RL35A_MOUSE
ID RL35A_MOUSE Reviewed; 110 AA.
AC O55142;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=60S ribosomal protein L35a;
GN Name=Rpl35a;
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].
RC STRAIN=DBA/2J; TISSUE=Erythroid cell;
RX PubMed=11448102; DOI=10.1006/cbir.2000.0695;
RA Pappas I.S., Vizirianakis I.S., Tsiftsoglou A.S.;
RT "Cloning, sequencing and expression of a cDNA encoding the mouse L35a
RT ribosomal protein during differentiation of murine erythroleukemia (MEL)
RT cells.";
RL Cell Biol. Int. 25:629-634(2001).
RN [2]
RP SEQUENCE REVISION TO 53.
RA Vizirianakis I.S.;
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, and 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).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-63, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-63, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Component of the large ribosomal subunit. The ribosome is a
CC large ribonucleoprotein complex responsible for the synthesis of
CC proteins in the cell. Required for the proliferation and viability of
CC hematopoietic cells. {ECO:0000250|UniProtKB:P18077}.
CC -!- SUBUNIT: Component of the large ribosomal subunit.
CC {ECO:0000250|UniProtKB:P18077}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P18077}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL33 family.
CC {ECO:0000305}.
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DR EMBL; Y16430; CAA76215.2; -; mRNA.
DR EMBL; AK028214; BAC25818.1; -; mRNA.
DR CCDS; CCDS28126.1; -.
DR RefSeq; NP_001123956.1; NM_001130484.1.
DR RefSeq; NP_001123957.1; NM_001130485.1.
DR RefSeq; NP_067313.2; NM_021338.3.
DR PDB; 6SWA; EM; 3.10 A; d=1-110.
DR PDB; 7LS1; EM; 3.30 A; Z2=1-110.
DR PDB; 7LS2; EM; 3.10 A; Z2=1-110.
DR PDBsum; 6SWA; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; O55142; -.
DR SMR; O55142; -.
DR BioGRID; 208332; 66.
DR ComplexPortal; CPX-5262; 60S cytosolic large ribosomal subunit.
DR IntAct; O55142; 1.
DR STRING; 10090.ENSMUSP00000110731; -.
DR iPTMnet; O55142; -.
DR PhosphoSitePlus; O55142; -.
DR SwissPalm; O55142; -.
DR EPD; O55142; -.
DR jPOST; O55142; -.
DR PaxDb; O55142; -.
DR PeptideAtlas; O55142; -.
DR PRIDE; O55142; -.
DR ProteomicsDB; 300487; -.
DR TopDownProteomics; O55142; -.
DR Antibodypedia; 33969; 63 antibodies from 16 providers.
DR DNASU; 100505110; -.
DR Ensembl; ENSMUST00000078804; ENSMUSP00000077857; ENSMUSG00000060636.
DR Ensembl; ENSMUST00000115075; ENSMUSP00000110727; ENSMUSG00000060636.
DR Ensembl; ENSMUST00000115076; ENSMUSP00000110728; ENSMUSG00000060636.
DR Ensembl; ENSMUST00000115078; ENSMUSP00000110730; ENSMUSG00000060636.
DR Ensembl; ENSMUST00000115079; ENSMUSP00000110731; ENSMUSG00000060636.
DR GeneID; 57808; -.
DR KEGG; mmu:57808; -.
DR UCSC; uc007yzu.2; mouse.
DR CTD; 6165; -.
DR MGI; MGI:1928894; Rpl35a.
DR VEuPathDB; HostDB:ENSMUSG00000060636; -.
DR eggNOG; KOG0887; Eukaryota.
DR GeneTree; ENSGT00390000016972; -.
DR HOGENOM; CLU_100745_5_0_1; -.
DR InParanoid; O55142; -.
DR OMA; FKRHGRL; -.
DR OrthoDB; 1448743at2759; -.
DR PhylomeDB; O55142; -.
DR TreeFam; TF300104; -.
DR Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-MMU-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-MMU-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-MMU-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-MMU-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR BioGRID-ORCS; 57808; 27 hits in 72 CRISPR screens.
DR ChiTaRS; Rpl35a; mouse.
DR PRO; PR:O55142; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; O55142; protein.
DR Bgee; ENSMUSG00000060636; Expressed in thymus and 78 other tissues.
DR ExpressionAtlas; O55142; baseline and differential.
DR Genevisible; O55142; MM.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IPI:ComplexPortal.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; ISO:MGI.
DR GO; GO:0006364; P:rRNA processing; ISO:MGI.
DR Gene3D; 2.40.10.190; -; 1.
DR HAMAP; MF_00573; Ribosomal_L35Ae; 1.
DR InterPro; IPR038661; L35A_sf.
DR InterPro; IPR001780; Ribosomal_L35A.
DR InterPro; IPR018266; Ribosomal_L35Ae_CS.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR10902; PTHR10902; 1.
DR Pfam; PF01247; Ribosomal_L35Ae; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR PROSITE; PS01105; RIBOSOMAL_L35AE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..110
FT /note="60S ribosomal protein L35a"
FT /id="PRO_0000192798"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P18077"
FT MOD_RES 63
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 63
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 110 AA; 12554 MW; 126B5E77E75F29F2 CRC64;
MSGRLWCKAI FAGYKRGLRN QREHTALLKI EGVYARDETE FYLGKRCAYV YKAKNNTVTP
GGKPNKTRVI WGKVTRAHGN SGMVRAKFRS NLPAKAIGHR IRVMLYPSRI
