ZBTB5_MOUSE
ID ZBTB5_MOUSE Reviewed; 670 AA.
AC Q7TQG0; Q3TVR7; Q6GV09; Q8BIB5;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Zinc finger and BTB domain-containing protein 5;
DE AltName: Full=Transcription factor ZNF-POZ;
GN Name=Zbtb5; Synonyms=Kiaa0354;
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 [MRNA].
RC STRAIN=C57BL/6J;
RA Li Y.H., Tang X.J., Chen W., Li Y.P.;
RT "Cloning and characterization of a novel mouse gene ZNF-POZ cDNA encoding a
RT POZ/BTB domain zinc-finger protein.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC97934.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY635051; AAT47717.1; -; mRNA.
DR EMBL; AK160003; BAE35551.1; -; mRNA.
DR EMBL; AK129124; BAC97934.1; ALT_INIT; mRNA.
DR EMBL; BC054551; AAH54551.1; -; mRNA.
DR EMBL; BC057545; AAH57545.1; -; mRNA.
DR CCDS; CCDS18129.1; -.
DR RefSeq; NP_001156755.1; NM_001163283.1.
DR RefSeq; NP_001156756.1; NM_001163284.1.
DR RefSeq; NP_775575.2; NM_173399.3.
DR AlphaFoldDB; Q7TQG0; -.
DR SMR; Q7TQG0; -.
DR STRING; 10090.ENSMUSP00000103447; -.
DR iPTMnet; Q7TQG0; -.
DR PhosphoSitePlus; Q7TQG0; -.
DR PaxDb; Q7TQG0; -.
DR PRIDE; Q7TQG0; -.
DR ProteomicsDB; 302108; -.
DR Antibodypedia; 26273; 145 antibodies from 24 providers.
DR DNASU; 230119; -.
DR Ensembl; ENSMUST00000055028; ENSMUSP00000059919; ENSMUSG00000049657.
DR Ensembl; ENSMUST00000107817; ENSMUSP00000103447; ENSMUSG00000049657.
DR Ensembl; ENSMUST00000180217; ENSMUSP00000136507; ENSMUSG00000049657.
DR GeneID; 230119; -.
DR KEGG; mmu:230119; -.
DR UCSC; uc008ssc.2; mouse.
DR CTD; 9925; -.
DR MGI; MGI:1924601; Zbtb5.
DR VEuPathDB; HostDB:ENSMUSG00000049657; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000160246; -.
DR HOGENOM; CLU_407055_0_0_1; -.
DR InParanoid; Q7TQG0; -.
DR OMA; EKDHMRV; -.
DR OrthoDB; 339939at2759; -.
DR PhylomeDB; Q7TQG0; -.
DR TreeFam; TF330979; -.
DR BioGRID-ORCS; 230119; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q7TQG0; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q7TQG0; protein.
DR Bgee; ENSMUSG00000049657; Expressed in spermatid and 73 other tissues.
DR ExpressionAtlas; Q7TQG0; baseline and differential.
DR Genevisible; Q7TQG0; MM.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
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:MGI.
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:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; 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 SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..670
FT /note="Zinc finger and BTB domain-containing protein 5"
FT /id="PRO_0000047714"
FT DOMAIN 24..93
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 606..628
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 634..657
FT /note="C2H2-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 158..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15062"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15062"
FT CROSSLNK 239
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15062"
FT CROSSLNK 317
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15062"
FT CROSSLNK 325
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15062"
FT CROSSLNK 399
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15062"
FT CROSSLNK 410
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15062"
FT CROSSLNK 535
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15062"
FT CROSSLNK 587
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15062"
FT CROSSLNK 590
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15062"
FT CROSSLNK 638
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15062"
FT CROSSLNK 651
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15062"
FT CONFLICT 182
FT /note="R -> W (in Ref. 2; BAE35551)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 670 AA; 73215 MW; 0DFD572C5B01B2AE CRC64;
MDFPGHFEQI FQQLNYQRLH GQLCDCVIVV GNRHFKAHRS VLAACSTHFR ALFSVAEGDQ
TMNMIQLDSE VVTAEAFAAL IDMMYTSTLM LGESNVMDVL LAASHLHLNS VVKACKHYLT
TRTLPMSPSS ERAQEQSARM QRSFMLQQLG LSIVSSALSS SQSAEEPTAP MSSSMRSSLD
QRTPFPMRRL HKRKQSVEER ARQRLRSSME ESAISDVTPE SGPAGVHSRE EFFSPDSLKI
VDNPKPDGMA DNQEDGAMMF DRPFGAQEDA QVPSQSDGSA GNMASRATQV ETSFEQEAVA
EKGSFQCENP EVGLGEKEHM RVVVKSEPLS SPEPQDEVSD VTSQAEGSES VEVEGVVVSA
EKIDLSPESS DRSFSDPQSS TDRVGDIHIL EVTNNLEHKT SFSISNFLNK SRGSNFSASQ
STDDNLPNTT SDCRLEGEAP YLLSPEAGPA GGPSSAPGSH VENPFSEPAD SHFVRPMQEV
MGLPCVQTSG YQGEQFGMDF SRSGLGLHSS FSRAMMGSPR GGASNFPYYR RIAPKMPVVT
SVRSSQISEN SASSQLMMNG ATSFENGHTS QPGPPQLTRA SADVLSKCKK ALSEHNVLVV
EGARKYACKI CCKTFLTLTD CKKHIRVHTG EKPYACLKCG KRFSQSSHLY KHSKTTCLRW
QSSNLPSTLL
