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MCTS1_MOUSE
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   03-AUG-2022, entry version 152.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   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., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., 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., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., 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., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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 (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, 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 (By similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylation is critical for stabilization and promotion of
CC       cell proliferation. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MCTS1 family. {ECO:0000305}.
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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; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL845279; -; NOT_ANNOTATED_CDS; 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_006541598.1; XM_006541535.2.
DR   AlphaFoldDB; Q9DB27; -.
DR   SMR; Q9DB27; -.
DR   BioGRID; 213164; 38.
DR   IntAct; Q9DB27; 1.
DR   MINT; Q9DB27; -.
DR   STRING; 10090.ENSMUSP00000000365; -.
DR   iPTMnet; Q9DB27; -.
DR   PhosphoSitePlus; Q9DB27; -.
DR   SwissPalm; Q9DB27; -.
DR   EPD; Q9DB27; -.
DR   MaxQB; Q9DB27; -.
DR   PaxDb; Q9DB27; -.
DR   PeptideAtlas; Q9DB27; -.
DR   PRIDE; Q9DB27; -.
DR   ProteomicsDB; 295718; -. [Q9DB27-1]
DR   ProteomicsDB; 295719; -. [Q9DB27-2]
DR   Antibodypedia; 29908; 284 antibodies from 29 providers.
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   VEuPathDB; HostDB:ENSMUSG00000000355; -.
DR   eggNOG; KOG2523; Eukaryota.
DR   GeneTree; ENSGT00550000074964; -.
DR   HOGENOM; CLU_090468_0_1_1; -.
DR   InParanoid; Q9DB27; -.
DR   OMA; HDHIEIL; -.
DR   OrthoDB; 1257440at2759; -.
DR   PhylomeDB; Q9DB27; -.
DR   TreeFam; TF315123; -.
DR   BioGRID-ORCS; 68995; 12 hits in 72 CRISPR screens.
DR   ChiTaRS; Mcts1; mouse.
DR   PRO; PR:Q9DB27; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q9DB27; protein.
DR   Bgee; ENSMUSG00000000355; Expressed in facial nucleus and 244 other tissues.
DR   Genevisible; Q9DB27; MM.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; ISO:MGI.
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; ISO:MGI.
DR   GO; GO:0075522; P:IRES-dependent viral translational initiation; ISO:MGI.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   GO; GO:0032790; P:ribosome disassembly; ISO:MGI.
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   Alternative splicing; Cell cycle; Cytoplasm; DNA damage; Growth regulation;
KW   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_0000344787"
FT   DOMAIN          92..171
FT                   /note="PUA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00161"
FT   MOD_RES         81
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULC4"
FT   MOD_RES         118
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULC4"
FT   VAR_SEQ         1..4
FT                   /note="MFKK -> MGKGR (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="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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