RL35A_HUMAN
ID RL35A_HUMAN Reviewed; 110 AA.
AC P18077; Q08ES9; Q9BVN7;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 26-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=60S ribosomal protein L35a;
DE AltName: Full=Cell growth-inhibiting gene 33 protein;
DE AltName: Full=Large ribosomal subunit protein eL33 {ECO:0000303|PubMed:24524803};
GN Name=RPL35A; ORFNames=GIG33;
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].
RX PubMed=2388839; DOI=10.1093/nar/18.15.4600;
RA Herzog H., Hfferer L., Schneider R., Schweiger M.;
RT "cDNA encoding the human homologue of rat ribosomal protein L35a.";
RL Nucleic Acids Res. 18:4600-4600(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kim J.W., Kim H.K.;
RT "Identification of a cell growth-inhibiting gene.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, Colon, Ovary, and Placenta;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX PubMed=8786106; DOI=10.1006/geno.1996.0093;
RA Colombo P., Read M., Fried M.;
RT "The human L35a ribosomal protein (RPL35A) gene is located at chromosome
RT band 3q29-qter.";
RL Genomics 32:148-150(1996).
RN [6]
RP FUNCTION, AND VARIANTS DBA5 LEU-27 DEL AND ILE-33.
RX PubMed=18535205; DOI=10.1182/blood-2008-02-140012;
RA Farrar J.E., Nater M., Caywood E., McDevitt M.A., Kowalski J.,
RA Takemoto C.M., Talbot C.C. Jr., Meltzer P., Esposito D., Beggs A.H.,
RA Schneider H.E., Grabowska A., Ball S.E., Niewiadomska E., Sieff C.A.,
RA Vlachos A., Atsidaftos E., Ellis S.R., Lipton J.M., Gazda H.T.,
RA Arceci R.J.;
RT "Abnormalities of the large ribosomal subunit protein, Rpl35a, in Diamond-
RT Blackfan anemia.";
RL Blood 112:1582-1592(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-8, AND IDENTIFICATION BY MASS
RP 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 [8]
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 [9]
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 [10]
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 [11]
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 [12] {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).
CC -!- FUNCTION: Component of the large ribosomal subunit (PubMed:23636399,
CC PubMed:32669547). The ribosome is a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell (PubMed:23636399,
CC PubMed:32669547). Required for the proliferation and viability of
CC hematopoietic cells (PubMed:18535205). {ECO:0000269|PubMed:18535205,
CC ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547}.
CC -!- SUBUNIT: Component of the large ribosomal subunit.
CC {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547}.
CC -!- INTERACTION:
CC P18077; Q92993: KAT5; NbExp=3; IntAct=EBI-353383, EBI-399080;
CC P18077; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-353383, EBI-11742507;
CC P18077; P17252: PRKCA; NbExp=3; IntAct=EBI-353383, EBI-1383528;
CC P18077; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-353383, EBI-9090795;
CC P18077; P61981: YWHAG; NbExp=3; IntAct=EBI-353383, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}.
CC -!- DISEASE: Diamond-Blackfan anemia 5 (DBA5) [MIM:612528]: 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.
CC {ECO:0000269|PubMed:18535205}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Knockdown of RPL35A in hematopoietic cell lines results
CC in decreased cell proliferation, increased apoptosis, decreased
CC biogenesis of mature 60S ribosomal subunit, and abnormal processing of
CC large ribosomal subunit rRNA. {ECO:0000269|PubMed:18535205}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL33 family.
CC {ECO:0000305}.
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DR EMBL; X52966; CAA37138.1; -; mRNA.
DR EMBL; AY871273; AAX11429.1; -; mRNA.
DR EMBL; CH471252; EAW92249.1; -; Genomic_DNA.
DR EMBL; BC001037; AAH01037.1; -; mRNA.
DR EMBL; BC010949; AAH10949.1; -; mRNA.
DR EMBL; BC017093; AAH17093.1; -; mRNA.
DR EMBL; BC061890; AAH61890.1; -; mRNA.
DR EMBL; X94619; CAA64325.1; -; Genomic_DNA.
DR CCDS; CCDS33930.1; -.
DR PIR; S12710; R5HU35.
DR RefSeq; NP_000987.2; NM_000996.2.
DR RefSeq; NP_001303240.1; NM_001316311.1.
DR PDB; 4UG0; EM; -; Lf=1-110.
DR PDB; 4V6X; EM; 5.00 A; Cf=1-110.
DR PDB; 5AJ0; EM; 3.50 A; Af=1-110.
DR PDB; 5LKS; EM; 3.60 A; Lf=1-110.
DR PDB; 5T2C; EM; 3.60 A; Z=1-110.
DR PDB; 6IP5; EM; 3.90 A; 2Z=1-110.
DR PDB; 6IP6; EM; 4.50 A; 2Z=1-110.
DR PDB; 6IP8; EM; 3.90 A; 2Z=1-110.
DR PDB; 6LQM; EM; 3.09 A; u=1-110.
DR PDB; 6LSR; EM; 3.13 A; u=1-110.
DR PDB; 6LSS; EM; 3.23 A; n=1-110.
DR PDB; 6LU8; EM; 3.13 A; n=1-110.
DR PDB; 6OLE; EM; 3.10 A; g=2-110.
DR PDB; 6OLF; EM; 3.90 A; g=2-110.
DR PDB; 6OLG; EM; 3.40 A; Af=2-110.
DR PDB; 6OLI; EM; 3.50 A; g=2-110.
DR PDB; 6OLZ; EM; 3.90 A; Af=2-110.
DR PDB; 6OM0; EM; 3.10 A; g=2-110.
DR PDB; 6OM7; EM; 3.70 A; g=2-110.
DR PDB; 6QZP; EM; 2.90 A; Lf=2-110.
DR PDB; 6W6L; EM; 3.84 A; g=1-110.
DR PDB; 6XA1; EM; 2.80 A; Lf=2-110.
DR PDB; 6Y0G; EM; 3.20 A; Lf=1-110.
DR PDB; 6Y2L; EM; 3.00 A; Lf=1-110.
DR PDB; 6Y57; EM; 3.50 A; Lf=1-110.
DR PDB; 6Y6X; EM; 2.80 A; Lf=2-110.
DR PDB; 6Z6L; EM; 3.00 A; Lf=1-110.
DR PDB; 6Z6M; EM; 3.10 A; Lf=1-110.
DR PDB; 6Z6N; EM; 2.90 A; Lf=1-110.
DR PDB; 6ZM7; EM; 2.70 A; Lf=1-110.
DR PDB; 6ZME; EM; 3.00 A; Lf=1-110.
DR PDB; 6ZMI; EM; 2.60 A; Lf=1-110.
DR PDB; 6ZMO; EM; 3.10 A; Lf=1-110.
DR PDB; 7BHP; EM; 3.30 A; Lf=1-110.
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; 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; P18077; -.
DR SMR; P18077; -.
DR BioGRID; 112084; 344.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR CORUM; P18077; -.
DR IntAct; P18077; 62.
DR MINT; P18077; -.
DR STRING; 9606.ENSP00000419117; -.
DR GlyGen; P18077; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P18077; -.
DR MetOSite; P18077; -.
DR PhosphoSitePlus; P18077; -.
DR SwissPalm; P18077; -.
DR BioMuta; RPL35A; -.
DR SWISS-2DPAGE; P18077; -.
DR EPD; P18077; -.
DR jPOST; P18077; -.
DR MassIVE; P18077; -.
DR MaxQB; P18077; -.
DR PaxDb; P18077; -.
DR PeptideAtlas; P18077; -.
DR PRIDE; P18077; -.
DR ProteomicsDB; 53545; -.
DR TopDownProteomics; P18077; -.
DR Antibodypedia; 33969; 63 antibodies from 16 providers.
DR DNASU; 6165; -.
DR Ensembl; ENST00000448864.6; ENSP00000393393.1; ENSG00000182899.17.
DR Ensembl; ENST00000647248.2; ENSP00000495672.1; ENSG00000182899.17.
DR GeneID; 6165; -.
DR KEGG; hsa:6165; -.
DR MANE-Select; ENST00000647248.2; ENSP00000495672.1; NM_000996.4; NP_000987.2.
DR UCSC; uc003fyr.4; human.
DR CTD; 6165; -.
DR DisGeNET; 6165; -.
DR GeneCards; RPL35A; -.
DR GeneReviews; RPL35A; -.
DR HGNC; HGNC:10345; RPL35A.
DR HPA; ENSG00000182899; Low tissue specificity.
DR MalaCards; RPL35A; -.
DR MIM; 180468; gene.
DR MIM; 612528; phenotype.
DR neXtProt; NX_P18077; -.
DR OpenTargets; ENSG00000182899; -.
DR Orphanet; 124; Blackfan-Diamond anemia.
DR PharmGKB; PA34728; -.
DR VEuPathDB; HostDB:ENSG00000182899; -.
DR eggNOG; KOG0887; Eukaryota.
DR GeneTree; ENSGT00390000016972; -.
DR HOGENOM; CLU_100745_5_0_1; -.
DR InParanoid; P18077; -.
DR OMA; FKRHGRL; -.
DR OrthoDB; 1448743at2759; -.
DR PhylomeDB; P18077; -.
DR TreeFam; TF300104; -.
DR PathwayCommons; P18077; -.
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; P18077; -.
DR SIGNOR; P18077; -.
DR BioGRID-ORCS; 6165; 461 hits in 1021 CRISPR screens.
DR ChiTaRS; RPL35A; human.
DR GeneWiki; RPL35A; -.
DR GenomeRNAi; 6165; -.
DR Pharos; P18077; Tbio.
DR PRO; PR:P18077; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P18077; protein.
DR Bgee; ENSG00000182899; Expressed in tendon of biceps brachii and 202 other tissues.
DR ExpressionAtlas; P18077; baseline and differential.
DR Genevisible; P18077; 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:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
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; Diamond-Blackfan anemia;
KW Disease variant; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; tRNA-binding.
FT CHAIN 1..110
FT /note="60S ribosomal protein L35a"
FT /id="PRO_0000192796"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 63
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O55142"
FT MOD_RES 63
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O55142"
FT VARIANT 27
FT /note="Missing (in DBA5)"
FT /evidence="ECO:0000269|PubMed:18535205"
FT /id="VAR_055446"
FT VARIANT 33
FT /note="V -> I (in DBA5; may result in aberrant splicing;
FT dbSNP:rs116840808)"
FT /evidence="ECO:0000269|PubMed:18535205"
FT /id="VAR_055447"
FT CONFLICT 85
FT /note="R -> L (in Ref. 1; CAA37138)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 110 AA; 12538 MW; F32E4A26A25E79E8 CRC64;
MSGRLWSKAI FAGYKRGLRN QREHTALLKI EGVYARDETE FYLGKRCAYV YKAKNNTVTP
GGKPNKTRVI WGKVTRAHGN SGMVRAKFRS NLPAKAIGHR IRVMLYPSRI
