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Protein

60S ribosomal protein L8

Gene

RPL8

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

Functioni

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: ProtInc
  • rRNA binding Source: UniProtKB-KW
  • structural constituent of ribosome Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_9491. Viral mRNA Translation.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L8
Gene namesi
Name:RPL8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:10368. RPL8.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • cytosolic large ribosomal subunit Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleolus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi209 – 2091H → A or G: No incorporation into translating E.coli polysomes; ribosomes assembled normally. Significantly reduced translational activity. 1 Publication

Organism-specific databases

PharmGKBiPA34768.

Polymorphism and mutation databases

BioMutaiRPL8.
DMDMi51702823.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 25725660S ribosomal protein L8PRO_0000129743Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei216 – 2161(3S)-3-hydroxyhistidine1 Publication

Post-translational modificationi

Hydroxylated on His-216 by NO66. The modification is impaired by hypoxia.1 Publication

Keywords - PTMi

Hydroxylation

Proteomic databases

MaxQBiP62917.
PaxDbiP62917.
PRIDEiP62917.

PTM databases

PhosphoSiteiP62917.

Expressioni

Gene expression databases

BgeeiP62917.
CleanExiHS_RPL8.
ExpressionAtlasiP62917. baseline.
GenevestigatoriP62917.

Organism-specific databases

HPAiHPA045095.
HPA050165.

Interactioni

Subunit structurei

Interacts with CRY1.By similarity

Protein-protein interaction databases

BioGridi112052. 141 interactions.
DIPiDIP-37967N.
IntActiP62917. 35 interactions.
MINTiMINT-1135693.
STRINGi9606.ENSP00000262584.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CCMX-ray2.51C/D205-239[»]
4CCNX-ray2.23C/D205-239[»]
4CCOX-ray2.30C/D205-224[»]
4V6Xelectron microscopy5.00CA1-257[»]
ProteinModelPortaliP62917.
SMRiP62917. Positions 14-245.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L2P family.Curated

Phylogenomic databases

eggNOGiCOG0090.
GeneTreeiENSGT00390000009907.
HOVERGENiHBG079431.
InParanoidiP62917.
KOiK02938.
OMAiAHNPDTK.
PhylomeDBiP62917.
TreeFamiTF300748.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
2.40.50.140. 1 hit.
4.10.950.10. 1 hit.
HAMAPiMF_01320_A. Ribosomal_L2_A.
InterProiIPR012340. 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]
PANTHERiPTHR13691. PTHR13691. 1 hit.
PfamiPF00181. Ribosomal_L2. 1 hit.
PF03947. Ribosomal_L2_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002158. Ribosomal_L2. 1 hit.
SUPFAMiSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 1 hit.
PROSITEiPS00467. RIBOSOMAL_L2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P62917-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRVIRGQRK GAGSVFRAHV KHRKGAARLR AVDFAERHGY IKGIVKDIIH
60 70 80 90 100
DPGRGAPLAK VVFRDPYRFK KRTELFIAAE GIHTGQFVYC GKKAQLNIGN
110 120 130 140 150
VLPVGTMPEG TIVCCLEEKP GDRGKLARAS GNYATVISHN PETKKTRVKL
160 170 180 190 200
PSGSKKVISS ANRAVVGVVA GGGRIDKPIL KAGRAYHKYK AKRNCWPRVR
210 220 230 240 250
GVAMNPVEHP FGGGNHQHIG KPSTIRRDAP AGRKVGLIAA RRTGRLRGTK

TVQEKEN
Length:257
Mass (Da):28,025
Last modified:January 23, 2007 - v2
Checksum:iCE1610449749318B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti98 – 981I → V.2 Publications
Corresponds to variant rs17850886 [ dbSNP | Ensembl ].
VAR_019658

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS6433.1.
PIRiJN0923.
RefSeqiNP_000964.1. NM_000973.3.
NP_150644.1. NM_033301.1.
UniGeneiHs.178551.

Genome annotation databases

EnsembliENST00000262584; ENSP00000262584; ENSG00000161016.
ENST00000394920; ENSP00000378378; ENSG00000161016.
ENST00000528957; ENSP00000433464; ENSG00000161016.
GeneIDi6132.
KEGGihsa:6132.
UCSCiuc003zeb.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS6433.1.
PIRiJN0923.
RefSeqiNP_000964.1. NM_000973.3.
NP_150644.1. NM_033301.1.
UniGeneiHs.178551.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CCMX-ray2.51C/D205-239[»]
4CCNX-ray2.23C/D205-239[»]
4CCOX-ray2.30C/D205-224[»]
4V6Xelectron microscopy5.00CA1-257[»]
ProteinModelPortaliP62917.
SMRiP62917. Positions 14-245.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112052. 141 interactions.
DIPiDIP-37967N.
IntActiP62917. 35 interactions.
MINTiMINT-1135693.
STRINGi9606.ENSP00000262584.

PTM databases

PhosphoSiteiP62917.

Polymorphism and mutation databases

BioMutaiRPL8.
DMDMi51702823.

Proteomic databases

MaxQBiP62917.
PaxDbiP62917.
PRIDEiP62917.

Protocols and materials databases

DNASUi6132.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262584; ENSP00000262584; ENSG00000161016.
ENST00000394920; ENSP00000378378; ENSG00000161016.
ENST00000528957; ENSP00000433464; ENSG00000161016.
GeneIDi6132.
KEGGihsa:6132.
UCSCiuc003zeb.3. human.

Organism-specific databases

CTDi6132.
GeneCardsiGC08M146015.
HGNCiHGNC:10368. RPL8.
HPAiHPA045095.
HPA050165.
MIMi604177. gene.
neXtProtiNX_P62917.
PharmGKBiPA34768.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0090.
GeneTreeiENSGT00390000009907.
HOVERGENiHBG079431.
InParanoidiP62917.
KOiK02938.
OMAiAHNPDTK.
PhylomeDBiP62917.
TreeFamiTF300748.

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_9491. Viral mRNA Translation.

Miscellaneous databases

ChiTaRSiRPL8. human.
GeneWikiiRPL8.
GenomeRNAii6132.
NextBioi23815.
PROiP62917.
SOURCEiSearch...

Gene expression databases

BgeeiP62917.
CleanExiHS_RPL8.
ExpressionAtlasiP62917. baseline.
GenevestigatoriP62917.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
2.40.50.140. 1 hit.
4.10.950.10. 1 hit.
HAMAPiMF_01320_A. Ribosomal_L2_A.
InterProiIPR012340. 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]
PANTHERiPTHR13691. PTHR13691. 1 hit.
PfamiPF00181. Ribosomal_L2. 1 hit.
PF03947. Ribosomal_L2_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002158. Ribosomal_L2. 1 hit.
SUPFAMiSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 1 hit.
PROSITEiPS00467. RIBOSOMAL_L2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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, SUBCELLULAR LOCATION.
  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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: HYDROXYLATION AT HIS-216 BY NO66.
  14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRL8_HUMAN
AccessioniPrimary (citable) accession number: P62917
Secondary accession number(s): A8K094
, D3DWN2, P25120, Q567Q7, Q969V7, Q9BWQ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 23, 2007
Last modified: May 27, 2015
This is version 116 of the entry and version 2 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

Miscellaneous

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

Keywords - Technical termi

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

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Ribosomal proteins
    Ribosomal proteins families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.