Q02543 (RL18A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
60S ribosomal protein L18a

Gene names

Name:

RPL18A

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	176 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Subunit structure	Binds IPO9 with high affinity.
Sequence similarities	Belongs to the ribosomal protein L18Ae family.
Sequence caution	The sequence CAA56788.1 differs from that shown. Reason: Frameshift at position 65.

Ontologies

Keywords
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	endocrine pancreas development Traceable author statement. Source: Reactome mRNA metabolic process Traceable author statement. Source: Reactome translational elongation 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. Source: UniProtKB
Molecular function	RNA binding Traceable author statement. Source: ProtInc structural constituent of ribosome Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DDX56	Q9NY93	1	EBI-350523,EBI-372376
LYAR	Q9NX58	1	EBI-350523,EBI-713507
PSTPIP1	O43586	1	EBI-350523,EBI-1050964
RTCD1	O00442	1	EBI-350523,EBI-1045306

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 176	176	60S ribosomal protein L18a		PRO_0000213925
Amino acid modifications
	Modified residue	24	1	Phosphothreonine Ref.9
	Modified residue	63	1	Phosphotyrosine Ref.6
	Modified residue	71	1	Phosphoserine Ref.7 Ref.9 Ref.10 Ref.11 Ref.12
	Modified residue	123	1	Phosphoserine Ref.8 Ref.9 Ref.10
Experimental info
	Sequence conflict	83	1	R → S in CAA56788. Ref.2
	Sequence conflict	134	1	A → V in CAA56788. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q02543 [UniParc]. Last modified February 1, 1995. Version 2. Checksum: 5E501C6D835BE580	FASTA	176	20,762
	10 20 30 40 50 60 MKASGTLREY KVVGRCLPTP KCHTPPLYRM RIFAPNHVVA KSRFWYFVSQ LKKMKKSSGE 70 80 90 100 110 120 IVYCGQVFEK SPLRVKNFGI WLRYDSRSGT HNMYREYRDL TTAGAVTQCY RDMGARHRAR 130 140 150 160 170 AHSIQIMKVE EIAASKCRRP AVKQFHDSKI KFPLPHRVLR RQHKPRFTTK RPNTFF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Bhat K.S. Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Zenz K.I. Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed: 15057824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Muscle.
[5]	"Importins fulfil a dual function as nuclear import receptors and cytoplasmic chaperones for exposed basic domains." Jaekel S., Mingot J.-M., Schwarzmaier P., Hartmann E., Goerlich D. EMBO J. 21:377-386(2002) [PubMed: 11823430] [Abstract] Cited for: INTERACTION WITH IPO9.
[6]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-63, MASS SPECTROMETRY.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24; SER-71 AND SER-123, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71 AND SER-123, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, MASS SPECTROMETRY.
[12]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L05093 mRNA. Translation: AAC18781.1. X80822 mRNA. Translation: CAA56788.1. Frameshift. AC005796 Genomic DNA. Translation: AAC62828.1. BC007512 mRNA. Translation: AAH07512.1. BC066319 mRNA. Translation: AAH66319.1. BC071920 mRNA. Translation: AAH71920.1.
IPI	IPI00026202.
PIR	S47353.
RefSeq	NP_000971.1. NM_000980.2.
UniGene	Hs.337766.
3D structure databases
ProteinModelPortal	Q02543.
SMR	Q02543. Positions 3-166.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q02543. 13 interactions.
MINT	MINT-5000271.
STRING	Q02543.
PTM databases
PhosphoSite	Q02543.
Polymorphism databases
DMDM	730538.
2D gel databases
SWISS-2DPAGE	Q02543.
Proteomic databases
PeptideAtlas	Q02543.
PRIDE	Q02543.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000222247; ENSP00000222247; ENSG00000105640.
GeneID	6142.
KEGG	hsa:6142.
UCSC	uc002nhp.1. human.
Organism-specific databases
CTD	6142.
GeneCards	GC19P017970.
H-InvDB	HIX0014901.
HGNC	HGNC:10311. RPL18A.
MIM	604178. gene.
neXtProt	NX_Q02543.
PharmGKB	PA34680.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG11657.
HOGENOM	HBG319315.
HOVERGEN	HBG066281.
InParanoid	Q02543.
OMA	KSRYWYF.
PhylomeDB	Q02543.
Enzyme and pathway databases
Reactome	REACT_111045. Developmental Biology. REACT_111217. Metabolism. REACT_15380. Diabetes pathways. REACT_17015. Metabolism of proteins. REACT_1762. 3' -UTR-mediated translational regulation. REACT_6167. Influenza Infection. REACT_71. Gene Expression.
Gene expression databases
Bgee	Q02543.
CleanEx	HS_RPL18A.
Genevestigator	Q02543.
GermOnline	ENSG00000105640. Homo sapiens.
Family and domain databases
InterPro	IPR021138. Ribosomal_L18a. IPR023573. Ribosomal_L18a/LX. [Graphical view]
KO	K02882.
PANTHER	PTHR10052. PTHR10052. 1 hit.
Pfam	PF01775. Ribosomal_L18ae. 1 hit. [Graphical view]
PIRSF	PIRSF002190. Ribosomal_L18a. 1 hit.
ProtoNet	Search...
Other
NextBio	23861.
SOURCE	Search...

Entry information

Entry name

RL18A_HUMAN

Accession

Primary (citable) accession number: Q02543

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	February 1, 1995
Last modified:	January 25, 2012
This is version 112 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.