TCTP_HUMAN
ID TCTP_HUMAN Reviewed; 172 AA.
AC P13693; B2R7E5; Q6YLS2; Q7Z4J4; Q8TBK7; Q96EE2; Q9UC70;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=Translationally-controlled tumor protein;
DE Short=TCTP;
DE AltName: Full=Fortilin;
DE AltName: Full=Histamine-releasing factor;
DE Short=HRF;
DE AltName: Full=p23;
GN Name=TPT1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2813067; DOI=10.1093/nar/17.20.8367;
RA Gross B., Gaestel M., Boehm H., Bielka H.;
RT "cDNA sequence coding for a translationally controlled human tumor
RT protein.";
RL Nucleic Acids Res. 17:8367-8367(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RA Thiele H.;
RL Thesis (2000), Humboldt-University Berlin, Germany.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Gnanasekar M., Ramaswamy K.;
RT "Cloning and characterization of TCTP from human eosinophils.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Gao T.H., Duan F.L., Zhu W.L.;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Lung, and Placenta;
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 [10]
RP PROTEIN SEQUENCE OF 1-10.
RC TISSUE=Liver;
RX PubMed=1286669; DOI=10.1002/elps.11501301201;
RA Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
RA Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
RA Appel R.D., Hughes G.J.;
RT "Human liver protein map: a reference database established by
RT microsequencing and gel comparison.";
RL Electrophoresis 13:992-1001(1992).
RN [11]
RP PROTEIN SEQUENCE OF 1-4; 22-31; 39-45 AND 103-109.
RC TISSUE=Keratinocyte;
RX PubMed=1286667; DOI=10.1002/elps.11501301199;
RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA Vandekerckhove J.;
RT "Microsequences of 145 proteins recorded in the two-dimensional gel protein
RT database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [12]
RP PROTEIN SEQUENCE OF 1-19.
RC TISSUE=Mammary carcinoma;
RX PubMed=9150946; DOI=10.1002/elps.1150180342;
RA Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E., Simpson R.J.,
RA Dorow D.S.;
RT "Two-dimensional electrophoretic analysis of human breast carcinoma
RT proteins: mapping of proteins that bind to the SH3 domain of mixed lineage
RT kinase MLK2.";
RL Electrophoresis 18:588-598(1997).
RN [13]
RP PROTEIN SEQUENCE OF 1-18.
RX PubMed=7542803; DOI=10.1126/science.7542803;
RA MacDonald S.M., Rafnar T., Langdon J., Lichtenstein L.M.;
RT "Molecular identification of an IgE-dependent histamine-releasing factor.";
RL Science 269:688-690(1995).
RN [14]
RP PROTEIN SEQUENCE OF 6-34; 111-123 AND 131-164, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [15]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=9059837; DOI=10.1002/elps.1150180127;
RA Sanchez J.-C., Schaller D., Ravier F., Golaz O., Jaccoud S., Belet M.,
RA Wilkins M.R., James R., Deshusses J., Hochstrasser D.F.;
RT "Translationally controlled tumor protein: a protein identified in several
RT nontumoral cells including erythrocytes.";
RL Electrophoresis 18:150-155(1997).
RN [16]
RP PHOSPHORYLATION AT SER-46 AND SER-64.
RX PubMed=12167714; DOI=10.1128/mcb.22.17.6209-6221.2002;
RA Yarm F.R.;
RT "Plk phosphorylation regulates the microtubule-stabilizing protein TCTP.";
RL Mol. Cell. Biol. 22:6209-6221(2002).
RN [17]
RP INTERACTION WITH STEAP3.
RX PubMed=15319436; DOI=10.1074/jbc.m404850200;
RA Amzallag N., Passer B.J., Allanic D., Segura E., Thery C., Goud B.,
RA Amson R., Telerman A.;
RT "TSAP6 facilitates the secretion of translationally controlled tumor
RT protein/histamine-releasing factor via a nonclassical pathway.";
RL J. Biol. Chem. 279:46104-46112(2004).
RN [18]
RP CALCIUM-BINDING.
RX PubMed=15162379; DOI=10.1002/pros.20054;
RA Arcuri F., Papa S., Carducci A., Romagnoli R., Liberatori S.,
RA Riparbelli M.G., Sanchez J.-C., Tosi P., del Vecchio M.T.;
RT "Translationally controlled tumor protein (TCTP) in the human prostate and
RT prostate cancer cells: expression, distribution, and calcium binding
RT activity.";
RL Prostate 60:130-140(2004).
RN [19]
RP CALCIUM-BINDING.
RC TISSUE=Placenta;
RX PubMed=15958728; DOI=10.1095/biolreprod.105.042077;
RA Arcuri F., Papa S., Meini A., Carducci A., Romagnoli R., Bianchi L.,
RA Riparbelli M.G., Sanchez J.-C., Palmi M., Tosi P., Cintorino M.;
RT "The translationally controlled tumor protein is a novel calcium binding
RT protein of the human placenta and regulates calcium handling in trophoblast
RT cells.";
RL Biol. Reprod. 73:745-751(2005).
RN [20]
RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x;
RA Leong W.F., Chow V.T.;
RT "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal
RT differential cellular gene expression in response to enterovirus 71
RT infection.";
RL Cell. Microbiol. 8:565-580(2006).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-53, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [26]
RP STRUCTURE BY NMR.
RA Liu D.S., Feng Y.G., Wang J.F.;
RT "Solution structure of human translationally controlled tumor protein.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Involved in calcium binding and microtubule stabilization.
CC -!- SUBUNIT: Interacts with STEAP3. {ECO:0000269|PubMed:15319436}.
CC -!- INTERACTION:
CC P13693; P60709: ACTB; NbExp=4; IntAct=EBI-1783169, EBI-353944;
CC P13693; P05023: ATP1A1; NbExp=5; IntAct=EBI-1783169, EBI-358778;
CC P13693; P29692: EEF1D; NbExp=3; IntAct=EBI-1783169, EBI-358607;
CC P13693; P29692-2: EEF1D; NbExp=3; IntAct=EBI-1783169, EBI-5280572;
CC P13693; P38646: HSPA9; NbExp=4; IntAct=EBI-1783169, EBI-354932;
CC P13693; P04792: HSPB1; NbExp=2; IntAct=EBI-1783169, EBI-352682;
CC P13693; Q06830: PRDX1; NbExp=4; IntAct=EBI-1783169, EBI-353193;
CC P13693; Q15382: RHEB; NbExp=2; IntAct=EBI-1783169, EBI-1055287;
CC P13693; P04637: TP53; NbExp=7; IntAct=EBI-1783169, EBI-366083;
CC P13693; Q15645: TRIP13; NbExp=3; IntAct=EBI-1783169, EBI-358993;
CC P13693; Q15714: TSC22D1; NbExp=5; IntAct=EBI-1783169, EBI-712609;
CC P13693; Q9BQE3: TUBA1C; NbExp=4; IntAct=EBI-1783169, EBI-1103245;
CC P13693; P13010: XRCC5; NbExp=4; IntAct=EBI-1783169, EBI-357997;
CC P13693; P12956: XRCC6; NbExp=8; IntAct=EBI-1783169, EBI-353208;
CC P13693; P67809: YBX1; NbExp=4; IntAct=EBI-1783169, EBI-354065;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9059837}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P13693-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P13693-2; Sequence=VSP_054838;
CC -!- TISSUE SPECIFICITY: Found in several healthy and tumoral cells
CC including erythrocytes, hepatocytes, macrophages, platelets,
CC keratinocytes, erythroleukemia cells, gliomas, melanomas,
CC hepatoblastomas, and lymphomas. It cannot be detected in kidney and
CC renal cell carcinoma (RCC). Expressed in placenta and prostate.
CC {ECO:0000269|PubMed:9059837}.
CC -!- INDUCTION: Down-regulated in response to enterovirus 71 (EV71)
CC infection. {ECO:0000269|PubMed:16548883}.
CC -!- SIMILARITY: Belongs to the TCTP family. {ECO:0000255|PROSITE-
CC ProRule:PRU01133}.
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DR EMBL; X16064; CAA34200.1; -; mRNA.
DR EMBL; AJ400717; CAB87812.1; -; Genomic_DNA.
DR EMBL; AY334563; AAQ01550.1; -; mRNA.
DR EMBL; AY117678; AAM51565.1; -; mRNA.
DR EMBL; CR457036; CAG33317.1; -; mRNA.
DR EMBL; AK312951; BAG35792.1; -; mRNA.
DR EMBL; AL138963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08731.1; -; Genomic_DNA.
DR EMBL; CH471075; EAX08732.1; -; Genomic_DNA.
DR EMBL; BC003352; AAH03352.1; -; mRNA.
DR EMBL; BC012431; AAH12431.1; -; mRNA.
DR EMBL; BC022436; AAH22436.1; -; mRNA.
DR EMBL; BC052333; AAH52333.1; -; mRNA.
DR CCDS; CCDS66538.1; -. [P13693-2]
DR CCDS; CCDS9397.1; -. [P13693-1]
DR PIR; S06590; S06590.
DR RefSeq; NP_001273202.1; NM_001286273.1. [P13693-2]
DR RefSeq; NP_003286.1; NM_003295.3. [P13693-1]
DR PDB; 1YZ1; X-ray; 2.00 A; A/B/C/D=1-172.
DR PDB; 2HR9; NMR; -; A=1-172.
DR PDB; 3EBM; X-ray; 2.60 A; A/B/C/D=1-172.
DR PDB; 4Z9V; X-ray; 2.10 A; C/D/E/F/G/H=11-31.
DR PDB; 5O9L; X-ray; 1.75 A; A/B=1-172.
DR PDB; 5O9M; X-ray; 1.40 A; A/B=1-172.
DR PDB; 6IZB; X-ray; 1.90 A; A=1-172.
DR PDB; 6IZE; X-ray; 2.29 A; A/B/C/D=1-172.
DR PDBsum; 1YZ1; -.
DR PDBsum; 2HR9; -.
DR PDBsum; 3EBM; -.
DR PDBsum; 4Z9V; -.
DR PDBsum; 5O9L; -.
DR PDBsum; 5O9M; -.
DR PDBsum; 6IZB; -.
DR PDBsum; 6IZE; -.
DR AlphaFoldDB; P13693; -.
DR BMRB; P13693; -.
DR SMR; P13693; -.
DR BioGRID; 113030; 200.
DR DIP; DIP-40097N; -.
DR IntAct; P13693; 141.
DR MINT; P13693; -.
DR STRING; 9606.ENSP00000477781; -.
DR DrugBank; DB11093; Calcium citrate.
DR DrugBank; DB11348; Calcium Phosphate.
DR DrugBank; DB14481; Calcium phosphate dihydrate.
DR Allergome; 3816; Hom s TCTP.
DR iPTMnet; P13693; -.
DR MetOSite; P13693; -.
DR PhosphoSitePlus; P13693; -.
DR SwissPalm; P13693; -.
DR BioMuta; TPT1; -.
DR DMDM; 136479; -.
DR DOSAC-COBS-2DPAGE; P13693; -.
DR OGP; P13693; -.
DR REPRODUCTION-2DPAGE; IPI00550900; -.
DR SWISS-2DPAGE; P13693; -.
DR EPD; P13693; -.
DR jPOST; P13693; -.
DR MassIVE; P13693; -.
DR MaxQB; P13693; -.
DR PaxDb; P13693; -.
DR PeptideAtlas; P13693; -.
DR PRIDE; P13693; -.
DR ProteomicsDB; 52972; -. [P13693-1]
DR ProteomicsDB; 74026; -.
DR TopDownProteomics; P13693-1; -. [P13693-1]
DR Antibodypedia; 23600; 573 antibodies from 39 providers.
DR DNASU; 7178; -.
DR Ensembl; ENST00000379055.5; ENSP00000368344.1; ENSG00000133112.17. [P13693-2]
DR Ensembl; ENST00000379056.5; ENSP00000368345.1; ENSG00000133112.17. [P13693-2]
DR Ensembl; ENST00000530705.6; ENSP00000431872.2; ENSG00000133112.17. [P13693-1]
DR GeneID; 7178; -.
DR KEGG; hsa:7178; -.
DR MANE-Select; ENST00000530705.6; ENSP00000431872.2; NM_003295.4; NP_003286.1.
DR UCSC; uc001uzy.3; human. [P13693-1]
DR CTD; 7178; -.
DR DisGeNET; 7178; -.
DR GeneCards; TPT1; -.
DR HGNC; HGNC:12022; TPT1.
DR HPA; ENSG00000133112; Tissue enhanced (skeletal).
DR MIM; 600763; gene.
DR neXtProt; NX_P13693; -.
DR OpenTargets; ENSG00000133112; -.
DR PharmGKB; PA36701; -.
DR VEuPathDB; HostDB:ENSG00000133112; -.
DR eggNOG; KOG1727; Eukaryota.
DR GeneTree; ENSGT00390000006051; -.
DR HOGENOM; CLU_095877_0_1_1; -.
DR InParanoid; P13693; -.
DR OMA; IVYEADC; -.
DR PhylomeDB; P13693; -.
DR TreeFam; TF300238; -.
DR PathwayCommons; P13693; -.
DR SignaLink; P13693; -.
DR SIGNOR; P13693; -.
DR BioGRID-ORCS; 7178; 642 hits in 1065 CRISPR screens.
DR ChiTaRS; TPT1; human.
DR EvolutionaryTrace; P13693; -.
DR GeneWiki; TPT1; -.
DR GeneWiki; Translationally-controlled_tumor_protein; -.
DR GenomeRNAi; 7178; -.
DR Pharos; P13693; Tbio.
DR PRO; PR:P13693; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; P13693; protein.
DR Bgee; ENSG00000133112; Expressed in ileal mucosa and 213 other tissues.
DR ExpressionAtlas; P13693; baseline and differential.
DR Genevisible; P13693; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005771; C:multivesicular body; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; IC:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IC:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
DR GO; GO:2000384; P:negative regulation of ectoderm development; IEA:Ensembl.
DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; NAS:UniProtKB.
DR GO; GO:0009615; P:response to virus; IEP:UniProtKB.
DR GO; GO:0019827; P:stem cell population maintenance; IEA:Ensembl.
DR DisProt; DP01972; -.
DR Gene3D; 2.170.150.10; -; 1.
DR IDEAL; IID00651; -.
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; Alternative splicing; Calcium; Cytoplasm;
KW Direct protein sequencing; Phosphoprotein; Reference proteome.
FT CHAIN 1..172
FT /note="Translationally-controlled tumor protein"
FT /id="PRO_0000211268"
FT DOMAIN 1..172
FT /note="TCTP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01133"
FT MOD_RES 46
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000269|PubMed:12167714,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 64
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000269|PubMed:12167714"
FT VAR_SEQ 1..34
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054838"
FT VARIANT 146
FT /note="V -> F (in dbSNP:rs3087989)"
FT /id="VAR_052273"
FT CONFLICT 53..54
FT /note="SA -> YG (in Ref. 9; AAH12431)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="E -> K (in Ref. 3; AAQ01550)"
FT /evidence="ECO:0000305"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:5O9M"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:5O9M"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:5O9M"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:5O9M"
FT TURN 24..27
FT /evidence="ECO:0007829|PDB:5O9M"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:5O9M"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:5O9M"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:2HR9"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:5O9M"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:5O9M"
FT HELIX 71..76
FT /evidence="ECO:0007829|PDB:5O9M"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:5O9M"
FT HELIX 85..106
FT /evidence="ECO:0007829|PDB:5O9M"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:5O9M"
FT HELIX 111..127
FT /evidence="ECO:0007829|PDB:5O9M"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:5O9M"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:5O9M"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:5O9M"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:5O9M"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:5O9M"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:5O9M"
SQ SEQUENCE 172 AA; 19595 MW; BD31399B71CA62F9 CRC64;
MIIYRDLISH DEMFSDIYKI REIADGLCLE VEGKMVSRTE GNIDDSLIGG NASAEGPEGE
GTESTVITGV DIVMNHHLQE TSFTKEAYKK YIKDYMKSIK GKLEEQRPER VKPFMTGAAE
QIKHILANFK NYQFFIGENM NPDGMVALLD YREDGVTPYM IFFKDGLEME KC
