ZBTB4_RAT
ID ZBTB4_RAT Reviewed; 984 AA.
AC D4A8X0;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Zinc finger and BTB domain-containing protein 4;
GN Name=Zbtb4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Transcriptional repressor with bimodal DNA-binding
CC specificity. Represses transcription in a methyl-CpG-dependent manner.
CC Binds with a higher affinity to methylated CpG dinucleotides in the
CC consensus sequence 5'-CGCG-3' but can also bind to the non-methylated
CC consensus sequence 5'-CTGCNA-3' also known as the consensus kaiso
CC binding site (KBS). Can also bind specifically to a single methyl-CpG
CC pair and can bind hemimethylated DNA but with a lower affinity compared
CC to methylated DNA. Plays a role in postnatal myogenesis, may be
CC involved in the regulation of satellite cells self-renewal (By
CC similarity). {ECO:0000250|UniProtKB:Q5F293,
CC ECO:0000250|UniProtKB:Q9P1Z0}.
CC -!- SUBUNIT: Interacts with HIPK2. Interacts with CBFA2T3. Interacts with
CC ZBTB38. {ECO:0000250|UniProtKB:Q9P1Z0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9P1Z0}.
CC Chromosome {ECO:0000250|UniProtKB:Q9P1Z0}. Note=Localizes to
CC chromocenters. {ECO:0000250|UniProtKB:Q9P1Z0}.
CC -!- PTM: Phosphorylated by HIPK2. This phosphorylation reduces stability
CC and triggers ZBTB4 protein degradation in response to DNA damage.
CC {ECO:0000250|UniProtKB:Q9P1Z0}.
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DR EMBL; AABR07029862; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001291281.1; NM_001304352.1.
DR RefSeq; XP_006246906.1; XM_006246844.3.
DR RefSeq; XP_017452580.1; XM_017597091.1.
DR AlphaFoldDB; D4A8X0; -.
DR SMR; D4A8X0; -.
DR STRING; 10116.ENSRNOP00000019687; -.
DR PaxDb; D4A8X0; -.
DR PRIDE; D4A8X0; -.
DR Ensembl; ENSRNOT00000019687; ENSRNOP00000019687; ENSRNOG00000014689.
DR GeneID; 287441; -.
DR KEGG; rno:287441; -.
DR UCSC; RGD:1307184; rat.
DR CTD; 57659; -.
DR RGD; 1307184; Zbtb4.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161268; -.
DR HOGENOM; CLU_007011_1_0_1; -.
DR InParanoid; D4A8X0; -.
DR OMA; THEVLCK; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; D4A8X0; -.
DR TreeFam; TF333100; -.
DR PRO; PR:D4A8X0; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000014689; Expressed in frontal cortex and 18 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008327; F:methyl-CpG binding; ISO:RGD.
DR GO; GO:0010428; F:methyl-CpNpG binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
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; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 1: Evidence at protein level;
KW Chromosome; Coiled coil; DNA-binding; Isopeptide bond; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..984
FT /note="Zinc finger and BTB domain-containing protein 4"
FT /id="PRO_0000434409"
FT DOMAIN 30..131
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 210..232
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 285..307
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 313..335
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 341..364
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 697..719
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 736..758
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 71..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..324
FT /note="Interaction with CBFA2T3"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Z0"
FT REGION 172..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..509
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..629
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..966
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Z0"
FT MOD_RES 766
FT /note="Phosphothreonine; by HIPK2"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Z0"
FT MOD_RES 768
FT /note="Phosphothreonine; by HIPK2"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Z0"
FT MOD_RES 955
FT /note="Phosphothreonine; by HIPK2"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Z0"
FT CROSSLNK 40
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Z0"
FT CROSSLNK 548
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Z0"
FT CROSSLNK 590
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Z0"
SQ SEQUENCE 984 AA; 103210 MW; D7223FA77F7A896B CRC64;
MPPPAEVTDP SHAPAVLRQL NEQRLRGLFC DVTLIAGDTK FPAHRSVLAA SSPFFREALL
ASAPLPLPPV TGGSAPSPAT TTAASSSSSP PPPASPHSSS PPRVLELPGV PAAAFSDVLN
FIYSARLALP GGGGDGAAVA EIGALGRRLG ISRLQGLGEG GDTWVPPAPS SMVTSEPNED
SLGPGLRTDG GWEGDKAEPL TPDSQPRRPF PCPRCGKSFI HPKRLQTHEA QCRRGSNTRG
SAGLGPGGSG PGGPAGVDAS ALPQPVSFRD GPEHVVKVVG GHVLYVCAAC ERSYVTLSSL
KRHSNVHSWR RKYPCRYCEK VFALAEYRTK HEVWHTGERR YQCIFCWETF VTYYNLKTHQ
RAFHGISPGL LASEKTPNGG YKPKLNTLKL YRLLPMRAAK RPYKTYSQGA PEAPLSPSLH
TPVPAVMPAS PQPLLPSVPE PGPPHSVITF AHPAPSVIVH GSSSSGAAGG GPVGTGGSQA
ASVITYTTPP RPPKKREYPP PPPEPAATPT SPASTAVIPA TAAGPATATE EAKGRNLRAG
RTLTYTAKPV GGVSGSGGSP TGTGRGSSQL QAPPPLCQIT VRIGEEAIVK RRISETDLRP
GELSGEEVEE SEEEEEEEEE EDQEDQEESK AGGEDQLWRP YYSYKPKRKA GATASGLSGL
PRGRRPPRWR QKLERRGWEE TPAVEGPGGR GRGERRHRCG DCAQAFATLR KLRKHQEAHS
GGSHNSRTGR RSSTRFTCPH CAKVCKTAAA LNRHGQRHAV ERPGGTPTPV IAYSKGSIGT
RPTDVKEEAP QEMQVSSSSG EAGGGSAAAA AAEASESASL QDPVISGGEE PPVAGGGGYV
YPPVQEFPLA LIGGSRDPGA GKGKPGNEGP VGASEGNRME EMGTAKVTFY PEPYPLVYGP
QLLAAYPYNF SNLAALPVAL NMVLPDEKGG GALPFLPGVF GYAVNPQTAP PTPPTPPPPL
PLPVPPKGVG EMTGVERTQK GDVG
