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 27-MAR-2024, entry version 180. 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). CC -!- FUNCTION: Anti-oncogene that plays a role in cell cycle regulation; CC decreases cell doubling time and anchorage-dependent growth; shortens CC the duration of G1 transit time and G1/S transition. When CC constitutively expressed, increases CDK4 and CDK6 kinases activity and CC CCND1/cyclin D1 protein level, as well as G1 cyclin/CDK complex CC formation. Involved in translation initiation; promotes recruitment of CC aminoacetyled initiator tRNA to P site of 40S ribosomes. Can promote CC release of deacylated tRNA and mRNA from recycled 40S subunits CC following ABCE1-mediated dissociation of post-termination ribosomal CC complexes into subunits. Plays a role as translation enhancer; recruits CC the density-regulated protein/DENR and binds to the cap complex of the CC 5'-terminus of mRNAs, subsequently altering the mRNA translation CC profile; up-regulates protein levels of BCL2L2, TFDP1, MRE11, CCND1 and CC E2F1, while mRNA levels remains constant. Hyperactivates DNA damage CC signaling pathway; increased gamma-irradiation-induced phosphorylation CC of histone H2AX, and induces damage foci formation. Increases the CC overall number of chromosomal abnormalities such as larger chromosomes CC formation and multiple chromosomal fusions when overexpressed in gamma- CC irradiated cells. May play a role in promoting lymphoid tumor CC development: lymphoid cell lines overexpressing MCTS1 exhibit increased CC growth rates and display increased protection against apoptosis. May CC contribute to the pathogenesis and progression of breast cancer via CC promotion of angiogenesis through the decline of inhibitory CC THBS1/thrombospondin-1, and inhibition of apoptosis. Involved in the CC process of proteasome degradation to down-regulate Tumor suppressor CC p53/TP53 in breast cancer cell; Positively regulates phosphorylation of CC MAPK1 and MAPK3. Involved in translation initiation; promotes CC aminoacetyled initiator tRNA to P site of 40S ribosomes. Can promote CC release of deacylated tRNA and mRNA from recycled 40S subunits CC following ABCE1-mediated dissociation of post-termination ribosomal CC complexes into subunits. {ECO:0000269|PubMed:10440924, CC ECO:0000269|PubMed:11709712, ECO:0000269|PubMed:12637315, CC ECO:0000269|PubMed:15897892, ECO:0000269|PubMed:16322206, CC ECO:0000269|PubMed:16982740, ECO:0000269|PubMed:17016429, CC ECO:0000269|PubMed:17416211, ECO:0000269|PubMed:20713520, CC ECO:0000269|PubMed:9766643}. CC -!- SUBUNIT: Interacts (via PUA domain) with DENR. CC {ECO:0000269|PubMed:16982740}. CC -!- INTERACTION: CC Q9ULC4; O43583: DENR; NbExp=7; 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 -!- 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_001137554.1. [Q9ULC4-3] DR RefSeq; NP_054779.1; NM_014060.2. [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; 127. DR IntAct; Q9ULC4; 27. 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 EPD; Q9ULC4; -. DR jPOST; Q9ULC4; -. DR MassIVE; Q9ULC4; -. DR MaxQB; 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; 309 antibodies from 29 providers. DR DNASU; 28985; -. DR Ensembl; ENST00000371315.3; ENSP00000360365.3; ENSG00000232119.8. [Q9ULC4-3] DR Ensembl; ENST00000371317.10; ENSP00000360367.5; ENSG00000232119.8. [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 CTD; 28985; -. DR DisGeNET; 28985; -. DR GeneCards; MCTS1; -. DR HGNC; HGNC:23357; MCTS1. DR HPA; ENSG00000232119; Low tissue specificity. DR MIM; 300587; gene. DR neXtProt; NX_Q9ULC4; -. DR OpenTargets; ENSG00000232119; -. DR PharmGKB; PA128394649; -. DR VEuPathDB; HostDB:ENSG00000232119; -. DR eggNOG; KOG2523; Eukaryota. DR GeneTree; ENSGT00550000074964; -. DR HOGENOM; CLU_090468_0_1_1; -. DR InParanoid; Q9ULC4; -. DR OMA; SINKGHG; -. DR OrthoDB; 5036262at2759; -. DR PhylomeDB; Q9ULC4; -. DR TreeFam; TF315123; -. DR PathwayCommons; Q9ULC4; -. DR SignaLink; Q9ULC4; -. DR SIGNOR; Q9ULC4; -. DR BioGRID-ORCS; 28985; 172 hits in 762 CRISPR screens. DR ChiTaRS; MCTS1; human. 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; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. 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:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc. DR GO; GO:0032790; P:ribosome disassembly; IDA:UniProtKB. DR CDD; cd11609; MCT1_N; 1. DR CDD; cd21155; PUA_MCTS-1-like; 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. DR Genevisible; Q9ULC4; HS. 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 Reference proteome; Transcription; Transcription regulation; KW 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 //