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Protein

60S acidic ribosomal protein P2

Gene

RPLP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays an important role in the elongation step of protein synthesis.

GO - Molecular functioni

  • structural constituent of ribosome Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiR-HSA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-HSA-156902. Peptide chain elongation.
R-HSA-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-HSA-192823. Viral mRNA Translation.
R-HSA-2408557. Selenocysteine synthesis.
R-HSA-72689. Formation of a pool of free 40S subunits.
R-HSA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-HSA-72764. Eukaryotic Translation Termination.
R-HSA-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
60S acidic ribosomal protein P2
Alternative name(s):
Renal carcinoma antigen NY-REN-44
Gene namesi
Name:RPLP2
Synonyms:D11S2243E, RPP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:10377. RPLP2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • cytosolic large ribosomal subunit Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34776.

Protein family/group databases

Allergomei1276. Hom s P2.

Polymorphism and mutation databases

BioMutaiRPLP2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11511560S acidic ribosomal protein P2PRO_0000157640Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei17 – 171PhosphoserineCombined sources
Modified residuei21 – 211N6-acetyllysine; alternateCombined sources
Modified residuei21 – 211N6-succinyllysine; alternateBy similarity
Modified residuei79 – 791PhosphoserineCombined sources
Modified residuei86 – 861PhosphoserineCombined sources
Modified residuei102 – 1021Phosphoserine1 Publication
Modified residuei105 – 1051PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP05387.
PaxDbiP05387.
PeptideAtlasiP05387.
PRIDEiP05387.
TopDownProteomicsiP05387.

2D gel databases

SWISS-2DPAGEP05387.

PTM databases

iPTMnetiP05387.
PhosphoSiteiP05387.
SwissPalmiP05387.

Expressioni

Gene expression databases

BgeeiP05387.
CleanExiHS_RPLP2.
ExpressionAtlasiP05387. baseline and differential.
GenevisibleiP05387. HS.

Organism-specific databases

HPAiHPA053635.

Interactioni

Subunit structurei

Heterodimer with RPLP1 at the lateral ribosomal stalk of the large ribosomal subunit.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
RPLP1P053862EBI-352813,EBI-354582

Protein-protein interaction databases

BioGridi112096. 130 interactions.
IntActiP05387. 22 interactions.
MINTiMINT-4999550.
STRINGi9606.ENSP00000322419.

Structurei

Secondary structure

115
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1 – 33Combined sources
Helixi4 – 1310Combined sources
Helixi20 – 289Combined sources
Turni29 – 313Combined sources
Helixi38 – 469Combined sources
Helixi51 – 555Combined sources
Beta strandi59 – 613Combined sources
Beta strandi63 – 664Combined sources
Turni91 – 944Combined sources
Beta strandi106 – 1138Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S4JNMR-A103-115[»]
2JDLX-ray2.20C/D105-115[»]
2LBFNMR-B1-69[»]
2W1ONMR-A/B1-69[»]
4BEHNMR-B1-115[»]
4V6Xelectron microscopy5.00Cu/Cv1-115[»]
ProteinModelPortaliP05387.
SMRiP05387. Positions 1-115.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05387.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L12P family.Curated

Phylogenomic databases

eggNOGiKOG3449. Eukaryota.
COG2058. LUCA.
GeneTreeiENSGT00550000074828.
HOGENOMiHOG000229897.
HOVERGENiHBG014761.
InParanoidiP05387.
KOiK02943.
OMAiVISELHG.
OrthoDBiEOG7JMGHH.
PhylomeDBiP05387.
TreeFamiTF320650.

Family and domain databases

HAMAPiMF_01478. Ribosomal_L12_arch.
InterProiIPR027534. Ribosomal_L12.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P05387-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRYVASYLLA ALGGNSSPSA KDIKKILDSV GIEADDDRLN KVISELNGKN
60 70 80 90 100
IEDVIAQGIG KLASVPAGGA VAVSAAPGSA APAAGSAPAA AEEKKDEKKE
110
ESEESDDDMG FGLFD
Length:115
Mass (Da):11,665
Last modified:November 1, 1988 - v1
Checksum:iB5ECFE2510A756BF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17887 mRNA. Translation: AAA36472.1.
AB061837 Genomic DNA. Translation: BAB79475.1.
AK311954 mRNA. Translation: BAG34894.1.
CR542212 mRNA. Translation: CAG47008.1.
CR542248 mRNA. Translation: CAG47044.1.
AP006621 Genomic DNA. No translation available.
CH471158 Genomic DNA. Translation: EAX02393.1.
BC005354 mRNA. Translation: AAH05354.1.
BC005920 mRNA. Translation: AAH05920.1.
BC007573 mRNA. Translation: AAH07573.1.
BC062314 mRNA. Translation: AAH62314.1.
CCDSiCCDS7717.1.
PIRiC27125. R6HUP2.
RefSeqiNP_000995.1. NM_001004.3.
UniGeneiHs.437594.

Genome annotation databases

EnsembliENST00000321153; ENSP00000322419; ENSG00000177600.
ENST00000530797; ENSP00000431240; ENSG00000177600.
GeneIDi6181.
KEGGihsa:6181.
UCSCiuc001lrq.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17887 mRNA. Translation: AAA36472.1.
AB061837 Genomic DNA. Translation: BAB79475.1.
AK311954 mRNA. Translation: BAG34894.1.
CR542212 mRNA. Translation: CAG47008.1.
CR542248 mRNA. Translation: CAG47044.1.
AP006621 Genomic DNA. No translation available.
CH471158 Genomic DNA. Translation: EAX02393.1.
BC005354 mRNA. Translation: AAH05354.1.
BC005920 mRNA. Translation: AAH05920.1.
BC007573 mRNA. Translation: AAH07573.1.
BC062314 mRNA. Translation: AAH62314.1.
CCDSiCCDS7717.1.
PIRiC27125. R6HUP2.
RefSeqiNP_000995.1. NM_001004.3.
UniGeneiHs.437594.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S4JNMR-A103-115[»]
2JDLX-ray2.20C/D105-115[»]
2LBFNMR-B1-69[»]
2W1ONMR-A/B1-69[»]
4BEHNMR-B1-115[»]
4V6Xelectron microscopy5.00Cu/Cv1-115[»]
ProteinModelPortaliP05387.
SMRiP05387. Positions 1-115.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112096. 130 interactions.
IntActiP05387. 22 interactions.
MINTiMINT-4999550.
STRINGi9606.ENSP00000322419.

Protein family/group databases

Allergomei1276. Hom s P2.

PTM databases

iPTMnetiP05387.
PhosphoSiteiP05387.
SwissPalmiP05387.

Polymorphism and mutation databases

BioMutaiRPLP2.

2D gel databases

SWISS-2DPAGEP05387.

Proteomic databases

EPDiP05387.
PaxDbiP05387.
PeptideAtlasiP05387.
PRIDEiP05387.
TopDownProteomicsiP05387.

Protocols and materials databases

DNASUi6181.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000321153; ENSP00000322419; ENSG00000177600.
ENST00000530797; ENSP00000431240; ENSG00000177600.
GeneIDi6181.
KEGGihsa:6181.
UCSCiuc001lrq.2. human.

Organism-specific databases

CTDi6181.
GeneCardsiRPLP2.
HGNCiHGNC:10377. RPLP2.
HPAiHPA053635.
MIMi180530. gene.
neXtProtiNX_P05387.
PharmGKBiPA34776.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3449. Eukaryota.
COG2058. LUCA.
GeneTreeiENSGT00550000074828.
HOGENOMiHOG000229897.
HOVERGENiHBG014761.
InParanoidiP05387.
KOiK02943.
OMAiVISELHG.
OrthoDBiEOG7JMGHH.
PhylomeDBiP05387.
TreeFamiTF320650.

Enzyme and pathway databases

ReactomeiR-HSA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-HSA-156902. Peptide chain elongation.
R-HSA-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-HSA-192823. Viral mRNA Translation.
R-HSA-2408557. Selenocysteine synthesis.
R-HSA-72689. Formation of a pool of free 40S subunits.
R-HSA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-HSA-72764. Eukaryotic Translation Termination.
R-HSA-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

ChiTaRSiRPLP2. human.
EvolutionaryTraceiP05387.
GeneWikiiRPLP2.
GenomeRNAii6181.
NextBioi24001.
PROiP05387.
SOURCEiSearch...

Gene expression databases

BgeeiP05387.
CleanExiHS_RPLP2.
ExpressionAtlasiP05387. baseline and differential.
GenevisibleiP05387. HS.

Family and domain databases

HAMAPiMF_01478. Ribosomal_L12_arch.
InterProiIPR027534. Ribosomal_L12.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "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].
    Tissue: Thymus.
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: Kidney, Ovary, Prostate and Skin.
  9. "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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-10.
    Tissue: Liver.
  10. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
    Tissue: Renal cell carcinoma.
  11. "Identification and characterization of phosphorylated proteins in the human pituitary."
    Giorgianni F., Beranova-Giorgianni S., Desiderio D.M.
    Proteomics 4:587-598(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-102.
    Tissue: Pituitary.
  12. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-79 AND SER-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  19. "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-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79 AND SER-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "Solution structure of the dimerization domain of ribosomal protein P2 provides insights for the structural organization of eukaryotic stalk."
    Lee K.M., Yu C.W., Chan D.S., Chiu T.Y., Zhu G., Sze K.H., Shaw P.C., Wong K.B.
    Nucleic Acids Res. 38:5206-5216(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-69, SUBUNIT.
  26. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.

Entry informationi

Entry nameiRLA2_HUMAN
AccessioniPrimary (citable) accession number: P05387
Secondary accession number(s): Q6FG96
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: May 11, 2016
This is version 181 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Ribosomal proteins
    Ribosomal proteins families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.