Full text data of MCTS1
MCTS1
(MCT1)
[Confidence: low (only semi-automatic identification from reviews)]
Malignant T-cell-amplified sequence 1; MCT-1 (Multiple copies T-cell malignancies)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Malignant T-cell-amplified sequence 1; MCT-1 (Multiple copies T-cell malignancies)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9ULC4
ID MCTS1_HUMAN Reviewed; 181 AA.
AC Q9ULC4; B4DGY2; Q502X6;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 111.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
RP 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
RT across 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA 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.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA 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.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA 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.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA 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.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RT candidate 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.,
RA Osipo C., Jordan V.C., Volpert O.V., Satcher R.L. Jr.,
RA Gartenhaus R.B.;
RT "MCT-1 oncogene contributes to increased in vivo tumorigenicity of
RT MCF7 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.,
RA Bachman K.E., He H., Gartenhaus R.B.;
RT "MCT-1 protein interacts with the cap complex and modulates messenger
RT RNA 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.,
RA Shu C.-L., Chu K.-L., Chen Y.-R., Hsu H.-F., Gartenhaus R.B.;
RT "MCT-1 oncogene downregulates p53 and destabilizes genome structure in
RT the 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
RP THR-81 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.,
RA He H., Gartenhaus R.B.;
RT "Phosphorylation of MCT-1 by p44/42 MAPK is required for its
RT stabilization in response to DNA damage.";
RL Oncogene 26:2283-2289(2007).
RN [15]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Anti-oncogene that play a role in cell cycle regulation;
CC decreases cell doubling time and anchorage-dependent growth;
CC shortens the duration of G1 transit time and G1/S transition. When
CC constituvely expressed, increases CDK4 and CDK6 kinases activity
CC and CCND1/cyclin D1 protein level, as well as G1 cyclin/CDK
CC complex formation. Plays a role as translation enhancer; Recruits
CC the density-regulated protein/DENR and binds to the cap complex of
CC the 5'-terminus of mRNAs, subsequently altering the mRNA
CC translation profile; Up-regulates protein levels of BCL2L2, TFDP1,
CC MRE11A, CCND1 and E2F1, while mRNA levels remains constant.
CC Hyperactivates DNA damage signaling pathway; increased gamma-
CC irradiation-induced phosphorylation of histone H2AX, and induces
CC damage foci formation. Increases the overall number of chromosomal
CC abnormalities such as larger chromosomes formation and multiples
CC chromosomal fusions when overexpressed in gamma-irradiated cells.
CC May play a role in promoting lymphoid tumor development: lymphoid
CC cell lines overexpressing MCTS1 exhibit increased growth rates and
CC display increased protection against apoptosis. May contribute to
CC the pathogenesis and progression of breast cancer via promotion of
CC angiogenesis through the decline of inhibitory
CC THBS1/thrombospondin-1, and inhibition of apoptosis. Involved in
CC the process of proteasome degradation to down-regulate Tumor
CC suppressor p53/TP53 in breast cancer cell; Positively regulates
CC phosphorylation of MAPK1 and MAPK3.
CC -!- SUBUNIT: Interacts (via PUA domain) with DENR.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Nuclear relocalization after
CC DNA 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
CC cell lines and in non-Hodgkin lymphoma cell lines as well as in a
CC subset of primary large B-cell lymphomas.
CC -!- INDUCTION: By DNA damaging agents such as gamma irradiation,
CC adriamycin or taxol in lymphoid cells, but not by stress stimuli
CC such as heat shock. This induction of protein expression does not
CC occur at the RNA level, and does not require new protein
CC synthesis.
CC -!- DOMAIN: The PUA RNA-binding domain is critical for cap binding,
CC but not sufficient for translation enhancer function. MCT1 N-
CC terminal region is required to enhance translation possibly
CC through interaction with other proteins.
CC -!- PTM: Phosphorylation is critical for stabilization and promotion
CC of cell proliferation.
CC -!- SIMILARITY: Belongs to the MCTS1 family.
CC -!- SIMILARITY: Contains 1 PUA domain.
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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 RefSeq; NP_001131026.1; NM_001137554.1.
DR RefSeq; NP_054779.1; NM_014060.2.
DR UniGene; Hs.102696; -.
DR UniGene; Hs.670803; -.
DR PDB; 3R90; X-ray; 1.70 A; A/B/C/D/E/F/G/H/I/J/K/L=1-181.
DR PDBsum; 3R90; -.
DR ProteinModelPortal; Q9ULC4; -.
DR SMR; Q9ULC4; 1-181.
DR IntAct; Q9ULC4; 1.
DR MINT; MINT-1405141; -.
DR STRING; 9606.ENSP00000360365; -.
DR PhosphoSite; Q9ULC4; -.
DR DMDM; 74735052; -.
DR PaxDb; Q9ULC4; -.
DR PeptideAtlas; Q9ULC4; -.
DR PRIDE; Q9ULC4; -.
DR DNASU; 28985; -.
DR Ensembl; ENST00000371315; ENSP00000360365; ENSG00000232119.
DR Ensembl; ENST00000371317; ENSP00000360367; ENSG00000232119.
DR GeneID; 28985; -.
DR KEGG; hsa:28985; -.
DR UCSC; uc004esx.3; human.
DR CTD; 28985; -.
DR GeneCards; GC0XP119727; -.
DR HGNC; HGNC:23357; MCTS1.
DR MIM; 300587; gene.
DR neXtProt; NX_Q9ULC4; -.
DR PharmGKB; PA128394649; -.
DR eggNOG; COG2016; -.
DR HOGENOM; HOG000223988; -.
DR HOVERGEN; HBG105551; -.
DR KO; K07575; -.
DR OMA; GSNIMCP; -.
DR OrthoDB; EOG7S7SG1; -.
DR PhylomeDB; Q9ULC4; -.
DR GenomeRNAi; 28985; -.
DR NextBio; 51887; -.
DR PRO; PR:Q9ULC4; -.
DR Bgee; Q9ULC4; -.
DR CleanEx; HS_MCTS1; -.
DR Genevestigator; Q9ULC4; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
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:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 2.30.130.10; -; 1.
DR InterPro; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_domain.
DR InterPro; IPR016437; Transl_RNA-bd_prd.
DR InterPro; IPR004521; Uncharacterised_CHP00451.
DR PANTHER; PTHR22798; PTHR22798; 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; Complete proteome;
KW Cytoplasm; DNA damage; Growth regulation; Phosphoprotein;
KW Polymorphism; Reference proteome; Transcription;
KW Transcription regulation; Tumor suppressor.
FT CHAIN 1 181 Malignant T-cell-amplified sequence 1.
FT /FTId=PRO_0000344786.
FT DOMAIN 92 171 PUA.
FT MOD_RES 81 81 Phosphothreonine; by MAPK1 and MAPK3.
FT MOD_RES 118 118 Phosphoserine; by CDK1.
FT VAR_SEQ 1 22 MFKKFDEKENVSNCIQLKTSVI -> MENYSFLDKE (in
FT isoform 2).
FT /FTId=VSP_034856.
FT VAR_SEQ 1 4 MFKK -> MGKGR (in isoform 3).
FT /FTId=VSP_041352.
FT VARIANT 106 106 L -> H (in dbSNP:rs2233110).
FT /FTId=VAR_045632.
FT MUTAGEN 81 81 T->A: No phosphorylation by MAPK1;
FT decreased stability of MCTS1 protein;
FT Significant cell growth reduction.
FT MUTAGEN 118 118 S->A: No phosphorylation by CDK1; No cell
FT growth alteration.
FT CONFLICT 25 25 I -> L (in Ref. 6; AAH95461).
FT HELIX 7 10
FT STRAND 11 16
FT HELIX 19 32
FT HELIX 34 39
FT HELIX 40 43
FT STRAND 50 55
FT HELIX 56 58
FT STRAND 59 64
FT STRAND 67 73
FT HELIX 82 87
FT HELIX 89 91
FT STRAND 94 97
FT HELIX 99 101
FT HELIX 102 105
FT TURN 106 108
FT HELIX 114 117
FT STRAND 131 136
FT STRAND 143 150
FT HELIX 152 158
FT STRAND 161 169
FT HELIX 173 177
FT STRAND 179 181
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
//
ID MCTS1_HUMAN Reviewed; 181 AA.
AC Q9ULC4; B4DGY2; Q502X6;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 111.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
RP 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
RT across 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA 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.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA 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.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA 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.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA 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.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RT candidate 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.,
RA Osipo C., Jordan V.C., Volpert O.V., Satcher R.L. Jr.,
RA Gartenhaus R.B.;
RT "MCT-1 oncogene contributes to increased in vivo tumorigenicity of
RT MCF7 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.,
RA Bachman K.E., He H., Gartenhaus R.B.;
RT "MCT-1 protein interacts with the cap complex and modulates messenger
RT RNA 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.,
RA Shu C.-L., Chu K.-L., Chen Y.-R., Hsu H.-F., Gartenhaus R.B.;
RT "MCT-1 oncogene downregulates p53 and destabilizes genome structure in
RT the 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
RP THR-81 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.,
RA He H., Gartenhaus R.B.;
RT "Phosphorylation of MCT-1 by p44/42 MAPK is required for its
RT stabilization in response to DNA damage.";
RL Oncogene 26:2283-2289(2007).
RN [15]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Anti-oncogene that play a role in cell cycle regulation;
CC decreases cell doubling time and anchorage-dependent growth;
CC shortens the duration of G1 transit time and G1/S transition. When
CC constituvely expressed, increases CDK4 and CDK6 kinases activity
CC and CCND1/cyclin D1 protein level, as well as G1 cyclin/CDK
CC complex formation. Plays a role as translation enhancer; Recruits
CC the density-regulated protein/DENR and binds to the cap complex of
CC the 5'-terminus of mRNAs, subsequently altering the mRNA
CC translation profile; Up-regulates protein levels of BCL2L2, TFDP1,
CC MRE11A, CCND1 and E2F1, while mRNA levels remains constant.
CC Hyperactivates DNA damage signaling pathway; increased gamma-
CC irradiation-induced phosphorylation of histone H2AX, and induces
CC damage foci formation. Increases the overall number of chromosomal
CC abnormalities such as larger chromosomes formation and multiples
CC chromosomal fusions when overexpressed in gamma-irradiated cells.
CC May play a role in promoting lymphoid tumor development: lymphoid
CC cell lines overexpressing MCTS1 exhibit increased growth rates and
CC display increased protection against apoptosis. May contribute to
CC the pathogenesis and progression of breast cancer via promotion of
CC angiogenesis through the decline of inhibitory
CC THBS1/thrombospondin-1, and inhibition of apoptosis. Involved in
CC the process of proteasome degradation to down-regulate Tumor
CC suppressor p53/TP53 in breast cancer cell; Positively regulates
CC phosphorylation of MAPK1 and MAPK3.
CC -!- SUBUNIT: Interacts (via PUA domain) with DENR.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Nuclear relocalization after
CC DNA 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
CC cell lines and in non-Hodgkin lymphoma cell lines as well as in a
CC subset of primary large B-cell lymphomas.
CC -!- INDUCTION: By DNA damaging agents such as gamma irradiation,
CC adriamycin or taxol in lymphoid cells, but not by stress stimuli
CC such as heat shock. This induction of protein expression does not
CC occur at the RNA level, and does not require new protein
CC synthesis.
CC -!- DOMAIN: The PUA RNA-binding domain is critical for cap binding,
CC but not sufficient for translation enhancer function. MCT1 N-
CC terminal region is required to enhance translation possibly
CC through interaction with other proteins.
CC -!- PTM: Phosphorylation is critical for stabilization and promotion
CC of cell proliferation.
CC -!- SIMILARITY: Belongs to the MCTS1 family.
CC -!- SIMILARITY: Contains 1 PUA domain.
CC -----------------------------------------------------------------------
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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 RefSeq; NP_001131026.1; NM_001137554.1.
DR RefSeq; NP_054779.1; NM_014060.2.
DR UniGene; Hs.102696; -.
DR UniGene; Hs.670803; -.
DR PDB; 3R90; X-ray; 1.70 A; A/B/C/D/E/F/G/H/I/J/K/L=1-181.
DR PDBsum; 3R90; -.
DR ProteinModelPortal; Q9ULC4; -.
DR SMR; Q9ULC4; 1-181.
DR IntAct; Q9ULC4; 1.
DR MINT; MINT-1405141; -.
DR STRING; 9606.ENSP00000360365; -.
DR PhosphoSite; Q9ULC4; -.
DR DMDM; 74735052; -.
DR PaxDb; Q9ULC4; -.
DR PeptideAtlas; Q9ULC4; -.
DR PRIDE; Q9ULC4; -.
DR DNASU; 28985; -.
DR Ensembl; ENST00000371315; ENSP00000360365; ENSG00000232119.
DR Ensembl; ENST00000371317; ENSP00000360367; ENSG00000232119.
DR GeneID; 28985; -.
DR KEGG; hsa:28985; -.
DR UCSC; uc004esx.3; human.
DR CTD; 28985; -.
DR GeneCards; GC0XP119727; -.
DR HGNC; HGNC:23357; MCTS1.
DR MIM; 300587; gene.
DR neXtProt; NX_Q9ULC4; -.
DR PharmGKB; PA128394649; -.
DR eggNOG; COG2016; -.
DR HOGENOM; HOG000223988; -.
DR HOVERGEN; HBG105551; -.
DR KO; K07575; -.
DR OMA; GSNIMCP; -.
DR OrthoDB; EOG7S7SG1; -.
DR PhylomeDB; Q9ULC4; -.
DR GenomeRNAi; 28985; -.
DR NextBio; 51887; -.
DR PRO; PR:Q9ULC4; -.
DR Bgee; Q9ULC4; -.
DR CleanEx; HS_MCTS1; -.
DR Genevestigator; Q9ULC4; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
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:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 2.30.130.10; -; 1.
DR InterPro; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_domain.
DR InterPro; IPR016437; Transl_RNA-bd_prd.
DR InterPro; IPR004521; Uncharacterised_CHP00451.
DR PANTHER; PTHR22798; PTHR22798; 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; Complete proteome;
KW Cytoplasm; DNA damage; Growth regulation; Phosphoprotein;
KW Polymorphism; Reference proteome; Transcription;
KW Transcription regulation; Tumor suppressor.
FT CHAIN 1 181 Malignant T-cell-amplified sequence 1.
FT /FTId=PRO_0000344786.
FT DOMAIN 92 171 PUA.
FT MOD_RES 81 81 Phosphothreonine; by MAPK1 and MAPK3.
FT MOD_RES 118 118 Phosphoserine; by CDK1.
FT VAR_SEQ 1 22 MFKKFDEKENVSNCIQLKTSVI -> MENYSFLDKE (in
FT isoform 2).
FT /FTId=VSP_034856.
FT VAR_SEQ 1 4 MFKK -> MGKGR (in isoform 3).
FT /FTId=VSP_041352.
FT VARIANT 106 106 L -> H (in dbSNP:rs2233110).
FT /FTId=VAR_045632.
FT MUTAGEN 81 81 T->A: No phosphorylation by MAPK1;
FT decreased stability of MCTS1 protein;
FT Significant cell growth reduction.
FT MUTAGEN 118 118 S->A: No phosphorylation by CDK1; No cell
FT growth alteration.
FT CONFLICT 25 25 I -> L (in Ref. 6; AAH95461).
FT HELIX 7 10
FT STRAND 11 16
FT HELIX 19 32
FT HELIX 34 39
FT HELIX 40 43
FT STRAND 50 55
FT HELIX 56 58
FT STRAND 59 64
FT STRAND 67 73
FT HELIX 82 87
FT HELIX 89 91
FT STRAND 94 97
FT HELIX 99 101
FT HELIX 102 105
FT TURN 106 108
FT HELIX 114 117
FT STRAND 131 136
FT STRAND 143 150
FT HELIX 152 158
FT STRAND 161 169
FT HELIX 173 177
FT STRAND 179 181
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
//
MIM
300587
*RECORD*
*FIELD* NO
300587
*FIELD* TI
*300587 MALIGNANT T-CELL AMPLIFIED SEQUENCE 1; MCTS1
;;MCT1
*FIELD* TX
CLONING
Prosniak et al. (1998) identified MCTS1, which they called MCT1, based
read moreon its amplification in a T-cell lymphoma cell line derived from a
patient with Sezary syndrome. Using 5-prime RACE, they obtained a
full-length MCT1 cDNA. The deduced 181-amino acid protein has a
calculated molecular mass of 20 kD. MCT1 has 4 phosphorylation sites and
a 58-amino acid C-terminal domain similar to the protein-protein
interaction domain of cyclin H (CCNH; 601953). Northern blot analysis
detected low ubiquitous expression of an MCT1 transcript smaller than 1
kb.
GENE FUNCTION
Prosniak et al. (1998) found that overexpression of MCT1 in mouse
fibroblasts increased the cell proliferative rate by decreasing the
length of the G1 phase without a reciprocal increase in the S and G2-M
phases. Overexpression of MCT1 also supported anchorage-independent
growth.
Shi et al. (2003) found increased MCT1 protein expression in a panel of
T-cell lymphoid cell lines, in non-Hodgkin lymphoma cell lines, and in a
subset of primary diffuse large B-cell lymphomas. All transformed
follicular lymphomas demonstrated elevated MCT1 protein levels. MCT1
protein was not detected in leukemic cells from patients with chronic
lymphocytic leukemia or in any healthy lymphoid tissue examined.
Lymphoid cell lines overexpressing MCT1 exhibited increased growth and
were protected from serum starvation-induced apoptosis.
MCT1-overexpressing cells showed constitutively higher levels of
phosphorylated AKT (164730) protein, especially under serum starvation.
GENE STRUCTURE
Shi et al. (2003) determined that the MCTS1 promoter is TATA-less, and
they identified an enhancer region required for maximum MCTS1
transcription.
MAPPING
By FISH, Prosniak et al. (1998) mapped the MCTS1 gene to chromosome
Xq22-q24.
*FIELD* RF
1. Prosniak, M.; Dierov, J.; Okami, K.; Tilton, B.; Jameson, B.; Sawaya,
B. E.; Gartenhaus, R. B.: A novel candidate oncogene, MCT-1, is involved
in cell cycle progression. Cancer Res. 58: 4233-4237, 1998.
2. Shi, B.; Hsu, H.-L.; Evens, A. M.; Gordon, L. I.; Gartenhaus, R.
B.: Expression of the candidate MCT-1 oncogene in B- and T-cell lymphoid
malignancies. Blood 102: 297-302, 2003.
3. Shi, B.; Levenson, V.; Gartenhaus, R. B.: Identification and characterization
of a novel enhancer for the human MCT-1 oncogene promoter. J. Cell.
Biochem. 90: 68-79, 2003.
*FIELD* CD
Patricia A. Hartz: 4/25/2006
*FIELD* ED
mgross: 04/25/2006
*RECORD*
*FIELD* NO
300587
*FIELD* TI
*300587 MALIGNANT T-CELL AMPLIFIED SEQUENCE 1; MCTS1
;;MCT1
*FIELD* TX
CLONING
Prosniak et al. (1998) identified MCTS1, which they called MCT1, based
read moreon its amplification in a T-cell lymphoma cell line derived from a
patient with Sezary syndrome. Using 5-prime RACE, they obtained a
full-length MCT1 cDNA. The deduced 181-amino acid protein has a
calculated molecular mass of 20 kD. MCT1 has 4 phosphorylation sites and
a 58-amino acid C-terminal domain similar to the protein-protein
interaction domain of cyclin H (CCNH; 601953). Northern blot analysis
detected low ubiquitous expression of an MCT1 transcript smaller than 1
kb.
GENE FUNCTION
Prosniak et al. (1998) found that overexpression of MCT1 in mouse
fibroblasts increased the cell proliferative rate by decreasing the
length of the G1 phase without a reciprocal increase in the S and G2-M
phases. Overexpression of MCT1 also supported anchorage-independent
growth.
Shi et al. (2003) found increased MCT1 protein expression in a panel of
T-cell lymphoid cell lines, in non-Hodgkin lymphoma cell lines, and in a
subset of primary diffuse large B-cell lymphomas. All transformed
follicular lymphomas demonstrated elevated MCT1 protein levels. MCT1
protein was not detected in leukemic cells from patients with chronic
lymphocytic leukemia or in any healthy lymphoid tissue examined.
Lymphoid cell lines overexpressing MCT1 exhibited increased growth and
were protected from serum starvation-induced apoptosis.
MCT1-overexpressing cells showed constitutively higher levels of
phosphorylated AKT (164730) protein, especially under serum starvation.
GENE STRUCTURE
Shi et al. (2003) determined that the MCTS1 promoter is TATA-less, and
they identified an enhancer region required for maximum MCTS1
transcription.
MAPPING
By FISH, Prosniak et al. (1998) mapped the MCTS1 gene to chromosome
Xq22-q24.
*FIELD* RF
1. Prosniak, M.; Dierov, J.; Okami, K.; Tilton, B.; Jameson, B.; Sawaya,
B. E.; Gartenhaus, R. B.: A novel candidate oncogene, MCT-1, is involved
in cell cycle progression. Cancer Res. 58: 4233-4237, 1998.
2. Shi, B.; Hsu, H.-L.; Evens, A. M.; Gordon, L. I.; Gartenhaus, R.
B.: Expression of the candidate MCT-1 oncogene in B- and T-cell lymphoid
malignancies. Blood 102: 297-302, 2003.
3. Shi, B.; Levenson, V.; Gartenhaus, R. B.: Identification and characterization
of a novel enhancer for the human MCT-1 oncogene promoter. J. Cell.
Biochem. 90: 68-79, 2003.
*FIELD* CD
Patricia A. Hartz: 4/25/2006
*FIELD* ED
mgross: 04/25/2006