RL7A_HUMAN
ID RL7A_HUMAN Reviewed; 266 AA.
AC P62424; P11518; Q5T8U4;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=60S ribosomal protein L7a;
DE AltName: Full=Large ribosomal subunit protein eL8 {ECO:0000303|PubMed:24524803};
DE AltName: Full=PLA-X polypeptide;
DE AltName: Full=Surfeit locus protein 3;
GN Name=RPL7A; Synonyms=SURF-3, SURF3;
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].
RC TISSUE=Placenta;
RX PubMed=2966065; DOI=10.1002/j.1460-2075.1988.tb02794.x;
RA Kozma S.C., Redmond S.M.S., Saurer S.M., Groner B., Hynes N.E.;
RT "Activation of the receptor kinase domain of the trk oncogene by
RT recombination with two different cellular sequences.";
RL EMBO J. 7:147-154(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1756182; DOI=10.1016/0167-4781(91)90218-b;
RA Colombo P., Yon J., Fried M.;
RT "The organization and expression of the human L7a ribosomal protein gene.";
RL Biochim. Biophys. Acta 1129:93-95(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8482538; DOI=10.1016/0378-1119(93)90371-9;
RA De Falco S., Russo G., Angiolillo A., Pietropaolo C.;
RT "Human L7a ribosomal protein: sequence, structural organization, and
RT expression of a functional gene.";
RL Gene 126:227-235(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1696715; DOI=10.1073/pnas.87.16.6039;
RA Ben-Ishai R., Scharf R., Sharon R., Kapten I.;
RT "A human cellular sequence implicated in trk oncogene activation is DNA
RT damage inducible.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:6039-6043(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell, Eye, Lung, Placenta, Skin, and Uterus;
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [10]
RP INTERACTION WITH AGO2; DICER1; EIF6; MOV10 AND TARBP2.
RX PubMed=17507929; DOI=10.1038/nature05841;
RA Chendrimada T.P., Finn K.J., Ji X., Baillat D., Gregory R.I.,
RA Liebhaber S.A., Pasquinelli A.E., Shiekhattar R.;
RT "MicroRNA silencing through RISC recruitment of eIF6.";
RL Nature 447:823-828(2007).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-34; LYS-97 AND LYS-217, AND
RP IDENTIFICATION 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 [12]
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 [13]
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 [14]
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 [15]
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 [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-11; LYS-20; LYS-21; LYS-48;
RP LYS-97; LYS-125 AND LYS-245, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP 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 [17]
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 [18] {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). {ECO:0000269|PubMed:23636399,
CC ECO:0000269|PubMed:32669547}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (PubMed:23636399,
CC PubMed:32669547). Interacts with CRY1 (By similarity). Interacts with
CC DICER1, AGO2, TARBP2, MOV10 and EIF6; they form a large RNA-induced
CC silencing complex (RISC) (PubMed:17507929).
CC {ECO:0000250|UniProtKB:P12970, ECO:0000269|PubMed:17507929,
CC ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547}.
CC -!- INTERACTION:
CC P62424; O95793: STAU1; NbExp=2; IntAct=EBI-354172, EBI-358174;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}.
CC -!- DISEASE: Note=Chromosomal recombination involving RPL7A activates the
CC receptor kinase domain of the TRK oncogene.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL8 family.
CC {ECO:0000305}.
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DR EMBL; X06705; CAA29889.1; -; mRNA.
DR EMBL; X52138; CAA36383.1; -; Genomic_DNA.
DR EMBL; X61923; CAA43925.1; -; Genomic_DNA.
DR EMBL; M36072; AAA60282.1; -; mRNA.
DR EMBL; AK291123; BAF83812.1; -; mRNA.
DR EMBL; AK311743; BAG34686.1; -; mRNA.
DR EMBL; AL158826; CAI12832.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW88063.1; -; Genomic_DNA.
DR EMBL; BC005128; AAH05128.1; -; mRNA.
DR EMBL; BC021979; AAH21979.1; -; mRNA.
DR EMBL; BC023594; AAH23594.1; -; mRNA.
DR EMBL; BC023624; AAH23624.1; -; mRNA.
DR EMBL; BC071900; AAH71900.1; -; mRNA.
DR EMBL; BC071901; AAH71901.1; -; mRNA.
DR EMBL; BC073802; AAH73802.1; -; mRNA.
DR EMBL; BC105290; AAI05291.1; -; mRNA.
DR CCDS; CCDS6965.1; -.
DR PIR; S19717; R5HU7A.
DR RefSeq; NP_000963.1; NM_000972.2.
DR PDB; 4UG0; EM; -; LG=1-266.
DR PDB; 4V6X; EM; 5.00 A; CG=1-266.
DR PDB; 5AJ0; EM; 3.50 A; AG=1-266.
DR PDB; 5LKS; EM; 3.60 A; LG=1-266.
DR PDB; 5T2C; EM; 3.60 A; n=1-266.
DR PDB; 6IP5; EM; 3.90 A; 2B=1-266.
DR PDB; 6IP6; EM; 4.50 A; 2B=1-266.
DR PDB; 6IP8; EM; 3.90 A; 2B=1-266.
DR PDB; 6LQM; EM; 3.09 A; G=1-266.
DR PDB; 6LSR; EM; 3.13 A; G=1-266.
DR PDB; 6LSS; EM; 3.23 A; G=1-266.
DR PDB; 6LU8; EM; 3.13 A; G=1-266.
DR PDB; 6OLE; EM; 3.10 A; I=29-262.
DR PDB; 6OLF; EM; 3.90 A; I=29-262.
DR PDB; 6OLG; EM; 3.40 A; AG=29-262.
DR PDB; 6OLI; EM; 3.50 A; I=29-262.
DR PDB; 6OLZ; EM; 3.90 A; AG=29-262.
DR PDB; 6OM0; EM; 3.10 A; I=29-262.
DR PDB; 6OM7; EM; 3.70 A; I=29-262.
DR PDB; 6QZP; EM; 2.90 A; LG=26-266.
DR PDB; 6W6L; EM; 3.84 A; I=1-266.
DR PDB; 6XA1; EM; 2.80 A; LG=26-266.
DR PDB; 6Y0G; EM; 3.20 A; LG=1-266.
DR PDB; 6Y2L; EM; 3.00 A; LG=1-266.
DR PDB; 6Y57; EM; 3.50 A; LG=1-266.
DR PDB; 6Y6X; EM; 2.80 A; LG=26-266.
DR PDB; 6Z6L; EM; 3.00 A; LG=1-266.
DR PDB; 6Z6M; EM; 3.10 A; LG=1-266.
DR PDB; 6Z6N; EM; 2.90 A; LG=1-266.
DR PDB; 6ZM7; EM; 2.70 A; LG=1-266.
DR PDB; 6ZME; EM; 3.00 A; LG=1-266.
DR PDB; 6ZMI; EM; 2.60 A; LG=1-266.
DR PDB; 6ZMO; EM; 3.10 A; LG=1-266.
DR PDB; 6ZVK; EM; 3.49 A; V2=26-266.
DR PDB; 7A01; EM; 3.60 A; V2=26-266.
DR PDB; 7BHP; EM; 3.30 A; LG=1-266.
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; 6ZVK; -.
DR PDBsum; 7A01; -.
DR PDBsum; 7BHP; -.
DR AlphaFoldDB; P62424; -.
DR SMR; P62424; -.
DR BioGRID; 112050; 558.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR CORUM; P62424; -.
DR DIP; DIP-31502N; -.
DR IntAct; P62424; 131.
DR MINT; P62424; -.
DR STRING; 9606.ENSP00000361076; -.
DR GlyGen; P62424; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62424; -.
DR PhosphoSitePlus; P62424; -.
DR SwissPalm; P62424; -.
DR BioMuta; RPL7A; -.
DR DMDM; 54039239; -.
DR SWISS-2DPAGE; P62424; -.
DR EPD; P62424; -.
DR jPOST; P62424; -.
DR MassIVE; P62424; -.
DR PaxDb; P62424; -.
DR PeptideAtlas; P62424; -.
DR PRIDE; P62424; -.
DR ProteomicsDB; 57400; -.
DR TopDownProteomics; P62424; -.
DR Antibodypedia; 31830; 149 antibodies from 27 providers.
DR DNASU; 6130; -.
DR Ensembl; ENST00000323345.11; ENSP00000361076.3; ENSG00000148303.17.
DR Ensembl; ENST00000630979.3; ENSP00000487443.1; ENSG00000280858.3.
DR GeneID; 6130; -.
DR KEGG; hsa:6130; -.
DR MANE-Select; ENST00000323345.11; ENSP00000361076.3; NM_000972.3; NP_000963.1.
DR UCSC; uc004cde.2; human.
DR CTD; 6130; -.
DR DisGeNET; 6130; -.
DR GeneCards; RPL7A; -.
DR HGNC; HGNC:10364; RPL7A.
DR HPA; ENSG00000148303; Low tissue specificity.
DR MIM; 185640; gene.
DR neXtProt; NX_P62424; -.
DR OpenTargets; ENSG00000148303; -.
DR PharmGKB; PA34760; -.
DR VEuPathDB; HostDB:ENSG00000148303; -.
DR eggNOG; KOG3166; Eukaryota.
DR GeneTree; ENSGT00940000153294; -.
DR HOGENOM; CLU_055193_0_1_1; -.
DR InParanoid; P62424; -.
DR OMA; WLPALCK; -.
DR OrthoDB; 1200503at2759; -.
DR PhylomeDB; P62424; -.
DR TreeFam; TF300788; -.
DR PathwayCommons; P62424; -.
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; P62424; -.
DR SIGNOR; P62424; -.
DR BioGRID-ORCS; 6130; 744 hits in 1100 CRISPR screens.
DR ChiTaRS; RPL7A; human.
DR GeneWiki; RPL7A; -.
DR GenomeRNAi; 6130; -.
DR Pharos; P62424; Tbio.
DR PRO; PR:P62424; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P62424; protein.
DR Bgee; ENSG00000148303; Expressed in left ovary and 98 other tissues.
DR ExpressionAtlas; P62424; baseline and differential.
DR Genevisible; P62424; HS.
DR GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
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:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0005730; C:nucleolus; IDA:CACAO.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0042788; C:polysomal ribosome; IDA:HGNC-UCL.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
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:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
DR Gene3D; 3.30.1330.30; -; 1.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR001921; Ribosomal_L7A/L8.
DR InterPro; IPR004038; Ribosomal_L7Ae/L30e/S12e/Gad45.
DR InterPro; IPR018492; Ribosomal_L7Ae/L8/Nhp2.
DR InterPro; IPR004037; Ribosomal_L7Ae_CS.
DR Pfam; PF01248; Ribosomal_L7Ae; 1.
DR PRINTS; PR00881; L7ARS6FAMILY.
DR PRINTS; PR00882; RIBOSOMALL7A.
DR SUPFAM; SSF55315; SSF55315; 1.
DR PROSITE; PS01082; RIBOSOMAL_L7AE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromosomal rearrangement; Cytoplasm;
KW Isopeptide bond; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT CHAIN 1..266
FT /note="60S ribosomal protein L7a"
FT /id="PRO_0000136747"
FT MOD_RES 34
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 97
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 217
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 11
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 20
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 21
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 97
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 125
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 245
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
SQ SEQUENCE 266 AA; 29996 MW; 54EF43F221D9F704 CRC64;
MPKGKKAKGK KVAPAPAVVK KQEAKKVVNP LFEKRPKNFG IGQDIQPKRD LTRFVKWPRY
IRLQRQRAIL YKRLKVPPAI NQFTQALDRQ TATQLLKLAH KYRPETKQEK KQRLLARAEK
KAAGKGDVPT KRPPVLRAGV NTVTTLVENK KAQLVVIAHD VDPIELVVFL PALCRKMGVP
YCIIKGKARL GRLVHRKTCT TVAFTQVNSE DKGALAKLVE AIRTNYNDRY DEIRRHWGGN
VLGPKSVARI AKLEKAKAKE LATKLG
