TPD53_MOUSE
ID TPD53_MOUSE Reviewed; 204 AA.
AC O54818;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Tumor protein D53;
DE Short=mD53;
DE AltName: Full=Tumor protein D52-like 1;
GN Name=Tpd52l1;
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].
RX PubMed=8812487; DOI=10.1006/geno.1996.0393;
RA Byrne J.A., Mattei M.-G., Basset P.;
RT "Definition of the tumor protein D52 (TPD52) gene family through cloning of
RT D52 homologues in human (hD53) and mouse (mD52).";
RL Genomics 35:523-532(1996).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- SUBUNIT: Forms a homodimer or heterodimer with other members of the
CC family. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TPD52 family. {ECO:0000305}.
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DR EMBL; AF004428; AAC98476.1; -; mRNA.
DR CCDS; CCDS35877.1; -.
DR RefSeq; NP_033439.1; NM_009413.1.
DR AlphaFoldDB; O54818; -.
DR SMR; O54818; -.
DR STRING; 10090.ENSMUSP00000000305; -.
DR iPTMnet; O54818; -.
DR PhosphoSitePlus; O54818; -.
DR MaxQB; O54818; -.
DR PaxDb; O54818; -.
DR PRIDE; O54818; -.
DR ProteomicsDB; 297504; -.
DR Antibodypedia; 32681; 257 antibodies from 35 providers.
DR DNASU; 21987; -.
DR Ensembl; ENSMUST00000000305; ENSMUSP00000000305; ENSMUSG00000000296.
DR GeneID; 21987; -.
DR KEGG; mmu:21987; -.
DR UCSC; uc007ets.1; mouse.
DR CTD; 7164; -.
DR MGI; MGI:1298386; Tpd52l1.
DR VEuPathDB; HostDB:ENSMUSG00000000296; -.
DR eggNOG; KOG4010; Eukaryota.
DR GeneTree; ENSGT00940000159202; -.
DR HOGENOM; CLU_080743_0_0_1; -.
DR InParanoid; O54818; -.
DR OrthoDB; 1225782at2759; -.
DR PhylomeDB; O54818; -.
DR TreeFam; TF317562; -.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR BioGRID-ORCS; 21987; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Tpd52l1; mouse.
DR PRO; PR:O54818; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; O54818; protein.
DR Bgee; ENSMUSG00000000296; Expressed in seminal vesicle and 247 other tissues.
DR ExpressionAtlas; O54818; baseline and differential.
DR Genevisible; O54818; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:MGI.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:MGI.
DR InterPro; IPR007327; TPD52.
DR PANTHER; PTHR19307; PTHR19307; 1.
DR Pfam; PF04201; TPD52; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Methylation; Phosphoprotein; Reference proteome.
FT CHAIN 1..204
FT /note="Tumor protein D53"
FT /id="PRO_0000185742"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 22..73
FT /evidence="ECO:0000255"
FT COMPBIAS 174..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16890"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16890"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16890"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16890"
FT MOD_RES 133
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q16890"
FT MOD_RES 146
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16890"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16890"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16890"
SQ SEQUENCE 204 AA; 22515 MW; BAA49DAC7B7F6BE8 CRC64;
MEAQAQGLLE TEPLQGRDGD AVGSADFSSM LSEEEKEELK AELIQLEDEI TTLRQVLSAK
ERHLVEIKQK LGMNLMNELK QNFSRSWHDM QTTTAYKKTH ETLSHAGQKA TAAFNNVGTA
ISKKFGDMRY SIRHSISMPA MRNSSTFKSF EERVETTVAS LKTKVGGTNH GGGSFEEVLN
STAHASSQNA SAGSRQTKDE ELQC
