ID MCTS1_HUMAN Reviewed; 181 AA. AC Q9ULC4; B4DGY2; Q502X6; DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 28-JAN-2026, entry version 188. DE RecName: Full=Malignant T-cell-amplified sequence 1; DE Short=MCT-1; DE AltName: Full=Multiple copies T-cell malignancies; GN Name=MCTS1; Synonyms=MCT1; 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), FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=9766643; RA Prosniak M., Dierov J., Okami K., Tilton B., Jameson B., Sawaya B.E., RA Gartenhaus R.B.; RT "A novel candidate oncogene, MCT-1, is involved in cell cycle RT progression."; RL Cancer Res. 58:4233-4237(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=16533400; DOI=10.1186/1471-2164-7-48; RA Kemmer D., Podowski R.M., Arenillas D., Lim J., Hodges E., Roth P., RA Sonnhammer E.L.L., Hoeoeg C., Wasserman W.W.; RT "NovelFam3000 -- uncharacterized human protein domains conserved across RT model organisms."; RL BMC Genomics 7:48-48(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Brain; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [5] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Chondrosarcoma, and Eye; 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 [7] RP FUNCTION. RX PubMed=10440924; RX DOI=10.1002/(sici)1097-4644(19990915)74:4<544::aid-jcb4>3.3.co;2-w; RA Dierov J., Prosniak M., Gallia G., Gartenhaus R.B.; RT "Increased G1 cyclin/cdk activity in cells overexpressing the candidate RT oncogene, MCT-1."; RL J. Cell. Biochem. 74:544-550(1999). RN [8] RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION. RX PubMed=11709712; DOI=10.1038/sj.onc.1204881; RA Herbert G.B., Shi B., Gartenhaus R.B.; RT "Expression and stabilization of the MCT-1 protein by DNA damaging RT agents."; RL Oncogene 20:6777-6783(2001). RN [9] RP FUNCTION. RX PubMed=12637315; DOI=10.1182/blood-2002-11-3486; RA Shi B., Hsu H.-L., Evens A.M., Gordon L.I., Gartenhaus R.B.; RT "Expression of the candidate MCT-1 oncogene in B- and T-cell lymphoid RT malignancies."; RL Blood 102:297-302(2003). RN [10] RP FUNCTION. RX PubMed=16322206; DOI=10.1158/0008-5472.can-05-0845; RA Levenson A.S., Thurn K.E., Simons L.A., Veliceasa D., Jarrett J., Osipo C., RA Jordan V.C., Volpert O.V., Satcher R.L. Jr., Gartenhaus R.B.; RT "MCT-1 oncogene contributes to increased in vivo tumorigenicity of MCF7 RT cells by promotion of angiogenesis and inhibition of apoptosis."; RL Cancer Res. 65:10651-10656(2005). RN [11] RP FUNCTION. RX PubMed=15897892; DOI=10.1038/sj.onc.1208680; RA Hsu H.-L., Shi B., Gartenhaus R.B.; RT "The MCT-1 oncogene product impairs cell cycle checkpoint control and RT transforms human mammary epithelial cells."; RL Oncogene 24:4956-4964(2005). RN [12] RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN PUA, AND INTERACTION WITH DENR. RX PubMed=16982740; DOI=10.1158/0008-5472.can-06-1999; RA Reinert L.S., Shi B., Nandi S., Mazan-Mamczarz K., Vitolo M., Bachman K.E., RA He H., Gartenhaus R.B.; RT "MCT-1 protein interacts with the cap complex and modulates messenger RNA RT translational profiles."; RL Cancer Res. 66:8994-9001(2006). RN [13] RP FUNCTION. RX PubMed=17416211; DOI=10.1016/j.dnarep.2007.02.028; RA Hsu H.-L., Choy C.O., Kasiappan R., Shih H.-J., Sawyer J.R., Shu C.-L., RA Chu K.-L., Chen Y.-R., Hsu H.-F., Gartenhaus R.B.; RT "MCT-1 oncogene downregulates p53 and destabilizes genome structure in the RT response to DNA double-strand damage."; RL DNA Repair 6:1319-1332(2007). RN [14] RP FUNCTION, PHOSPHORYLATION AT THR-81 AND SER-118, AND MUTAGENESIS OF THR-81 RP AND SER-118. RX PubMed=17016429; DOI=10.1038/sj.onc.1210030; RA Nandi S., Reinert L.S., Hachem A., Mazan-Mamczarz K., Hagner P., He H., RA Gartenhaus R.B.; RT "Phosphorylation of MCT-1 by p44/42 MAPK is required for its stabilization RT in response to DNA damage."; RL Oncogene 26:2283-2289(2007). RN [15] RP FUNCTION. RX PubMed=20713520; DOI=10.1101/gad.1957510; RA Skabkin M.A., Skabkina O.V., Dhote V., Komar A.A., Hellen C.U., RA Pestova T.V.; RT "Activities of ligatin and MCT-1/DENR in eukaryotic translation initiation RT and ribosomal recycling."; RL Genes Dev. 24:1787-1801(2010). RN [16] 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 [17] 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 [18] RP FUNCTION, INTERACTION WITH DENR, AND INVOLVEMENT IN IMD118. RX PubMed=37875108; DOI=10.1016/j.cell.2023.09.024; RA Bohlen J., Zhou Q., Philippot Q., Ogishi M., Rinchai D., Nieminen T., RA Seyedpour S., Parvaneh N., Rezaei N., Yazdanpanah N., Momenilandi M., RA Conil C., Neehus A.L., Schmidt C., Arango-Franco C.A., Voyer T.L., Khan T., RA Yang R., Puchan J., Erazo L., Roiuk M., Vatovec T., Janda Z., Bagaric I., RA Materna M., Gervais A., Li H., Rosain J., Peel J.N., Seeleuthner Y., RA Han J.E., L'Honneur A.S., Moncada-Velez M., Martin-Fernandez M., RA Horesh M.E., Kochetkov T., Schmidt M., AlShehri M.A., Salo E., Saxen H., RA ElGhazali G., Yatim A., Soudee C., Sallusto F., Ensser A., Marr N., RA Zhang P., Bogunovic D., Cobat A., Shahrooei M., Beziat V., Abel L., RA Wang X., Boisson-Dupuis S., Teleman A.A., Bustamante J., Zhang Q., RA Casanova J.L.; RT "Human MCTS1-dependent translation of JAK2 is essential for IFN-gamma RT immunity to mycobacteria."; RL Cell 186:5114.27-5134.e27(2023). CC -!- FUNCTION: Translation regulator forming a complex with DENR to promote CC translation reinitiation. Translation reinitiation is the process where CC the small ribosomal subunit remains attached to the mRNA following CC termination of translation of a regulatory upstream ORF (uORF), and CC resume scanning on the same mRNA molecule to initiate translation of a CC downstream ORF, usually the main ORF (mORF). The MCTS1/DENR complex is CC pivotal to two linked mechanisms essential for translation CC reinitiation. Firstly, the dissociation of deacylated tRNAs from post- CC termination 40S ribosomal complexes during ribosome recycling. CC Secondly, the recruitment in an EIF2-independent manner of CC aminoacylated initiator tRNA to P site of 40S ribosomes for a new round CC of translation (PubMed:16982740, PubMed:20713520, PubMed:37875108). CC This regulatory mechanism governs the translation of more than 150 CC genes which translation reinitiation is MCTS1/DENR complex-dependent CC (PubMed:16982740, PubMed:20713520, PubMed:37875108). Consequently, CC modulates various unrelated biological processes including cell cycle CC regulation and DNA damage signaling and repair (PubMed:10440924, CC PubMed:11709712, PubMed:12637315, PubMed:15897892, PubMed:16322206, CC PubMed:17016429, PubMed:17416211, PubMed:9766643). Notably, it CC positively regulates interferon gamma immunity to mycobacteria by CC enhancing the translation of JAK2 (PubMed:37875108). CC {ECO:0000269|PubMed:10440924, ECO:0000269|PubMed:11709712, CC ECO:0000269|PubMed:12637315, ECO:0000269|PubMed:15897892, CC ECO:0000269|PubMed:16322206, ECO:0000269|PubMed:16982740, CC ECO:0000269|PubMed:17016429, ECO:0000269|PubMed:17416211, CC ECO:0000269|PubMed:20713520, ECO:0000269|PubMed:37875108, CC ECO:0000269|PubMed:9766643}. CC -!- SUBUNIT: Interacts (via PUA domain) with DENR; the complex regulates CC translation reinitiation. {ECO:0000269|PubMed:16982740, CC ECO:0000269|PubMed:37875108}. CC -!- INTERACTION: CC Q9ULC4; O43583: DENR; NbExp=11; IntAct=EBI-716076, EBI-716083; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11709712, CC ECO:0000269|PubMed:16982740}. Note=Nuclear relocalization after DNA CC damage. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9ULC4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9ULC4-2; Sequence=VSP_034856; CC Name=3; CC IsoId=Q9ULC4-3; Sequence=VSP_041352; CC -!- TISSUE SPECIFICITY: Ubiquitous. Over-expressed in T-cell lymphoid cell CC lines and in non-Hodgkin lymphoma cell lines as well as in a subset of CC primary large B-cell lymphomas. {ECO:0000269|PubMed:9766643}. CC -!- INDUCTION: By DNA damaging agents such as gamma irradiation, adriamycin CC or taxol in lymphoid cells, but not by stress stimuli such as heat CC shock. This induction of protein expression does not occur at the RNA CC level, and does not require new protein synthesis. CC {ECO:0000269|PubMed:11709712}. CC -!- DOMAIN: The PUA RNA-binding domain is critical for cap binding, but not CC sufficient for translation enhancer function. MCT1 N-terminal region is CC required to enhance translation possibly through interaction with other CC proteins. {ECO:0000269|PubMed:16982740}. CC -!- PTM: Phosphorylation is critical for stabilization and promotion of CC cell proliferation. {ECO:0000269|PubMed:17016429}. CC -!- DISEASE: Immunodeficiency 118 (IMD118) [MIM:301115]: An X-linked CC recessive disorder characterized by increased susceptibility to CC disseminated mycobacterial infections in infancy, notably after CC Bacillus Calmette-Guerin (BCG) vaccination. Initial clinical features CC include fever, lymphadenopathy, hepatosplenomegaly, abscesses, and CC osteomyelitis. Affected males usually recover with treatment, have no CC other infections, and show normal growth and development. CC {ECO:0000269|PubMed:37875108}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the MCTS1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB034206; BAA86055.1; -; mRNA. DR EMBL; AY364258; AAQ76817.1; -; mRNA. DR EMBL; AK294834; BAG57943.1; -; mRNA. DR EMBL; AK311993; BAG34931.1; -; mRNA. DR EMBL; AC011890; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471107; EAX11874.1; -; Genomic_DNA. DR EMBL; BC001013; AAH01013.1; -; mRNA. DR EMBL; BC095461; AAH95461.1; -; mRNA. DR CCDS; CCDS14601.1; -. [Q9ULC4-1] DR CCDS; CCDS48160.1; -. [Q9ULC4-3] DR RefSeq; NP_001131026.1; NM_001137554.2. [Q9ULC4-3] DR RefSeq; NP_054779.1; NM_014060.3. [Q9ULC4-1] DR PDB; 3R90; X-ray; 1.70 A; A/B/C/D/E/F/G/H/I/J/K/L=1-181. DR PDB; 5ONS; X-ray; 2.14 A; A=1-181. DR PDB; 5VYC; X-ray; 6.00 A; k1/k2/k3/k4/k5/k6=1-181. DR PDB; 6MS4; X-ray; 2.00 A; A=1-181. DR PDBsum; 3R90; -. DR PDBsum; 5ONS; -. DR PDBsum; 5VYC; -. DR PDBsum; 6MS4; -. DR AlphaFoldDB; Q9ULC4; -. DR SMR; Q9ULC4; -. DR BioGRID; 118806; 142. DR FunCoup; Q9ULC4; 1511. DR IntAct; Q9ULC4; 66. DR MINT; Q9ULC4; -. DR STRING; 9606.ENSP00000360365; -. DR BindingDB; Q9ULC4; -. DR GlyGen; Q9ULC4; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9ULC4; -. DR MetOSite; Q9ULC4; -. DR PhosphoSitePlus; Q9ULC4; -. DR SwissPalm; Q9ULC4; -. DR BioMuta; MCTS1; -. DR DMDM; 74735052; -. DR jPOST; Q9ULC4; -. DR MassIVE; Q9ULC4; -. DR PaxDb; 9606-ENSP00000360365; -. DR PeptideAtlas; Q9ULC4; -. DR ProteomicsDB; 84976; -. [Q9ULC4-1] DR ProteomicsDB; 84977; -. [Q9ULC4-2] DR ProteomicsDB; 84978; -. [Q9ULC4-3] DR Pumba; Q9ULC4; -. DR Antibodypedia; 29908; 279 antibodies from 28 providers. DR DNASU; 28985; -. DR Ensembl; ENST00000371315.3; ENSP00000360365.3; ENSG00000232119.9. [Q9ULC4-3] DR Ensembl; ENST00000371317.10; ENSP00000360367.5; ENSG00000232119.9. [Q9ULC4-1] DR GeneID; 28985; -. DR KEGG; hsa:28985; -. DR MANE-Select; ENST00000371317.10; ENSP00000360367.5; NM_014060.3; NP_054779.1. DR UCSC; uc004esx.4; human. [Q9ULC4-1] DR AGR; HGNC:23357; -. DR ClinPGx; PA128394649; -. DR CTD; 28985; -. DR DisGeNET; 28985; -. DR GeneCards; MCTS1; -. DR HGNC; HGNC:23357; MCTS1. DR HPA; ENSG00000232119; Low tissue specificity. DR MalaCards; MCTS1; -. DR MIM; 300587; gene. DR MIM; 301115; phenotype. DR OpenTargets; ENSG00000232119; -. DR VEuPathDB; HostDB:ENSG00000232119; -. DR eggNOG; KOG2523; Eukaryota. DR GeneTree; ENSGT00550000074964; -. DR HOGENOM; CLU_090468_0_1_1; -. DR InParanoid; Q9ULC4; -. DR OMA; GVENIHY; -. DR OrthoDB; 10249667at2759; -. DR PAN-GO; Q9ULC4; 1 GO annotation based on evolutionary models. DR PhylomeDB; Q9ULC4; -. DR PathwayCommons; Q9ULC4; -. DR SignaLink; Q9ULC4; -. DR SIGNOR; Q9ULC4; -. DR Agora; ENSG00000232119; -. DR BioGRID-ORCS; 28985; 172 hits in 762 CRISPR screens. DR CD-CODE; 91857CE7; Nucleolus. DR CD-CODE; DEE660B4; Stress granule. DR ChiTaRS; MCTS1; human. DR EvolutionaryTrace; Q9ULC4; -. DR GenomeRNAi; 28985; -. DR Pharos; Q9ULC4; Tbio. DR PRO; PR:Q9ULC4; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q9ULC4; protein. DR Bgee; ENSG00000232119; Expressed in cortical plate and 103 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0043024; F:ribosomal small subunit binding; IDA:UniProtKB. DR GO; GO:0000339; F:RNA cap binding; IDA:UniProtKB. DR GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB. DR GO; GO:0006974; P:DNA damage response; IEA:UniProtKB-KW. DR GO; GO:0001731; P:formation of translation preinitiation complex; IDA:UniProtKB. DR GO; GO:0075522; P:IRES-dependent viral translational initiation; IDA:UniProtKB. DR GO; GO:0032790; P:ribosome disassembly; IDA:UniProtKB. DR GO; GO:0002188; P:translation reinitiation; IMP:UniProtKB. DR CDD; cd11609; MCT1_N; 1. DR CDD; cd21155; PUA_MCTS-1-like; 1. DR FunFam; 3.10.400.20:FF:000001; Malignant T-cell-amplified sequence 1; 1. DR Gene3D; 3.10.400.20; -; 1. DR InterPro; IPR016437; MCT-1/Tma20. DR InterPro; IPR041366; Pre-PUA. DR InterPro; IPR002478; PUA. DR InterPro; IPR015947; PUA-like_sf. DR InterPro; IPR004521; Uncharacterised_CHP00451. DR NCBIfam; TIGR00451; unchar_dom_2; 1. DR PANTHER; PTHR22798:SF0; MALIGNANT T-CELL-AMPLIFIED SEQUENCE 1; 1. DR PANTHER; PTHR22798; MCT-1 PROTEIN; 1. DR Pfam; PF17832; Pre-PUA; 1. DR Pfam; PF01472; PUA; 1. DR PIRSF; PIRSF005067; Tma_RNA-bind_prd; 1. DR SMART; SM00359; PUA; 1. DR SUPFAM; SSF88697; PUA domain-like; 1. DR PROSITE; PS50890; PUA; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell cycle; Cytoplasm; DNA damage; KW Growth regulation; Initiation factor; Phosphoprotein; Protein biosynthesis; KW Proteomics identification; Reference proteome; Transcription; KW Transcription regulation; Tumor suppressor. FT CHAIN 1..181 FT /note="Malignant T-cell-amplified sequence 1" FT /id="PRO_0000344786" FT DOMAIN 92..171 FT /note="PUA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00161" FT MOD_RES 81 FT /note="Phosphothreonine; by MAPK1 and MAPK3" FT /evidence="ECO:0000269|PubMed:17016429" FT MOD_RES 118 FT /note="Phosphoserine; by CDK1" FT /evidence="ECO:0000269|PubMed:17016429" FT VAR_SEQ 1..22 FT /note="MFKKFDEKENVSNCIQLKTSVI -> MENYSFLDKE (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_034856" FT VAR_SEQ 1..4 FT /note="MFKK -> MGKGR (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_041352" FT VARIANT 106 FT /note="L -> H (in dbSNP:rs2233110)" FT /id="VAR_045632" FT MUTAGEN 81 FT /note="T->A: No phosphorylation by MAPK1; decreased FT stability of MCTS1 protein; Significant cell growth FT reduction." FT /evidence="ECO:0000269|PubMed:17016429" FT MUTAGEN 118 FT /note="S->A: No phosphorylation by CDK1; No cell growth FT alteration." FT /evidence="ECO:0000269|PubMed:17016429" FT CONFLICT 25 FT /note="I -> L (in Ref. 6; AAH95461)" FT /evidence="ECO:0000305" FT STRAND 3..5 FT /evidence="ECO:0007829|PDB:6MS4" FT HELIX 7..10 FT /evidence="ECO:0007829|PDB:3R90" FT STRAND 11..16 FT /evidence="ECO:0007829|PDB:3R90" FT HELIX 19..32 FT /evidence="ECO:0007829|PDB:3R90" FT HELIX 34..39 FT /evidence="ECO:0007829|PDB:3R90" FT HELIX 40..43 FT /evidence="ECO:0007829|PDB:3R90" FT STRAND 50..55 FT /evidence="ECO:0007829|PDB:3R90" FT HELIX 56..58 FT /evidence="ECO:0007829|PDB:3R90" FT STRAND 59..64 FT /evidence="ECO:0007829|PDB:3R90" FT STRAND 67..73 FT /evidence="ECO:0007829|PDB:3R90" FT HELIX 82..87 FT /evidence="ECO:0007829|PDB:3R90" FT HELIX 89..91 FT /evidence="ECO:0007829|PDB:3R90" FT STRAND 94..97 FT /evidence="ECO:0007829|PDB:3R90" FT HELIX 99..101 FT /evidence="ECO:0007829|PDB:3R90" FT HELIX 102..105 FT /evidence="ECO:0007829|PDB:3R90" FT TURN 106..108 FT /evidence="ECO:0007829|PDB:3R90" FT HELIX 114..117 FT /evidence="ECO:0007829|PDB:3R90" FT STRAND 131..136 FT /evidence="ECO:0007829|PDB:3R90" FT STRAND 143..150 FT /evidence="ECO:0007829|PDB:3R90" FT HELIX 152..158 FT /evidence="ECO:0007829|PDB:3R90" FT STRAND 161..169 FT /evidence="ECO:0007829|PDB:3R90" FT HELIX 173..177 FT /evidence="ECO:0007829|PDB:3R90" FT STRAND 179..181 FT /evidence="ECO:0007829|PDB:3R90" SQ SEQUENCE 181 AA; 20555 MW; 2FC00C7A992E24EB CRC64; MFKKFDEKEN VSNCIQLKTS VIKGIKNQLI EQFPGIEPWL NQIMPKKDPV KIVRCHEHIE ILTVNGELLF FRQREGPFYP TLRLLHKYPF ILPHQQVDKG AIKFVLSGAN IMCPGLTSPG AKLYPAAVDT IVAIMAEGKQ HALCVGVMKM SAEDIEKVNK GIGIENIHYL NDGLWHMKTY K //