ZBT49_MOUSE
ID ZBT49_MOUSE Reviewed; 756 AA.
AC Q8BXX2; Q8CID4; Q8K2Z6;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Zinc finger and BTB domain-containing protein 49;
DE AltName: Full=Zinc finger protein 509;
GN Name=Zbtb49; Synonyms=Zfp509, Znf509;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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] (ISOFORMS 2 AND 3).
RC STRAIN=FVB/N-3; 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 TISSUE SPECIFICITY.
RX PubMed=25245946; DOI=10.1093/nar/gku857;
RA Jeon B.N., Kim M.K., Yoon J.H., Kim M.Y., An H., Noh H.J., Choi W.I.,
RA Koh D.I., Hur M.W.;
RT "Two ZNF509 (ZBTB49) isoforms induce cell-cycle arrest by activating
RT transcription of p21/CDKN1A and RB upon exposure to genotoxic stress.";
RL Nucleic Acids Res. 42:11447-11461(2014).
CC -!- FUNCTION: Transcription factor. Inhibits cell proliferation by
CC activating either CDKN1A/p21 transcription or RB1 transcription.
CC {ECO:0000250|UniProtKB:Q6ZSB9}.
CC -!- SUBUNIT: Interacts with EP300, KAT5/Tip60 and ZBTB17. The interaction
CC with EP300 is direct and leads to synergistic induction of CDKN1A. On
CC the CDKN1A promoter, forms a complex with ZBTB17; this interaction
CC leads to additive CDKN1A transactivation. The interaction with ZBTB17
CC may block ZBTB17 repressor activity. {ECO:0000250|UniProtKB:Q6ZSB9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6ZSB9}. Nucleus
CC {ECO:0000250|UniProtKB:Q6ZSB9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BXX2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BXX2-2; Sequence=VSP_016345, VSP_016346;
CC Name=3;
CC IsoId=Q8BXX2-3; Sequence=VSP_016344;
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in white
CC adipose tissue and kidney, intermediate levels in brain, liver and
CC heart, and lowest levels in spleen, brown adipose tissue and muscle.
CC {ECO:0000269|PubMed:25245946}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AK043044; BAC31447.1; -; mRNA.
DR EMBL; AK140546; BAE24420.1; -; mRNA.
DR EMBL; BC028988; AAH28988.1; -; mRNA.
DR EMBL; BC029122; AAH29122.1; -; mRNA.
DR CCDS; CCDS19252.1; -. [Q8BXX2-1]
DR RefSeq; NP_083438.1; NM_029162.2. [Q8BXX2-1]
DR RefSeq; XP_006504228.1; XM_006504165.3.
DR AlphaFoldDB; Q8BXX2; -.
DR SMR; Q8BXX2; -.
DR STRING; 10090.ENSMUSP00000092429; -.
DR iPTMnet; Q8BXX2; -.
DR PhosphoSitePlus; Q8BXX2; -.
DR PaxDb; Q8BXX2; -.
DR PRIDE; Q8BXX2; -.
DR ProteomicsDB; 302103; -. [Q8BXX2-1]
DR ProteomicsDB; 302104; -. [Q8BXX2-2]
DR ProteomicsDB; 302105; -. [Q8BXX2-3]
DR Antibodypedia; 9229; 105 antibodies from 21 providers.
DR DNASU; 75079; -.
DR Ensembl; ENSMUST00000094833; ENSMUSP00000092429; ENSMUSG00000029127. [Q8BXX2-1]
DR GeneID; 75079; -.
DR KEGG; mmu:75079; -.
DR UCSC; uc008xgc.1; mouse. [Q8BXX2-1]
DR UCSC; uc008xge.1; mouse. [Q8BXX2-3]
DR CTD; 166793; -.
DR MGI; MGI:1922329; Zbtb49.
DR VEuPathDB; HostDB:ENSMUSG00000029127; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158750; -.
DR HOGENOM; CLU_018392_0_0_1; -.
DR InParanoid; Q8BXX2; -.
DR OMA; AVYGPYV; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8BXX2; -.
DR TreeFam; TF330993; -.
DR BioGRID-ORCS; 75079; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Zbtb49; mouse.
DR PRO; PR:Q8BXX2; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BXX2; protein.
DR Bgee; ENSMUSG00000029127; Expressed in spermatocyte and 109 other tissues.
DR ExpressionAtlas; Q8BXX2; baseline and differential.
DR Genevisible; Q8BXX2; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0001227; F:DNA-binding transcription repressor 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:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0001223; F:transcription coactivator binding; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
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 Pfam; PF00096; zf-C2H2; 5.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 2: Evidence at transcript level;
KW Activator; Alternative splicing; Cell cycle; Cytoplasm; DNA-binding;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..756
FT /note="Zinc finger and BTB domain-containing protein 49"
FT /id="PRO_0000047627"
FT DOMAIN 25..91
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 386..408
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 414..436
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 442..464
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 470..492
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 498..520
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 526..548
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 554..576
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 176..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..508
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016344"
FT VAR_SEQ 1..284
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016345"
FT VAR_SEQ 285..424
FT /note="DPLSEPPAKQMRLKKAMHLKKLNFLKSQQSAECTSHPEPDNGLARREESAAK
FT EDAVERAGSQTAEEKGRGELGPESSREEELPGAPASWEDPSQALQPQKQYACELCGKPF
FT KHPSNLELHKRSHTGEKPFECNICGKHFS -> MGWPGGRSLLLRKMQWRELEARLLKK
FT KGGENWVQRAAVRRSCQEPQLPGKTRPRLSSPRNSMHVNCVGSLLNTQAIWSCTNGLI
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016346"
SQ SEQUENCE 756 AA; 83091 MW; 0D7E6261C61F3225 CRC64;
MDPVAVHSCH LLQQLREQRI QGLLCDCMLV VRGVCFKAHK NVLAAFSQYF RSLFQNSSSQ
KNDVFHLDVT NVSGIGQILD FMYTSRLDLN QDNIQVMLDT AQCLQVQNVL NLCHTFLKSA
PAAQLPGLPC AGGFSLQSVA LDGTCAVSEH YPPPSLQECP VEGPQAKVPA EVNARAPSAN
FSRPTEVSKP DAAGGSCPEL PCKQPNHYYK LRTLYSKQYY KQTACPSQVP ATQQPLTRSA
STDLAAADSQ PPVEGRPAVL ETPEHLPSTF VAPPVRNSGN DSEADPLSEP PAKQMRLKKA
MHLKKLNFLK SQQSAECTSH PEPDNGLARR EESAAKEDAV ERAGSQTAEE KGRGELGPES
SREEELPGAP ASWEDPSQAL QPQKQYACEL CGKPFKHPSN LELHKRSHTG EKPFECNICG
KHFSQAGNLQ THLRRHSGEK PYICEICGKR FAASGDVQRH IIIHSGEKPH LCDTCGRGFS
NFSNLKEHKK THTADKVFTC DECGKSFNMQ RKLVKHRVRH TGERPYSCPA CGKCFGGSGD
LRRHVRTHTG EKPYSCEVCS KCFTRSAVLR RHKRMHGRAD ARSPVVLGEL SRPIEPSDLD
RSQSSDSFSQ DVSVTLMPVS VKLPVQPVES SVAGFDGHCS GSYCKLRSML RPPGMSDQDR
LSLEPSKLAK PPELQSQPQA YAYSDVEPSA GVEQPQADGM AVSRSSLATL DNHCTEPLGS
RAPSVTYRNS EGQFFSSMTL WGLAMKTLQN EHELEQ
