ZBT38_HUMAN
ID ZBT38_HUMAN Reviewed; 1195 AA.
AC Q8NAP3; D3DNF6;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Zinc finger and BTB domain-containing protein 38;
GN Name=ZBTB38 {ECO:0000312|HGNC:HGNC:26636};
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=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [2]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|EMBL:BAC03868.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-775.
RC TISSUE=Brain {ECO:0000312|EMBL:BAC03868.1};
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [5]
RP FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION, AND INTERACTION WITH ZBTB4.
RX PubMed=16354688; DOI=10.1128/mcb.26.1.169-181.2006;
RA Filion G.J., Zhenilo S., Salozhin S., Yamada D., Prokhortchouk E.,
RA Defossez P.A.;
RT "A family of human zinc finger proteins that bind methylated DNA and
RT repress transcription.";
RL Mol. Cell. Biol. 26:169-181(2006).
RN [6]
RP POLYMORPHISM.
RX PubMed=18391952; DOI=10.1038/ng.121;
RG Diabetes Genetics Initiative;
RG Wellcome Trust Case Control Consortium;
RG Cambridge GEM Consortium;
RA Weedon M.N., Lango H., Lindgren C.M., Wallace C., Evans D.M., Mangino M.,
RA Freathy R.M., Perry J.R., Stevens S., Hall A.S., Samani N.J., Shields B.,
RA Prokopenko I., Farrall M., Dominiczak A., Johnson T., Bergmann S.,
RA Beckmann J.S., Vollenweider P., Waterworth D.M., Mooser V., Palmer C.N.,
RA Morris A.D., Ouwehand W.H., Zhao J.H., Li S., Loos R.J., Barroso I.,
RA Deloukas P., Sandhu M.S., Wheeler E., Soranzo N., Inouye M., Wareham N.J.,
RA Caulfield M., Munroe P.B., Hattersley A.T., McCarthy M.I., Frayling T.M.;
RT "Genome-wide association analysis identifies 20 loci that influence adult
RT height.";
RL Nat. Genet. 40:575-583(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP INTERACTION WITH CBFA2T3.
RX PubMed=23251453; DOI=10.1371/journal.pone.0051205;
RA Barrett C.W., Smith J.J., Lu L.C., Markham N., Stengel K.R., Short S.P.,
RA Zhang B., Hunt A.A., Fingleton B.M., Carnahan R.H., Engel M.E., Chen X.,
RA Beauchamp R.D., Wilson K.T., Hiebert S.W., Reynolds A.B., Williams C.S.;
RT "Kaiso directs the transcriptional corepressor MTG16 to the Kaiso binding
RT site in target promoters.";
RL PLoS ONE 7:E51205-E51205(2012).
RN [9]
RP FUNCTION, INTERACTION WITH RBBP6, AND UBIQUITINATION.
RX PubMed=24726359; DOI=10.1016/j.celrep.2014.03.030;
RA Miotto B., Chibi M., Xie P., Koundrioukoff S., Moolman-Smook H., Pugh D.,
RA Debatisse M., He F., Zhang L., Defossez P.A.;
RT "The RBBP6/ZBTB38/MCM10 axis regulates DNA replication and common fragile
RT site stability.";
RL Cell Rep. 7:575-587(2014).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-43; LYS-145; LYS-758; LYS-814 AND
RP LYS-977, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-43; LYS-145 AND LYS-758, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-43; LYS-145; LYS-557 AND LYS-977,
RP AND IDENTIFICATION BY MASS 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 [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-43; LYS-148; LYS-151; LYS-259;
RP LYS-550; LYS-557; LYS-754; LYS-758; LYS-763; LYS-804; LYS-814; LYS-821;
RP LYS-842; LYS-850; LYS-857; LYS-923; LYS-964; LYS-969; LYS-977; LYS-981;
RP LYS-991; LYS-1017; LYS-1026; LYS-1109; LYS-1132; LYS-1135; LYS-1150 AND
RP LYS-1183, AND 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).
RN [14]
RP VARIANT ILE-1067.
RX PubMed=28837730; DOI=10.1167/iovs.16-20941;
RA Wang B., Liu Y., Chen S., Wu Y., Lin S., Duan Y., Zheng K., Zhang L.,
RA Gu X., Hong W., Shao H., Zeng X., Sun B., Duan S.;
RT "A novel potentially causative variant of NDUFAF7 revealed by mutation
RT screening in a chinese family with pathologic myopia.";
RL Invest. Ophthalmol. Vis. Sci. 58:4182-4192(2017).
CC -!- FUNCTION: Transcriptional regulator with bimodal DNA-binding
CC specificity. Binds with a higher affinity to methylated CpG
CC dinucleotides in the consensus sequence 5'-CGCG-3' but can also bind to
CC E-box elements (5'-CACGTG-3'). Can also bind specifically to a single
CC methyl-CpG pair. Represses transcription in a methyl-CpG-dependent
CC manner (PubMed:16354688). Plays an important role in regulating DNA
CC replication and common fragile sites (CFS) stability in a RBBP6- and
CC MCM10-dependent manner; represses expression of MCM10 which plays an
CC important role in DNA-replication (PubMed:24726359). Acts as a
CC transcriptional activator. May be involved in the differentiation
CC and/or survival of late postmitotic neurons (By similarity).
CC {ECO:0000250|UniProtKB:Q5EXX3, ECO:0000269|PubMed:16354688,
CC ECO:0000269|PubMed:24726359}.
CC -!- SUBUNIT: Interacts with CBFA2T3. Interacts with ZBTB4. Interacts with
CC RBBP6. {ECO:0000269|PubMed:16354688, ECO:0000269|PubMed:23251453,
CC ECO:0000269|PubMed:24726359}.
CC -!- INTERACTION:
CC Q8NAP3; Q8N187: CARF; NbExp=3; IntAct=EBI-5235984, EBI-745541;
CC Q8NAP3; P50570-2: DNM2; NbExp=3; IntAct=EBI-5235984, EBI-10968534;
CC Q8NAP3; O14773: TPP1; NbExp=3; IntAct=EBI-5235984, EBI-2800203;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16354688}. Chromosome
CC {ECO:0000269|PubMed:16354688}. Note=Localizes to chromocenters.
CC {ECO:0000269|PubMed:16354688}.
CC -!- DOMAIN: The BTB domain is not required for activation of transcription
CC or self-association. {ECO:0000250|UniProtKB:Q5EXX3}.
CC -!- PTM: Ubiquitinated by RBBP6; leading to its degradation by the
CC proteasome. {ECO:0000269|PubMed:24726359}.
CC -!- POLYMORPHISM: Genetic variations in ZBTB38 define the stature
CC quantitative trait locus 10 (STQTL10) [MIM:612221]. Adult height is an
CC easily observable and highly heritable complex continuous trait.
CC Because of this, it is a model trait for studying genetic influence on
CC quantitative traits. {ECO:0000269|PubMed:18391952}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC03868.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC010184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79004.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79005.1; -; Genomic_DNA.
DR EMBL; AK092355; BAC03868.1; ALT_FRAME; mRNA.
DR CCDS; CCDS43157.1; -.
DR RefSeq; NP_001073881.2; NM_001080412.2.
DR RefSeq; XP_005247314.1; XM_005247257.1.
DR RefSeq; XP_005247315.1; XM_005247258.1.
DR RefSeq; XP_005247318.1; XM_005247261.3.
DR RefSeq; XP_011510913.1; XM_011512611.1.
DR RefSeq; XP_016861541.1; XM_017006052.1.
DR RefSeq; XP_016861542.1; XM_017006053.1.
DR RefSeq; XP_016861543.1; XM_017006054.1.
DR RefSeq; XP_016861544.1; XM_017006055.1.
DR RefSeq; XP_016861545.1; XM_017006056.1.
DR RefSeq; XP_016861546.1; XM_017006057.1.
DR RefSeq; XP_016861547.1; XM_017006058.1.
DR RefSeq; XP_016861548.1; XM_017006059.1.
DR RefSeq; XP_016861549.1; XM_017006060.1.
DR RefSeq; XP_016861550.1; XM_017006061.1.
DR PDB; 6E93; X-ray; 1.75 A; A=1006-1124.
DR PDB; 6E94; X-ray; 1.59 A; A=1006-1124.
DR PDBsum; 6E93; -.
DR PDBsum; 6E94; -.
DR AlphaFoldDB; Q8NAP3; -.
DR SASBDB; Q8NAP3; -.
DR SMR; Q8NAP3; -.
DR BioGRID; 128969; 143.
DR IntAct; Q8NAP3; 33.
DR MINT; Q8NAP3; -.
DR STRING; 9606.ENSP00000426387; -.
DR iPTMnet; Q8NAP3; -.
DR PhosphoSitePlus; Q8NAP3; -.
DR BioMuta; ZBTB38; -.
DR DMDM; 68566212; -.
DR EPD; Q8NAP3; -.
DR jPOST; Q8NAP3; -.
DR MassIVE; Q8NAP3; -.
DR MaxQB; Q8NAP3; -.
DR PaxDb; Q8NAP3; -.
DR PeptideAtlas; Q8NAP3; -.
DR PRIDE; Q8NAP3; -.
DR ProteomicsDB; 72688; -.
DR Antibodypedia; 8856; 183 antibodies from 29 providers.
DR DNASU; 253461; -.
DR Ensembl; ENST00000321464.7; ENSP00000372635.5; ENSG00000177311.12.
DR Ensembl; ENST00000441582.2; ENSP00000406955.2; ENSG00000177311.12.
DR Ensembl; ENST00000514251.5; ENSP00000426387.1; ENSG00000177311.12.
DR Ensembl; ENST00000637056.1; ENSP00000490041.1; ENSG00000177311.12.
DR GeneID; 253461; -.
DR KEGG; hsa:253461; -.
DR MANE-Select; ENST00000321464.7; ENSP00000372635.5; NM_001376113.1; NP_001363042.1.
DR UCSC; uc062olr.1; human.
DR CTD; 253461; -.
DR DisGeNET; 253461; -.
DR GeneCards; ZBTB38; -.
DR HGNC; HGNC:26636; ZBTB38.
DR HPA; ENSG00000177311; Low tissue specificity.
DR MIM; 612218; gene.
DR MIM; 612221; phenotype.
DR neXtProt; NX_Q8NAP3; -.
DR OpenTargets; ENSG00000177311; -.
DR PharmGKB; PA142670542; -.
DR VEuPathDB; HostDB:ENSG00000177311; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161449; -.
DR InParanoid; Q8NAP3; -.
DR OMA; MRKVNWK; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8NAP3; -.
DR TreeFam; TF333100; -.
DR PathwayCommons; Q8NAP3; -.
DR SignaLink; Q8NAP3; -.
DR BioGRID-ORCS; 253461; 11 hits in 1136 CRISPR screens.
DR ChiTaRS; ZBTB38; human.
DR GenomeRNAi; 253461; -.
DR Pharos; Q8NAP3; Tbio.
DR PRO; PR:Q8NAP3; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8NAP3; protein.
DR Bgee; ENSG00000177311; Expressed in superficial temporal artery and 208 other tissues.
DR ExpressionAtlas; Q8NAP3; baseline and differential.
DR Genevisible; Q8NAP3; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
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; ISS:UniProtKB.
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:0008327; F:methyl-CpG binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006275; P:regulation of DNA replication; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; 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; 3.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Chromosome; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1195
FT /note="Zinc finger and BTB domain-containing protein 38"
FT /id="PRO_0000047742"
FT DOMAIN 33..100
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 342..364
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 371..395
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 460..482
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 488..510
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 516..539
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1010..1032
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1038..1060
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1066..1088
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1094..1116
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1125..1147
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 264..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..523
FT /note="Interaction with CBFA2T3"
FT /evidence="ECO:0000269|PubMed:23251453"
FT REGION 745..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..786
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT CROSSLNK 43
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 145
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364"
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 151
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 259
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 550
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 557
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 754
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 758
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 763
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 804
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 814
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 821
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 842
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 850
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 857
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 923
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 964
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 969
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 977
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 981
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 991
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1017
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1026
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1109
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1132
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1135
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1150
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1183
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 319
FT /note="S -> A (in dbSNP:rs16851435)"
FT /id="VAR_052917"
FT VARIANT 615
FT /note="T -> M (in dbSNP:rs17787670)"
FT /id="VAR_052918"
FT VARIANT 809
FT /note="A -> T (in dbSNP:rs3732867)"
FT /id="VAR_052919"
FT VARIANT 1067
FT /note="V -> I (found in patients with pathologic myopia;
FT unknown pathological significance; dbSNP:rs202147729)"
FT /evidence="ECO:0000269|PubMed:28837730"
FT /id="VAR_079610"
FT TURN 1013..1015
FT /evidence="ECO:0007829|PDB:6E94"
FT STRAND 1018..1021
FT /evidence="ECO:0007829|PDB:6E94"
FT HELIX 1022..1033
FT /evidence="ECO:0007829|PDB:6E94"
FT TURN 1041..1043
FT /evidence="ECO:0007829|PDB:6E94"
FT STRAND 1046..1049
FT /evidence="ECO:0007829|PDB:6E94"
FT HELIX 1050..1061
FT /evidence="ECO:0007829|PDB:6E94"
FT TURN 1069..1071
FT /evidence="ECO:0007829|PDB:6E94"
FT STRAND 1074..1077
FT /evidence="ECO:0007829|PDB:6E94"
FT HELIX 1078..1089
FT /evidence="ECO:0007829|PDB:6E94"
FT STRAND 1097..1100
FT /evidence="ECO:0007829|PDB:6E94"
FT STRAND 1102..1105
FT /evidence="ECO:0007829|PDB:6E94"
FT HELIX 1106..1118
FT /evidence="ECO:0007829|PDB:6E94"
SQ SEQUENCE 1195 AA; 134257 MW; A44561D86ACCC2D8 CRC64;
MTVMSLSRDL KDDFHSDTVL SILNEQRIRG ILCDVTIIVE DTKFKAHSNV LAASSLYFKN
IFWSHTICIS SHVLELDDLK AEVFTEILNY IYSSTVVVKR QETVTDLAAA GKKLGISFLE
DLTDRNFSNS PGPYVFCITE KGVVKEEKNE KRHEEPAITN GPRITNAFSI IETENSNNMF
SPLDLRASFK KVSDSMRTAS LCLERTDVCH EAEPVRTLAE HSYAVSSVAE AYRSQPVREH
DGSSPGNTGK ENCEALAAKP KTCRKPKTFS IPQDSDSATE NIPPPPVSNL EVNQERSPQP
AAVLTRSKSP NNEGDVHFSR EDENQSSDVP GPPAAEVPPL VYNCSCCSKA FDSSTLLSAH
MQLHKPTQEP LVCKYCNKQF TTLNRLDRHE QICMRSSHMP IPGGNQRFLE NYPTIGQNGG
SFTGPEPLLS ENRIGEFSST GSTLPDTDHM VKFVNGQMLY SCVVCKRSYV TLSSLRRHAN
VHSWRRTYPC HYCNKVFALA EYRTRHEIWH TGERRYQCIF CLETFMTYYI LKNHQKSFHA
IDHRLSISKK TANGGLKPSV YPYKLYRLLP MKCKRAPYKS YRNSSYENAR ENSQMNESAP
GTYVVQNPHS SELPTLNFQD TVNTLTNSPA IPLETSACQD IPTSANVQNA EGTKWGEEAL
KMDLDNNFYS TEVSVSSTEN AVSSDLRAGD VPVLSLSNSS ENAASVISYS GSAPSVIVHS
SQFSSVIMHS NAIAAMTSSN HRAFSDPAVS QSLKDDSKPE PDKVGRFASR PKSIKEKKKT
TSHTRGEIPE ESNYVADPGG SLSKTTNIAE ETSKIETYIA KPALPGTSTN SNVAPLCQIT
VKIGNEAIVK RHILGSKLFY KRGRRPKYQM QEEPLPQGND PEPSGDSPLG LCQSECMEMS
EVFDDASDQD STDKPWRPYY NYKPKKKSRQ LKKMRKVNWR KEHGNRSPSH KCKYPAELDC
AVGKAPQDKP FEEEETKEMP KLQCELCDGD KAVGAGNQGR PHRHLTSRPY ACELCAKQFQ
SPSTLKMHMR CHTGEKPYQC KTCGRCFSVQ GNLQKHERIH LGLKEFVCQY CNKAFTLNET
LKIHERIHTG EKRYHCQFCF QRFLYLSTKR NHEQRHIREH NGKGYACFQC PKICKTAAAL
GMHQKKHLFK SPSQQEKIGD VCHENSNPLE NQHFIGSEDN DQKDNIQTGV ENVVL
