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RPRM_MOUSE
ID   RPRM_MOUSE              Reviewed;         109 AA.
AC   Q9JJ72; Q8K1G8;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Protein reprimo;
GN   Name=Rprm;
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, INDUCTION, AND
RP   GLYCOSYLATION AT ASN-7 AND ASN-18.
RX   PubMed=10930422; DOI=10.1074/jbc.c000235200;
RA   Ohki R., Nemoto J., Murasawa H., Oda E., Inazawa J., Tanaka N.,
RA   Taniguchi T.;
RT   "Reprimo, a new candidate mediator of the p53-mediated cell cycle arrest at
RT   the G2 phase.";
RL   J. Biol. Chem. 275:22627-22630(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic stem cell, and Head;
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 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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Uterus;
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
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 be involved in the regulation of p53-dependent G2 arrest
CC       of the cell cycle. Seems to induce cell cycle arrest by inhibiting CDK1
CC       activity and nuclear translocation of the CDC2 cyclin B1 complex.
CC       {ECO:0000269|PubMed:10930422}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10930422}. Membrane
CC       {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC   -!- INDUCTION: By p53/TP53, following X-ray irradiation.
CC       {ECO:0000269|PubMed:10930422}.
CC   -!- MISCELLANEOUS: 'Reprimo' signifies stop/repress.
CC   -!- SIMILARITY: Belongs to the reprimo family. {ECO:0000305}.
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DR   EMBL; AB043586; BAB01514.1; -; mRNA.
DR   EMBL; AK010465; BAB26960.1; -; mRNA.
DR   EMBL; AK014769; BAB29541.1; -; mRNA.
DR   EMBL; AL844850; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC030065; AAH30065.1; -; mRNA.
DR   CCDS; CCDS16040.1; -.
DR   RefSeq; NP_075885.1; NM_023396.5.
DR   AlphaFoldDB; Q9JJ72; -.
DR   STRING; 10090.ENSMUSP00000097667; -.
DR   GlyGen; Q9JJ72; 2 sites.
DR   iPTMnet; Q9JJ72; -.
DR   PhosphoSitePlus; Q9JJ72; -.
DR   PaxDb; Q9JJ72; -.
DR   PRIDE; Q9JJ72; -.
DR   ProteomicsDB; 299950; -.
DR   Antibodypedia; 54148; 90 antibodies from 15 providers.
DR   DNASU; 67874; -.
DR   Ensembl; ENSMUST00000100089; ENSMUSP00000097667; ENSMUSG00000075334.
DR   GeneID; 67874; -.
DR   KEGG; mmu:67874; -.
DR   UCSC; uc008jrp.1; mouse.
DR   CTD; 56475; -.
DR   MGI; MGI:1915124; Rprm.
DR   VEuPathDB; HostDB:ENSMUSG00000075334; -.
DR   eggNOG; ENOG502S262; Eukaryota.
DR   GeneTree; ENSGT00390000010523; -.
DR   HOGENOM; CLU_170456_0_0_1; -.
DR   InParanoid; Q9JJ72; -.
DR   OMA; ERNLFIM; -.
DR   OrthoDB; 1529294at2759; -.
DR   PhylomeDB; Q9JJ72; -.
DR   TreeFam; TF332720; -.
DR   BioGRID-ORCS; 67874; 1 hit in 71 CRISPR screens.
DR   ChiTaRS; Rprm; mouse.
DR   PRO; PR:Q9JJ72; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q9JJ72; protein.
DR   Bgee; ENSMUSG00000075334; Expressed in piriform cortex and 171 other tissues.
DR   Genevisible; Q9JJ72; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051726; P:regulation of cell cycle; IDA:MGI.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; IDA:MGI.
DR   InterPro; IPR033356; Reprimo.
DR   InterPro; IPR043383; Reprimo_fam.
DR   PANTHER; PTHR28649; PTHR28649; 1.
DR   PANTHER; PTHR28649:SF2; PTHR28649:SF2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..109
FT                   /note="Protein reprimo"
FT                   /id="PRO_0000312753"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         98
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CARBOHYD        7
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:10930422"
FT   CARBOHYD        18
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:10930422"
FT   CONFLICT        17
FT                   /note="V -> A (in Ref. 4; AAH30065)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   109 AA;  11820 MW;  954F7C6397A84F9E CRC64;
     MNSVLGNQTD VAGLFLVNSS EALERAVRCC TQASVVTDDG FAEGGPDERS LYIMRVVQIA
     VMCVLSLTVV FGIFFLGCNL LIKSEGMINF LVKDRRPSKE VEAVVVGPY
 
 
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