TCTP_MOUSE
ID TCTP_MOUSE Reviewed; 172 AA.
AC P63028; P14701; Q3TMT0; Q3TWS8; Q3TWX0; Q3UAG7; Q569M9;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Translationally-controlled tumor protein;
DE Short=TCTP;
DE AltName: Full=21 kDa polypeptide;
DE AltName: Full=p21;
DE AltName: Full=p23;
GN Name=Tpt1; Synonyms=Trt;
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=3357792; DOI=10.1093/nar/16.5.2350;
RA Makrides S., Chitpatima S.T., Bandyopadhyay R., Brawerman G.;
RT "Nucleotide sequence of a major messenger RNA for a 21 kilodalton
RT polypeptide that is under translational control in mouse tumor cells.";
RL Nucleic Acids Res. 16:2350-2350(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=2479380;
RA Boehm H., Beendorf R., Gaestel M., Gross B., Nuernberg P., Kraft R.,
RA Otto A., Bielka H.;
RT "The growth-related protein P23 of the Ehrlich ascites tumor: translational
RT control, cloning and primary structure.";
RL Biochem. Int. 19:277-286(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=12782126; DOI=10.1016/s0888-7543(03)00047-8;
RA Fiucci G., Lespagnol A., Stumptner-Cuvelette P., Beaucourt S., Duflaut D.,
RA Susini L., Amson R., Telerman A.;
RT "Genomic organization and expression of mouse Tpt1 gene.";
RL Genomics 81:570-578(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, C57BL/6J, DBA/2J, and NOD;
RC TISSUE=Bone marrow, Brain, Placenta, and 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [6]
RP PROTEIN SEQUENCE OF 6-19, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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 -!- FUNCTION: Involved in calcium binding and microtubule stabilization.
CC {ECO:0000250}.
CC -!- SUBUNIT: Seems to self-interact. Interacts with STEAP3 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC P63028; P09405: Ncl; NbExp=4; IntAct=EBI-1635228, EBI-641864;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Preferentially synthesized in cells of the early
CC growth phase of Ehrlich ascites tumor. {ECO:0000269|PubMed:2479380}.
CC -!- SIMILARITY: Belongs to the TCTP family. {ECO:0000255|PROSITE-
CC ProRule:PRU01133}.
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DR EMBL; X06407; CAA29697.1; -; mRNA.
DR EMBL; AY186881; AAP23875.1; -; Genomic_DNA.
DR EMBL; AK149695; BAE29032.1; -; mRNA.
DR EMBL; AK150300; BAE29452.1; -; mRNA.
DR EMBL; AK150500; BAE29613.1; -; mRNA.
DR EMBL; AK150858; BAE29913.1; -; mRNA.
DR EMBL; AK151059; BAE30076.1; -; mRNA.
DR EMBL; AK151266; BAE30253.1; -; mRNA.
DR EMBL; AK151375; BAE30347.1; -; mRNA.
DR EMBL; AK151894; BAE30778.1; -; mRNA.
DR EMBL; AK152690; BAE31421.1; -; mRNA.
DR EMBL; AK152808; BAE31513.1; -; mRNA.
DR EMBL; AK159516; BAE35146.1; -; mRNA.
DR EMBL; AK159565; BAE35188.1; -; mRNA.
DR EMBL; AK165736; BAE38361.1; -; mRNA.
DR EMBL; AK166584; BAE38873.1; -; mRNA.
DR EMBL; AK167413; BAE39502.1; -; mRNA.
DR EMBL; AK167936; BAE39940.1; -; mRNA.
DR EMBL; AK168151; BAE40116.1; -; mRNA.
DR EMBL; AK169730; BAE41334.1; -; mRNA.
DR EMBL; BC092381; AAH92381.1; -; mRNA.
DR CCDS; CCDS36980.1; -.
DR PIR; S00775; S00775.
DR RefSeq; NP_033455.1; NM_009429.3.
DR PDB; 5O9K; X-ray; 4.01 A; A/B=1-172.
DR PDBsum; 5O9K; -.
DR AlphaFoldDB; P63028; -.
DR SMR; P63028; -.
DR BioGRID; 204334; 89.
DR IntAct; P63028; 11.
DR MINT; P63028; -.
DR STRING; 10090.ENSMUSP00000106519; -.
DR iPTMnet; P63028; -.
DR PhosphoSitePlus; P63028; -.
DR SwissPalm; P63028; -.
DR REPRODUCTION-2DPAGE; IPI00129685; -.
DR REPRODUCTION-2DPAGE; P63028; -.
DR SWISS-2DPAGE; P63028; -.
DR EPD; P63028; -.
DR jPOST; P63028; -.
DR MaxQB; P63028; -.
DR PaxDb; P63028; -.
DR PeptideAtlas; P63028; -.
DR PRIDE; P63028; -.
DR ProteomicsDB; 262843; -.
DR TopDownProteomics; P63028; -.
DR Antibodypedia; 23600; 573 antibodies from 39 providers.
DR DNASU; 22070; -.
DR Ensembl; ENSMUST00000110894; ENSMUSP00000106519; ENSMUSG00000060126.
DR GeneID; 22070; -.
DR KEGG; mmu:22070; -.
DR UCSC; uc007uqz.2; mouse.
DR CTD; 7178; -.
DR MGI; MGI:104890; Tpt1.
DR VEuPathDB; HostDB:ENSMUSG00000060126; -.
DR eggNOG; KOG1727; Eukaryota.
DR GeneTree; ENSGT00390000006051; -.
DR InParanoid; P63028; -.
DR OMA; IVYEADC; -.
DR OrthoDB; 1439384at2759; -.
DR PhylomeDB; P63028; -.
DR TreeFam; TF300238; -.
DR BioGRID-ORCS; 22070; 24 hits in 75 CRISPR screens.
DR ChiTaRS; Tpt1; mouse.
DR PRO; PR:P63028; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P63028; protein.
DR Bgee; ENSMUSG00000060126; Expressed in ventricular zone and 61 other tissues.
DR ExpressionAtlas; P63028; baseline and differential.
DR Genevisible; P63028; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005771; C:multivesicular body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:2000384; P:negative regulation of ectoderm development; IMP:BHF-UCL.
DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; ISO:MGI.
DR GO; GO:0009615; P:response to virus; IEA:Ensembl.
DR GO; GO:0019827; P:stem cell population maintenance; IMP:BHF-UCL.
DR DisProt; DP02800; -.
DR Gene3D; 2.170.150.10; -; 1.
DR InterPro; IPR011057; Mss4-like_sf.
DR InterPro; IPR011323; Mss4/transl-control_tumour.
DR InterPro; IPR034737; TCTP.
DR InterPro; IPR018103; Translation_control_tumour_CS.
DR InterPro; IPR018105; Translational_control_tumour_p.
DR PANTHER; PTHR11991; PTHR11991; 1.
DR Pfam; PF00838; TCTP; 1.
DR PRINTS; PR01653; TCTPROTEIN.
DR SUPFAM; SSF51316; SSF51316; 1.
DR PROSITE; PS01002; TCTP_1; 1.
DR PROSITE; PS01003; TCTP_2; 1.
DR PROSITE; PS51797; TCTP_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cytoplasm; Direct protein sequencing;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..172
FT /note="Translationally-controlled tumor protein"
FT /id="PRO_0000211269"
FT DOMAIN 1..172
FT /note="TCTP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01133"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13693"
FT MOD_RES 64
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:P13693"
FT CONFLICT 17
FT /note="I -> N (in Ref. 4; BAE30347)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="A -> V (in Ref. 4; BAE35146)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="P -> Q (in Ref. 4; BAE35188)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="E -> G (in Ref. 4; BAE29613/BAE38361)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 172 AA; 19462 MW; 7F46751DA2D281D2 CRC64;
MIIYRDLISH DELFSDIYKI REIADGLCLE VEGKMVSRTE GAIDDSLIGG NASAEGPEGE
GTESTVVTGV DIVMNHHLQE TSFTKEAYKK YIKDYMKSLK GKLEEQKPER VKPFMTGAAE
QIKHILANFN NYQFFIGENM NPDGMVALLD YREDGVTPFM IFFKDGLEME KC
