TBRG1_MOUSE
ID TBRG1_MOUSE Reviewed; 406 AA.
AC Q3UB74; Q3TLE7; Q3UCG2; Q3YBR3; Q6P067; Q80XA1; Q8CGC5;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Transforming growth factor beta regulator 1;
DE AltName: Full=Nuclear interactor of ARF and Mdm2;
GN Name=Tbrg1; Synonyms=Niam;
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], FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH CDKN2A AND MDM2.
RC TISSUE=Liver;
RX PubMed=17110379; DOI=10.1074/jbc.m609612200;
RA Tompkins V.S., Hagen J., Frazier A.A., Lushnikova T., Fitzgerald M.P.,
RA di Tommaso A.D., Ladeveze V., Domann F.E., Eischen C.M., Quelle D.E.;
RT "A novel nuclear interactor of ARF and MDM2 (NIAM) that maintains
RT chromosomal stability.";
RL J. Biol. Chem. 282:1322-1333(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
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 STRAIN=C57BL/6J, FVB/N, and FVB/N-3;
RC TISSUE=Brain, Kidney, Mammary gland, 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).
RN [4]
RP INDUCTION.
RX PubMed=7654366; DOI=10.1002/mrd.1080410203;
RA Babalola G.O., Schultz R.M.;
RT "Modulation of gene expression in the preimplantation mouse embryo by TGF-
RT alpha and TGF-beta.";
RL Mol. Reprod. Dev. 41:133-139(1995).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT THR-13, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC -!- FUNCTION: Acts as a growth inhibitor. Can activate p53/TP53, causes G1
CC arrest and collaborates with CDKN2A to restrict proliferation, but does
CC not require either protein to inhibit DNA synthesis. Redistributes
CC CDKN2A into the nucleoplasm. Involved in maintaining chromosomal
CC stability. {ECO:0000269|PubMed:17110379}.
CC -!- SUBUNIT: Interacts with CDKN2A and MDM2. {ECO:0000269|PubMed:17110379}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17110379}.
CC -!- INDUCTION: Induced in cells undergoing arrest in response to DNA damage
CC and TGFB1 treatment. {ECO:0000269|PubMed:7654366}.
CC -!- PTM: Ubiquitinated; mediated by MDM2 and leading to its subsequent
CC proteasomal degradation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TBRG1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH21331.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH40813.3; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH43022.3; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH65795.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ144541; AAZ76015.1; -; mRNA.
DR EMBL; AK150549; BAE29651.1; -; mRNA.
DR EMBL; AK151075; BAE30090.1; -; mRNA.
DR EMBL; AK151457; BAE30416.1; -; mRNA.
DR EMBL; AK151209; BAE30204.1; -; mRNA.
DR EMBL; AK166547; BAE38845.1; -; mRNA.
DR EMBL; BC021331; AAH21331.1; ALT_INIT; mRNA.
DR EMBL; BC040813; AAH40813.3; ALT_INIT; mRNA.
DR EMBL; BC043022; AAH43022.3; ALT_INIT; mRNA.
DR EMBL; BC065795; AAH65795.1; ALT_INIT; mRNA.
DR CCDS; CCDS52771.1; -.
DR RefSeq; NP_079565.2; NM_025289.3.
DR AlphaFoldDB; Q3UB74; -.
DR SMR; Q3UB74; -.
DR BioGRID; 203980; 6.
DR IntAct; Q3UB74; 1.
DR MINT; Q3UB74; -.
DR STRING; 10090.ENSMUSP00000112600; -.
DR iPTMnet; Q3UB74; -.
DR PhosphoSitePlus; Q3UB74; -.
DR EPD; Q3UB74; -.
DR MaxQB; Q3UB74; -.
DR PaxDb; Q3UB74; -.
DR PeptideAtlas; Q3UB74; -.
DR PRIDE; Q3UB74; -.
DR ProteomicsDB; 263013; -.
DR Antibodypedia; 45986; 147 antibodies from 25 providers.
DR DNASU; 21376; -.
DR Ensembl; ENSMUST00000117654; ENSMUSP00000112600; ENSMUSG00000011114.
DR GeneID; 21376; -.
DR KEGG; mmu:21376; -.
DR UCSC; uc009ovh.1; mouse.
DR CTD; 84897; -.
DR MGI; MGI:1100877; Tbrg1.
DR VEuPathDB; HostDB:ENSMUSG00000011114; -.
DR eggNOG; KOG4443; Eukaryota.
DR GeneTree; ENSGT00390000013374; -.
DR HOGENOM; CLU_037126_0_0_1; -.
DR InParanoid; Q3UB74; -.
DR OMA; FFGISHP; -.
DR OrthoDB; 1397649at2759; -.
DR PhylomeDB; Q3UB74; -.
DR TreeFam; TF324736; -.
DR BioGRID-ORCS; 21376; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Tbrg1; mouse.
DR PRO; PR:Q3UB74; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q3UB74; protein.
DR Bgee; ENSMUSG00000011114; Expressed in ectoplacental cone and 277 other tissues.
DR ExpressionAtlas; Q3UB74; baseline and differential.
DR Genevisible; Q3UB74; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:HGNC-UCL.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; ISS:HGNC-UCL.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:HGNC-UCL.
DR GO; GO:1990173; P:protein localization to nucleoplasm; ISS:HGNC-UCL.
DR GO; GO:0050821; P:protein stabilization; ISS:HGNC-UCL.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:HGNC-UCL.
DR InterPro; IPR003889; FYrich_C.
DR InterPro; IPR003888; FYrich_N.
DR InterPro; IPR040092; TBRG1.
DR PANTHER; PTHR22715; PTHR22715; 1.
DR Pfam; PF05965; FYRC; 1.
DR Pfam; PF05964; FYRN; 1.
DR SMART; SM00542; FYRC; 1.
DR SMART; SM00541; FYRN; 1.
DR PROSITE; PS51543; FYRC; 1.
DR PROSITE; PS51542; FYRN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Nucleus; Phosphoprotein; Reference proteome;
KW Tumor suppressor; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:17242355"
FT CHAIN 2..406
FT /note="Transforming growth factor beta regulator 1"
FT /id="PRO_0000274219"
FT DOMAIN 177..236
FT /note="FYR N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00875"
FT DOMAIN 237..316
FT /note="FYR C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00876"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 13
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT CONFLICT 32
FT /note="K -> M (in Ref. 2; BAE29651)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="I -> T (in Ref. 2; BAE30090)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="Y -> C (in Ref. 2; BAE30090)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="Y -> N (in Ref. 2; BAE29651)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="L -> P (in Ref. 2; BAE30090)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="S -> G (in Ref. 2; BAE38845)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="P -> L (in Ref. 3; AAH43022)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="H -> Y (in Ref. 2; BAE38845)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 406 AA; 44881 MW; EBF4AED368200625 CRC64;
MSVLSGLASE PRTPLSSKAR MKRLPRKSQN EKYRLKYLRL RRAAKATVFE NASICDEIAR
LEEKFLKAKE ERRYLLKKLL QIHALTEGEP QAAAPSHSSS LPLPYGVTSS VGTMQGAGPS
TGAEEPFAKK SKKEKKEKGK ENSKLEVLKK TSKKKKMEGG ARKLVRPIAL DPSGQPVFPI
GLGGLTVYSL GEIITNRPGF HDENAIYPVG YCSTRVYASM KCPDQKCLYT CQIKDGGVQP
QFEIVPEDDP QNTIVGSSAD ACYEELLRAI SATTGKLMPN PLSCGADFFG FSHPTIHNLI
QSCPEAQNCV NYQWVKFDAC KPRKGQLSQE LPENDATMSL EAFQTQTFDD DHDDSILPGS
LDLPELQHEA FVSSYQPEFL THEPLVDTDL QHLKSPSQCS PIQSSD
