P05387 (RLA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
60S acidic ribosomal protein P2

Alternative name(s):
Renal carcinoma antigen NY-REN-44

Gene names

Name:	RPLP2
Synonyms:	D11S2243E, RPP2

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	115 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays an important role in the elongation step of protein synthesis.
Subunit structure	P1 and P2 exist as dimers at the large ribosomal subunit.
Sequence similarities	Belongs to the ribosomal protein L12P family.

Ontologies

Keywords
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing 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...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 115

115

60S acidic ribosomal protein P2

PRO_0000157640

Amino acid modifications

Modified residue

16

1

Phosphoserine Ref.15 Ref.20

Modified residue

17

1

Phosphoserine Ref.9 Ref.10 Ref.15 Ref.17 Ref.19 Ref.20 Ref.21

Modified residue

21

1

N6-acetyllysine Ref.22

Modified residue

49

1

N6-acetyllysine Ref.22

Modified residue

79

1

Phosphoserine Ref.16 Ref.17 Ref.19 Ref.20 Ref.21

Modified residue

86

1

Phosphoserine Ref.17 Ref.19

Modified residue

102

1

Phosphoserine Ref.7 Ref.8 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.21

Modified residue

105

1

Phosphoserine Ref.8 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.21

Secondary structure

1

.

.

.

115

Helix Strand Turn

Details...

Beta strand

106 – 113

8

Sequences

	Sequence		Length	Mass (Da)
	P05387 [UniParc]. Last modified November 1, 1988. Version 1. Checksum: B5ECFE2510A756BF	FASTA	115	11,665
	10 20 30 40 50 60 MRYVASYLLA ALGGNSSPSA KDIKKILDSV GIEADDDRLN KVISELNGKN IEDVIAQGIG 70 80 90 100 110 KLASVPAGGA VAVSAAPGSA APAAGSAPAA AEEKKDEKKE ESEESDDDMG FGLFD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of cDNA clones, in vitro synthesis, and assembly." Rich B.E., Steitz J.A. Mol. Cell. Biol. 7:4065-4074(1987) [PubMed: 3323886] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"A sequence previously identified as metastasis-related encodes an acidic ribosomal phosphoprotein, P2." Sharp M.G.F., Adams S.M., Elvin P., Walker R.A., Brammar W.J., Varley J.M. Br. J. Cancer 61:83-88(1990) [PubMed: 2153399] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Mammary carcinoma.
[3]	"The human ribosomal protein genes: sequencing and comparative analysis of 73 genes." Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N. Genome Res. 12:379-390(2002) [PubMed: 11875025] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [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: Kidney, Ovary, Prostate and Skin.
[5]	"Human liver protein map: a reference database established by microsequencing and gel comparison." Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J. Electrophoresis 13:992-1001(1992) [PubMed: 1286669] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-10. Tissue: Liver.
[6]	"Antigens recognized by autologous antibody in patients with renal-cell carcinoma." Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J. Int. J. Cancer 83:456-464(1999) [PubMed: 10508479] [Abstract] Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN. Tissue: Renal cell carcinoma.
[7]	"Identification and characterization of phosphorylated proteins in the human pituitary." Giorgianni F., Beranova-Giorgianni S., Desiderio D.M. Proteomics 4:587-598(2004) [PubMed: 14997482] [Abstract] Cited for: PHOSPHORYLATION AT SER-102. Tissue: Pituitary.
[8]	"Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-105, MASS SPECTROMETRY. Tissue: Colon adenocarcinoma.
[9]	"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-17, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Phosphoproteomic analysis of the human pituitary." Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F. Pituitary 9:109-120(2006) [PubMed: 16807684] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-105, MASS SPECTROMETRY. Tissue: Pituitary.
[12]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, MASS SPECTROMETRY. Tissue: Cervix adenocarcinoma.
[13]	"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line." Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S. Electrophoresis 28:2027-2034(2007) [PubMed: 17487921] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-105, MASS SPECTROMETRY. Tissue: Prostate cancer.
[14]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-105, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[15]	"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-16; SER-17; SER-102 AND SER-105, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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 SER-79; SER-102 AND SER-105, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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-17; SER-79; SER-86; SER-102 AND SER-105, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-105, MASS SPECTROMETRY. Tissue: Liver.
[19]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-79 AND SER-86, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[20]	"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-16; SER-17; SER-79; SER-102 AND SER-105, MASS SPECTROMETRY.
[21]	"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-17; SER-79; SER-102 AND SER-105, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[22]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21 AND LYS-49, MASS SPECTROMETRY.
[23]	"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

M17887 mRNA. Translation: AAA36472.1.
AB061837 Genomic DNA. Translation: BAB79475.1.
BC005354 mRNA. Translation: AAH05354.1.
BC005920 mRNA. Translation: AAH05920.1.
BC007573 mRNA. Translation: AAH07573.1.
BC062314 mRNA. Translation: AAH62314.1.

IPI

IPI00008529.

PIR

R6HUP2. C27125.

RefSeq

NP_000995.1. NM_001004.3.

UniGene

Hs.437594.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1S4J	NMR	-	A	103-115	[»]
2JDL	X-ray	2.20	C/D	105-115	[»]
2W1O	NMR	-	A/B	1-69	[»]

ProteinModelPortal

P05387.

SMR

P05387. Positions 1-69.

ModBase

Search...

Protein-protein interaction databases

IntAct

P05387. 14 interactions.

MINT

MINT-4999550.

STRING

P05387.

Protein family/group databases

Allergome

1276. Hom s P2.

PTM databases

PhosphoSite

P05387.

Polymorphism databases

DMDM

133061.

2D gel databases

SWISS-2DPAGE

P05387.

PHCI-2DPAGE

P05387.

Proteomic databases

PeptideAtlas

P05387.

PRIDE

P05387.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000321153; ENSP00000322419; ENSG00000177600.

GeneID

6181.

KEGG

hsa:6181.

UCSC

uc001lrq.1. human.

Organism-specific databases

CTD

6181.

GeneCards

GC11P000799.

H-InvDB

HIX0018031.
HIX0200997.

HGNC

HGNC:10377. RPLP2.

MIM

180530. gene.

neXtProt

NX_P05387.

PharmGKB

PA34776.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG21412.

HOGENOM

HBG744999.

HOVERGEN

HBG014761.

InParanoid

P05387.

OMA

AVLGGNE.

OrthoDB

EOG4F4SCS.

PhylomeDB

P05387.

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

ArrayExpress

P05387.

Bgee

P05387.

CleanEx

HS_RPLP2.

Genevestigator

P05387.

GermOnline

ENSG00000177600. Homo sapiens.

Family and domain databases

InterPro

IPR001813. Ribosomal_60S.
[Graphical view]

KO

K02943.

Pfam

PF00428. Ribosomal_60s. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

24001.

SOURCE

Search...

Entry information

Entry name

RLA2_HUMAN

Accession

Primary (citable) accession number: P05387

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	November 1, 1988
Last modified:	January 25, 2012
This is version 135 of the entry and version 1 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.