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Database: UniProt
Entry: ZBTB9_MOUSE
LinkDB: ZBTB9_MOUSE
Original site: ZBTB9_MOUSE 
ID   ZBTB9_MOUSE             Reviewed;         459 AA.
AC   Q8CDC7; Q3U3B2; Q9CYQ0;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 148.
DE   RecName: Full=Zinc finger and BTB domain-containing protein 9;
GN   Name=Zbtb9;
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, and NOD; TISSUE=Testis;
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   STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and 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).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR   EMBL; AK014458; BAB29365.1; -; mRNA.
DR   EMBL; AK030262; BAC26866.1; -; mRNA.
DR   EMBL; AK154850; BAE32876.1; -; mRNA.
DR   EMBL; BC049933; AAH49933.1; -; mRNA.
DR   EMBL; BC054732; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC060527; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS37520.1; -.
DR   RefSeq; NP_001005916.1; NM_001005916.2.
DR   AlphaFoldDB; Q8CDC7; -.
DR   SMR; Q8CDC7; -.
DR   BioGRID; 243089; 10.
DR   IntAct; Q8CDC7; 5.
DR   STRING; 10090.ENSMUSP00000112778; -.
DR   PhosphoSitePlus; Q8CDC7; -.
DR   EPD; Q8CDC7; -.
DR   jPOST; Q8CDC7; -.
DR   MaxQB; Q8CDC7; -.
DR   PaxDb; 10090-ENSMUSP00000112778; -.
DR   PeptideAtlas; Q8CDC7; -.
DR   ProteomicsDB; 275056; -.
DR   DNASU; 474156; -.
DR   Ensembl; ENSMUST00000120016.3; ENSMUSP00000112778.2; ENSMUSG00000079605.6.
DR   Ensembl; ENSMUST00000133257.9; ENSMUSP00000115777.3; ENSMUSG00000117819.2.
DR   Ensembl; ENSMUST00000237633.2; ENSMUSP00000157541.2; ENSMUSG00000079605.6.
DR   GeneID; 474156; -.
DR   KEGG; mmu:474156; -.
DR   UCSC; uc008bfb.1; mouse.
DR   AGR; MGI:1918022; -.
DR   AGR; MGI:6303071; -.
DR   CTD; 221504; -.
DR   MGI; MGI:1918022; Zbtb9.
DR   VEuPathDB; HostDB:ENSMUSG00000079605; -.
DR   VEuPathDB; HostDB:ENSMUSG00000117819; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000162408; -.
DR   HOGENOM; CLU_029118_2_0_1; -.
DR   InParanoid; Q8CDC7; -.
DR   OMA; PGGWCIR; -.
DR   OrthoDB; 1777466at2759; -.
DR   PhylomeDB; Q8CDC7; -.
DR   BioGRID-ORCS; 474156; 3 hits in 47 CRISPR screens.
DR   ChiTaRS; Zbtb9; mouse.
DR   PRO; PR:Q8CDC7; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q8CDC7; Protein.
DR   Bgee; ENSMUSG00000079605; Expressed in spermatocyte and 76 other cell types or tissues.
DR   Genevisible; Q8CDC7; MM.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; 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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 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   PANTHER; PTHR46105; AGAP004733-PA; 1.
DR   PANTHER; PTHR46105:SF13; ZINC FINGER AND BTB DOMAIN-CONTAINING PROTEIN 9; 1.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR   SUPFAM; SSF54695; POZ domain; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW   Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..459
FT                   /note="Zinc finger and BTB domain-containing protein 9"
FT                   /id="PRO_0000047724"
FT   DOMAIN          48..112
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   ZN_FING         397..419
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         424..446
FT                   /note="C2H2-type 2; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          178..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          212..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          293..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..235
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..313
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        285
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96C00"
FT   CROSSLNK        293
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96C00"
FT   CROSSLNK        368
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96C00"
FT   CONFLICT        251
FT                   /note="P -> T (in Ref. 1; BAB29365)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        425
FT                   /note="A -> V (in Ref. 1; BAB29365)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   459 AA;  49536 MW;  1984B0D0242F06D1 CRC64;
     MDASTPLPPA SSSPRCNPAP QTIHIEFPHH SSSLLESLNR HRLEGKFCDV SLLVQGRELR
     AHKAVLAAAS PYFHDKLLLG DAPRLTLPNV IEADAFEGLL QLIYSGSLHL PLDALPAHLL
     VASGLQMWQV VDRCSEILRE LETSGGISAG GRASSLTLIS TTSSGGWCIR SSPFQNPVRS
     SASTENSVLP ESPAGGEGSE LEGMLQIQVK VEEEEEQGSA APLFQTPQPE RVSGGVSQAC
     GSHPLPTPAL PSKPSEDESS TVDPPAPPVQ ASQILYVNQE NVECKEEIAR GTKEKTKVLS
     GEDSEEKEEL RYLLSSGGGE SSGAGDPSWK PVDLHGNEIL SGDGGPGGTG QAMHGPVKLG
     GTPPADGKCF ACLCGKRFAV KPKRDRHIML TFSLRPFGCG ICNKRFKLKH HLTEHMKTHA
     RALHACPHCG RRFRVQAFFL RHRDLCKGQG WPTYHWTYK
//
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