918996, EBI-11954419;
CC Q9HCK0; P63165: SUMO1; NbExp=8; IntAct=EBI-3918996, EBI-80140;
CC Q9HCK0; G2XKQ0: SUMO1P1; NbExp=3; IntAct=EBI-3918996, EBI-10175576;
CC Q9HCK0; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-3918996, EBI-3650647;
CC Q9HCK0; Q8WV44: TRIM41; NbExp=5; IntAct=EBI-3918996, EBI-725997;
CC Q9HCK0; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-3918996, EBI-744794;
CC Q9HCK0; P63279: UBE2I; NbExp=3; IntAct=EBI-3918996, EBI-80168;
CC Q9HCK0; Q9Y330: ZBTB12; NbExp=3; IntAct=EBI-3918996, EBI-12377219;
CC Q9HCK0; Q9HCK0: ZBTB26; NbExp=7; IntAct=EBI-3918996, EBI-3918996;
CC Q9HCK0; Q8NCN2: ZBTB34; NbExp=3; IntAct=EBI-3918996, EBI-11317716;
CC Q9HCK0; P10074: ZBTB48; NbExp=3; IntAct=EBI-3918996, EBI-744864;
CC Q9HCK0; Q15916: ZBTB6; NbExp=6; IntAct=EBI-3918996, EBI-7227791;
CC Q9HCK0; Q96C00: ZBTB9; NbExp=3; IntAct=EBI-3918996, EBI-395708;
CC Q9HCK0; Q9UJ78-2: ZMYM5; NbExp=3; IntAct=EBI-3918996, EBI-17634549;
CC Q9HCK0; Q9H9D4: ZNF408; NbExp=3; IntAct=EBI-3918996, EBI-347633;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13398.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF323460; AAL55969.1; -; mRNA.
DR EMBL; AB046792; BAB13398.1; ALT_INIT; mRNA.
DR EMBL; AK057445; BAG51915.1; -; mRNA.
DR EMBL; BC018748; AAH18748.1; -; mRNA.
DR CCDS; CCDS6847.1; -.
DR RefSeq; NP_001291292.1; NM_001304363.1.
DR RefSeq; NP_001291293.1; NM_001304364.1.
DR RefSeq; NP_065975.1; NM_020924.3.
DR AlphaFoldDB; Q9HCK0; -.
DR SMR; Q9HCK0; -.
DR BioGRID; 121711; 41.
DR IntAct; Q9HCK0; 36.
DR STRING; 9606.ENSP00000362760; -.
DR iPTMnet; Q9HCK0; -.
DR PhosphoSitePlus; Q9HCK0; -.
DR BioMuta; ZBTB26; -.
DR DMDM; 20177845; -.
DR EPD; Q9HCK0; -.
DR jPOST; Q9HCK0; -.
DR MassIVE; Q9HCK0; -.
DR MaxQB; Q9HCK0; -.
DR PaxDb; Q9HCK0; -.
DR PeptideAtlas; Q9HCK0; -.
DR PRIDE; Q9HCK0; -.
DR ProteomicsDB; 81742; -.
DR Antibodypedia; 16160; 157 antibodies from 18 providers.
DR DNASU; 57684; -.
DR Ensembl; ENST00000373654.1; ENSP00000362758.1; ENSG00000171448.9.
DR Ensembl; ENST00000373656.4; ENSP00000362760.3; ENSG00000171448.9.
DR GeneID; 57684; -.
DR KEGG; hsa:57684; -.
DR MANE-Select; ENST00000373656.4; ENSP00000362760.3; NM_020924.4; NP_065975.1.
DR UCSC; uc004bnj.4; human.
DR CTD; 57684; -.
DR GeneCards; ZBTB26; -.
DR HGNC; HGNC:23383; ZBTB26.
DR HPA; ENSG00000171448; Low tissue specificity.
DR neXtProt; NX_Q9HCK0; -.
DR OpenTargets; ENSG00000171448; -.
DR PharmGKB; PA134914020; -.
DR VEuPathDB; HostDB:ENSG00000171448; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000157920; -.
DR HOGENOM; CLU_037856_1_0_1; -.
DR InParanoid; Q9HCK0; -.
DR OMA; RGIDKGL; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9HCK0; -.
DR TreeFam; TF333162; -.
DR PathwayCommons; Q9HCK0; -.
DR SignaLink; Q9HCK0; -.
DR BioGRID-ORCS; 57684; 11 hits in 1131 CRISPR screens.
DR ChiTaRS; ZBTB26; human.
DR GenomeRNAi; 57684; -.
DR Pharos; Q9HCK0; Tdark.
DR PRO; PR:Q9HCK0; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9HCK0; protein.
DR Bgee; ENSG00000171448; Expressed in sperm and 171 other tissues.
DR Genevisible; Q9HCK0; 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:0042802; F:identical protein binding; IPI:IntAct.
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:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
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; 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 DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..441
FT /note="Zinc finger and BTB domain-containing protein 26"
FT /id="PRO_0000047739"
FT DOMAIN 33..97
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 273..295
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 298..320
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 326..348
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 354..377
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 134..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 184
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 255
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 329
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 236
FT /note="H -> R (in dbSNP:rs7856488)"
FT /id="VAR_052916"
SQ SEQUENCE 441 AA; 49953 MW; AC89C960820BEC83 CRC64;
MSERSDLLHF KFENYGDSML QKMNKLREEN KFCDVTVLID DIEVQGHKIV FAAGSPFLRD
QFLLNDSREV KISILQSSEV GRQLLLSCYS GVLEFPEMEL VNYLTAASFL QMSHIVERCT
QALWKFIKPK QPMDSKEGCE PQSASPQSKE QQGDARGSPK QDSPCIHPSE DSMDMEDSDI
QIVKVESIGD VSEVRSKKDQ NQFISSEPTA LHSSEPQHSL INSTVENRVS EIEQNHLHNY
ALSYTGSDNI IMASKDVFGP NIRGVDKGLQ WHHQCPKCTR VFRHLENYAN HLKMHKLFMC
LLCGKTFTQK GNLHRHMRVH AGIKPFQCKI CGKTFSQKCS LQDHLNLHSG DKPHKCNYCD
MVFAHKPVLR KHLKQLHGKN SFDNANERNV QDLTVDFDSF ACTTVTDSKG CQPQPDATQV
LDAGKLAQAV LNLRNDSTCV N
