ID   TBRG1_RAT               Reviewed;         406 AA.
AC   Q5PQK8;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 2.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Transforming growth factor beta regulator 1;
GN   Name=Tbrg1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=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).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CDKN2A and MDM2. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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=AAH87142.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC087142; AAH87142.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001009344.2; NM_001009344.2.
DR   AlphaFoldDB; Q5PQK8; -.
DR   SMR; Q5PQK8; -.
DR   STRING; 10116.ENSRNOP00000037323; -.
DR   iPTMnet; Q5PQK8; -.
DR   PhosphoSitePlus; Q5PQK8; -.
DR   PaxDb; Q5PQK8; -.
DR   PRIDE; Q5PQK8; -.
DR   Ensembl; ENSRNOT00000039729; ENSRNOP00000037323; ENSRNOG00000023850.
DR   GeneID; 300521; -.
DR   KEGG; rno:300521; -.
DR   UCSC; RGD:1305123; rat.
DR   CTD; 84897; -.
DR   RGD; 1305123; Tbrg1.
DR   eggNOG; KOG4443; Eukaryota.
DR   GeneTree; ENSGT00390000013374; -.
DR   HOGENOM; CLU_037126_0_0_1; -.
DR   InParanoid; Q5PQK8; -.
DR   OMA; FFGISHP; -.
DR   OrthoDB; 1397649at2759; -.
DR   PhylomeDB; Q5PQK8; -.
DR   TreeFam; TF324736; -.
DR   PRO; PR:Q5PQK8; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000023850; Expressed in ovary and 19 other tissues.
DR   Genevisible; Q5PQK8; RN.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; ISO:RGD.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR   GO; GO:1990173; P:protein localization to nucleoplasm; ISO:RGD.
DR   GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR   GO; GO:0051726; P:regulation of cell cycle; ISO:RGD.
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   2: Evidence at transcript level;
KW   Acetylation; Cell cycle; Nucleus; Phosphoprotein; Reference proteome;
KW   Tumor suppressor; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q3YBR2"
FT   CHAIN           2..406
FT                   /note="Transforming growth factor beta regulator 1"
FT                   /id="PRO_0000274220"
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..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          116..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:0000250|UniProtKB:Q3YBR2"
FT   MOD_RES         13
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UB74"
SQ   SEQUENCE   406 AA;  44785 MW;  9A35F69DFF8BEE18 CRC64;
     MSVLSGLASE PRTPLSSKAR MKRLPKKNQN EKYRLKYLRL RRAAKATVFE NAAVCDEIAR
     LEEKFLKAKE ERRYLLKKLL QIHALTEGEP QAAAPSHSSS LPLAYGVTSS VGTIQGAGPS
     TGAEEPFAKK SKKEKKEKGK ENSKLEVLKK TSKRKKMEGG ARKLVRPIAL DPSGQPVFPI
     GLGGLTVYSL GEIITNRPGF HDENAIYPVG YCSTRVYASM KCPDQKCLYT CQIKDGGVQP
     QFEIVPEDDP RNTIVGSSAD ACYEELLRAI SAATGKLMPN PLSCGADFFG FSHPTIHNLI
     QSCPEAQNCV NYQWVKFDAC KPRKGQLSQE LPENDAAMSL EAFPTQTFDD DHEDSILPGS
     LDLPELQHEA FVSSYQPEFL THEPLVDTDL QHLKSPSQCS PIQSSD