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RM04_MOUSE
ID   RM04_MOUSE              Reviewed;         294 AA.
AC   Q9DCU6; Q811L8; Q8JZU9; Q9JJB3;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=39S ribosomal protein L4, mitochondrial;
DE            Short=L4mt;
DE            Short=MRP-L4;
GN   Name=Mrpl4; ORFNames=MNCb-3848;
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].
RX   PubMed=11279069; DOI=10.1074/jbc.m100432200;
RA   Suzuki T., Terasaki M., Takemoto-Hori C., Hanada T., Ueda T., Wada A.,
RA   Watanabe K.;
RT   "Structural compensation for the deficit of rRNA with proteins in the
RT   mammalian mitochondrial ribosome. Systematic analysis of protein components
RT   of the large ribosomal subunit from mammalian mitochondria.";
RL   J. Biol. Chem. 276:21724-21736(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT   "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT   oligo-capping method.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Brain, Colon, and 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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Pancreas, Spleen,
RC   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   -!- SUBUNIT: Component of the mitochondrial ribosome large subunit (39S)
CC       which comprises a 16S rRNA and about 50 distinct proteins. Interacts
CC       with MIEF1 upstream open reading frame protein.
CC       {ECO:0000250|UniProtKB:Q9BYD3}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9BYD3}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH37064.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAA95082.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AB049634; BAB40839.1; -; mRNA.
DR   EMBL; AB041599; BAA95082.1; ALT_FRAME; mRNA.
DR   EMBL; AK002464; BAB22118.1; -; mRNA.
DR   EMBL; BC037064; AAH37064.1; ALT_INIT; mRNA.
DR   EMBL; BC039983; AAH39983.2; -; mRNA.
DR   EMBL; BC061095; AAH61095.1; -; mRNA.
DR   CCDS; CCDS40548.1; -.
DR   RefSeq; NP_075656.2; NM_023167.2.
DR   AlphaFoldDB; Q9DCU6; -.
DR   SMR; Q9DCU6; -.
DR   BioGRID; 211261; 3.
DR   ComplexPortal; CPX-5302; 39S mitochondrial large ribosomal subunit.
DR   STRING; 10090.ENSMUSP00000003386; -.
DR   PhosphoSitePlus; Q9DCU6; -.
DR   SwissPalm; Q9DCU6; -.
DR   EPD; Q9DCU6; -.
DR   jPOST; Q9DCU6; -.
DR   MaxQB; Q9DCU6; -.
DR   PaxDb; Q9DCU6; -.
DR   PeptideAtlas; Q9DCU6; -.
DR   PRIDE; Q9DCU6; -.
DR   ProteomicsDB; 299828; -.
DR   Antibodypedia; 25237; 97 antibodies from 25 providers.
DR   DNASU; 66163; -.
DR   Ensembl; ENSMUST00000003386; ENSMUSP00000003386; ENSMUSG00000003299.
DR   GeneID; 66163; -.
DR   KEGG; mmu:66163; -.
DR   UCSC; uc009oju.1; mouse.
DR   CTD; 51073; -.
DR   MGI; MGI:2137210; Mrpl4.
DR   VEuPathDB; HostDB:ENSMUSG00000003299; -.
DR   eggNOG; KOG1624; Eukaryota.
DR   GeneTree; ENSGT00390000014512; -.
DR   HOGENOM; CLU_041575_3_3_1; -.
DR   InParanoid; Q9DCU6; -.
DR   OMA; PQVHILE; -.
DR   OrthoDB; 1592747at2759; -.
DR   PhylomeDB; Q9DCU6; -.
DR   TreeFam; TF313913; -.
DR   Reactome; R-MMU-5389840; Mitochondrial translation elongation.
DR   Reactome; R-MMU-5419276; Mitochondrial translation termination.
DR   BioGRID-ORCS; 66163; 27 hits in 111 CRISPR screens.
DR   ChiTaRS; Mrpl4; mouse.
DR   PRO; PR:Q9DCU6; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q9DCU6; protein.
DR   Bgee; ENSMUSG00000003299; Expressed in interventricular septum and 268 other tissues.
DR   ExpressionAtlas; Q9DCU6; baseline and differential.
DR   Genevisible; Q9DCU6; MM.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IC:ComplexPortal.
DR   GO; GO:0005762; C:mitochondrial large ribosomal subunit; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR   Gene3D; 3.40.1370.10; -; 1.
DR   HAMAP; MF_01328_B; Ribosomal_L4_B; 1.
DR   InterPro; IPR002136; Ribosomal_L4/L1e.
DR   InterPro; IPR023574; Ribosomal_L4_dom_sf.
DR   InterPro; IPR013005; Ribosomal_uL4/L1e.
DR   PANTHER; PTHR10746; PTHR10746; 1.
DR   Pfam; PF00573; Ribosomal_L4; 1.
DR   SUPFAM; SSF52166; SSF52166; 1.
DR   TIGRFAMs; TIGR03953; rplD_bact; 1.
PE   1: Evidence at protein level;
KW   Methylation; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein.
FT   CHAIN           1..294
FT                   /note="39S ribosomal protein L4, mitochondrial"
FT                   /id="PRO_0000238950"
FT   REGION          119..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         147
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BYD3"
FT   CONFLICT        147
FT                   /note="R -> L (in Ref. 2; BAA95082)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        268
FT                   /note="F -> L (in Ref. 2; BAA95082)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   294 AA;  33073 MW;  EED72D7728ABEB02 CRC64;
     MLRLFQAASR ASLRLSGSRV IHSLAEGAER PAEISEPRDS AGLLDPVLRK CELRIPVHRR
     PVQAWVESLR GFEQERIGLA ELHPDVFATA PRLDIVHQVA IWQRNFRRIS YANTKTRAEV
     SGGGRKPWQQ KGSGRARHGS IRSPLWRGGG VAHGPRGPTS YYYMLPMKVR ALGLKVALTV
     KLMQDDLHIV DSLELPTADP QYLTELAQYR HWGSSVLLVD LTHEEMPKNV VAATSGLNSF
     NLIPAVGLNV YSMLKHQTLV LTLPSVAFLE DKLLWQDSRY TPLYPFRLPY SDFP
 
 
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