MYCT1_MOUSE
ID MYCT1_MOUSE Reviewed; 188 AA.
AC Q8R411; Q3UQ11; Q8C6M8; Q9D182;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Myc target protein 1;
DE AltName: Full=Myc target in myeloid cells protein 1;
GN Name=Myct1; Synonyms=Mtmc1;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11909865; DOI=10.1074/jbc.m200860200;
RA Yin X., Grove L., Rogulski K., Prochownik E.V.;
RT "Myc target in myeloid cells-1, a novel c-Myc target, recapitulates
RT multiple c-Myc phenotypes.";
RL J. Biol. Chem. 277:19998-20010(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Head, Lung, and Oviduct;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-90; SER-93 AND
RP SER-101, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
RC Spleen;
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: May regulate certain MYC target genes, MYC seems to be a
CC direct upstream transcriptional activator. Does not seem to
CC significantly affect growth cell capacity. Overexpression seems to
CC mediate many of the known phenotypic features associated with MYC,
CC including promotion of apoptosis, alteration of morphology, enhancement
CC of anchorage-independent growth, tumorigenic conversion, promotion of
CC genomic instability and inhibition of hematopoietic differentiation.
CC {ECO:0000269|PubMed:11909865}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in lung, heart, and skeletal
CC muscle. Expressed in brain, eye, liver, kidney, smooth muscle,
CC pancreas, thyroid, thymus, submaxillary gland, spleen, testis, ovary,
CC prostate, epididymis, and uterus. Deregulated expression promotes
CC apoptosis in response to growth factor deprivation. Overexpression in
CC synergy with CCNB1 may promote genomic instability.
CC {ECO:0000269|PubMed:11909865}.
CC -!- DEVELOPMENTAL STAGE: Low levels of expression seen in 7-, 11-, 15- and
CC 17-day embryos. {ECO:0000269|PubMed:11909865}.
CC -!- SIMILARITY: Belongs to the MYCT1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC35696.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE25233.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY090114; AAM14631.1; -; mRNA.
DR EMBL; AK030706; BAE20454.1; -; mRNA.
DR EMBL; AK003845; BAB23032.1; -; mRNA.
DR EMBL; AK054222; BAC35696.1; ALT_INIT; mRNA.
DR EMBL; AK142963; BAE25233.1; ALT_FRAME; mRNA.
DR EMBL; AF499468; AAM22183.1; -; Genomic_DNA.
DR EMBL; BC096559; AAH96559.1; -; mRNA.
DR CCDS; CCDS56681.1; -.
DR RefSeq; NP_081069.1; NM_026793.2.
DR AlphaFoldDB; Q8R411; -.
DR BioGRID; 212964; 1.
DR STRING; 10090.ENSMUSP00000050430; -.
DR iPTMnet; Q8R411; -.
DR PhosphoSitePlus; Q8R411; -.
DR MaxQB; Q8R411; -.
DR PaxDb; Q8R411; -.
DR PRIDE; Q8R411; -.
DR ProteomicsDB; 287650; -.
DR Antibodypedia; 55356; 129 antibodies from 23 providers.
DR Ensembl; ENSMUST00000051809; ENSMUSP00000050430; ENSMUSG00000046916.
DR GeneID; 68632; -.
DR KEGG; mmu:68632; -.
DR UCSC; uc007egl.2; mouse.
DR CTD; 80177; -.
DR MGI; MGI:1915882; Myct1.
DR VEuPathDB; HostDB:ENSMUSG00000046916; -.
DR eggNOG; ENOG502RXWU; Eukaryota.
DR GeneTree; ENSGT00390000011642; -.
DR HOGENOM; CLU_104680_0_0_1; -.
DR InParanoid; Q8R411; -.
DR OMA; PEFHWSN; -.
DR OrthoDB; 1364750at2759; -.
DR PhylomeDB; Q8R411; -.
DR TreeFam; TF333196; -.
DR BioGRID-ORCS; 68632; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Myct1; mouse.
DR PRO; PR:Q8R411; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8R411; protein.
DR Bgee; ENSMUSG00000046916; Expressed in lumbar dorsal root ganglion and 166 other tissues.
DR Genevisible; Q8R411; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; IMP:MGI.
DR InterPro; IPR029180; Myc_target_1.
DR PANTHER; PTHR14869; PTHR14869; 1.
DR Pfam; PF15179; Myc_target_1; 1.
PE 1: Evidence at protein level;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..188
FT /note="Myc target protein 1"
FT /id="PRO_0000310960"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 47..65
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 16
FT /note="F -> L (in Ref. 2; BAB23032)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="P -> R (in Ref. 2; BAE25233)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 188 AA; 21079 MW; 7B4FC2D5CE66929B CRC64;
MANNTTSLGS PWPENFWEDL IMSFTVSVAI GLAIGGFLWA LFVFLSRRRR ASAPISQWSP
TRRPRSSYNH GLNRTGFYRH SGYERRSNLS LASLTFQRQA SMELVNSFPR KSSFRASTFH
PFLQCPPLPV ETESQLMTLS ASTTPSTLST AHSPSRPDFR WSSNSLRMGL STPPPPAYES
IIKAFPDS
