BTBD1_MOUSE
ID BTBD1_MOUSE Reviewed; 488 AA.
AC P58544; Q6GQU7; Q8BTZ0; Q8K0J0;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=BTB/POZ domain-containing protein 1;
DE AltName: Full=Glucose signal-repressing protein;
GN Name=Btbd1; Synonyms=Gsrp;
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] OF 1-391.
RC STRAIN=NOD; TISSUE=Thymus;
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 Kidney;
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 FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP 1-MET--ALA-108.
RX PubMed=15486563; DOI=10.1038/sj.cdd.4401479;
RA Pisani D.F., Cabane C., Derijard B., Dechesne C.A.;
RT "The topoisomerase 1-interacting protein BTBD1 is essential for muscle cell
RT differentiation.";
RL Cell Death Differ. 11:1157-1165(2004).
RN [4]
RP FUNCTION.
RX PubMed=17462629; DOI=10.1016/j.yexcr.2007.03.030;
RA Pisani D.F., Coldefy A.S., Elabd C., Cabane C., Salles J., Le Cunff M.,
RA Derijard B., Amri E.Z., Dani C., Leger J.J., Dechesne C.A.;
RT "Involvement of BTBD1 in mesenchymal differentiation.";
RL Exp. Cell Res. 313:2417-2426(2007).
CC -!- FUNCTION: Probable substrate-specific adapter of an E3 ubiquitin-
CC protein ligase complex which mediates the ubiquitination and subsequent
CC proteasomal degradation of target proteins (By similarity). Seems to
CC regulate expression levels and/or subnuclear distribution of TOP1, via
CC an unknown mechanism (PubMed:15486563, PubMed:17462629). May play a
CC role in mesenchymal differentiation where it promotes myogenic
CC differentiation and suppresses adipogenesis (PubMed:15486563,
CC PubMed:17462629). {ECO:0000250|UniProtKB:Q9H0C5,
CC ECO:0000269|PubMed:15486563, ECO:0000269|PubMed:17462629}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts (via C-terminus) with TOP1. Interacts with TRIM5
CC isoform Delta. Interacts with CUL3. {ECO:0000250|UniProtKB:Q9H0C5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15486563}.
CC Note=Localizes to punctate or elongated cytoplasmic bodies.
CC {ECO:0000250|UniProtKB:Q9H0C5}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in heart and skeletal muscle.
CC Weakly expressed in myoblast C2C12 cells, but strongly up-regulated
CC upon their differentiation into myotubes.
CC {ECO:0000269|PubMed:15486563}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH31192.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK088345; BAC40296.1; -; mRNA.
DR EMBL; BC031192; AAH31192.1; ALT_INIT; mRNA.
DR EMBL; BC072618; AAH72618.1; -; mRNA.
DR CCDS; CCDS21407.1; -.
DR RefSeq; NP_666305.2; NM_146193.2.
DR AlphaFoldDB; P58544; -.
DR SMR; P58544; -.
DR BioGRID; 219989; 1.
DR IntAct; P58544; 1.
DR MINT; P58544; -.
DR STRING; 10090.ENSMUSP00000026093; -.
DR iPTMnet; P58544; -.
DR PhosphoSitePlus; P58544; -.
DR EPD; P58544; -.
DR MaxQB; P58544; -.
DR PaxDb; P58544; -.
DR PeptideAtlas; P58544; -.
DR PRIDE; P58544; -.
DR ProteomicsDB; 273849; -.
DR Antibodypedia; 28167; 182 antibodies from 27 providers.
DR DNASU; 83962; -.
DR Ensembl; ENSMUST00000026093; ENSMUSP00000026093; ENSMUSG00000025103.
DR GeneID; 83962; -.
DR KEGG; mmu:83962; -.
DR UCSC; uc009icn.1; mouse.
DR CTD; 53339; -.
DR MGI; MGI:1933765; Btbd1.
DR VEuPathDB; HostDB:ENSMUSG00000025103; -.
DR eggNOG; KOG2075; Eukaryota.
DR GeneTree; ENSGT00940000156756; -.
DR HOGENOM; CLU_015899_2_1_1; -.
DR InParanoid; P58544; -.
DR OMA; IDKNTMD; -.
DR OrthoDB; 590115at2759; -.
DR PhylomeDB; P58544; -.
DR TreeFam; TF106482; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 83962; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Btbd1; mouse.
DR PRO; PR:P58544; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P58544; protein.
DR Bgee; ENSMUSG00000025103; Expressed in spermatid and 65 other tissues.
DR Genevisible; P58544; MM.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0097602; F:cullin family protein binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0022008; P:neurogenesis; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.120.820; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR012983; PHR.
DR InterPro; IPR038648; PHR_sf.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF08005; PHR; 1.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Differentiation; Methylation; Myogenesis; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..488
FT /note="BTB/POZ domain-containing protein 1"
FT /id="PRO_0000186209"
FT DOMAIN 75..151
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 190..290
FT /note="BACK"
FT /evidence="ECO:0000255"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..40
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 85
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0C5"
FT MUTAGEN 1..108
FT /note="Missing: Fails to induce myogenic differentiation in
FT C2C12 cells."
FT /evidence="ECO:0000269|PubMed:15486563"
FT CONFLICT 21
FT /note="G -> R (in Ref. 1; BAC40296)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="H -> P (in Ref. 1; BAC40296)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 488 AA; 53233 MW; 0CBDCA93EA10430F CRC64;
MASLGSAAAG EPATGAEAEP GPPAPPPPPP PPPAPSPSAL GPLLPLQREP LYNWQATKAS
LKERFAFLFN SELLSDVRFV LGKGRGAAAA GGPQRIPAHR FVLAAGSAVF DAMFNGGMAT
TSAEIELPDV EPAAFLALLR FLYSDEVQIG PETVMTTLYT AKKYAVPALE AHCVEFLTKH
LRADNAFMLL TQARLFDEPQ LASLCLDTID KSTVDAISAE GFTDIDIDTL CAVLERDTLS
IRESRLFGAI VRWAEAECQR QQLAVTFGNK QKVLGKALSL IRFPLMTIEE FAAGPAQSGI
LSDREVVNLF LHFTVNPKPR VEYIDRPRCC LRGKECCINR FQQVESRWGY SGTSDRIRFT
VNRRISVVGF GLYGSIHGPT DYQVNIQIIE YEKKQTLGQN DTGFSCDGTA NTFRVMFKEP
IEILPNVCYT ACATLKGPDS HYGTKGLKKV VHETPAASKT VFLFFSSPGN NNGTSIEDGQ
IPEIIFYT
