Full text data of RPL31
RPL31
[Confidence: low (only semi-automatic identification from reviews)]
60S ribosomal protein L31
Note: presumably soluble (membrane word is not in UniProt keywords or features)
60S ribosomal protein L31
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P62899
ID RL31_HUMAN Reviewed; 125 AA.
AC P62899; B7Z4K2; D3DVJ4; P12947; Q53SQ5; Q6IRZ0; Q6LBJ6;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 31-AUG-2004, sequence version 1.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=60S ribosomal protein L31;
GN Name=RPL31;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT analysis of 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Malcolm A.D.B.;
RT "Identification of a human ribosomal protein mRNA with increased
RT expression in colorectal tumours.";
RL Biochim. Biophys. Acta 1009:297-300(1989).
RN [8]
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
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND MASS
RP SPECTROMETRY.
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 [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-75, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [13]
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.,
RA Buerckstuemmer T., 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
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).
CC -!- INTERACTION:
CC Q9NVP2:ASF1B; NbExp=1; IntAct=EBI-1053664, EBI-1055650;
CC P62633:CNBP; NbExp=1; IntAct=EBI-1053664, EBI-1047529;
CC Q9NY93:DDX56; NbExp=1; IntAct=EBI-1053664, EBI-372376;
CC Q9NX58:LYAR; NbExp=1; IntAct=EBI-1053664, EBI-713507;
CC O15479:MAGEB2; NbExp=1; IntAct=EBI-1053664, EBI-1057615;
CC Q96BK5:PINX1; NbExp=1; IntAct=EBI-1053664, EBI-721782;
CC O43586:PSTPIP1; NbExp=1; IntAct=EBI-1053664, EBI-1050964;
CC Q9UHQ7:WBP5; NbExp=1; IntAct=EBI-1053664, EBI-1051372;
CC P63104:YWHAZ; NbExp=1; IntAct=EBI-1053664, EBI-347088;
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 Note=No experimental confirmation available;
CC Name=3;
CC IsoId=P62899-3; Sequence=VSP_043224;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the ribosomal protein L31e family.
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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 PIR; S05576; R5HU31.
DR RefSeq; NP_000984.1; NM_000993.4.
DR RefSeq; NP_001092047.1; NM_001098577.2.
DR RefSeq; NP_001093163.1; NM_001099693.1.
DR UniGene; Hs.469473; -.
DR PDB; 3J3B; EM; 5.00 A; d=1-125.
DR PDBsum; 3J3B; -.
DR ProteinModelPortal; P62899; -.
DR SMR; P62899; 12-124.
DR IntAct; P62899; 24.
DR MINT; MINT-5000327; -.
DR STRING; 9606.ENSP00000386717; -.
DR PhosphoSite; P62899; -.
DR DMDM; 51702807; -.
DR SWISS-2DPAGE; P62899; -.
DR PaxDb; P62899; -.
DR PRIDE; P62899; -.
DR DNASU; 6160; -.
DR Ensembl; ENST00000264258; ENSP00000264258; ENSG00000071082.
DR Ensembl; ENST00000409028; ENSP00000386717; ENSG00000071082.
DR Ensembl; ENST00000409320; ENSP00000387163; ENSG00000071082.
DR Ensembl; ENST00000409733; ENSP00000386681; ENSG00000071082.
DR GeneID; 6160; -.
DR KEGG; hsa:6160; -.
DR UCSC; uc002taq.4; human.
DR CTD; 6160; -.
DR GeneCards; GC02P101618; -.
DR H-InvDB; HIX0017577; -.
DR HGNC; HGNC:10334; RPL31.
DR neXtProt; NX_P62899; -.
DR PharmGKB; PA34715; -.
DR eggNOG; COG2097; -.
DR HOGENOM; HOG000216660; -.
DR HOVERGEN; HBG001549; -.
DR KO; K02910; -.
DR OMA; HIWSKGI; -.
DR PhylomeDB; P62899; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; RPL31; human.
DR GeneWiki; 60S_ribosomal_protein_L31; -.
DR GenomeRNAi; 6160; -.
DR NextBio; 23923; -.
DR PRO; PR:P62899; -.
DR ArrayExpress; P62899; -.
DR Bgee; P62899; -.
DR CleanEx; HS_RPL31; -.
DR Genevestigator; P62899; -.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0006414; P:translational elongation; TAS:Reactome.
DR GO; GO:0006413; P:translational initiation; TAS:Reactome.
DR GO; GO:0006415; P:translational termination; TAS:Reactome.
DR GO; GO:0019083; P:viral transcription; TAS:Reactome.
DR Gene3D; 3.10.440.10; -; 1.
DR InterPro; IPR000054; Ribosomal_L31e.
DR InterPro; IPR020052; Ribosomal_L31e_CS.
DR InterPro; IPR023621; Ribosomal_L31e_dom.
DR PANTHER; PTHR10956; PTHR10956; 1.
DR Pfam; PF01198; Ribosomal_L31e; 1.
DR ProDom; PD006030; 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; Complete proteome;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT CHAIN 1 125 60S ribosomal protein L31.
FT /FTId=PRO_0000153763.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 75 75 N6-acetyllysine.
FT MOD_RES 98 98 Phosphoserine.
FT VAR_SEQ 116 125 NLQTVNVDEN -> ISVLNSVTVAKSP (in isoform
FT 2).
FT /FTId=VSP_042572.
FT VAR_SEQ 116 125 NLQTVNVDEN -> SKFSIP (in isoform 3).
FT /FTId=VSP_043224.
SQ SEQUENCE 125 AA; 14463 MW; BA9DBE79B9E1C071 CRC64;
MAPAKKGGEK KKGRSAINEV VTREYTINIH KRIHGVGFKK RAPRALKEIR KFAMKEMGTP
DVRIDTRLNK AVWAKGIRNV PYRIRVRLSR KRNEDEDSPN KLYTLVTYVP VTTFKNLQTV
NVDEN
//
ID RL31_HUMAN Reviewed; 125 AA.
AC P62899; B7Z4K2; D3DVJ4; P12947; Q53SQ5; Q6IRZ0; Q6LBJ6;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 31-AUG-2004, sequence version 1.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=60S ribosomal protein L31;
GN Name=RPL31;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT analysis of 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Malcolm A.D.B.;
RT "Identification of a human ribosomal protein mRNA with increased
RT expression in colorectal tumours.";
RL Biochim. Biophys. Acta 1009:297-300(1989).
RN [8]
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
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND MASS
RP SPECTROMETRY.
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 [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-75, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [13]
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.,
RA Buerckstuemmer T., 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
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).
CC -!- INTERACTION:
CC Q9NVP2:ASF1B; NbExp=1; IntAct=EBI-1053664, EBI-1055650;
CC P62633:CNBP; NbExp=1; IntAct=EBI-1053664, EBI-1047529;
CC Q9NY93:DDX56; NbExp=1; IntAct=EBI-1053664, EBI-372376;
CC Q9NX58:LYAR; NbExp=1; IntAct=EBI-1053664, EBI-713507;
CC O15479:MAGEB2; NbExp=1; IntAct=EBI-1053664, EBI-1057615;
CC Q96BK5:PINX1; NbExp=1; IntAct=EBI-1053664, EBI-721782;
CC O43586:PSTPIP1; NbExp=1; IntAct=EBI-1053664, EBI-1050964;
CC Q9UHQ7:WBP5; NbExp=1; IntAct=EBI-1053664, EBI-1051372;
CC P63104:YWHAZ; NbExp=1; IntAct=EBI-1053664, EBI-347088;
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 Note=No experimental confirmation available;
CC Name=3;
CC IsoId=P62899-3; Sequence=VSP_043224;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the ribosomal protein L31e family.
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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 PIR; S05576; R5HU31.
DR RefSeq; NP_000984.1; NM_000993.4.
DR RefSeq; NP_001092047.1; NM_001098577.2.
DR RefSeq; NP_001093163.1; NM_001099693.1.
DR UniGene; Hs.469473; -.
DR PDB; 3J3B; EM; 5.00 A; d=1-125.
DR PDBsum; 3J3B; -.
DR ProteinModelPortal; P62899; -.
DR SMR; P62899; 12-124.
DR IntAct; P62899; 24.
DR MINT; MINT-5000327; -.
DR STRING; 9606.ENSP00000386717; -.
DR PhosphoSite; P62899; -.
DR DMDM; 51702807; -.
DR SWISS-2DPAGE; P62899; -.
DR PaxDb; P62899; -.
DR PRIDE; P62899; -.
DR DNASU; 6160; -.
DR Ensembl; ENST00000264258; ENSP00000264258; ENSG00000071082.
DR Ensembl; ENST00000409028; ENSP00000386717; ENSG00000071082.
DR Ensembl; ENST00000409320; ENSP00000387163; ENSG00000071082.
DR Ensembl; ENST00000409733; ENSP00000386681; ENSG00000071082.
DR GeneID; 6160; -.
DR KEGG; hsa:6160; -.
DR UCSC; uc002taq.4; human.
DR CTD; 6160; -.
DR GeneCards; GC02P101618; -.
DR H-InvDB; HIX0017577; -.
DR HGNC; HGNC:10334; RPL31.
DR neXtProt; NX_P62899; -.
DR PharmGKB; PA34715; -.
DR eggNOG; COG2097; -.
DR HOGENOM; HOG000216660; -.
DR HOVERGEN; HBG001549; -.
DR KO; K02910; -.
DR OMA; HIWSKGI; -.
DR PhylomeDB; P62899; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; RPL31; human.
DR GeneWiki; 60S_ribosomal_protein_L31; -.
DR GenomeRNAi; 6160; -.
DR NextBio; 23923; -.
DR PRO; PR:P62899; -.
DR ArrayExpress; P62899; -.
DR Bgee; P62899; -.
DR CleanEx; HS_RPL31; -.
DR Genevestigator; P62899; -.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0006414; P:translational elongation; TAS:Reactome.
DR GO; GO:0006413; P:translational initiation; TAS:Reactome.
DR GO; GO:0006415; P:translational termination; TAS:Reactome.
DR GO; GO:0019083; P:viral transcription; TAS:Reactome.
DR Gene3D; 3.10.440.10; -; 1.
DR InterPro; IPR000054; Ribosomal_L31e.
DR InterPro; IPR020052; Ribosomal_L31e_CS.
DR InterPro; IPR023621; Ribosomal_L31e_dom.
DR PANTHER; PTHR10956; PTHR10956; 1.
DR Pfam; PF01198; Ribosomal_L31e; 1.
DR ProDom; PD006030; 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; Complete proteome;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT CHAIN 1 125 60S ribosomal protein L31.
FT /FTId=PRO_0000153763.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 75 75 N6-acetyllysine.
FT MOD_RES 98 98 Phosphoserine.
FT VAR_SEQ 116 125 NLQTVNVDEN -> ISVLNSVTVAKSP (in isoform
FT 2).
FT /FTId=VSP_042572.
FT VAR_SEQ 116 125 NLQTVNVDEN -> SKFSIP (in isoform 3).
FT /FTId=VSP_043224.
SQ SEQUENCE 125 AA; 14463 MW; BA9DBE79B9E1C071 CRC64;
MAPAKKGGEK KKGRSAINEV VTREYTINIH KRIHGVGFKK RAPRALKEIR KFAMKEMGTP
DVRIDTRLNK AVWAKGIRNV PYRIRVRLSR KRNEDEDSPN KLYTLVTYVP VTTFKNLQTV
NVDEN
//