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Protein

60S ribosomal protein L8

Gene

Rpl8

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

ReactomeiREACT_279505. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_292264. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_302277. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_308559. Formation of a pool of free 40S subunits.
REACT_311765. Peptide chain elongation.
REACT_319670. Eukaryotic Translation Termination.
REACT_331340. SRP-dependent cotranslational protein targeting to membrane.
REACT_340387. L13a-mediated translational silencing of Ceruloplasmin expression.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L8
Gene namesi
Name:Rpl8
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1350927. Rpl8.

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 25725660S ribosomal protein L8PRO_0000129744Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei216 – 2161(3S)-3-hydroxyhistidineBy similarity

Post-translational modificationi

Hydroxylated on His-216 by NO66. The modification is impaired by hypoxia.By similarity

Keywords - PTMi

Hydroxylation

Proteomic databases

MaxQBiP62918.
PaxDbiP62918.
PRIDEiP62918.

Expressioni

Gene expression databases

BgeeiP62918.
CleanExiMM_RPL8.
ExpressionAtlasiP62918. baseline and differential.
GenevisibleiP62918. MM.

Interactioni

Subunit structurei

Interacts with CRY1.1 Publication

Protein-protein interaction databases

BioGridi205087. 8 interactions.
IntActiP62918. 8 interactions.
MINTiMINT-1857612.
STRINGi10090.ENSMUSP00000004072.

Structurei

3D structure databases

ProteinModelPortaliP62918.
SMRiP62918. Positions 14-245.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L2P family.Curated

Phylogenomic databases

eggNOGiCOG0090.
GeneTreeiENSGT00390000009907.
HOGENOMiHOG000232983.
HOVERGENiHBG079431.
InParanoidiP62918.
KOiK02938.
OMAiAHNPDTK.
OrthoDBiEOG7ZKSBZ.
PhylomeDBiP62918.
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.

P62918-1 [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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U67771 mRNA. Translation: AAC35587.1.
AK088263 mRNA. Translation: BAC40244.1.
AK131970 mRNA. Translation: BAE20910.1.
AK145498 mRNA. Translation: BAE26472.1.
AK167775 mRNA. Translation: BAE39807.1.
AK168769 mRNA. Translation: BAE40605.1.
BC043017 mRNA. Translation: AAH43017.1.
CCDSiCCDS27595.1.
RefSeqiNP_036183.1. NM_012053.2.
UniGeneiMm.30066.

Genome annotation databases

EnsembliENSMUST00000004072; ENSMUSP00000004072; ENSMUSG00000003970.
GeneIDi26961.
KEGGimmu:26961.
UCSCiuc007wmt.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U67771 mRNA. Translation: AAC35587.1.
AK088263 mRNA. Translation: BAC40244.1.
AK131970 mRNA. Translation: BAE20910.1.
AK145498 mRNA. Translation: BAE26472.1.
AK167775 mRNA. Translation: BAE39807.1.
AK168769 mRNA. Translation: BAE40605.1.
BC043017 mRNA. Translation: AAH43017.1.
CCDSiCCDS27595.1.
RefSeqiNP_036183.1. NM_012053.2.
UniGeneiMm.30066.

3D structure databases

ProteinModelPortaliP62918.
SMRiP62918. Positions 14-245.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205087. 8 interactions.
IntActiP62918. 8 interactions.
MINTiMINT-1857612.
STRINGi10090.ENSMUSP00000004072.

Proteomic databases

MaxQBiP62918.
PaxDbiP62918.
PRIDEiP62918.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000004072; ENSMUSP00000004072; ENSMUSG00000003970.
GeneIDi26961.
KEGGimmu:26961.
UCSCiuc007wmt.2. mouse.

Organism-specific databases

CTDi6132.
MGIiMGI:1350927. Rpl8.

Phylogenomic databases

eggNOGiCOG0090.
GeneTreeiENSGT00390000009907.
HOGENOMiHOG000232983.
HOVERGENiHBG079431.
InParanoidiP62918.
KOiK02938.
OMAiAHNPDTK.
OrthoDBiEOG7ZKSBZ.
PhylomeDBiP62918.
TreeFamiTF300748.

Enzyme and pathway databases

ReactomeiREACT_279505. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_292264. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_302277. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_308559. Formation of a pool of free 40S subunits.
REACT_311765. Peptide chain elongation.
REACT_319670. Eukaryotic Translation Termination.
REACT_331340. SRP-dependent cotranslational protein targeting to membrane.
REACT_340387. L13a-mediated translational silencing of Ceruloplasmin expression.

Miscellaneous databases

ChiTaRSiRpl8. mouse.
NextBioi304899.
PROiP62918.
SOURCEiSearch...

Gene expression databases

BgeeiP62918.
CleanExiMM_RPL8.
ExpressionAtlasiP62918. baseline and differential.
GenevisibleiP62918. MM.

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. Rocha D., Carrier A., Victorero G., Mattei M.-G., Szatanik M., Guenet J.-L., Jordan B.
    Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Liver and Thymus.
  3. "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].
    Strain: C57BL/6.
    Tissue: Brain.
  4. "Molecular characterization of Mybbp1a as a co-repressor on the Period2 promoter."
    Hara Y., Onishi Y., Oishi K., Miyazaki K., Fukamizu A., Ishida N.
    Nucleic Acids Res. 37:1115-1126(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CRY1.

Entry informationi

Entry nameiRL8_MOUSE
AccessioniPrimary (citable) accession number: P62918
Secondary accession number(s): P25120, Q3V288
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. 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.