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60S ribosomal protein L13a (23 kDa highly basic protein) (Large ribosomal subunit protein uL13)

 RL13A_HUMAN             Reviewed;         203 AA.
P40429; A8K505;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
20-JUN-2018, entry version 176.
RecName: Full=60S ribosomal protein L13a;
AltName: Full=23 kDa highly basic protein;
AltName: Full=Large ribosomal subunit protein uL13 {ECO:0000303|PubMed:24524803};
Name=RPL13A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1282492; DOI=10.1016/S0888-7543(05)80117-X;
Price S.R., Nightingale M.S., Bobak D.A., Tsuchiya M., Moss J.,
Vaughan M.;
"Conservation of a 23-kDa human transplantation antigen in mammalian
species.";
Genomics 14:959-964(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10580157; DOI=10.1016/S0378-1119(99)00429-1;
Higa S., Yoshihama M., Tanaka T., Kenmochi N.;
"Gene organization and sequence of the region containing the ribosomal
protein genes RPL13A and RPS11 in the human genome and conserved
features in the mouse genome.";
Gene 240:371-377(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, Lymph, Muscle, Pancreas, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 2-12; 38-49; 104-115 AND 135-159, CLEAVAGE OF
INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Cervix carcinoma;
Bienvenut W.V., Waridel P., Quadroni M.;
Submitted (MAR-2009) to UniProtKB.
[7]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=14567916; DOI=10.1016/S0092-8674(03)00773-6;
Mazumder B., Sampath P., Seshadri V., Maitra R.K., DiCorleto P.E.,
Fox P.L.;
"Regulated release of L13a from the 60S ribosomal subunit as a
mechanism of transcript-specific translational control.";
Cell 115:187-198(2003).
[8]
ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY, AND
SUBUNIT.
PubMed=12962325; DOI=10.1023/A:1025068419698;
Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R.,
Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B.,
Karpova G.G.;
"Characterization and analysis of posttranslational modifications of
the human large cytoplasmic ribosomal subunit proteins by mass
spectrometry and Edman sequencing.";
J. Protein Chem. 22:249-258(2003).
[9]
IDENTIFICATION IN THE GAIT COMPLEX.
PubMed=15479637; DOI=10.1016/j.cell.2004.09.030;
Sampath P., Mazumder B., Seshadri V., Gerber C.A., Chavatte L.,
Kinter M., Ting S.M., Dignam J.D., Kim S., Driscoll D.M., Fox P.L.;
"Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-
specific silencing of translation.";
Cell 119:195-208(2004).
[10]
FUNCTION, AND INTERACTION WITH EIF4G1.
PubMed=17218275; DOI=10.1016/j.molcel.2006.11.028;
Kapasi P., Chaudhuri S., Vyas K., Baus D., Komar A.A., Fox P.L.,
Merrick W.C., Mazumder B.;
"L13a blocks 48S assembly: role of a general initiation factor in
mRNA-specific translational control.";
Mol. Cell 25:113-126(2007).
[11]
FUNCTION.
PubMed=17921318; DOI=10.1261/rna.694007;
Chaudhuri S., Vyas K., Kapasi P., Komar A.A., Dinman J.D., Barik S.,
Mazumder B.;
"Human ribosomal protein L13a is dispensable for canonical ribosome
function but indispensable for efficient rRNA methylation.";
RNA 13:2224-2237(2007).
[12]
PHOSPHORYLATION AT SER-77, AND MUTAGENESIS OF SER-77.
PubMed=18995835; DOI=10.1016/j.molcel.2008.09.019;
Mukhopadhyay R., Ray P.S., Arif A., Brady A.K., Kinter M., Fox P.L.;
"DAPK-ZIPK-L13a axis constitutes a negative-feedback module regulating
inflammatory gene expression.";
Mol. Cell 32:371-382(2008).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-191, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
FUNCTION, AND RECONSTITUTION OF THE GAIT COMPLEX.
PubMed=23071094; DOI=10.1128/MCB.01168-12;
Arif A., Chatterjee P., Moodt R.A., Fox P.L.;
"Heterotrimeric GAIT complex drives transcript-selective translation
inhibition in murine macrophages.";
Mol. Cell. Biol. 32:5046-5055(2012).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[19]
NOMENCLATURE.
PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
Williamson J.R., Wilson D., Yonath A., Yusupov M.;
"A new system for naming ribosomal proteins.";
Curr. Opin. Struct. Biol. 24:165-169(2014).
[20]
ACETYLATION AT ALA-2, AND CLEAVAGE OF INITIATOR METHIONINE.
PubMed=25489052; DOI=10.1093/hmg/ddu611;
Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A.,
Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H.,
Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K.,
Arnesen T.;
"Biochemical and cellular analysis of Ogden syndrome reveals
downstream Nt-acetylation defects.";
Hum. Mol. Genet. 24:1956-1976(2015).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[22]
STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.
PubMed=23636399; DOI=10.1038/nature12104;
Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
Wilson D.N., Beckmann R.;
"Structures of the human and Drosophila 80S ribosome.";
Nature 497:80-85(2013).
-!- FUNCTION: Associated with ribosomes but is not required for
canonical ribosome function and has extra-ribosomal functions.
Component of the GAIT (gamma interferon-activated inhibitor of
translation) complex which mediates interferon-gamma-induced
transcript-selective translation inhibition in inflammation
processes. Upon interferon-gamma activation and subsequent
phosphorylation dissociates from the ribosome and assembles into
the GAIT complex which binds to stem loop-containing GAIT elements
in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin)
and suppresses their translation. In the GAIT complex interacts
with m7G cap-bound eIF4G at or near the eIF3-binding site and
blocks the recruitment of the 43S ribosomal complex. Involved in
methylation of rRNA. {ECO:0000269|PubMed:14567916,
ECO:0000269|PubMed:17218275, ECO:0000269|PubMed:17921318,
ECO:0000269|PubMed:23071094}.
-!- SUBUNIT: Component of the 60S ribosome. Component of the GAIT
complex. Interacts with EIF4G1. {ECO:0000269|PubMed:14567916,
ECO:0000269|PubMed:15479637, ECO:0000269|PubMed:17218275,
ECO:0000305|PubMed:12962325}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:14567916}.
-!- PTM: Phosphorylation at Ser-77 upon interferon-gamma treatment in
monocytes involves a DAPK1-DAPK3 kinase cascade and is causing
release from the ribosome, association with the GAIT complex and
subsequent involvement in transcript-selective translation
inhibition. {ECO:0000269|PubMed:14567916,
ECO:0000269|PubMed:18995835}.
-!- PTM: Citrullinated by PADI4. {ECO:0000250}.
-!- SIMILARITY: Belongs to the universal ribosomal protein uL13
family. {ECO:0000305}.
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EMBL; X56932; CAA40254.1; -; mRNA.
EMBL; AB028893; BAA88214.1; -; Genomic_DNA.
EMBL; AK291120; BAF83809.1; -; mRNA.
EMBL; CH471177; EAW52495.1; -; Genomic_DNA.
EMBL; BC000514; AAH00514.1; -; mRNA.
EMBL; BC001675; AAH01675.1; -; mRNA.
EMBL; BC001836; AAH01836.1; -; mRNA.
EMBL; BC062537; AAH62537.1; -; mRNA.
EMBL; BC065236; AAH65236.1; -; mRNA.
EMBL; BC070223; AAH70223.1; -; mRNA.
EMBL; BC071929; AAH71929.1; -; mRNA.
CCDS; CCDS12768.1; -.
PIR; S29539; S29539.
RefSeq; NP_001257420.1; NM_001270491.1.
RefSeq; NP_036555.1; NM_012423.3.
UniGene; Hs.523185; -.
PDB; 4UG0; EM; -; LO=1-203.
PDB; 4V6X; EM; 5.00 A; CO=1-203.
PDB; 5AJ0; EM; 3.50 A; AO=1-203.
PDB; 5LKS; EM; 3.60 A; LO=1-203.
PDB; 5T2C; EM; 3.60 A; I=1-203.
PDB; 6EK0; EM; 2.90 A; LO=1-203.
PDBsum; 4UG0; -.
PDBsum; 4V6X; -.
PDBsum; 5AJ0; -.
PDBsum; 5LKS; -.
PDBsum; 5T2C; -.
PDBsum; 6EK0; -.
ProteinModelPortal; P40429; -.
SMR; P40429; -.
BioGrid; 117068; 142.
CORUM; P40429; -.
IntAct; P40429; 51.
MINT; P40429; -.
STRING; 9606.ENSP00000375730; -.
DrugBank; DB02494; Alpha-Hydroxy-Beta-Phenyl-Propionic Acid.
DrugBank; DB07374; Anisomycin.
DrugBank; DB08437; Puromycin.
MoonProt; P40429; -.
iPTMnet; P40429; -.
PhosphoSitePlus; P40429; -.
SwissPalm; P40429; -.
BioMuta; RPL13A; -.
DMDM; 730451; -.
EPD; P40429; -.
MaxQB; P40429; -.
PaxDb; P40429; -.
PeptideAtlas; P40429; -.
PRIDE; P40429; -.
ProteomicsDB; 55374; -.
TopDownProteomics; P40429; -.
DNASU; 23521; -.
Ensembl; ENST00000391857; ENSP00000375730; ENSG00000142541.
GeneID; 23521; -.
KEGG; hsa:23521; -.
UCSC; uc002pny.5; human.
CTD; 23521; -.
DisGeNET; 23521; -.
EuPathDB; HostDB:ENSG00000142541.16; -.
GeneCards; RPL13A; -.
H-InvDB; HIX0027968; -.
H-InvDB; HIX0158081; -.
HGNC; HGNC:10304; RPL13A.
HPA; HPA038751; -.
neXtProt; NX_P40429; -.
OpenTargets; ENSG00000142541; -.
PharmGKB; PA38122; -.
eggNOG; KOG3204; Eukaryota.
eggNOG; COG0102; LUCA.
GeneTree; ENSGT00390000010799; -.
HOGENOM; HOG000225289; -.
HOVERGEN; HBG062176; -.
InParanoid; P40429; -.
KO; K02872; -.
PhylomeDB; P40429; -.
TreeFam; TF300159; -.
Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-HSA-156902; Peptide chain elongation.
Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
Reactome; R-HSA-192823; Viral mRNA Translation.
Reactome; R-HSA-2408557; Selenocysteine synthesis.
Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
Reactome; R-HSA-72764; Eukaryotic Translation Termination.
Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
SIGNOR; P40429; -.
ChiTaRS; RPL13A; human.
GeneWiki; RPL13A; -.
GenomeRNAi; 23521; -.
PRO; PR:P40429; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000142541; -.
CleanEx; HS_RPL13A; -.
ExpressionAtlas; P40429; baseline and differential.
Genevisible; P40429; HS.
GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0022625; C:cytosolic large ribosomal subunit; HDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0097452; C:GAIT complex; IDA:UniProtKB.
GO; GO:0015934; C:large ribosomal subunit; TAS:ProtInc.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005730; C:nucleolus; HDA:UniProtKB.
GO; GO:0005634; C:nucleus; HDA:UniProtKB.
GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
GO; GO:0071346; P:cellular response to interferon-gamma; IDA:UniProtKB.
GO; GO:1901194; P:negative regulation of formation of translation preinitiation complex; IDA:UniProtKB.
GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
GO; GO:0006412; P:translation; NAS:UniProtKB.
GO; GO:0006413; P:translational initiation; TAS:Reactome.
CDD; cd00392; Ribosomal_L13; 1.
Gene3D; 3.90.1180.10; -; 1.
HAMAP; MF_01366; Ribosomal_L13; 1.
InterPro; IPR005822; Ribosomal_L13.
InterPro; IPR023563; Ribosomal_L13_CS.
InterPro; IPR005755; Ribosomal_L13_euk/arc.
InterPro; IPR036899; Ribosomal_L13_sf.
PANTHER; PTHR11545; PTHR11545; 1.
PANTHER; PTHR11545:SF3; PTHR11545:SF3; 1.
Pfam; PF00572; Ribosomal_L13; 1.
PIRSF; PIRSF002181; Ribosomal_L13; 1.
SUPFAM; SSF52161; SSF52161; 1.
TIGRFAMs; TIGR01077; L13_A_E; 1.
PROSITE; PS00783; RIBOSOMAL_L13; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Citrullination; Complete proteome;
Cytoplasm; Direct protein sequencing; Phosphoprotein;
Reference proteome; Ribonucleoprotein; Ribosomal protein;
Translation regulation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:12962325,
ECO:0000269|PubMed:25489052,
ECO:0000269|Ref.6}.
CHAIN 2 203 60S ribosomal protein L13a.
/FTId=PRO_0000133769.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:12962325,
ECO:0000269|PubMed:25489052,
ECO:0000269|Ref.6}.
MOD_RES 59 59 Citrulline. {ECO:0000250}.
MOD_RES 77 77 Phosphoserine; by ZIPK/DAPK3.
{ECO:0000269|PubMed:18995835}.
MOD_RES 140 140 Citrulline. {ECO:0000250}.
MOD_RES 191 191 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MUTAGEN 77 77 S->A: Loss of interferon-gamma induced
phosphorylation.
{ECO:0000269|PubMed:18995835}.
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


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30-186 Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. MRPS12 is the 28S subunit protein that belongs to the ribosomal protein S12P family. The protein is a ke 0.05 mg
EIAAB35293 39S ribosomal protein L27 homolog,39S ribosomal protein L41, mitochondrial,Bcl-2-interacting mitochondrial ribosomal protein L41,BMRP,Cell proliferation-inducing gene 3 protein,Homo sapiens,Human,L41m
GTX102228 ribosomal protein L13a 100 µl
29-214 RPL9 is a ribosomal protein that is a component of the 60S subunit. RPL9 belongs to the L6P family of ribosomal proteins. It is located in the cytoplasm. As is typical for genes encoding ribosomal pro 0.1 mg
29-215 RPL9 is a ribosomal protein that is a component of the 60S subunit. RPL9 belongs to the L6P family of ribosomal proteins. It is located in the cytoplasm. As is typical for genes encoding ribosomal pro 0.1 mg
CSB-EL020130DO Dog 60S ribosomal protein L13a(RPL13A) ELISA kit 96T
201-20-4976 RPL13A{ribosomal protein L13a}rabbit.pAb 0.2ml
E1637h Bovine ELISA Kit FOR 60S ribosomal protein L13a 96T
CSB-EL020130RA Rat 60S ribosomal protein L13a(RPL13A) ELISA kit 96T
E6097h Human Ribosomal Protein L13A ELISA Kit 96T
EIAAB34939 60S ribosomal protein L13a,Pig,RPL13A,Sus scrofa
EIAAB36455 Mouse,Mus musculus,Ribosomal large subunit pseudouridine synthase C-like protein,Rlucl,RNA pseudouridylate synthase domain-containing protein 1,Rpusd1
EIAAB35298 28S ribosomal protein S32, mitochondrial,39S ribosomal protein L31, mitochondrial,39S ribosomal protein L42, mitochondrial,Homo sapiens,HSPC204,Human,L31mt,L42mt,MRPL31,MRP-L31,MRPL42,MRP-L42,MRPS32,M
CSB-EL020130HU Human 60S ribosomal protein L13a(RPL13A) ELISA kit 96T
EIAAB34937 60S ribosomal protein L13a,Rat,Rattus norvegicus,Rpl13a
G7956 Ribosomal Protein L13A (RPL13A) , Human, ELISA Kit 96T
CSB-EL020130DO Dog 60S ribosomal protein L13a(RPL13A) ELISA kit SpeciesDog 96T
CSB-EL020130PI Pig 60S ribosomal protein L13a(RPL13A) ELISA kit SpeciesPig 96T
EIAAB34938 60S ribosomal protein L13a,Bos taurus,Bovine,RPL13A
CSB-EL020130BO Bovine 60S ribosomal protein L13a(RPL13A) ELISA kit 96T
CSB-EL020130RA Rat 60S ribosomal protein L13a(RPL13A) ELISA kit SpeciesRat 96T
CSB-EL020130MO Mouse 60S ribosomal protein L13a(RPL13A) ELISA kit 96T
29-216 RPL6 is a ribosomal protein that is a component of the 60S subunit. RPL6 belongs to the L6E family of ribosomal proteins. It is located in the cytoplasm. The protein can bind specifically to domain C 0.1 mg
EIAAB36454 C16orf40,Homo sapiens,Human,Ribosomal large subunit pseudouridine synthase C-like protein,RLUCL,RNA pseudouridylate synthase domain-containing protein 1,RPUSD1


 

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