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Reviewed, UniProtKB/Swiss-Prot P05387 (RLA2_HUMAN)

Last modified June 16, 2009. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    60S acidic ribosomal protein P2
Alternative name(s):
    Renal carcinoma antigen NY-REN-44
Gene names
Name: RPLP2
Synonyms: D11S2243E, RPP2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length115 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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 functionRibonucleoprotein
Ribosomal protein
   PTMPhosphoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processtranslational elongation

Inferred from Experiment. Source: Reactome

   Cellular componentcytosolic large ribosomal subunit Ref.1

Traceable author statement. Source: ProtInc

   Molecular functionRNA binding Ref.1

Traceable author statement. Source: ProtInc

structural constituent of ribosome Ref.1

Traceable author statement. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11511560S acidic ribosomal protein P2
PRO_0000157640

Amino acid modifications

Modified residue161Phosphoserine Ref.15
Modified residue171Phosphoserine Ref.15 Ref.9 Ref.10 Ref.17
Modified residue791Phosphoserine Ref.17 Ref.16
Modified residue861Phosphoserine Ref.17
Modified residue1021Phosphoserine Ref.15 Ref.17 Ref.16 Ref.7 Ref.8 Ref.11 Ref.12 Ref.13 Ref.14 Ref.18
Modified residue1051Phosphoserine Ref.15 Ref.17 Ref.16 Ref.8 Ref.11 Ref.13 Ref.14 Ref.18

Secondary structure

... 115
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05387-1 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: B5ECFE2510A756BF

FASTA11511,665
        10         20         30         40         50         60 
MRYVASYLLA ALGGNSSPSA KDIKKILDSV GIEADDDRLN KVISELNGKN IEDVIAQGIG 

        70         80         90        100        110 
KLASVPAGGA VAVSAAPGSA APAAGSAPAA AEEKKDEKKE ESEESDDDMG FGLFD 

« Hide

References

« Hide '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.
[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: Epithelium.
[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: Epithelium.
[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: Epithelium.
[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.
[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.
[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.
[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.
[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.
[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]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
IPIIPI00008529.
PIRR6HUP2. C27125.
RefSeqNP_000995.1.
UniGeneHs.437594

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1S4JNMR-A103-115[»]
2JDLX-ray2.20C/D105-115[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP05387. 11 interactions.

PTM databases

PhosphoSiteP05387.

2-D gel databases

SWISS-2DPAGEP05387.
PHCI-2DPAGEP05387.

Proteomic databases

PeptideAtlasP05387.
PRIDEP05387.

Genome annotation databases

EnsemblENSG00000177600. Homo sapiens. [Contig view]
GeneID6181.
KEGGhsa:6181.

Organism-specific databases

GeneCardsGC11P000799.
H-InvDBHIX0018031.
HGNCHGNC:10377. RPLP2.
MIM180530. gene.
PharmGKBPA34776.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP05387.
HOVERGENP05387.
OMAP05387. VIGELNG.

Enzyme and pathway databases

ReactomeREACT_1762. 3' -UTR-mediated translational regulation.
REACT_6167. Influenza Infection.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP05387.
BgeeP05387.
CleanExHS_RPLP2.
GermOnlineENSG00000177600. Homo sapiens.

Family and domain databases

InterProIPR001813. Ribosomal_60S.
[Graphical view]
PfamPF00428. Ribosomal_60s. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio24001.
SOURCESearch...

Entry information

Entry nameRLA2_HUMAN
AccessionPrimary (citable) accession number: P05387
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: June 16, 2009
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Ribosomal proteins

Ribosomal proteins families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents