RM01_MOUSE
ID RM01_MOUSE Reviewed; 336 AA.
AC Q99N96; Q3UQP5; Q8K351; Q9CWW4;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=39S ribosomal protein L1, mitochondrial;
DE Short=L1mt;
DE Short=MRP-L1;
DE Flags: Precursor;
GN Name=Mrpl1;
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].
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell, and Heart;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland, and Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-336.
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Pancreas, and
RC 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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH61042.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB26866.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB26866.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB40837.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK010343; BAB26866.1; ALT_SEQ; mRNA.
DR EMBL; AK142249; BAE24994.1; -; mRNA.
DR EMBL; BC028774; AAH28774.1; -; mRNA.
DR EMBL; BC061042; AAH61042.1; ALT_INIT; mRNA.
DR EMBL; AB049632; BAB40837.1; ALT_INIT; mRNA.
DR CCDS; CCDS19449.1; -.
DR RefSeq; NP_444388.2; NM_053158.3.
DR RefSeq; XP_006535355.1; XM_006535292.1.
DR AlphaFoldDB; Q99N96; -.
DR SMR; Q99N96; -.
DR BioGRID; 220433; 26.
DR ComplexPortal; CPX-5302; 39S mitochondrial large ribosomal subunit.
DR STRING; 10090.ENSMUSP00000112451; -.
DR iPTMnet; Q99N96; -.
DR PhosphoSitePlus; Q99N96; -.
DR EPD; Q99N96; -.
DR jPOST; Q99N96; -.
DR MaxQB; Q99N96; -.
DR PaxDb; Q99N96; -.
DR PeptideAtlas; Q99N96; -.
DR PRIDE; Q99N96; -.
DR ProteomicsDB; 299905; -.
DR Antibodypedia; 24877; 213 antibodies from 27 providers.
DR DNASU; 94061; -.
DR Ensembl; ENSMUST00000036437; ENSMUSP00000037046; ENSMUSG00000029486.
DR Ensembl; ENSMUST00000117766; ENSMUSP00000112977; ENSMUSG00000029486.
DR GeneID; 94061; -.
DR KEGG; mmu:94061; -.
DR UCSC; uc008yfi.2; mouse.
DR CTD; 65008; -.
DR MGI; MGI:2137202; Mrpl1.
DR VEuPathDB; HostDB:ENSMUSG00000029486; -.
DR eggNOG; KOG1569; Eukaryota.
DR GeneTree; ENSGT00940000162168; -.
DR HOGENOM; CLU_074129_0_0_1; -.
DR InParanoid; Q99N96; -.
DR OMA; INTMRPK; -.
DR OrthoDB; 1432931at2759; -.
DR PhylomeDB; Q99N96; -.
DR Reactome; R-MMU-5389840; Mitochondrial translation elongation.
DR Reactome; R-MMU-5419276; Mitochondrial translation termination.
DR BioGRID-ORCS; 94061; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Mrpl1; mouse.
DR PRO; PR:Q99N96; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q99N96; protein.
DR Bgee; ENSMUSG00000029486; Expressed in interventricular septum and 249 other tissues.
DR ExpressionAtlas; Q99N96; baseline and differential.
DR Genevisible; Q99N96; MM.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IC:ComplexPortal.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR GO; GO:0006412; P:translation; ISO:MGI.
DR CDD; cd00403; Ribosomal_L1; 1.
DR Gene3D; 3.40.50.790; -; 1.
DR InterPro; IPR023674; Ribosomal_L1-like.
DR InterPro; IPR028364; Ribosomal_L1/biogenesis.
DR InterPro; IPR016095; Ribosomal_L1_3-a/b-sand.
DR InterPro; IPR005879; Ribosomal_L1_mit.
DR Pfam; PF00687; Ribosomal_L1; 1.
DR SUPFAM; SSF56808; SSF56808; 1.
DR TIGRFAMs; TIGR01170; rplA_mito; 1.
PE 1: Evidence at protein level;
KW Mitochondrion; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Transit peptide.
FT TRANSIT 1..50
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 51..336
FT /note="39S ribosomal protein L1, mitochondrial"
FT /id="PRO_0000252441"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 56
FT /note="K -> E (in Ref. 2; BAB26866)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="K -> R (in Ref. 2; BAB26866)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="D -> G (in Ref. 2; BAB26866)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="T -> R (in Ref. 2; BAB26866)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="K -> R (in Ref. 2; BAB26866)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="A -> V (in Ref. 2; BAB26866)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 336 AA; 37597 MW; 328783081296B824 CRC64;
MAAAVRCLRR VLIHHQRHCL CKMASQASLY PCSVNSLLHN RHFAAAAAAA TKPARKIKKG
AKEKTSDEKP VDDIEKIKSY TYMESDPEDD VYLKRLYPRR IYEVEKAIHL LKKFQVLDFT
NPKQGVYLDL TLDMALGKKK TVEPFASVIA LPHLFSSEVN KVAVFTANAS EIKIAEENGA
AFAGGTDLVK KIMDDEVVVD FYVAVPEIMG ELNPLRKKLK KRFPKATRNS IGRDIPKMLE
LFKTAHEIMV DEERQNFLST KIATLDMPSD QIAANLQAVI NEVCKHRPLN LGPFVVRAFL
RSSTSEGLLL KTDSLLPKEA KTTEAETEET QTAEAA
