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 02-SEP-2026, entry version 185. 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; Q96EB6: SIRT1; NbExp=3; IntAct=EBI-5235984, EBI-1802965; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_001080412.3. DR RefSeq; NP_001337028.1; NM_001350099.2. DR RefSeq; NP_001337029.1; NM_001350100.2. DR RefSeq; NP_001363041.1; NM_001376112.1. DR RefSeq; NP_001363042.1; NM_001376113.1. DR RefSeq; NP_001363043.1; NM_001376114.1. DR RefSeq; NP_001363044.1; NM_001376115.1. DR RefSeq; NP_001363045.1; NM_001376116.1. DR RefSeq; NP_001363046.1; NM_001376117.1. DR RefSeq; NP_001363047.1; NM_001376118.1. DR RefSeq; NP_001363048.1; NM_001376119.1. DR RefSeq; NP_001363049.1; NM_001376120.1. DR RefSeq; NP_001363050.1; NM_001376121.1. DR RefSeq; NP_001363051.1; NM_001376122.1. DR RefSeq; NP_001363052.1; NM_001376123.1. DR RefSeq; NP_001363053.1; NM_001376124.1. DR RefSeq; NP_001363054.1; NM_001376125.1. DR RefSeq; NP_001363055.1; NM_001376126.1. DR RefSeq; NP_001363056.1; NM_001376127.1. DR RefSeq; NP_001363057.1; NM_001376128.1. DR RefSeq; NP_001363071.1; NM_001376142.1. DR RefSeq; NP_001363072.1; NM_001376143.1. DR RefSeq; NP_001363079.1; NM_001376150.1. DR RefSeq; NP_001363081.1; NM_001376152.1. DR RefSeq; NP_001363086.1; NM_001376157.1. DR RefSeq; NP_001363087.1; NM_001376158.1. DR RefSeq; NP_001363088.1; NM_001376159.1. DR RefSeq; NP_001363089.1; NM_001376160.1. DR RefSeq; NP_001363090.1; NM_001376161.1. DR RefSeq; NP_001363091.1; NM_001376162.1. DR RefSeq; NP_001363092.1; NM_001376163.1. DR RefSeq; NP_001363093.1; NM_001376164.1. DR RefSeq; NP_001363094.1; NM_001376165.1. DR RefSeq; NP_001363095.1; NM_001376166.1. DR RefSeq; NP_001363096.1; NM_001376167.1. DR RefSeq; NP_001363097.1; NM_001376168.1. DR RefSeq; NP_001363098.1; NM_001376169.1. DR RefSeq; NP_001363099.1; NM_001376170.1. DR RefSeq; NP_001363100.1; NM_001376171.1. DR RefSeq; NP_001363101.1; NM_001376172.1. DR RefSeq; NP_001363102.1; NM_001376173.1. DR RefSeq; NP_001363103.1; NM_001376174.1. DR RefSeq; NP_001363104.1; NM_001376175.1. DR RefSeq; NP_001363105.1; NM_001376176.1. DR RefSeq; NP_001363106.1; NM_001376177.1. DR RefSeq; NP_001363107.1; NM_001376178.1. DR RefSeq; NP_001363108.1; NM_001376179.1. DR RefSeq; NP_001363109.1; NM_001376180.1. DR RefSeq; NP_001363110.1; NM_001376181.1. DR RefSeq; NP_001363111.1; NM_001376182.1. DR RefSeq; NP_001363112.1; NM_001376183.1. DR RefSeq; NP_001363113.1; NM_001376184.1. DR RefSeq; NP_001363114.1; NM_001376185.1. DR RefSeq; NP_001363115.1; NM_001376186.1. DR RefSeq; NP_001363116.1; NM_001376187.1. DR RefSeq; NP_001363117.1; NM_001376188.1. DR RefSeq; NP_001363118.1; NM_001376189.1. DR RefSeq; NP_001363119.1; NM_001376190.1. DR RefSeq; NP_001374870.1; NM_001387941.1. DR RefSeq; NP_001374874.1; NM_001387945.1. DR RefSeq; NP_001374876.1; NM_001387947.1. DR RefSeq; NP_001374877.1; NM_001387948.1. DR RefSeq; NP_001374879.1; NM_001387950.1. DR RefSeq; NP_001374881.1; NM_001387952.1. DR RefSeq; NP_001374882.1; NM_001387953.1. DR RefSeq; NP_001374886.1; NM_001387957.1. DR RefSeq; NP_001374888.1; NM_001387959.1. DR RefSeq; NP_001374889.1; NM_001387960.1. DR RefSeq; NP_001374891.1; NM_001387962.1. DR RefSeq; NP_001374895.1; NM_001387966.1. DR RefSeq; NP_001374896.1; NM_001387967.1. DR RefSeq; NP_001374897.1; NM_001387968.1. DR RefSeq; NP_001374898.1; NM_001387969.1. DR RefSeq; NP_001374899.1; NM_001387970.1. DR RefSeq; NP_001374900.1; NM_001387971.1. DR RefSeq; NP_001374901.1; NM_001387972.1. DR RefSeq; NP_001374902.1; NM_001387973.1. DR RefSeq; NP_001374903.1; NM_001387974.1. DR RefSeq; NP_001374904.1; NM_001387975.1. DR RefSeq; NP_001374905.1; NM_001387976.1. DR RefSeq; NP_001374906.1; NM_001387977.1. DR RefSeq; NP_001374907.1; NM_001387978.1. DR RefSeq; NP_001374908.1; NM_001387979.1. DR RefSeq; NP_001374909.1; NM_001387980.1. DR RefSeq; NP_001374910.1; NM_001387981.1. DR RefSeq; XP_047303811.1; XM_047447855.1. DR RefSeq; XP_047303812.1; XM_047447856.1. DR RefSeq; XP_047303813.1; XM_047447857.1. DR RefSeq; XP_047303814.1; XM_047447858.1. DR RefSeq; XP_047303815.1; XM_047447859.1. DR RefSeq; XP_047303816.1; XM_047447860.1. DR RefSeq; XP_047303817.1; XM_047447861.1. DR RefSeq; XP_047303818.1; XM_047447862.1. DR RefSeq; XP_047303819.1; XM_047447863.1. DR RefSeq; XP_047303820.1; XM_047447864.1. DR RefSeq; XP_047303821.1; XM_047447865.1. DR RefSeq; XP_047303822.1; XM_047447866.1. DR RefSeq; XP_047303823.1; XM_047447867.1. DR RefSeq; XP_047303824.1; XM_047447868.1. DR RefSeq; XP_047303825.1; XM_047447869.1. DR RefSeq; XP_047303826.1; XM_047447870.1. DR RefSeq; XP_047303827.1; XM_047447871.1. DR PDB; 6E93; X-ray; 1.75 A; A=1006-1124. DR PDB; 6E94; X-ray; 1.59 A; A=1006-1124. DR AlphaFoldDB; Q8NAP3; -. DR SASBDB; Q8NAP3; -. DR SMR; Q8NAP3; -. DR BioGRID; 128969; 152. DR FunCoup; Q8NAP3; 1136. DR IntAct; Q8NAP3; 35. DR MINT; Q8NAP3; -. DR STRING; 9606.ENSP00000426387; -. DR GlyGen; Q8NAP3; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8NAP3; -. DR PhosphoSitePlus; Q8NAP3; -. DR BioMuta; ZBTB38; -. DR DMDM; 68566212; -. DR jPOST; Q8NAP3; -. DR MassIVE; Q8NAP3; -. DR PaxDb; 9606-ENSP00000426387; -. DR PeptideAtlas; Q8NAP3; -. DR ProteomicsDB; 72688; -. DR Pumba; Q8NAP3; -. DR Antibodypedia; 8856; 183 antibodies from 30 providers. DR DNASU; 253461; -. DR Ensembl; ENST00000321464.7; ENSP00000372635.5; ENSG00000177311.13. DR Ensembl; ENST00000441582.2; ENSP00000406955.2; ENSG00000177311.13. DR Ensembl; ENST00000514251.5; ENSP00000426387.1; ENSG00000177311.13. DR Ensembl; ENST00000637056.1; ENSP00000490041.1; ENSG00000177311.13. DR Ensembl; ENST00000860260.1; ENSP00000530319.1; ENSG00000177311.13. DR Ensembl; ENST00000860261.1; ENSP00000530320.1; ENSG00000177311.13. DR Ensembl; ENST00000860262.1; ENSP00000530321.1; ENSG00000177311.13. DR Ensembl; ENST00000860263.1; ENSP00000530322.1; ENSG00000177311.13. DR Ensembl; ENST00000860264.1; ENSP00000530323.1; ENSG00000177311.13. DR Ensembl; ENST00000860265.1; ENSP00000530324.1; ENSG00000177311.13. DR Ensembl; ENST00000860266.1; ENSP00000530325.1; ENSG00000177311.13. DR Ensembl; ENST00000860267.1; ENSP00000530326.1; ENSG00000177311.13. DR Ensembl; ENST00000860268.1; ENSP00000530327.1; ENSG00000177311.13. DR Ensembl; ENST00000860269.1; ENSP00000530328.1; ENSG00000177311.13. DR Ensembl; ENST00000860270.1; ENSP00000530329.1; ENSG00000177311.13. DR Ensembl; ENST00000860271.1; ENSP00000530330.1; ENSG00000177311.13. DR Ensembl; ENST00000860272.1; ENSP00000530331.1; ENSG00000177311.13. DR Ensembl; ENST00000860273.1; ENSP00000530332.1; ENSG00000177311.13. DR Ensembl; ENST00000860274.1; ENSP00000530333.1; ENSG00000177311.13. DR Ensembl; ENST00000860275.1; ENSP00000530334.1; ENSG00000177311.13. DR Ensembl; ENST00000860276.1; ENSP00000530335.1; ENSG00000177311.13. DR Ensembl; ENST00000860277.1; ENSP00000530336.1; ENSG00000177311.13. DR Ensembl; ENST00000860278.1; ENSP00000530337.1; ENSG00000177311.13. DR Ensembl; ENST00000860279.1; ENSP00000530338.1; ENSG00000177311.13. DR Ensembl; ENST00000860280.1; ENSP00000530339.1; ENSG00000177311.13. DR Ensembl; ENST00000860281.1; ENSP00000530340.1; ENSG00000177311.13. DR Ensembl; ENST00000860282.1; ENSP00000530341.1; ENSG00000177311.13. DR Ensembl; ENST00000928306.1; ENSP00000598365.1; ENSG00000177311.13. DR Ensembl; ENST00000961278.1; ENSP00000631337.1; ENSG00000177311.13. DR Ensembl; ENST00000961279.1; ENSP00000631338.1; ENSG00000177311.13. DR Ensembl; ENST00000961280.1; ENSP00000631339.1; ENSG00000177311.13. DR Ensembl; ENST00000961281.1; ENSP00000631340.1; ENSG00000177311.13. DR Ensembl; ENST00000961282.1; ENSP00000631341.1; ENSG00000177311.13. DR Ensembl; ENST00000961283.1; ENSP00000631342.1; ENSG00000177311.13. DR Ensembl; ENST00000961284.1; ENSP00000631343.1; ENSG00000177311.13. DR Ensembl; ENST00000961285.1; ENSP00000631344.1; ENSG00000177311.13. DR Ensembl; ENST00000961286.1; ENSP00000631345.1; ENSG00000177311.13. DR Ensembl; ENST00000961287.1; ENSP00000631346.1; ENSG00000177311.13. 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 AGR; HGNC:26636; -. DR ClinPGx; PA142670542; -. 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 OpenTargets; ENSG00000177311; -. DR VEuPathDB; HostDB:ENSG00000177311; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000161449; -. DR InParanoid; Q8NAP3; -. DR OMA; SECVEMN; -. DR OrthoDB; 8922241at2759; -. DR PAN-GO; Q8NAP3; 3 GO annotations based on evolutionary models. DR PhylomeDB; Q8NAP3; -. DR PathwayCommons; Q8NAP3; -. DR SignaLink; Q8NAP3; -. DR SIGNOR; Q8NAP3; -. DR Agora; ENSG00000177311; -. DR BioGRID-ORCS; 253461; 13 hits in 1215 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 210 other cell types or tissues. DR ExpressionAtlas; Q8NAP3; baseline and differential. DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB. DR GO; GO:0005694; C:chromosome; EXP:UniProtKB. 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: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:DNA damage response; IMP:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; 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 DNA-templated transcription; IBA:GO_Central. DR CDD; cd18223; BTB_POZ_ZBTB38_CIBZ; 1. DR FunFam; 3.30.160.60:FF:000325; ZFP90 zinc finger protein; 1. DR FunFam; 3.30.160.60:FF:000235; Zinc finger and BTB domain containing 38; 1. DR FunFam; 3.30.160.60:FF:000437; zinc finger and BTB domain-containing protein 38; 1. DR FunFam; 3.30.160.60:FF:001058; zinc finger and BTB domain-containing protein 38; 1. DR FunFam; 3.30.160.60:FF:001251; zinc finger and BTB domain-containing protein 38; 1. DR FunFam; 3.30.160.60:FF:001331; zinc finger and BTB domain-containing protein 38; 1. DR FunFam; 3.30.160.60:FF:001428; zinc finger and BTB domain-containing protein 38; 1. DR FunFam; 3.30.160.60:FF:001474; zinc finger and BTB domain-containing protein 38; 1. DR FunFam; 3.30.710.10:FF:000081; zinc finger and BTB domain-containing protein 38; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 8. DR Gene3D; 3.30.710.10; Potassium Channel Kv1.1, Chain A; 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 PANTHER; PTHR24394:SF58; ZINC FINGER AND BTB DOMAIN CONTAINING 33; 1. DR PANTHER; PTHR24394; ZINC FINGER PROTEIN; 1. DR Pfam; PF00651; BTB; 1. DR Pfam; PF00096; zf-C2H2; 3. DR SMART; SM00225; BTB; 1. DR SMART; SM00355; ZnF_C2H2; 10. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 4. DR SUPFAM; SSF54695; POZ domain; 1. DR PROSITE; PS50097; BTB; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9. DR PDBsum; 6E93; -. DR PDBsum; 6E94; -. PE 1: Evidence at protein level; KW 3D-structure; Activator; Chromosome; DNA-binding; Isopeptide bond; KW Metal-binding; Nucleus; Phosphoprotein; Proteomics identification; KW Reference proteome; Repeat; Repressor; Transcription; KW Transcription regulation; Ubl conjugation; Zinc; 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 270..280 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 314..323 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 753..765 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 uncertain 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 //