RL35_HUMAN
ID RL35_HUMAN Reviewed; 123 AA.
AC P42766; A8K4V7; Q4VBY5; Q5JTN5; Q6IBC7; Q96QJ7; Q9BYF4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=60S ribosomal protein L35;
DE AltName: Full=Large ribosomal subunit protein uL29 {ECO:0000303|PubMed:24524803};
GN Name=RPL35;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Patel S.K., Chandraratna R., Nagpal S.;
RT "Human cDNA sequence of ribosomal protein L35.";
RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Lung, Muscle, and Prostate;
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 [6]
RP PROTEIN SEQUENCE OF 2-13, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP AND SUBUNIT.
RX PubMed=12962325; DOI=10.1023/a:1025068419698;
RA Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R.,
RA Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B., Karpova G.G.;
RT "Characterization and analysis of posttranslational modifications of the
RT human large cytoplasmic ribosomal subunit proteins by mass spectrometry and
RT Edman sequencing.";
RL J. Protein Chem. 22:249-258(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-63.
RX PubMed=11401437; DOI=10.1006/geno.2000.6470;
RA Uechi T., Tanaka T., Kenmochi N.;
RT "A complete map of the human ribosomal protein genes: assignment of 80
RT genes to the cytogenetic map and implications for human disorders.";
RL Genomics 72:223-230(2001).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-19 AND LYS-43, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP NOMENCLATURE.
RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT "A new system for naming ribosomal proteins.";
RL Curr. Opin. Struct. Biol. 24:165-169(2014).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-25, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [15]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
RN [16] {ECO:0007744|PDB:6LQM, ECO:0007744|PDB:6LSR, ECO:0007744|PDB:6LSS, ECO:0007744|PDB:6LU8}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.09 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=32669547; DOI=10.1038/s41467-020-17237-x;
RA Liang X., Zuo M.Q., Zhang Y., Li N., Ma C., Dong M.Q., Gao N.;
RT "Structural snapshots of human pre-60S ribosomal particles before and after
RT nuclear export.";
RL Nat. Commun. 11:3542-3542(2020).
RN [17]
RP VARIANT DBA19 ASN-77, AND INVOLVEMENT IN DBA19.
RX PubMed=28280134; DOI=10.1136/jmedgenet-2016-104346;
RA Mirabello L., Khincha P.P., Ellis S.R., Giri N., Brodie S.,
RA Chandrasekharappa S.C., Donovan F.X., Zhou W., Hicks B.D., Boland J.F.,
RA Yeager M., Jones K., Zhu B., Wang M., Alter B.P., Savage S.A.;
RT "Novel and known ribosomal causes of Diamond-Blackfan anaemia identified
RT through comprehensive genomic characterisation.";
RL J. Med. Genet. 54:417-425(2017).
CC -!- FUNCTION: Component of the large ribosomal subunit (PubMed:12962325,
CC PubMed:23636399, PubMed:32669547). The ribosome is a large
CC ribonucleoprotein complex responsible for the synthesis of proteins in
CC the cell (PubMed:12962325, PubMed:23636399, PubMed:32669547).
CC {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547,
CC ECO:0000305|PubMed:12962325}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (PubMed:12962325,
CC PubMed:23636399, PubMed:32669547). {ECO:0000269|PubMed:23636399,
CC ECO:0000269|PubMed:32669547, ECO:0000305|PubMed:12962325}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}.
CC -!- DISEASE: Diamond-Blackfan anemia 19 (DBA19) [MIM:618312]: A form of
CC Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic
CC anemia that usually presents early in infancy. Diamond-Blackfan anemia
CC is characterized by a moderate to severe macrocytic anemia,
CC erythroblastopenia, and an increased risk of malignancy. 30 to 40% of
CC Diamond-Blackfan anemia patients present with short stature and
CC congenital anomalies, the most frequent being craniofacial (Pierre-
CC Robin syndrome and cleft palate), thumb and urogenital anomalies. DBA19
CC inheritance is autosomal dominant. {ECO:0000269|PubMed:28280134}.
CC Note=The disease may be caused by variants affecting the gene
CC represented in this entry.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL29 family.
CC {ECO:0000305}.
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DR EMBL; U12465; AAA51648.1; -; mRNA.
DR EMBL; CR456877; CAG33158.1; -; mRNA.
DR EMBL; AK291072; BAF83761.1; -; mRNA.
DR EMBL; AL354928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000348; AAH00348.1; -; mRNA.
DR EMBL; BC010919; AAH10919.1; -; mRNA.
DR EMBL; BC071915; AAH71915.1; -; mRNA.
DR EMBL; BC094828; AAH94828.1; -; mRNA.
DR EMBL; AB046409; BAB21255.1; -; Genomic_DNA.
DR CCDS; CCDS6858.1; -.
DR PIR; G01477; G01477.
DR RefSeq; NP_009140.1; NM_007209.3.
DR PDB; 4UG0; EM; -; Lh=1-123.
DR PDB; 4V6X; EM; 5.00 A; Ch=1-123.
DR PDB; 5AJ0; EM; 3.50 A; Ah=1-123.
DR PDB; 5LKS; EM; 3.60 A; Lh=1-123.
DR PDB; 5T2C; EM; 3.60 A; b=1-123.
DR PDB; 6IP5; EM; 3.90 A; 2b=1-123.
DR PDB; 6IP6; EM; 4.50 A; 2b=1-123.
DR PDB; 6IP8; EM; 3.90 A; 2b=1-123.
DR PDB; 6LQM; EM; 3.09 A; H=1-123.
DR PDB; 6LSR; EM; 3.13 A; H=1-123.
DR PDB; 6LSS; EM; 3.23 A; H=1-123.
DR PDB; 6LU8; EM; 3.13 A; H=1-123.
DR PDB; 6OLE; EM; 3.10 A; i=2-123.
DR PDB; 6OLF; EM; 3.90 A; i=2-123.
DR PDB; 6OLG; EM; 3.40 A; Ah=2-123.
DR PDB; 6OLI; EM; 3.50 A; i=2-123.
DR PDB; 6OLZ; EM; 3.90 A; Ah=2-123.
DR PDB; 6OM0; EM; 3.10 A; i=2-123.
DR PDB; 6OM7; EM; 3.70 A; i=2-123.
DR PDB; 6QZP; EM; 2.90 A; Lh=2-123.
DR PDB; 6SXO; EM; 3.30 A; Lh=1-123.
DR PDB; 6W6L; EM; 3.84 A; i=1-123.
DR PDB; 6XA1; EM; 2.80 A; Lh=2-123.
DR PDB; 6Y0G; EM; 3.20 A; Lh=1-123.
DR PDB; 6Y2L; EM; 3.00 A; Lh=1-123.
DR PDB; 6Y57; EM; 3.50 A; Lh=1-123.
DR PDB; 6Y6X; EM; 2.80 A; Lh=2-123.
DR PDB; 6Z6L; EM; 3.00 A; Lh=1-123.
DR PDB; 6Z6M; EM; 3.10 A; Lh=1-123.
DR PDB; 6Z6N; EM; 2.90 A; Lh=1-123.
DR PDB; 6ZM7; EM; 2.70 A; Lh=1-123.
DR PDB; 6ZME; EM; 3.00 A; Lh=1-123.
DR PDB; 6ZMI; EM; 2.60 A; Lh=1-123.
DR PDB; 6ZMO; EM; 3.10 A; Lh=1-123.
DR PDB; 7BHP; EM; 3.30 A; Lh=1-123.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 5AJ0; -.
DR PDBsum; 5LKS; -.
DR PDBsum; 5T2C; -.
DR PDBsum; 6IP5; -.
DR PDBsum; 6IP6; -.
DR PDBsum; 6IP8; -.
DR PDBsum; 6LQM; -.
DR PDBsum; 6LSR; -.
DR PDBsum; 6LSS; -.
DR PDBsum; 6LU8; -.
DR PDBsum; 6OLE; -.
DR PDBsum; 6OLF; -.
DR PDBsum; 6OLG; -.
DR PDBsum; 6OLI; -.
DR PDBsum; 6OLZ; -.
DR PDBsum; 6OM0; -.
DR PDBsum; 6OM7; -.
DR PDBsum; 6QZP; -.
DR PDBsum; 6SXO; -.
DR PDBsum; 6W6L; -.
DR PDBsum; 6XA1; -.
DR PDBsum; 6Y0G; -.
DR PDBsum; 6Y2L; -.
DR PDBsum; 6Y57; -.
DR PDBsum; 6Y6X; -.
DR PDBsum; 6Z6L; -.
DR PDBsum; 6Z6M; -.
DR PDBsum; 6Z6N; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 7BHP; -.
DR AlphaFoldDB; P42766; -.
DR SMR; P42766; -.
DR BioGRID; 116392; 460.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR CORUM; P42766; -.
DR IntAct; P42766; 78.
DR MINT; P42766; -.
DR STRING; 9606.ENSP00000259469; -.
DR DrugBank; DB11638; Artenimol.
DR CarbonylDB; P42766; -.
DR iPTMnet; P42766; -.
DR PhosphoSitePlus; P42766; -.
DR SwissPalm; P42766; -.
DR BioMuta; RPL35; -.
DR SWISS-2DPAGE; P42766; -.
DR EPD; P42766; -.
DR jPOST; P42766; -.
DR MassIVE; P42766; -.
DR MaxQB; P42766; -.
DR PaxDb; P42766; -.
DR PeptideAtlas; P42766; -.
DR PRIDE; P42766; -.
DR ProteomicsDB; 55549; -.
DR TopDownProteomics; P42766; -.
DR Antibodypedia; 1246; 169 antibodies from 27 providers.
DR DNASU; 11224; -.
DR Ensembl; ENST00000348462.6; ENSP00000259469.4; ENSG00000136942.15.
DR GeneID; 11224; -.
DR KEGG; hsa:11224; -.
DR MANE-Select; ENST00000348462.6; ENSP00000259469.4; NM_007209.4; NP_009140.1.
DR UCSC; uc004boy.2; human.
DR CTD; 11224; -.
DR DisGeNET; 11224; -.
DR GeneCards; RPL35; -.
DR GeneReviews; RPL35; -.
DR HGNC; HGNC:10344; RPL35.
DR HPA; ENSG00000136942; Low tissue specificity.
DR MalaCards; RPL35; -.
DR MIM; 618312; phenotype.
DR MIM; 618315; gene.
DR neXtProt; NX_P42766; -.
DR OpenTargets; ENSG00000136942; -.
DR Orphanet; 124; Blackfan-Diamond anemia.
DR PharmGKB; PA34727; -.
DR VEuPathDB; HostDB:ENSG00000136942; -.
DR eggNOG; KOG3436; Eukaryota.
DR GeneTree; ENSGT00390000016384; -.
DR HOGENOM; CLU_110381_1_1_1; -.
DR InParanoid; P42766; -.
DR OMA; VMNQKAR; -.
DR OrthoDB; 1468839at2759; -.
DR PhylomeDB; P42766; -.
DR TreeFam; TF314951; -.
DR PathwayCommons; P42766; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-156902; Peptide chain elongation.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-192823; Viral mRNA Translation.
DR Reactome; R-HSA-2408557; Selenocysteine synthesis.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-HSA-72764; Eukaryotic Translation Termination.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency.
DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P42766; -.
DR SIGNOR; P42766; -.
DR BioGRID-ORCS; 11224; 774 hits in 1077 CRISPR screens.
DR ChiTaRS; RPL35; human.
DR GeneWiki; 60S_ribosomal_protein_L35; -.
DR GenomeRNAi; 11224; -.
DR Pharos; P42766; Tbio.
DR PRO; PR:P42766; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P42766; protein.
DR Bgee; ENSG00000136942; Expressed in skin of abdomen and 204 other tissues.
DR ExpressionAtlas; P42766; baseline and differential.
DR Genevisible; P42766; HS.
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; IDA:FlyBase.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; TAS:ProtInc.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; IC:FlyBase.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
DR Gene3D; 1.10.287.310; -; 1.
DR HAMAP; MF_00374; Ribosomal_L29; 1.
DR InterPro; IPR001854; Ribosomal_L29/L35.
DR InterPro; IPR036049; Ribosomal_L29/L35_sf.
DR InterPro; IPR018254; Ribosomal_L29_CS.
DR InterPro; IPR045059; RL35.
DR PANTHER; PTHR45722; PTHR45722; 1.
DR Pfam; PF00831; Ribosomal_L29; 1.
DR SUPFAM; SSF46561; SSF46561; 1.
DR TIGRFAMs; TIGR00012; L29; 1.
DR PROSITE; PS00579; RIBOSOMAL_L29; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Diamond-Blackfan anemia;
KW Direct protein sequencing; Disease variant; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12962325"
FT CHAIN 2..123
FT /note="60S ribosomal protein L35"
FT /id="PRO_0000130533"
FT REGION 85..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 43
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 25
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 77
FT /note="K -> N (in DBA19; unknown pathological significance;
FT dbSNP:rs1564307664)"
FT /evidence="ECO:0000269|PubMed:28280134"
FT /id="VAR_081936"
FT CONFLICT 122
FT /note="K -> R (in Ref. 5; AAH10919)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 123 AA; 14551 MW; 92B7694A97AC725D CRC64;
MAKIKARDLR GKKKEELLKQ LDDLKVELSQ LRVAKVTGGA ASKLSKIRVV RKSIARVLTV
INQTQKENLR KFYKGKKYKP LDLRPKKTRA MRRRLNKHEE NLKTKKQQRK ERLYPLRKYA
VKA
