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P40429 (RL13A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
60S ribosomal protein L13a
Alternative name(s):
23 kDa highly basic protein
Gene names
Name:RPL13A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length203 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.7 Ref.10 Ref.11 Ref.16

Subunit structure

Component of the 60S ribosome. Component of the GAIT complex. Interacts with EIF4G1. Ref.7 Ref.9 Ref.10

Subcellular location

Cytoplasm Probable Ref.7.

Post-translational modification

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. HAMAP-Rule MF_01366

Citrullinated by PADI4 By similarity. HAMAP-Rule MF_01366

Sequence similarities

Belongs to the ribosomal protein L13P family.

Ontologies

Keywords
   Biological processTranslation regulation
   Cellular componentCytoplasm
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMAcetylation
Citrullination
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

SRP-dependent cotranslational protein targeting to membrane

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

cellular response to interferon-gamma

Inferred from direct assay Ref.9. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

negative regulation of formation of translation preinitiation complex

Inferred from direct assay Ref.10. Source: UniProtKB

negative regulation of translation

Inferred from direct assay Ref.7Ref.16. Source: UniProtKB

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Traceable author statement. Source: Reactome

translation

Non-traceable author statement Ref.8. Source: UniProtKB

translational elongation

Traceable author statement. Source: Reactome

translational initiation

Traceable author statement. Source: Reactome

translational termination

Traceable author statement. Source: Reactome

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

viral transcription

Traceable author statement. Source: Reactome

   Cellular_componentGAIT complex

Inferred from direct assay Ref.9Ref.16. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

cytosolic large ribosomal subunit

Inferred from direct assay Ref.8. Source: UniProtKB

large ribosomal subunit

Traceable author statement Ref.2. Source: ProtInc

ribonucleoprotein complex

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

structural constituent of ribosome

Non-traceable author statement Ref.8. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 20320260S ribosomal protein L13a HAMAP-Rule MF_01366
PRO_0000133769

Amino acid modifications

Modified residue21N-acetylalanine Ref.6 Ref.8 Ref.13 Ref.17 Ref.18
Modified residue591Citrulline By similarity
Modified residue771Phosphoserine; by ZIPK/DAPK3 Ref.12
Modified residue1401Citrulline By similarity
Modified residue1911N6-acetyllysine Ref.14

Experimental info

Mutagenesis771S → A: Loss of interferon-gamma induced phosphorylation. Ref.12

Sequences

Sequence LengthMass (Da)Tools
P40429 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 3E80D0AB77A0D406

FASTA20323,577
        10         20         30         40         50         60 
MAEVQVLVLD GRGHLLGRLA AIVAKQVLLG RKVVVVRCEG INISGNFYRN KLKYLAFLRK 

        70         80         90        100        110        120 
RMNTNPSRGP YHFRAPSRIF WRTVRGMLPH KTKRGQAALD RLKVFDGIPP PYDKKKRMVV 

       130        140        150        160        170        180 
PAALKVVRLK PTRKFAYLGR LAHEVGWKYQ AVTATLEEKR KEKAKIHYRK KKQLMRLRKQ 

       190        200 
AEKNVEKKID KYTEVLKTHG LLV 

« Hide

References

« Hide 'large scale' references
[1]"Conservation of a 23-kDa human transplantation antigen in mammalian species."
Price S.R., Nightingale M.S., Bobak D.A., Tsuchiya M., Moss J., Vaughan M.
Genomics 14:959-964(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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."
Higa S., Yoshihama M., Tanaka T., Kenmochi N.
Gene 240:371-377(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung, Lymph, Muscle, Pancreas and Skin.
[6]Bienvenut W.V., Waridel P., Quadroni M.
Submitted (MAR-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-12; 38-49; 104-115 AND 135-159, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[7]"Regulated release of L13a from the 60S ribosomal subunit as a mechanism of transcript-specific translational control."
Mazumder B., Sampath P., Seshadri V., Maitra R.K., DiCorleto P.E., Fox P.L.
Cell 115:187-198(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, PHOSPHORYLATION.
[8]"Characterization and analysis of posttranslational modifications of the human large cytoplasmic ribosomal subunit proteins by mass spectrometry and Edman sequencing."
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.
J. Protein Chem. 22:249-258(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
[9]"Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-specific silencing of translation."
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.
Cell 119:195-208(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE GAIT COMPLEX.
[10]"L13a blocks 48S assembly: role of a general initiation factor in mRNA-specific translational control."
Kapasi P., Chaudhuri S., Vyas K., Baus D., Komar A.A., Fox P.L., Merrick W.C., Mazumder B.
Mol. Cell 25:113-126(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EIF4G1.
[11]"Human ribosomal protein L13a is dispensable for canonical ribosome function but indispensable for efficient rRNA methylation."
Chaudhuri S., Vyas K., Kapasi P., Komar A.A., Dinman J.D., Barik S., Mazumder B.
RNA 13:2224-2237(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"DAPK-ZIPK-L13a axis constitutes a negative-feedback module regulating inflammatory gene expression."
Mukhopadhyay R., Ray P.S., Arif A., Brady A.K., Kinter M., Fox P.L.
Mol. Cell 32:371-382(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-77, MUTAGENESIS OF SER-77.
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-191, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Heterotrimeric GAIT complex drives transcript-selective translation inhibition in murine macrophages."
Arif A., Chatterjee P., Moodt R.A., Fox P.L.
Mol. Cell. Biol. 32:5046-5055(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, RECONSTITUTION OF THE GAIT COMPLEX.
[17]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Structures of the human and Drosophila 80S ribosome."
Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M., Wilson D.N., Beckmann R.
Nature 497:80-85(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56932 mRNA. Translation: CAA40254.1.
AB028893 Genomic DNA. Translation: BAA88214.1.
AK291120 mRNA. Translation: BAF83809.1.
CH471177 Genomic DNA. Translation: EAW52495.1.
BC000514 mRNA. Translation: AAH00514.1.
BC001675 mRNA. Translation: AAH01675.1.
BC001836 mRNA. Translation: AAH01836.1.
BC062537 mRNA. Translation: AAH62537.1.
BC065236 mRNA. Translation: AAH65236.1.
BC070223 mRNA. Translation: AAH70223.1.
BC071929 mRNA. Translation: AAH71929.1.
PIRS29539.
RefSeqNP_001257420.1. NM_001270491.1.
NP_036555.1. NM_012423.3.
UniGeneHs.523185.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Belectron microscopy5.00O1-203[»]
ProteinModelPortalP40429.
SMRP40429. Positions 2-203.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117068. 35 interactions.
IntActP40429. 24 interactions.
MINTMINT-1417412.
STRING9606.ENSP00000375730.

PTM databases

PhosphoSiteP40429.

Polymorphism databases

DMDM730451.

Proteomic databases

PaxDbP40429.
PRIDEP40429.

Protocols and materials databases

DNASU23521.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000391857; ENSP00000375730; ENSG00000142541.
GeneID23521.
KEGGhsa:23521.
UCSCuc002pny.4. human.

Organism-specific databases

CTD23521.
GeneCardsGC19P049991.
H-InvDBHIX0027968.
HIX0158081.
HGNCHGNC:10304. RPL13A.
HPAHPA038751.
neXtProtNX_P40429.
PharmGKBPA38122.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0102.
HOGENOMHOG000225289.
HOVERGENHBG062176.
InParanoidP40429.
KOK02872.
OrthoDBEOG7H1JMP.
PhylomeDBP40429.
TreeFamTF300159.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

BgeeP40429.
CleanExHS_RPL13A.
GenevestigatorP40429.

Family and domain databases

Gene3D3.90.1180.10. 1 hit.
HAMAPMF_01366. Ribosomal_L13.
InterProIPR005822. Ribosomal_L13.
IPR023563. Ribosomal_L13_CS.
IPR023564. Ribosomal_L13_dom.
IPR005755. Ribosomal_L13_euk/arc.
[Graphical view]
PANTHERPTHR11545. PTHR11545. 1 hit.
PTHR11545:SF3. PTHR11545:SF3. 1 hit.
PfamPF00572. Ribosomal_L13. 1 hit.
[Graphical view]
SUPFAMSSF52161. SSF52161. 1 hit.
TIGRFAMsTIGR01077. L13_A_E. 1 hit.
PROSITEPS00783. RIBOSOMAL_L13. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPL13A. human.
GeneWikiRPL13A.
GenomeRNAi23521.
NextBio45973.
PROP40429.

Entry information

Entry nameRL13A_HUMAN
AccessionPrimary (citable) accession number: P40429
Secondary accession number(s): A8K505
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM