ZBTB1_MOUSE
ID ZBTB1_MOUSE Reviewed; 713 AA.
AC Q91VL9; Q8CDP7; Q99LD2;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Zinc finger and BTB domain-containing protein 1;
GN Name=Zbtb1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355 AND THR-356, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION.
RX PubMed=22201126; DOI=10.1084/jem.20112084;
RA Siggs O.M., Li X., Xia Y., Beutler B.;
RT "ZBTB1 is a determinant of lymphoid development.";
RL J. Exp. Med. 209:19-27(2012).
RN [5]
RP FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=22753936; DOI=10.4049/jimmunol.1200623;
RA Punwani D., Simon K., Choi Y., Dutra A., Gonzalez-Espinosa D., Pak E.,
RA Naradikian M., Song C.H., Zhang J., Bodine D.M., Puck J.M.;
RT "Transcription factor zinc finger and BTB domain 1 is essential for
RT lymphocyte development.";
RL J. Immunol. 189:1253-1264(2012).
CC -!- FUNCTION: Acts as a transcriptional repressor (By similarity).
CC Represses cAMP-responsive element (CRE)-mediated transcriptional
CC activation (By similarity). In addition, has a role in translesion DNA
CC synthesis. Requires for UV-inducible RAD18 loading, PCNA
CC monoubiquitination, POLH recruitment to replication factories and
CC efficient translesion DNA synthesis (By similarity). Plays a key role
CC in the transcriptional regulation of T lymphocyte development
CC (PubMed:22201126, PubMed:22753936). {ECO:0000250|UniProtKB:Q9Y2K1,
CC ECO:0000269|PubMed:22201126, ECO:0000269|PubMed:22753936}.
CC -!- SUBUNIT: Homodimer (By similarity). Homodimer (PubMed:22753936).
CC Interacts (via BTB domain) with TRIM28 (unphosphorylated or
CC phosphorylated form) (By similarity). {ECO:0000250|UniProtKB:Q9Y2K1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y2K1}. Nucleus,
CC nucleoplasm {ECO:0000250|UniProtKB:Q9Y2K1}. Note=Localized in dot-like
CC structures in the nucleus. Colocalized with SMRT in nuclear bodies. The
CC sumoylated form is preferentially located in the nucleoplasm outside
CC the nuclear bodies (By similarity). {ECO:0000250|UniProtKB:Q9Y2K1}.
CC -!- TISSUE SPECIFICITY: Expressed strongly in thymus and spleen, less in
CC lymph nodes and peripheral blood mononuclear cells (PBMCs) and weakly
CC in bone marrow. Strongly expressed in immature, but weakly in mature
CC bone marrow-lymphocyte B. {ECO:0000269|PubMed:22753936}.
CC -!- DOMAIN: Both the BTB domain and C2H2-type motifs are necessary for
CC transcriptional repression activity. The BTB domain is also necessary
CC for oligomerization and efficient sumoylation. The hydrophobic cluster
CC preceding Lys-328 enhanced sumoylation efficiency (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y2K1}.
CC -!- DOMAIN: The UBZ-type zinc finger domain is required for targeting ZBTB1
CC to UV damage sites and for PCNA monoubiquitination. UBZ-type zinc
CC finger domain mediates binding to 'Lys-63'-linked polyubiquitin chains
CC (in vitro). {ECO:0000250|UniProtKB:Q9Y2K1}.
CC -!- PTM: Sumoylated with SUMO2 at Lys-328 and to a lesser extent at Lys-
CC 266. Sumoylation inhibits its transcriptional repression activity and
CC regulates its subcellular localization (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y2K1}.
CC -!- DISRUPTION PHENOTYPE: Thymus of embryos show a small number of T-cell
CC progenitors that are unable to progress through thymic differentiation.
CC Adult mice show vestigial thymus and lymph nodes and a reduced spleen
CC size. In the periphery and in the spleen, display an absence of mature
CC T-cells, a reduced number of NK cells, but a normal number of mature B-
CC cells. {ECO:0000269|PubMed:22753936}.
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DR EMBL; AK029762; BAC26603.1; -; mRNA.
DR EMBL; AK035036; BAC28921.1; -; mRNA.
DR EMBL; AK049397; BAC33733.1; -; mRNA.
DR EMBL; BC003372; AAH03372.1; -; mRNA.
DR EMBL; BC012239; AAH12239.1; -; mRNA.
DR CCDS; CCDS25992.1; -.
DR RefSeq; NP_848859.1; NM_178744.2.
DR RefSeq; XP_006515958.1; XM_006515895.3.
DR AlphaFoldDB; Q91VL9; -.
DR SMR; Q91VL9; -.
DR BioGRID; 234520; 1.
DR IntAct; Q91VL9; 1.
DR STRING; 10090.ENSMUSP00000041955; -.
DR iPTMnet; Q91VL9; -.
DR PhosphoSitePlus; Q91VL9; -.
DR EPD; Q91VL9; -.
DR jPOST; Q91VL9; -.
DR MaxQB; Q91VL9; -.
DR PaxDb; Q91VL9; -.
DR PRIDE; Q91VL9; -.
DR ProteomicsDB; 275266; -.
DR Antibodypedia; 24644; 78 antibodies from 23 providers.
DR DNASU; 268564; -.
DR Ensembl; ENSMUST00000042779; ENSMUSP00000041955; ENSMUSG00000033454.
DR GeneID; 268564; -.
DR KEGG; mmu:268564; -.
DR UCSC; uc007nyd.2; mouse.
DR CTD; 22890; -.
DR MGI; MGI:2442326; Zbtb1.
DR VEuPathDB; HostDB:ENSMUSG00000033454; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000157501; -.
DR HOGENOM; CLU_028599_0_0_1; -.
DR InParanoid; Q91VL9; -.
DR OMA; EGGEPDH; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q91VL9; -.
DR TreeFam; TF332229; -.
DR BioGRID-ORCS; 268564; 4 hits in 112 CRISPR screens.
DR ChiTaRS; Zbtb1; mouse.
DR PRO; PR:Q91VL9; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q91VL9; protein.
DR Bgee; ENSMUSG00000033454; Expressed in cumulus cell and 261 other tissues.
DR ExpressionAtlas; Q91VL9; baseline and differential.
DR Genevisible; Q91VL9; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS: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:0030183; P:B cell differentiation; IMP:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0034644; P:cellular response to UV; ISO:MGI.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0032825; P:positive regulation of natural killer cell differentiation; IMP:UniProtKB.
DR GO; GO:2000176; P:positive regulation of pro-T cell differentiation; IMP:UniProtKB.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; IMP:UniProtKB.
DR GO; GO:0002711; P:positive regulation of T cell mediated immunity; IDA:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
DR GO; GO:0048538; P:thymus development; IMP:UniProtKB.
DR GO; GO:0019985; P:translesion synthesis; ISS:UniProtKB.
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 SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
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 Differentiation; DNA-binding; Immunity; Innate immunity; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..713
FT /note="Zinc finger and BTB domain-containing protein 1"
FT /id="PRO_0000047708"
FT DOMAIN 24..91
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 216..242
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 448..470
FT /note="C2H2-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 533..558
FT /note="UBZ-type"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K1"
FT ZN_FING 578..600
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 606..628
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 634..656
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 662..684
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 686..709
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 270..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 356
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 3
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K1"
FT CROSSLNK 200
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K1"
FT CROSSLNK 205
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K1"
FT CROSSLNK 261
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K1"
FT CROSSLNK 266
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K1"
FT CROSSLNK 276
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K1"
FT CROSSLNK 284
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K1"
FT CROSSLNK 304
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K1"
FT CROSSLNK 316
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K1"
FT CROSSLNK 328
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K1"
FT CROSSLNK 340
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K1"
FT CROSSLNK 346
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K1"
FT CROSSLNK 381
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K1"
FT CROSSLNK 528
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K1"
FT CROSSLNK 563
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K1"
FT CONFLICT 472
FT /note="E -> K (in Ref. 2; AAH03372)"
FT /evidence="ECO:0000305"
FT CONFLICT 643
FT /note="N -> K (in Ref. 1; BAC26603)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 713 AA; 81952 MW; 7ECD7EA1E9C88500 CRC64;
MAKPSHSSYV LQQLNNQREW GFLCDCCIAI DDIYFQAHKA VLAACSSYFR MFFMNHQHST
AQLNLSNMKI SAECFDLILQ FMYLGKIMTA PSSFEQFKVA MNYLQLYNVP DCLEDIQDAD
CSSSKCSSSA SSRQSSKMIF GVRMYEDTVA RNGNEANRWC AEPSSTVNTP HHREPEEESL
QLANFPEPLF DVCKKSSVSK LSTPKERVSR RFGRSFTCDS CGFGFSCEKL LDEHVLTCTN
RHSYQNTTRA YHRIVDIRDG KDSNIKAELA EKDSSKTFSA QPDKYREDAN QAPDDSASTT
GSRKSTVEAG IAGEEKSRAT ETKRIIIKME PEDIPADDMK DFNIIKVTEK DCNESTDNDE
LEDEPEEPFY RYYVEEDVGI KKSGRKTLKP RMSISVDERG GLENMRPPNN TSPIQEDAEN
ASCELCGLTI TEEDLSSHYL AKHIENICAC GKCGQILVKG RQLQEHAQRC GEPQDLTMNG
LGNADEKMDM EENPDEQSEI RDMFVEMLDD FRDNHYQINS IQKKQLFKHS ACPFRCPNCG
QRFETENLVV EHMSSCLDQD MFKGAIMEEN ERDHRRKHFC NLCGKGFYQR CHLREHYTVH
TKEKQFVCQT CGKQFLRERQ LRLHNDMHKG MARYVCSICD QGNFRKHDHV RHMISHLSGG
ETICQVCFQI FPNNEQLEQH MDVHLYTCGI CGAKFNLRKD MRSHYNAKHL KRT
