ZBT11_HUMAN
ID ZBT11_HUMAN Reviewed; 1053 AA.
AC O95625; Q2NKP9;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Zinc finger and BTB domain-containing protein 11 {ECO:0000305};
GN Name=ZBTB11 {ECO:0000303|PubMed:28397838, ECO:0000312|HGNC:HGNC:16740};
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].
RA Tang C.M., Seto E.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 IDENTIFICATION BY 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1050, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1043, AND IDENTIFICATION BY MASS
RP 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 [8]
RP VARIANT MRT69 GLN-880.
RX PubMed=28397838; DOI=10.1038/mp.2017.60;
RA Harripaul R., Vasli N., Mikhailov A., Rafiq M.A., Mittal K.,
RA Windpassinger C., Sheikh T.I., Noor A., Mahmood H., Downey S., Johnson M.,
RA Vleuten K., Bell L., Ilyas M., Khan F.S., Khan V., Moradi M., Ayaz M.,
RA Naeem F., Heidari A., Ahmed I., Ghadami S., Agha Z., Zeinali S., Qamar R.,
RA Mozhdehipanah H., John P., Mir A., Ansar M., French L., Ayub M.,
RA Vincent J.B.;
RT "Mapping autosomal recessive intellectual disability: combined microarray
RT and exome sequencing identifies 26 novel candidate genes in 192
RT consanguineous families.";
RL Mol. Psychiatry 23:973-984(2018).
RN [9]
RP VARIANTS MRT69 TYR-729 AND GLN-880, SUBCELLULAR LOCATION, AND
RP CHARACTERIZATION OF VARIANTS MRT69 TYR-729 AND GLN-880.
RX PubMed=29893856; DOI=10.1093/hmg/ddy220;
RA Fattahi Z., Sheikh T.I., Musante L., Rasheed M., Taskiran I.I.,
RA Harripaul R., Hu H., Kazeminasab S., Alam M.R., Hosseini M., Larti F.,
RA Ghaderi Z., Celik A., Ayub M., Ansar M., Haddadi M., Wienker T.F.,
RA Ropers H.H., Kahrizi K., Vincent J.B., Najmabadi H.;
RT "Biallelic missense variants in ZBTB11 can cause intellectual disability in
RT humans.";
RL Hum. Mol. Genet. 27:3177-3188(2018).
CC -!- FUNCTION: May be involved in transcriptional regulation. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:29893856}.
CC -!- DISEASE: Intellectual developmental disorder, autosomal recessive 69
CC (MRT69) [MIM:618383]: A form of intellectual disability, a disorder
CC characterized by significantly below average general intellectual
CC functioning associated with impairments in adaptive behavior and
CC manifested during the developmental period.
CC {ECO:0000269|PubMed:28397838, ECO:0000269|PubMed:29893856}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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DR EMBL; U69274; AAD00172.1; -; mRNA.
DR EMBL; AK312859; BAG35711.1; -; mRNA.
DR EMBL; CH471052; EAW79786.1; -; Genomic_DNA.
DR EMBL; BC111700; AAI11701.1; -; mRNA.
DR CCDS; CCDS2943.1; -.
DR RefSeq; NP_055230.2; NM_014415.3.
DR AlphaFoldDB; O95625; -.
DR SMR; O95625; -.
DR BioGRID; 118005; 113.
DR IntAct; O95625; 22.
DR MINT; O95625; -.
DR STRING; 9606.ENSP00000326200; -.
DR iPTMnet; O95625; -.
DR PhosphoSitePlus; O95625; -.
DR BioMuta; ZBTB11; -.
DR EPD; O95625; -.
DR jPOST; O95625; -.
DR MassIVE; O95625; -.
DR MaxQB; O95625; -.
DR PaxDb; O95625; -.
DR PeptideAtlas; O95625; -.
DR PRIDE; O95625; -.
DR ProteomicsDB; 50956; -.
DR Antibodypedia; 15941; 127 antibodies from 22 providers.
DR DNASU; 27107; -.
DR Ensembl; ENST00000312938.5; ENSP00000326200.4; ENSG00000066422.6.
DR GeneID; 27107; -.
DR KEGG; hsa:27107; -.
DR MANE-Select; ENST00000312938.5; ENSP00000326200.4; NM_014415.4; NP_055230.2.
DR UCSC; uc003dve.5; human.
DR CTD; 27107; -.
DR DisGeNET; 27107; -.
DR GeneCards; ZBTB11; -.
DR HGNC; HGNC:16740; ZBTB11.
DR HPA; ENSG00000066422; Low tissue specificity.
DR MalaCards; ZBTB11; -.
DR MIM; 618181; gene.
DR MIM; 618383; phenotype.
DR neXtProt; NX_O95625; -.
DR OpenTargets; ENSG00000066422; -.
DR PharmGKB; PA134907354; -.
DR VEuPathDB; HostDB:ENSG00000066422; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00900000141090; -.
DR HOGENOM; CLU_010706_0_0_1; -.
DR InParanoid; O95625; -.
DR OMA; ENSGPQE; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; O95625; -.
DR TreeFam; TF332263; -.
DR PathwayCommons; O95625; -.
DR SignaLink; O95625; -.
DR BioGRID-ORCS; 27107; 638 hits in 1153 CRISPR screens.
DR GeneWiki; ZBTB11; -.
DR GenomeRNAi; 27107; -.
DR Pharos; O95625; Tdark.
DR PRO; PR:O95625; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O95625; protein.
DR Bgee; ENSG00000066422; Expressed in sperm and 211 other tissues.
DR ExpressionAtlas; O95625; baseline and differential.
DR Genevisible; O95625; HS.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
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; IPR041588; Integrase_H2C2.
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; PF17921; Integrase_H2C2; 1.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
PE 1: Evidence at protein level;
KW Disease variant; DNA-binding; Intellectual disability; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1053
FT /note="Zinc finger and BTB domain-containing protein 11"
FT /id="PRO_0000047727"
FT DOMAIN 214..282
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 569..591
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 597..619
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 651..673
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 679..701
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 707..729
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 735..757
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 766..788
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 794..816
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 822..846
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 858..880
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 886..908
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 914..937
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 141..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1050
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CROSSLNK 1043
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 44
FT /note="G -> S (in dbSNP:rs3749323)"
FT /id="VAR_021894"
FT VARIANT 350
FT /note="T -> N (in dbSNP:rs33957144)"
FT /id="VAR_047465"
FT VARIANT 729
FT /note="H -> Y (in MRT69; impaired localization to the
FT nucleolus; dbSNP:rs1559982532)"
FT /evidence="ECO:0000269|PubMed:29893856"
FT /id="VAR_082098"
FT VARIANT 880
FT /note="H -> Q (in MRT69; impaired localization to the
FT nucleolus; dbSNP:rs1559981249)"
FT /evidence="ECO:0000269|PubMed:28397838,
FT ECO:0000269|PubMed:29893856"
FT /id="VAR_080760"
FT CONFLICT 495
FT /note="D -> N (in Ref. 1; AAD00172)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1053 AA; 119384 MW; 156765B7334BF101 CRC64;
MSSEESYRAI LRYLTNEREP YAPGTEGNVK RKIRKAAACY VVRGGTLYYQ RRQRHRKTFA
ELEVVLQPER RRDLIEAAHL GPGGTHHTRH QTWHYLSKTY WWRGILKQVK DYIKQCSKCQ
EKLDRSRPIS DVSEMLEELG LDLESGEESN ESEDDLSNFT SSPTTASKPA KKKPVSKHEL
VFVDTKGVVK RSSPKHCQAV LKQLNEQRLS NQFCDVTLLI EGEEYKAHKS VLSANSEYFR
DLFIEKGAVS SHEAVVDLSG FCKASFLPLL EFAYTSVLSF DFCSMADVAI LARHLFMSEV
LEICESVHKL MEEKQLTVYK KGEVQTVAST QDLRVQNGGT APPVASSEGT TTSLPTELGD
CEIVLLVNGE LPEAEQNGEV GRQPEPQVSS EAESALSSVG CIADSHPEME SVDLITKNNQ
TELETSNNRE NNTVSNIHPK LSKENVISSS PEDSGMGNDI SAEDICAEDI PKHRQKVDQP
LKDQENLVAS TAKTDFGPDD DTYRSRLRQR SVNEGAYIRL HKGMEKKLQK RKAVPKSAVQ
QVAQKLVQRG KKMKQPKRDA KENTEEASHK CGECGMVFQR RYALIMHKLK HERARDYKCP
LCKKQFQYSA SLRAHLIRHT RKDAPSSSSS NSTSNEASGT SSEKGRTKRE FICSICGRTL
PKLYSLRIHM LKHTGVKPHA CQVCGKTFIY KHGLKLHQSL HQSQKQFQCE LCVKSFVTKR
SLQEHMSIHT GESKYLCSVC GKSFHRGSGL SKHFKKHQPK PEVRGYHCTQ CEKSFFEARD
LRQHMNKHLG VKPFQCQFCD KCYSWKKDWY SHVKSHSVTE PYRCNICGKE FYEKALFRRH
VKKATHGKKG RAKQNLERVC EKCGRKFTQL REYRRHMNNH EGVKPFECLT CGVAWADARS
LKRHVRTHTG ERPYVCPVCS EAYIDARTLR KHMTKFHRDY VPCKIMLEKD TLQFHNQGTQ
VAHAVSILTA GMQEQESSGP QELETVVVTG ETMEALEAVA ATEEYPSVST LSDQSIMQVV
NYVLAQQQGQ KLSEVAEAIQ TVKVEVAHIS GGE
