Full text data of RPL13A
RPL13A
[Confidence: low (only semi-automatic identification from reviews)]
60S ribosomal protein L13a (23 kDa highly basic protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
60S ribosomal protein L13a (23 kDa highly basic protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P40429
ID RL13A_HUMAN Reviewed; 203 AA.
AC P40429; A8K505;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 129.
DE RecName: Full=60S ribosomal protein L13a;
DE AltName: Full=23 kDa highly basic protein;
GN Name=RPL13A;
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].
RX PubMed=1282492; DOI=10.1016/S0888-7543(05)80117-X;
RA Price S.R., Nightingale M.S., Bobak D.A., Tsuchiya M., Moss J.,
RA Vaughan M.;
RT "Conservation of a 23-kDa human transplantation antigen in mammalian
RT species.";
RL Genomics 14:959-964(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10580157; DOI=10.1016/S0378-1119(99)00429-1;
RA Higa S., Yoshihama M., Tanaka T., Kenmochi N.;
RT "Gene organization and sequence of the region containing the ribosomal
RT protein genes RPL13A and RPS11 in the human genome and conserved
RT features in the mouse genome.";
RL Gene 240:371-377(1999).
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.,
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].
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, Lymph, Muscle, Pancreas, and Skin;
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 [6]
RP PROTEIN SEQUENCE OF 2-12; 38-49; 104-115 AND 135-159, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [7]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=14567916; DOI=10.1016/S0092-8674(03)00773-6;
RA Mazumder B., Sampath P., Seshadri V., Maitra R.K., DiCorleto P.E.,
RA Fox P.L.;
RT "Regulated release of L13a from the 60S ribosomal subunit as a
RT mechanism of transcript-specific translational control.";
RL Cell 115:187-198(2003).
RN [8]
RP MASS SPECTROMETRY, AND PROBABLE ACETYLATION AT ALA-2.
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.,
RA Karpova G.G.;
RT "Characterization and analysis of posttranslational modifications of
RT the human large cytoplasmic ribosomal subunit proteins by mass
RT spectrometry and Edman sequencing.";
RL J. Protein Chem. 22:249-258(2003).
RN [9]
RP IDENTIFICATION IN THE GAIT COMPLEX.
RX PubMed=15479637; DOI=10.1016/j.cell.2004.09.030;
RA Sampath P., Mazumder B., Seshadri V., Gerber C.A., Chavatte L.,
RA Kinter M., Ting S.M., Dignam J.D., Kim S., Driscoll D.M., Fox P.L.;
RT "Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-
RT specific silencing of translation.";
RL Cell 119:195-208(2004).
RN [10]
RP FUNCTION, AND INTERACTION WITH EIF4G1.
RX PubMed=17218275; DOI=10.1016/j.molcel.2006.11.028;
RA Kapasi P., Chaudhuri S., Vyas K., Baus D., Komar A.A., Fox P.L.,
RA Merrick W.C., Mazumder B.;
RT "L13a blocks 48S assembly: role of a general initiation factor in
RT mRNA-specific translational control.";
RL Mol. Cell 25:113-126(2007).
RN [11]
RP FUNCTION.
RX PubMed=17921318; DOI=10.1261/rna.694007;
RA Chaudhuri S., Vyas K., Kapasi P., Komar A.A., Dinman J.D., Barik S.,
RA Mazumder B.;
RT "Human ribosomal protein L13a is dispensable for canonical ribosome
RT function but indispensable for efficient rRNA methylation.";
RL RNA 13:2224-2237(2007).
RN [12]
RP PHOSPHORYLATION AT SER-77, AND MUTAGENESIS OF SER-77.
RX PubMed=18995835; DOI=10.1016/j.molcel.2008.09.019;
RA Mukhopadhyay R., Ray P.S., Arif A., Brady A.K., Kinter M., Fox P.L.;
RT "DAPK-ZIPK-L13a axis constitutes a negative-feedback module regulating
RT inflammatory gene expression.";
RL Mol. Cell 32:371-382(2008).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-191, 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 [15]
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 [16]
RP FUNCTION, AND RECONSTITUTION OF THE GAIT COMPLEX.
RX PubMed=23071094; DOI=10.1128/MCB.01168-12;
RA Arif A., Chatterjee P., Moodt R.A., Fox P.L.;
RT "Heterotrimeric GAIT complex drives transcript-selective translation
RT inhibition in murine macrophages.";
RL Mol. Cell. Biol. 32:5046-5055(2012).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, 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 [18]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.
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 -!- FUNCTION: Associated with ribosomes but is not required for
CC canonical ribosome function and has extra-ribosomal functions.
CC Component of the GAIT (gamma interferon-activated inhibitor of
CC translation) complex which mediates interferon-gamma-induced
CC transcript-selective translation inhibition in inflammation
CC processes. Upon interferon-gamma activation and subsequent
CC phosphorylation dissociates from the ribosome and assembles into
CC the GAIT complex which binds to stem loop-containing GAIT elements
CC in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin)
CC and suppresses their translation. In the GAIT complex interacts
CC with m7G cap-bound eIF4G at or near the eIF3-binding site and
CC blocks the recruitment of the 43S ribosomal complex. Involved in
CC methylation of rRNA.
CC -!- SUBUNIT: Component of the 60S ribosome. Component of the GAIT
CC complex. Interacts with EIF4G1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC -!- PTM: Phosphorylation at Ser-77 upon interferon-gamma treatment in
CC monocytes involves a DAPK1-DAPK3 kinase cascade and is causing
CC release from the ribosome, association with the GAIT complex and
CC subsequent involvement in transcript-selective translation
CC inhibition.
CC -!- SIMILARITY: Belongs to the ribosomal protein L13P family.
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DR EMBL; X56932; CAA40254.1; -; mRNA.
DR EMBL; AB028893; BAA88214.1; -; Genomic_DNA.
DR EMBL; AK291120; BAF83809.1; -; mRNA.
DR EMBL; CH471177; EAW52495.1; -; Genomic_DNA.
DR EMBL; BC000514; AAH00514.1; -; mRNA.
DR EMBL; BC001675; AAH01675.1; -; mRNA.
DR EMBL; BC001836; AAH01836.1; -; mRNA.
DR EMBL; BC062537; AAH62537.1; -; mRNA.
DR EMBL; BC065236; AAH65236.1; -; mRNA.
DR EMBL; BC070223; AAH70223.1; -; mRNA.
DR EMBL; BC071929; AAH71929.1; -; mRNA.
DR PIR; S29539; S29539.
DR RefSeq; NP_001257420.1; NM_001270491.1.
DR RefSeq; NP_036555.1; NM_012423.3.
DR UniGene; Hs.523185; -.
DR PDB; 3J3B; EM; 5.00 A; O=1-203.
DR PDBsum; 3J3B; -.
DR ProteinModelPortal; P40429; -.
DR SMR; P40429; 2-203.
DR IntAct; P40429; 24.
DR MINT; MINT-1417412; -.
DR STRING; 9606.ENSP00000375730; -.
DR PhosphoSite; P40429; -.
DR DMDM; 730451; -.
DR PaxDb; P40429; -.
DR PRIDE; P40429; -.
DR DNASU; 23521; -.
DR Ensembl; ENST00000391857; ENSP00000375730; ENSG00000142541.
DR GeneID; 23521; -.
DR KEGG; hsa:23521; -.
DR UCSC; uc002pny.4; human.
DR CTD; 23521; -.
DR GeneCards; GC19P049991; -.
DR H-InvDB; HIX0027968; -.
DR H-InvDB; HIX0158081; -.
DR HGNC; HGNC:10304; RPL13A.
DR HPA; HPA038751; -.
DR neXtProt; NX_P40429; -.
DR PharmGKB; PA38122; -.
DR eggNOG; COG0102; -.
DR HOGENOM; HOG000225289; -.
DR HOVERGEN; HBG062176; -.
DR InParanoid; P40429; -.
DR KO; K02872; -.
DR OrthoDB; EOG7H1JMP; -.
DR PhylomeDB; P40429; -.
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; RPL13A; human.
DR GeneWiki; RPL13A; -.
DR GenomeRNAi; 23521; -.
DR NextBio; 45973; -.
DR PRO; PR:P40429; -.
DR ArrayExpress; P40429; -.
DR Bgee; P40429; -.
DR CleanEx; HS_RPL13A; -.
DR Genevestigator; P40429; -.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0097452; C:GAIT complex; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:UniProtKB.
DR GO; GO:1901194; P:negative regulation of formation of translation preinitiation complex; IDA:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IDA: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; 3.90.1180.10; -; 1.
DR HAMAP; MF_01366; Ribosomal_L13; 1; -.
DR InterPro; IPR005822; Ribosomal_L13.
DR InterPro; IPR023563; Ribosomal_L13_CS.
DR InterPro; IPR023564; Ribosomal_L13_dom.
DR InterPro; IPR005755; Ribosomal_L13_euk/arc.
DR PANTHER; PTHR11545; PTHR11545; 1.
DR PANTHER; PTHR11545:SF3; PTHR11545:SF3; 1.
DR Pfam; PF00572; Ribosomal_L13; 1.
DR SUPFAM; SSF52161; SSF52161; 1.
DR TIGRFAMs; TIGR01077; L13_A_E; 1.
DR PROSITE; PS00783; RIBOSOMAL_L13; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Translation regulation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 203 60S ribosomal protein L13a.
FT /FTId=PRO_0000133769.
FT MOD_RES 2 2 N-acetylalanine; partial.
FT MOD_RES 77 77 Phosphoserine; by ZIPK/DAPK3.
FT MOD_RES 191 191 N6-acetyllysine.
FT MUTAGEN 77 77 S->A: Loss of interferon-gamma induced
FT phosphorylation.
SQ SEQUENCE 203 AA; 23577 MW; 3E80D0AB77A0D406 CRC64;
MAEVQVLVLD GRGHLLGRLA AIVAKQVLLG RKVVVVRCEG INISGNFYRN KLKYLAFLRK
RMNTNPSRGP YHFRAPSRIF WRTVRGMLPH KTKRGQAALD RLKVFDGIPP PYDKKKRMVV
PAALKVVRLK PTRKFAYLGR LAHEVGWKYQ AVTATLEEKR KEKAKIHYRK KKQLMRLRKQ
AEKNVEKKID KYTEVLKTHG LLV
//
ID RL13A_HUMAN Reviewed; 203 AA.
AC P40429; A8K505;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 129.
DE RecName: Full=60S ribosomal protein L13a;
DE AltName: Full=23 kDa highly basic protein;
GN Name=RPL13A;
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].
RX PubMed=1282492; DOI=10.1016/S0888-7543(05)80117-X;
RA Price S.R., Nightingale M.S., Bobak D.A., Tsuchiya M., Moss J.,
RA Vaughan M.;
RT "Conservation of a 23-kDa human transplantation antigen in mammalian
RT species.";
RL Genomics 14:959-964(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10580157; DOI=10.1016/S0378-1119(99)00429-1;
RA Higa S., Yoshihama M., Tanaka T., Kenmochi N.;
RT "Gene organization and sequence of the region containing the ribosomal
RT protein genes RPL13A and RPS11 in the human genome and conserved
RT features in the mouse genome.";
RL Gene 240:371-377(1999).
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.,
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].
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, Lymph, Muscle, Pancreas, and Skin;
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 [6]
RP PROTEIN SEQUENCE OF 2-12; 38-49; 104-115 AND 135-159, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [7]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=14567916; DOI=10.1016/S0092-8674(03)00773-6;
RA Mazumder B., Sampath P., Seshadri V., Maitra R.K., DiCorleto P.E.,
RA Fox P.L.;
RT "Regulated release of L13a from the 60S ribosomal subunit as a
RT mechanism of transcript-specific translational control.";
RL Cell 115:187-198(2003).
RN [8]
RP MASS SPECTROMETRY, AND PROBABLE ACETYLATION AT ALA-2.
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.,
RA Karpova G.G.;
RT "Characterization and analysis of posttranslational modifications of
RT the human large cytoplasmic ribosomal subunit proteins by mass
RT spectrometry and Edman sequencing.";
RL J. Protein Chem. 22:249-258(2003).
RN [9]
RP IDENTIFICATION IN THE GAIT COMPLEX.
RX PubMed=15479637; DOI=10.1016/j.cell.2004.09.030;
RA Sampath P., Mazumder B., Seshadri V., Gerber C.A., Chavatte L.,
RA Kinter M., Ting S.M., Dignam J.D., Kim S., Driscoll D.M., Fox P.L.;
RT "Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-
RT specific silencing of translation.";
RL Cell 119:195-208(2004).
RN [10]
RP FUNCTION, AND INTERACTION WITH EIF4G1.
RX PubMed=17218275; DOI=10.1016/j.molcel.2006.11.028;
RA Kapasi P., Chaudhuri S., Vyas K., Baus D., Komar A.A., Fox P.L.,
RA Merrick W.C., Mazumder B.;
RT "L13a blocks 48S assembly: role of a general initiation factor in
RT mRNA-specific translational control.";
RL Mol. Cell 25:113-126(2007).
RN [11]
RP FUNCTION.
RX PubMed=17921318; DOI=10.1261/rna.694007;
RA Chaudhuri S., Vyas K., Kapasi P., Komar A.A., Dinman J.D., Barik S.,
RA Mazumder B.;
RT "Human ribosomal protein L13a is dispensable for canonical ribosome
RT function but indispensable for efficient rRNA methylation.";
RL RNA 13:2224-2237(2007).
RN [12]
RP PHOSPHORYLATION AT SER-77, AND MUTAGENESIS OF SER-77.
RX PubMed=18995835; DOI=10.1016/j.molcel.2008.09.019;
RA Mukhopadhyay R., Ray P.S., Arif A., Brady A.K., Kinter M., Fox P.L.;
RT "DAPK-ZIPK-L13a axis constitutes a negative-feedback module regulating
RT inflammatory gene expression.";
RL Mol. Cell 32:371-382(2008).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-191, 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 [15]
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 [16]
RP FUNCTION, AND RECONSTITUTION OF THE GAIT COMPLEX.
RX PubMed=23071094; DOI=10.1128/MCB.01168-12;
RA Arif A., Chatterjee P., Moodt R.A., Fox P.L.;
RT "Heterotrimeric GAIT complex drives transcript-selective translation
RT inhibition in murine macrophages.";
RL Mol. Cell. Biol. 32:5046-5055(2012).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, 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 [18]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.
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 -!- FUNCTION: Associated with ribosomes but is not required for
CC canonical ribosome function and has extra-ribosomal functions.
CC Component of the GAIT (gamma interferon-activated inhibitor of
CC translation) complex which mediates interferon-gamma-induced
CC transcript-selective translation inhibition in inflammation
CC processes. Upon interferon-gamma activation and subsequent
CC phosphorylation dissociates from the ribosome and assembles into
CC the GAIT complex which binds to stem loop-containing GAIT elements
CC in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin)
CC and suppresses their translation. In the GAIT complex interacts
CC with m7G cap-bound eIF4G at or near the eIF3-binding site and
CC blocks the recruitment of the 43S ribosomal complex. Involved in
CC methylation of rRNA.
CC -!- SUBUNIT: Component of the 60S ribosome. Component of the GAIT
CC complex. Interacts with EIF4G1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC -!- PTM: Phosphorylation at Ser-77 upon interferon-gamma treatment in
CC monocytes involves a DAPK1-DAPK3 kinase cascade and is causing
CC release from the ribosome, association with the GAIT complex and
CC subsequent involvement in transcript-selective translation
CC inhibition.
CC -!- SIMILARITY: Belongs to the ribosomal protein L13P family.
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DR EMBL; X56932; CAA40254.1; -; mRNA.
DR EMBL; AB028893; BAA88214.1; -; Genomic_DNA.
DR EMBL; AK291120; BAF83809.1; -; mRNA.
DR EMBL; CH471177; EAW52495.1; -; Genomic_DNA.
DR EMBL; BC000514; AAH00514.1; -; mRNA.
DR EMBL; BC001675; AAH01675.1; -; mRNA.
DR EMBL; BC001836; AAH01836.1; -; mRNA.
DR EMBL; BC062537; AAH62537.1; -; mRNA.
DR EMBL; BC065236; AAH65236.1; -; mRNA.
DR EMBL; BC070223; AAH70223.1; -; mRNA.
DR EMBL; BC071929; AAH71929.1; -; mRNA.
DR PIR; S29539; S29539.
DR RefSeq; NP_001257420.1; NM_001270491.1.
DR RefSeq; NP_036555.1; NM_012423.3.
DR UniGene; Hs.523185; -.
DR PDB; 3J3B; EM; 5.00 A; O=1-203.
DR PDBsum; 3J3B; -.
DR ProteinModelPortal; P40429; -.
DR SMR; P40429; 2-203.
DR IntAct; P40429; 24.
DR MINT; MINT-1417412; -.
DR STRING; 9606.ENSP00000375730; -.
DR PhosphoSite; P40429; -.
DR DMDM; 730451; -.
DR PaxDb; P40429; -.
DR PRIDE; P40429; -.
DR DNASU; 23521; -.
DR Ensembl; ENST00000391857; ENSP00000375730; ENSG00000142541.
DR GeneID; 23521; -.
DR KEGG; hsa:23521; -.
DR UCSC; uc002pny.4; human.
DR CTD; 23521; -.
DR GeneCards; GC19P049991; -.
DR H-InvDB; HIX0027968; -.
DR H-InvDB; HIX0158081; -.
DR HGNC; HGNC:10304; RPL13A.
DR HPA; HPA038751; -.
DR neXtProt; NX_P40429; -.
DR PharmGKB; PA38122; -.
DR eggNOG; COG0102; -.
DR HOGENOM; HOG000225289; -.
DR HOVERGEN; HBG062176; -.
DR InParanoid; P40429; -.
DR KO; K02872; -.
DR OrthoDB; EOG7H1JMP; -.
DR PhylomeDB; P40429; -.
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; RPL13A; human.
DR GeneWiki; RPL13A; -.
DR GenomeRNAi; 23521; -.
DR NextBio; 45973; -.
DR PRO; PR:P40429; -.
DR ArrayExpress; P40429; -.
DR Bgee; P40429; -.
DR CleanEx; HS_RPL13A; -.
DR Genevestigator; P40429; -.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0097452; C:GAIT complex; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:UniProtKB.
DR GO; GO:1901194; P:negative regulation of formation of translation preinitiation complex; IDA:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IDA: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; 3.90.1180.10; -; 1.
DR HAMAP; MF_01366; Ribosomal_L13; 1; -.
DR InterPro; IPR005822; Ribosomal_L13.
DR InterPro; IPR023563; Ribosomal_L13_CS.
DR InterPro; IPR023564; Ribosomal_L13_dom.
DR InterPro; IPR005755; Ribosomal_L13_euk/arc.
DR PANTHER; PTHR11545; PTHR11545; 1.
DR PANTHER; PTHR11545:SF3; PTHR11545:SF3; 1.
DR Pfam; PF00572; Ribosomal_L13; 1.
DR SUPFAM; SSF52161; SSF52161; 1.
DR TIGRFAMs; TIGR01077; L13_A_E; 1.
DR PROSITE; PS00783; RIBOSOMAL_L13; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Translation regulation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 203 60S ribosomal protein L13a.
FT /FTId=PRO_0000133769.
FT MOD_RES 2 2 N-acetylalanine; partial.
FT MOD_RES 77 77 Phosphoserine; by ZIPK/DAPK3.
FT MOD_RES 191 191 N6-acetyllysine.
FT MUTAGEN 77 77 S->A: Loss of interferon-gamma induced
FT phosphorylation.
SQ SEQUENCE 203 AA; 23577 MW; 3E80D0AB77A0D406 CRC64;
MAEVQVLVLD GRGHLLGRLA AIVAKQVLLG RKVVVVRCEG INISGNFYRN KLKYLAFLRK
RMNTNPSRGP YHFRAPSRIF WRTVRGMLPH KTKRGQAALD RLKVFDGIPP PYDKKKRMVV
PAALKVVRLK PTRKFAYLGR LAHEVGWKYQ AVTATLEEKR KEKAKIHYRK KKQLMRLRKQ
AEKNVEKKID KYTEVLKTHG LLV
//