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P62917 (RL8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
60S ribosomal protein L8
Gene names
Name:RPL8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length257 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subcellular location

Cytoplasm HAMAP-Rule MF_01320_A.

Post-translational modification

Hydroxylated on His-216 by NO66. The modification is impaired by hypoxia. HAMAP-Rule MF_01320_A

Miscellaneous

This protein can be partially incorporated into E.coli polysomes in vivo, indicating it can replace the endogenous protein.

Sequence similarities

Belongs to the ribosomal protein L2P family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandRNA-binding
rRNA-binding
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMHydroxylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

SRP-dependent cotranslational protein targeting to membrane

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Traceable author statement. Source: Reactome

translation

Non-traceable author statement Ref.9. Source: UniProtKB

translational elongation

Traceable author statement. Source: Reactome

translational initiation

Traceable author statement. Source: Reactome

translational termination

Traceable author statement. Source: Reactome

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

viral transcription

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

cytosolic large ribosomal subunit

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_functionRNA binding

Traceable author statement Ref.1. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

rRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

structural constituent of ribosome

Non-traceable author statement Ref.9. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 25725660S ribosomal protein L8 HAMAP-Rule MF_01320_A
PRO_0000129743

Amino acid modifications

Modified residue2161(3S)-3-hydroxyhistidine HAMAP-Rule MF_01320_A

Natural variations

Natural variant981I → V. Ref.3 Ref.7
Corresponds to variant rs17850886 [ dbSNP | Ensembl ].
VAR_019658

Experimental info

Mutagenesis2091H → A or G: No incorporation into translating E.coli polysomes; ribosomes assembled normally. Significantly reduced translational activity.

Sequences

Sequence LengthMass (Da)Tools
P62917 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: CE1610449749318B

FASTA25728,025
        10         20         30         40         50         60 
MGRVIRGQRK GAGSVFRAHV KHRKGAARLR AVDFAERHGY IKGIVKDIIH DPGRGAPLAK 

        70         80         90        100        110        120 
VVFRDPYRFK KRTELFIAAE GIHTGQFVYC GKKAQLNIGN VLPVGTMPEG TIVCCLEEKP 

       130        140        150        160        170        180 
GDRGKLARAS GNYATVISHN PETKKTRVKL PSGSKKVISS ANRAVVGVVA GGGRIDKPIL 

       190        200        210        220        230        240 
KAGRAYHKYK AKRNCWPRVR GVAMNPVEHP FGGGNHQHIG KPSTIRRDAP AGRKVGLIAA 

       250 
RRTGRLRGTK TVQEKEN 

« Hide

References

« Hide 'large scale' references
[1]"Characterization by cDNA cloning of the mRNA of human ribosomal protein L8."
Hanes J., Klaudiny J., von der Kammer H., Scheit K.H.
Biochem. Biophys. Res. Commun. 197:1223-1228(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Ovary.
[2]"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].
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-98.
[4]"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].
[5]"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. expand/collapse author list , 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].
[6]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. expand/collapse author list , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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], VARIANT VAL-98.
Tissue: Kidney, Placenta, Skin and Spinal cord.
[8]"A map of 75 human ribosomal protein genes."
Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J., Tanaka T., Page D.C.
Genome Res. 8:509-523(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-134.
[9]"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: PROTEIN SEQUENCE OF 2-11, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"Functional implications of ribosomal protein L2 in protein biosynthesis as shown by in vivo replacement studies."
Uehlein M., Wegloehner W., Urlaub H., Wittmann-Liebold B.
Biochem. J. 331:423-430(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN REPLACEMENT STUDIES IN E.COLI, MUTAGENESIS.
[11]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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].
[13]"Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans."
Ge W., Wolf A., Feng T., Ho C.H., Sekirnik R., Zayer A., Granatino N., Cockman M.E., Loenarz C., Loik N.D., Hardy A.P., Claridge T.D., Hamed R.B., Chowdhury R., Gong L., Robinson C.V., Trudgian D.C., Jiang M. expand/collapse author list , Mackeen M.M., McCullagh J.S., Gordiyenko Y., Thalhammer A., Yamamoto A., Yang M., Liu-Yi P., Zhang Z., Schmidt-Zachmann M., Kessler B.M., Ratcliffe P.J., Preston G.M., Coleman M.L., Schofield C.J.
Nat. Chem. Biol. 8:960-962(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: HYDROXYLATION AT HIS-216 BY NO66.
[14]"Structures of the human and Drosophila 80S ribosome."
Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M., Wilson D.N., Beckmann R.
Nature 497:80-85(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z28407 mRNA. Translation: CAA82248.1.
AB061821 Genomic DNA. Translation: BAB79459.1.
BT007379 mRNA. Translation: AAP36043.1.
CR457046 mRNA. Translation: CAG33327.1.
AK289459 mRNA. Translation: BAF82148.1.
CH471162 Genomic DNA. Translation: EAW82048.1.
CH471162 Genomic DNA. Translation: EAW82051.1.
CH471162 Genomic DNA. Translation: EAW82052.1.
BC000047 mRNA. Translation: AAH00047.2.
BC000077 mRNA. Translation: AAH00077.1.
BC012197 mRNA. Translation: AAH12197.1.
BC013104 mRNA. Translation: AAH13104.1.
BC093064 mRNA. Translation: AAH93064.1.
AB007168 Genomic DNA. Translation: BAA25829.1.
PIRJN0923.
RefSeqNP_000964.1. NM_000973.3.
NP_150644.1. NM_033301.1.
UniGeneHs.178551.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Belectron microscopy5.00A1-257[»]
ProteinModelPortalP62917.
SMRP62917. Positions 2-256.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112052. 111 interactions.
IntActP62917. 34 interactions.
MINTMINT-1135693.
STRING9606.ENSP00000262584.

PTM databases

PhosphoSiteP62917.

Polymorphism databases

DMDM51702823.

Proteomic databases

PaxDbP62917.
PRIDEP62917.

Protocols and materials databases

DNASU6132.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262584; ENSP00000262584; ENSG00000161016.
ENST00000394920; ENSP00000378378; ENSG00000161016.
ENST00000528957; ENSP00000433464; ENSG00000161016.
GeneID6132.
KEGGhsa:6132.
UCSCuc003zeb.3. human.

Organism-specific databases

CTD6132.
GeneCardsGC08M145985.
HGNCHGNC:10368. RPL8.
HPAHPA045095.
HPA050165.
MIM604177. gene.
neXtProtNX_P62917.
PharmGKBPA34768.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0090.
HOVERGENHBG079431.
InParanoidP62917.
KOK02938.
OMAAHNPDTK.
PhylomeDBP62917.
TreeFamTF300748.

Enzyme and pathway databases

ReactomeREACT_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

ArrayExpressP62917.
BgeeP62917.
CleanExHS_RPL8.
GenevestigatorP62917.

Family and domain databases

Gene3D2.30.30.30. 1 hit.
2.40.50.140. 1 hit.
4.10.950.10. 1 hit.
HAMAPMF_01320_A. Ribosomal_L2_A.
InterProIPR012340. NA-bd_OB-fold.
IPR022666. Rbsml_prot_L2_RNA-bd_dom.
IPR014722. Rib_L2_dom2.
IPR002171. Ribosomal_L2.
IPR023672. Ribosomal_L2_arc.
IPR022669. Ribosomal_L2_C.
IPR022671. Ribosomal_L2_CS.
IPR014726. Ribosomal_L2_dom3.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERPTHR13691. PTHR13691. 1 hit.
PfamPF00181. Ribosomal_L2. 1 hit.
PF03947. Ribosomal_L2_C. 1 hit.
[Graphical view]
PIRSFPIRSF002158. Ribosomal_L2. 1 hit.
SUPFAMSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 1 hit.
PROSITEPS00467. RIBOSOMAL_L2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPL8. human.
GeneWikiRPL8.
GenomeRNAi6132.
NextBio23815.
PROP62917.
SOURCESearch...

Entry information

Entry nameRL8_HUMAN
AccessionPrimary (citable) accession number: P62917
Secondary accession number(s): A8K094 expand/collapse secondary AC list , D3DWN2, P25120, Q567Q7, Q969V7, Q9BWQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM