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ZBT38_RAT
ID   ZBT38_RAT               Reviewed;        1203 AA.
AC   Q5EXX3;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Zinc finger and BTB domain-containing protein 38;
DE   AltName: Full=Zinc finger protein expressed in neurons;
DE            Short=Zenon;
GN   Name=Zbtb38 {ECO:0000250|UniProtKB:Q8BW71};
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] {ECO:0000305, ECO:0000312|EMBL:AAT72920.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAT72920.1};
RC   TISSUE=Brain {ECO:0000312|EMBL:AAT72920.1};
RX   PubMed=15713629; DOI=10.1128/mcb.25.5.1713-1729.2005;
RA   Kiefer H., Chatail-Hermitte F., Ravassard P., Bayard E., Brunet I.,
RA   Mallet J.;
RT   "ZENON, a novel POZ Kruppel-like DNA binding protein associated with
RT   differentiation and/or survival of late postmitotic neurons.";
RL   Mol. Cell. Biol. 25:1713-1729(2005).
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. Plays an important role in regulating DNA-replication and
CC       common fragile sites (CFS) stability in a RBBP6- and MCM10-dependent
CC       manner; represses expression of MCM10 which plays an important role in
CC       DNA-replication (By similarity). Acts as a transcriptional activator.
CC       May be involved in the differentiation and/or survival of late
CC       postmitotic neurons (PubMed:15713629). {ECO:0000250|UniProtKB:Q8NAP3,
CC       ECO:0000269|PubMed:15713629, ECO:0000303|PubMed:15713629}.
CC   -!- SUBUNIT: Interacts with CBFA2T3, ZBTB4 and RBBP6.
CC       {ECO:0000250|UniProtKB:Q8NAP3}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15713629}. Chromosome
CC       {ECO:0000250|UniProtKB:Q8NAP3}. Note=Localizes to chromocenters.
CC       {ECO:0000250|UniProtKB:Q8NAP3}.
CC   -!- TISSUE SPECIFICITY: Widely expressed throughout the adult brain where
CC       it is found mainly in neurons. Also expressed in the adrenal medulla.
CC       Not detected in non-neural tissues including heart, spleen, liver and
CC       muscle. In the embryo, expressed in the developing brain and spinal
CC       cord but not in the migratory neural crest. Also expressed in the
CC       limbs, transiently in somites, and in the embryonic liver. In the
CC       embryonic neural tube, expression is restricted to late postmitotic
CC       neurons. {ECO:0000269|PubMed:15713629}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryo and adult. Embryonic
CC       expression is detected from E12. {ECO:0000269|PubMed:15713629}.
CC   -!- DOMAIN: The BTB domain is not required for activation of transcription
CC       or self-association. {ECO:0000269|PubMed:15713629}.
CC   -!- PTM: Ubiquitinated by RBBP6; leading to its degradation by the
CC       proteasome. {ECO:0000250|UniProtKB:Q8NAP3}.
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DR   EMBL; AY623002; AAT72920.1; -; mRNA.
DR   RefSeq; NP_001012489.1; NM_001012471.1.
DR   AlphaFoldDB; Q5EXX3; -.
DR   SMR; Q5EXX3; -.
DR   BioGRID; 261189; 1.
DR   STRING; 10116.ENSRNOP00000067350; -.
DR   PhosphoSitePlus; Q5EXX3; -.
DR   PaxDb; Q5EXX3; -.
DR   PRIDE; Q5EXX3; -.
DR   GeneID; 315936; -.
DR   KEGG; rno:315936; -.
DR   UCSC; RGD:1310136; rat.
DR   CTD; 253461; -.
DR   RGD; 1310136; Zbtb38.
DR   eggNOG; KOG1721; Eukaryota.
DR   InParanoid; Q5EXX3; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q5EXX3; -.
DR   PRO; PR:Q5EXX3; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA: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; ISO:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
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; ISS:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0006275; P:regulation of DNA replication; ISS: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; 5.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE   2: Evidence at transcript level;
KW   Activator; Chromosome; 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..1203
FT                   /note="Zinc finger and BTB domain-containing protein 38"
FT                   /id="PRO_0000047743"
FT   DOMAIN          33..100
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   ZN_FING         341..363
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         370..394
FT                   /note="C2H2-type 2; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         459..481
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         487..509
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         515..538
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1017..1039
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1045..1067
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1073..1095
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1101..1123
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1132..1154
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          230..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          299..522
FT                   /note="Interaction with CBFA2T3"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT   REGION          581..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          731..776
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          857..882
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          895..914
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1172..1203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..253
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        748..776
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        857..876
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1183..1203
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         130
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT   CROSSLNK        43
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT   CROSSLNK        145
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT   CROSSLNK        148
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT   CROSSLNK        151
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT   CROSSLNK        260
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT   CROSSLNK        549
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT   CROSSLNK        556
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT   CROSSLNK        750
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT   CROSSLNK        755
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT   CROSSLNK        796
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT   CROSSLNK        806
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT   CROSSLNK        813
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT   CROSSLNK        834
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT   CROSSLNK        842
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT   CROSSLNK        849
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT   CROSSLNK        915
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT   CROSSLNK        971
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT   CROSSLNK        976
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT   CROSSLNK        984
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT   CROSSLNK        988
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT   CROSSLNK        998
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT   CROSSLNK        1024
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT   CROSSLNK        1033
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT   CROSSLNK        1116
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT   CROSSLNK        1139
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT   CROSSLNK        1142
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT   CROSSLNK        1157
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NAP3"
FT   CROSSLNK        1190
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NAP3"
SQ   SEQUENCE   1203 AA;  135300 MW;  E5E15AF3A487A12B CRC64;
     MTVMSLSRDL KDDFHSDTVL SILNEQRIRG ILCDVTIIVE DTKFKAHSNV LAASSLYFKN
     IFWSHTICIS SHVLELDDLK AEVFTEILNY IYSSTVVVRR QETVTDLAAA GKRLGISFLE
     DLSDRNFSNS PGPYVVCITE KGVVKEEKNE KRHEEPAVTN GPRITNAFSI IETENSNSMF
     SPLDLRASFK KVSDAMRTTS LCQERASVCP EAEPVRTLAE HSYAVSSITE AYRSQPLREH
     DSSSSSGKTG KENGEALTTK AKPCRKPKTQ TQDSDSTTEN MPLPLVTCPE VNQERSPQPA
     PILSHSEPPS SEGDVHFPRE DENQPSETPG PPAAEVPPLV YNCSCCSKSF DSSTLLGAHM
     QLHKPTQDPF VCKYCNKQFT TLNRLDRHEQ ICMRSSHMPM PGGNQPFLEN YPTIGQDGGS
     FTSPDSLVPE SRIGELSSAG SALSDADHMV KFVNGQMLYS CVVCKRSYVT LSSLRRHANV
     HSWRRTYPCH YCNKVFALAE YRTRHEIWHT GERRYQCIFC LETFMTYYIL KNHQKSFHAI
     DHRLSISKKT ANGGLKPTVY PYKLYRLLPM RCKRAPYKSY RNSSYESAQG NRQRNESPPD
     TFVIPNLPSS EMPTLNFQDG RNSLTSSPAI PVETPSWQGT PTSAKVKNAE GLKWRKQALK
     TDLVDSAEVS ISSIGNSVST TLQAEPVCVS SGEHSASVIS YSGLVPSVIV HSSQFSSVIK
     HSNAIACLAN SNHQSPSQPV ASPSLIKDSK PEADKASKLA SRPKNSKEKK KTVPCNRGEI
     TEEAKYVADL GGSSGKTTNV VEETSKIETY IAKPALPGTS TNSNVAPLCQ ITVKIGNEAI
     VKRHILGSKL FYKRGRKPKY QMQEETLPRE SDPETRGDSP LGLCQADCVE MSEAFDEVSD
     QDSTDKPWRP YYNYKPKKKS KQLRKIRKVK WRKERGSRSP VGRRRYPAEL DRAEMGRRRY
     PAELDRCAEV KLPPDKASEE EENKEMPKLQ CELCDGDKAA GAGAEGKPHQ HLTLKPYICE
     LCAKQFQSSS TLKMHMRCHT GEKPYQCKTC GRRFSVQGNL QKHERIHLGV KEFICQYCNK
     AFTLNETLKI HERIHTGEKR YHCQFCFQGF LYLSTKRNHE RRHVREHDGK GFACFQCPKI
     CKTAAALRMH QKKHLFKTLT KQEETDDLCH ENSDLLESQP CTDSEDSDQK DDIKKPLLKM
     SFE
 
 
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