MCTS1_HUMAN
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 03-AUG-2022, entry version 171.
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>3.0.co;2-4;
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}.
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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; 95.
DR IntAct; Q9ULC4; 25.
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; Q9ULC4; -.
DR PeptideAtlas; Q9ULC4; -.
DR PRIDE; Q9ULC4; -.
DR ProteomicsDB; 84976; -. [Q9ULC4-1]
DR ProteomicsDB; 84977; -. [Q9ULC4-2]
DR ProteomicsDB; 84978; -. [Q9ULC4-3]
DR Antibodypedia; 29908; 284 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 Ensembl; ENST00000672136.1; ENSP00000500610.1; ENSG00000288295.1. [Q9ULC4-3]
DR Ensembl; ENST00000673335.1; ENSP00000500508.1; ENSG00000288295.1. [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 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; HDHIEIL; -.
DR OrthoDB; 1257440at2759; -.
DR PhylomeDB; Q9ULC4; -.
DR TreeFam; TF315123; -.
DR PathwayCommons; Q9ULC4; -.
DR SignaLink; Q9ULC4; -.
DR BioGRID-ORCS; 28985; 172 hits in 688 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 101 other tissues.
DR Genevisible; Q9ULC4; HS.
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:cellular response to DNA damage stimulus; 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:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0032790; P:ribosome disassembly; IDA:UniProtKB.
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 PANTHER; PTHR22798; PTHR22798; 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; SSF88697; 1.
DR TIGRFAMs; TIGR00451; unchar_dom_2; 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 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
