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Database: UniProt
Entry: Q9DB27
LinkDB: Q9DB27
Original site: Q9DB27 
ID   MCTS1_MOUSE             Reviewed;         181 AA.
AC   Q9DB27; Q3UUI6;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   01-OCT-2014, entry version 106.
DE   RecName: Full=Malignant T-cell-amplified sequence 1;
DE            Short=MCT-1;
DE   AltName: Full=Multiple copies T-cell malignancies 1;
GN   Name=Mcts1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, Hypothalamus, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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).
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. Involved in translation initiation; promotes
CC       recruitment of aminoacetyled initiator tRNA to P site of 40S
CC       ribosomes. Can promote release of deacylated tRNA and mRNA from
CC       recycled 40S subunits following ABCE1-mediated dissociation of
CC       post-termination ribosomal complexes into subunits. Plays a role
CC       as translation enhancer; recruits the density-regulated
CC       protein/DENR and binds to the cap complex of the 5'-terminus of
CC       mRNAs, subsequently altering the mRNA translation profile; up-
CC       regulates protein levels of BCL2L2, TFDP1, MRE11A, CCND1 and E2F1,
CC       while mRNA levels remains constant. Hyperactivates DNA damage
CC       signaling pathway; increased gamma-irradiation-induced
CC       phosphorylation of histone H2AX, and induces damage foci
CC       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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts (via PUA domain) with DENR. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9DB27-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9DB27-2; Sequence=VSP_034857;
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylation is critical for stabilization and promotion
CC       of cell proliferation. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MCTS1 family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 PUA domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00161}.
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DR   EMBL; AK005292; BAB23936.1; -; mRNA.
DR   EMBL; AK087975; BAC40069.1; -; mRNA.
DR   EMBL; AK138385; BAE23639.1; -; mRNA.
DR   EMBL; AL513356; CAM17146.1; -; Genomic_DNA.
DR   EMBL; AL845279; CAM17146.1; JOINED; Genomic_DNA.
DR   EMBL; AL845279; CAM20158.1; -; Genomic_DNA.
DR   EMBL; AL513356; CAM20158.1; JOINED; Genomic_DNA.
DR   EMBL; BC010486; AAH10486.1; -; mRNA.
DR   CCDS; CCDS30094.1; -. [Q9DB27-1]
DR   RefSeq; NP_081178.1; NM_026902.3. [Q9DB27-1]
DR   RefSeq; XP_006541597.1; XM_006541534.1. [Q9DB27-2]
DR   RefSeq; XP_006541598.1; XM_006541535.1. [Q9DB27-2]
DR   UniGene; Mm.262453; -.
DR   ProteinModelPortal; Q9DB27; -.
DR   SMR; Q9DB27; 1-181.
DR   IntAct; Q9DB27; 1.
DR   MINT; MINT-4128072; -.
DR   PhosphoSite; Q9DB27; -.
DR   MaxQB; Q9DB27; -.
DR   PaxDb; Q9DB27; -.
DR   PRIDE; Q9DB27; -.
DR   DNASU; 68995; -.
DR   Ensembl; ENSMUST00000000365; ENSMUSP00000000365; ENSMUSG00000000355. [Q9DB27-1]
DR   GeneID; 68995; -.
DR   KEGG; mmu:68995; -.
DR   UCSC; uc009tad.1; mouse. [Q9DB27-1]
DR   UCSC; uc009tae.1; mouse. [Q9DB27-2]
DR   CTD; 28985; -.
DR   MGI; MGI:1916245; Mcts1.
DR   eggNOG; COG2016; -.
DR   GeneTree; ENSGT00550000074964; -.
DR   HOGENOM; HOG000223988; -.
DR   HOVERGEN; HBG105551; -.
DR   KO; K07575; -.
DR   OMA; LVKCREH; -.
DR   OrthoDB; EOG7S7SG1; -.
DR   PhylomeDB; Q9DB27; -.
DR   TreeFam; TF315123; -.
DR   NextBio; 328373; -.
DR   PRO; PR:Q9DB27; -.
DR   Bgee; Q9DB27; -.
DR   Genevestigator; Q9DB27; -.
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:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; 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   2: Evidence at transcript level;
KW   Alternative splicing; Cell cycle; Complete proteome; Cytoplasm;
KW   DNA damage; Growth regulation; Initiation factor; Phosphoprotein;
KW   Protein biosynthesis; Reference proteome; Transcription;
KW   Transcription regulation; Tumor suppressor.
FT   CHAIN         1    181       Malignant T-cell-amplified sequence 1.
FT                                /FTId=PRO_0000344787.
FT   DOMAIN       92    171       PUA. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00161}.
FT   MOD_RES      81     81       Phosphothreonine. {ECO:0000250}.
FT   MOD_RES     118    118       Phosphoserine. {ECO:0000250}.
FT   VAR_SEQ       1      4       MFKK -> MGKGR (in isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_034857.
SQ   SEQUENCE   181 AA;  20555 MW;  A8E02C2F992B74BD CRC64;
     MFKKFDEKEN VSNCIQLKTS VIKGIKNQLL EQFPGIEPWL NQIMPKKDPV KIVRCHEHIE
     ILTVNGELLF FRQREGPFYP TLRLLHKYPF ILPHQQVDKG AIKFVLSGAN IMCPGLTSPG
     AKLYPAAVDT IVAIMAEGKQ HALCVGVMKM SAEDIEKVNK GIGIENIHYL NDGLWHMKTY
     K
//
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