P40429 (RL13A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
60S ribosomal protein L13a

Alternative name(s):
23 kDa highly basic protein

Gene names

Name:

RPL13A

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	203 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.15
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.
Sequence similarities	Belongs to the ribosomal protein L13P family.

Ontologies

Keywords
Biological process	Translation regulation
Cellular component	Cytoplasm
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	SRP-dependent cotranslational protein targeting to membrane Traceable author statement. Source: Reactome cellular response to interferon-gamma Inferred from direct assay Ref.9. Source: UniProtKB 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.15. Source: UniProtKB nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Traceable author statement. Source: Reactome translational elongation Traceable author statement. Source: Reactome translational initiation Traceable author statement. Source: Reactome translational termination Traceable author statement. Source: Reactome viral transcription Traceable author statement. Source: Reactome
Cellular_component	cytosolic large ribosomal subunit Inferred from direct assay Ref.8. Source: UniProtKB
Molecular_function	structural constituent of ribosome Non-traceable author statement Ref.8. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.6
	Chain	2 – 203	202	60S ribosomal protein L13a		PRO_0000133769
Amino acid modifications
	Modified residue	2	1	N-acetylalanine; partial Ref.6 Ref.8
	Modified residue	77	1	Phosphoserine; by ZIPK/DAPK3 Ref.12
	Modified residue	191	1	N6-acetyllysine Ref.13
Experimental info
	Mutagenesis	77	1	S → A: Loss of interferon-gamma induced phosphorylation. Ref.12

Sequences

	Sequence		Length	Mass (Da)
	P40429 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 3E80D0AB77A0D406	FASTA	203	23,577
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, 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: MASS SPECTROMETRY, PROBABLE ACETYLATION AT ALA-2.
[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]	"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, MASS SPECTROMETRY.
[14]	"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].
[15]	"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.
+	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.
IPI	IPI00304612.
PIR	S29539.
RefSeq	NP_001257420.1. NM_001270491.1. NP_036555.1. NM_012423.3.
UniGene	Hs.523185.
3D structure databases
ProteinModelPortal	P40429.
ModBase	Search...
Protein-protein interaction databases
IntAct	P40429. 19 interactions.
MINT	MINT-1417412.
STRING	9606.ENSP00000375730.
PTM databases
PhosphoSite	P40429.
Polymorphism databases
DMDM	730451.
Proteomic databases
PaxDb	P40429.
PRIDE	P40429.
Protocols and materials databases
DNASU	23521.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000391857; ENSP00000375730; ENSG00000142541.
GeneID	23521.
KEGG	hsa:23521.
UCSC	uc002pny.3. human.
Organism-specific databases
CTD	23521.
GeneCards	GC19P049991.
H-InvDB	HIX0027968. HIX0158081.
HGNC	HGNC:10304. RPL13A.
HPA	HPA038751.
neXtProt	NX_P40429.
PharmGKB	PA38122.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0102.
HOGENOM	HOG000225289.
HOVERGEN	HBG062176.
InParanoid	P40429.
KO	K02872.
OMA	FYRNKIK.
OrthoDB	EOG479F83.
PhylomeDB	P40429.
Enzyme and pathway databases
Reactome	REACT_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
ArrayExpress	P40429.
Bgee	P40429.
CleanEx	HS_RPL13A.
Genevestigator	P40429.
GermOnline	ENSG00000142541. Homo sapiens.
Family and domain databases
Gene3D	3.90.1180.10. 1 hit.
InterPro	IPR005822. Ribosomal_L13. IPR023563. Ribosomal_L13_CS. IPR023564. Ribosomal_L13_dom. IPR005755. Ribosomal_L13_euk/arc. [Graphical view]
PANTHER	PTHR11545. PTHR11545. 1 hit. PTHR11545:SF3. PTHR11545:SF3. 1 hit.
Pfam	PF00572. Ribosomal_L13. 1 hit. [Graphical view]
SUPFAM	SSF52161. Ribosomal_L13. 1 hit.
TIGRFAMs	TIGR01077. L13_A_E. 1 hit.
PROSITE	PS00783. RIBOSOMAL_L13. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	RPL13A. human.
GenomeRNAi	23521.
NextBio	45973.

Entry information

Entry name

RL13A_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 121 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.