RL31_HUMAN
ID RL31_HUMAN Reviewed; 125 AA.
AC P62899; B7Z4K2; D3DVJ4; P12947; Q53SQ5; Q6IRZ0; Q6LBJ6;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=60S ribosomal protein L31;
DE AltName: Full=Large ribosomal subunit protein eL31 {ECO:0000303|PubMed:24524803};
GN Name=RPL31;
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] (ISOFORM 1).
RX PubMed=2780320; DOI=10.1093/nar/17.17.7105;
RA Nobori T., Hexdall L.E., Carson D.A.;
RT "cDNA sequence of human ribosomal protein L31.";
RL Nucleic Acids Res. 17:7105-7105(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11875025; DOI=10.1101/gr.214202;
RA Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S.,
RA Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.;
RT "The human ribosomal protein genes: sequencing and comparative analysis of
RT 73 genes.";
RL Genome Res. 12:379-390(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, Liver, 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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-125 (ISOFORM 1).
RX PubMed=2597680; DOI=10.1016/0167-4781(89)90119-x;
RA Chester K.A., Robson L., Beyent R.H.J., Talbot I.C., Pringle J.H.,
RA Primrose L., Macpherson A.J.S., Boxer G., Southhall P., Malcolm A.D.B.;
RT "Identification of a human ribosomal protein mRNA with increased expression
RT in colorectal tumours.";
RL Biochim. Biophys. Acta 1009:297-300(1989).
RN [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-75, 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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
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 [18]
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 [19]
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 [20]
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 [21] {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.
CC {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547}.
CC -!- INTERACTION:
CC P62899; P28329-3: CHAT; NbExp=3; IntAct=EBI-1053664, EBI-25837549;
CC P62899; P22607: FGFR3; NbExp=3; IntAct=EBI-1053664, EBI-348399;
CC P62899; P06396: GSN; NbExp=3; IntAct=EBI-1053664, EBI-351506;
CC P62899; P42858: HTT; NbExp=3; IntAct=EBI-1053664, EBI-466029;
CC P62899; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-1053664, EBI-741480;
CC P62899; Q9Y649; NbExp=3; IntAct=EBI-1053664, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P62899-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P62899-2; Sequence=VSP_042572;
CC Name=3;
CC IsoId=P62899-3; Sequence=VSP_043224;
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL31 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X15940; CAA34066.1; -; mRNA.
DR EMBL; AB061830; BAB79468.1; -; Genomic_DNA.
DR EMBL; AK297483; BAH12588.1; -; mRNA.
DR EMBL; AC016738; AAY14823.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01826.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01827.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01829.1; -; Genomic_DNA.
DR EMBL; BC017343; AAH17343.1; -; mRNA.
DR EMBL; BC070210; AAH70210.1; -; mRNA.
DR EMBL; BC070373; AAH70373.1; -; mRNA.
DR EMBL; X69181; CAA48925.1; -; mRNA.
DR CCDS; CCDS2049.1; -. [P62899-1]
DR CCDS; CCDS46373.1; -. [P62899-2]
DR CCDS; CCDS46374.1; -. [P62899-3]
DR PIR; S05576; R5HU31.
DR RefSeq; NP_000984.1; NM_000993.4. [P62899-1]
DR RefSeq; NP_001092047.1; NM_001098577.2. [P62899-2]
DR RefSeq; NP_001093163.1; NM_001099693.1. [P62899-3]
DR PDB; 4UG0; EM; -; Ld=1-125.
DR PDB; 4V6X; EM; 5.00 A; Cd=1-125.
DR PDB; 5AJ0; EM; 3.50 A; Ad=1-125.
DR PDB; 5LKS; EM; 3.60 A; Ld=1-125.
DR PDB; 5T2C; EM; 3.60 A; X=1-125.
DR PDB; 6IP5; EM; 3.90 A; 2X=1-125.
DR PDB; 6IP6; EM; 4.50 A; 2X=1-125.
DR PDB; 6IP8; EM; 3.90 A; 2X=1-125.
DR PDB; 6LQM; EM; 3.09 A; T=1-125.
DR PDB; 6LSR; EM; 3.13 A; T=1-125.
DR PDB; 6LSS; EM; 3.23 A; j=1-125.
DR PDB; 6LU8; EM; 3.13 A; j=1-125.
DR PDB; 6OLE; EM; 3.10 A; e=18-123.
DR PDB; 6OLF; EM; 3.90 A; e=18-123.
DR PDB; 6OLG; EM; 3.40 A; Ad=18-123.
DR PDB; 6OLI; EM; 3.50 A; e=18-123.
DR PDB; 6OLZ; EM; 3.90 A; Ad=18-123.
DR PDB; 6OM0; EM; 3.10 A; e=18-123.
DR PDB; 6OM7; EM; 3.70 A; e=18-123.
DR PDB; 6QZP; EM; 2.90 A; Ld=18-124.
DR PDB; 6XA1; EM; 2.80 A; Ld=18-124.
DR PDB; 6Y0G; EM; 3.20 A; Ld=1-125.
DR PDB; 6Y2L; EM; 3.00 A; Ld=1-125.
DR PDB; 6Y57; EM; 3.50 A; Ld=1-125.
DR PDB; 6Y6X; EM; 2.80 A; Ld=18-124.
DR PDB; 6Z6L; EM; 3.00 A; Ld=1-125.
DR PDB; 6Z6M; EM; 3.10 A; Ld=1-125.
DR PDB; 6Z6N; EM; 2.90 A; Ld=1-125.
DR PDB; 6ZM7; EM; 2.70 A; Ld=1-125.
DR PDB; 6ZME; EM; 3.00 A; Ld=1-125.
DR PDB; 6ZMI; EM; 2.60 A; Ld=1-125.
DR PDB; 6ZMO; EM; 3.10 A; Ld=1-125.
DR PDB; 7BHP; EM; 3.30 A; Ld=1-125.
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; 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; P62899; -.
DR SMR; P62899; -.
DR BioGRID; 112079; 592.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR CORUM; P62899; -.
DR IntAct; P62899; 84.
DR MINT; P62899; -.
DR STRING; 9606.ENSP00000386717; -.
DR GlyGen; P62899; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62899; -.
DR MetOSite; P62899; -.
DR PhosphoSitePlus; P62899; -.
DR SwissPalm; P62899; -.
DR BioMuta; RPL31; -.
DR DMDM; 51702807; -.
DR SWISS-2DPAGE; P62899; -.
DR EPD; P62899; -.
DR jPOST; P62899; -.
DR MassIVE; P62899; -.
DR MaxQB; P62899; -.
DR PaxDb; P62899; -.
DR PeptideAtlas; P62899; -.
DR PRIDE; P62899; -.
DR ProteomicsDB; 57447; -. [P62899-1]
DR ProteomicsDB; 57448; -. [P62899-2]
DR ProteomicsDB; 57449; -. [P62899-3]
DR TopDownProteomics; P62899-1; -. [P62899-1]
DR Antibodypedia; 32888; 148 antibodies from 27 providers.
DR DNASU; 6160; -.
DR Ensembl; ENST00000264258.8; ENSP00000264258.3; ENSG00000071082.11. [P62899-1]
DR Ensembl; ENST00000409028.8; ENSP00000386717.3; ENSG00000071082.11. [P62899-2]
DR Ensembl; ENST00000409320.7; ENSP00000387163.3; ENSG00000071082.11. [P62899-3]
DR Ensembl; ENST00000409733.5; ENSP00000386681.1; ENSG00000071082.11. [P62899-1]
DR GeneID; 6160; -.
DR KEGG; hsa:6160; -.
DR MANE-Select; ENST00000264258.8; ENSP00000264258.3; NM_000993.5; NP_000984.1.
DR UCSC; uc002taq.5; human. [P62899-1]
DR CTD; 6160; -.
DR DisGeNET; 6160; -.
DR GeneCards; RPL31; -.
DR HGNC; HGNC:10334; RPL31.
DR HPA; ENSG00000071082; Low tissue specificity.
DR MalaCards; RPL31; -.
DR MIM; 617415; gene.
DR neXtProt; NX_P62899; -.
DR OpenTargets; ENSG00000071082; -.
DR Orphanet; 124; Blackfan-Diamond anemia.
DR PharmGKB; PA34715; -.
DR VEuPathDB; HostDB:ENSG00000071082; -.
DR eggNOG; KOG0893; Eukaryota.
DR GeneTree; ENSGT00950000183030; -.
DR InParanoid; P62899; -.
DR OMA; NMHKRLH; -.
DR OrthoDB; 1547011at2759; -.
DR PhylomeDB; P62899; -.
DR TreeFam; TF314858; -.
DR PathwayCommons; P62899; -.
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; P62899; -.
DR SIGNOR; P62899; -.
DR BioGRID-ORCS; 6160; 805 hits in 1056 CRISPR screens.
DR ChiTaRS; RPL31; human.
DR GeneWiki; 60S_ribosomal_protein_L31; -.
DR GenomeRNAi; 6160; -.
DR Pharos; P62899; Tbio.
DR PRO; PR:P62899; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P62899; protein.
DR Bgee; ENSG00000071082; Expressed in upper leg skin and 205 other tissues.
DR ExpressionAtlas; P62899; baseline and differential.
DR Genevisible; P62899; 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; IDA:UniProtKB.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0042788; C:polysomal ribosome; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
DR CDD; cd00463; Ribosomal_L31e; 1.
DR Gene3D; 3.10.440.10; -; 1.
DR InterPro; IPR000054; Ribosomal_L31e.
DR InterPro; IPR020052; Ribosomal_L31e_CS.
DR InterPro; IPR023621; Ribosomal_L31e_dom_sf.
DR PANTHER; PTHR10956; PTHR10956; 1.
DR Pfam; PF01198; Ribosomal_L31e; 1.
DR SMART; SM01380; Ribosomal_L31e; 1.
DR SUPFAM; SSF54575; SSF54575; 1.
DR PROSITE; PS01144; RIBOSOMAL_L31E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..125
FT /note="60S ribosomal protein L31"
FT /id="PRO_0000153763"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62900"
FT MOD_RES 55
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62900"
FT MOD_RES 70
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62900"
FT MOD_RES 75
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 75
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62900"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692"
FT VAR_SEQ 116..125
FT /note="NLQTVNVDEN -> ISVLNSVTVAKSP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042572"
FT VAR_SEQ 116..125
FT /note="NLQTVNVDEN -> SKFSIP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043224"
SQ SEQUENCE 125 AA; 14463 MW; BA9DBE79B9E1C071 CRC64;
MAPAKKGGEK KKGRSAINEV VTREYTINIH KRIHGVGFKK RAPRALKEIR KFAMKEMGTP
DVRIDTRLNK AVWAKGIRNV PYRIRVRLSR KRNEDEDSPN KLYTLVTYVP VTTFKNLQTV
NVDEN
