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Protein

60S ribosomal protein L22

Gene

Rpl22

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • heparin binding Source: MGI
  • poly(A) RNA binding Source: MGI
  • structural constituent of ribosome Source: InterPro

GO - Biological processi

  • alpha-beta T cell differentiation Source: MGI
  • translation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

Heparin-binding, RNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-MMU-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-MMU-6791226. Major pathway of rRNA processing in the nucleolus.
R-MMU-72689. Formation of a pool of free 40S subunits.
R-MMU-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-MMU-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-MMU-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L22
Alternative name(s):
Heparin-binding protein HBp15
Gene namesi
Name:Rpl22
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:99262. Rpl22.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosolic large ribosomal subunit Source: MGI
  • extracellular exosome Source: MGI
  • focal adhesion Source: MGI
  • intracellular ribonucleoprotein complex Source: MGI
  • nucleus Source: MGI
  • ribosome Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 12812760S ribosomal protein L22PRO_0000215502Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei62 – 621PhosphothreonineCombined sources
Modified residuei69 – 691N6-succinyllysineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP67984.
PaxDbiP67984.
PRIDEiP67984.

PTM databases

iPTMnetiP67984.
PhosphoSiteiP67984.

Expressioni

Gene expression databases

BgeeiP67984.
CleanExiMM_RPL22.
ExpressionAtlasiP67984. baseline and differential.
GenevisibleiP67984. MM.

Interactioni

Protein-protein interaction databases

BioGridi202971. 4 interactions.
IntActiP67984. 5 interactions.
MINTiMINT-1857768.
STRINGi10090.ENSMUSP00000099480.

Structurei

3D structure databases

ProteinModelPortaliP67984.
SMRiP67984. Positions 17-115.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi120 – 1289Asp/Glu-rich (highly acidic)

Sequence similaritiesi

Belongs to the ribosomal protein L22e family.Curated

Phylogenomic databases

eggNOGiKOG3434. Eukaryota.
ENOG4111UVJ. LUCA.
HOGENOMiHOG000198396.
HOVERGENiHBG004373.
InParanoidiP67984.
KOiK02891.
OMAiEVVTHIP.
OrthoDBiEOG72VH8D.
PhylomeDBiP67984.
TreeFamiTF313018.

Family and domain databases

InterProiIPR002671. Ribosomal_L22e.
[Graphical view]
PANTHERiPTHR10064. PTHR10064. 1 hit.
PfamiPF01776. Ribosomal_L22e. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P67984-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPVKKLVAK GGKKKKQVLK FTLDCTHPVE DGIMDAANFE QFLQERIKVN
60 70 80 90 100
GKAGNLGGGV VTIERSKSKI TVTSEVPFSK RYLKYLTKKY LKKNNLRDWL
110 120
RVVANSKESY ELRYFQINQD EEEEEDED
Length:128
Mass (Da):14,759
Last modified:January 23, 2007 - v2
Checksum:i3F29D8BE70DEF96C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D17653 mRNA. Translation: BAA04546.1.
BC007139 mRNA. Translation: AAH07139.1.
BC021344 mRNA. Translation: AAH21344.1.
CCDSiCCDS18999.1.
PIRiJC2119.
RefSeqiNP_033105.1. NM_009079.3.
XP_006544195.1. XM_006544132.2.
UniGeneiMm.307846.

Genome annotation databases

EnsembliENSMUST00000103191; ENSMUSP00000099480; ENSMUSG00000028936.
ENSMUST00000139685; ENSMUSP00000118787; ENSMUSG00000028936.
ENSMUST00000188151; ENSMUSP00000140276; ENSMUSG00000028936.
GeneIDi102642602.
19934.
KEGGimmu:102642602.
mmu:19934.
UCSCiuc008wah.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D17653 mRNA. Translation: BAA04546.1.
BC007139 mRNA. Translation: AAH07139.1.
BC021344 mRNA. Translation: AAH21344.1.
CCDSiCCDS18999.1.
PIRiJC2119.
RefSeqiNP_033105.1. NM_009079.3.
XP_006544195.1. XM_006544132.2.
UniGeneiMm.307846.

3D structure databases

ProteinModelPortaliP67984.
SMRiP67984. Positions 17-115.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202971. 4 interactions.
IntActiP67984. 5 interactions.
MINTiMINT-1857768.
STRINGi10090.ENSMUSP00000099480.

PTM databases

iPTMnetiP67984.
PhosphoSiteiP67984.

Proteomic databases

EPDiP67984.
PaxDbiP67984.
PRIDEiP67984.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000103191; ENSMUSP00000099480; ENSMUSG00000028936.
ENSMUST00000139685; ENSMUSP00000118787; ENSMUSG00000028936.
ENSMUST00000188151; ENSMUSP00000140276; ENSMUSG00000028936.
GeneIDi102642602.
19934.
KEGGimmu:102642602.
mmu:19934.
UCSCiuc008wah.2. mouse.

Organism-specific databases

CTDi6146.
MGIiMGI:99262. Rpl22.

Phylogenomic databases

eggNOGiKOG3434. Eukaryota.
ENOG4111UVJ. LUCA.
HOGENOMiHOG000198396.
HOVERGENiHBG004373.
InParanoidiP67984.
KOiK02891.
OMAiEVVTHIP.
OrthoDBiEOG72VH8D.
PhylomeDBiP67984.
TreeFamiTF313018.

Enzyme and pathway databases

ReactomeiR-MMU-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-MMU-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-MMU-6791226. Major pathway of rRNA processing in the nucleolus.
R-MMU-72689. Formation of a pool of free 40S subunits.
R-MMU-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-MMU-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-MMU-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

ChiTaRSiRpl22. mouse.
PROiP67984.
SOURCEiSearch...

Gene expression databases

BgeeiP67984.
CleanExiMM_RPL22.
ExpressionAtlasiP67984. baseline and differential.
GenevisibleiP67984. MM.

Family and domain databases

InterProiIPR002671. Ribosomal_L22e.
[Graphical view]
PANTHERiPTHR10064. PTHR10064. 1 hit.
PfamiPF01776. Ribosomal_L22e. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel heparin-binding protein, HBp15, is identified as mammalian ribosomal protein L22."
    Fujita Y., Okamoto T., Noshiro M., Kato Y., Takada K., Sato J.D., Ozaki T., McKeehan W.L., Crabb J.W., Whitney R.G.
    Biochem. Biophys. Res. Commun. 199:706-713(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
    Tissue: Submandibular gland.
  2. "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: Mammary tumor and Salivary gland.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-69, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiRL22_MOUSE
AccessioniPrimary (citable) accession number: P67984
Secondary accession number(s): P41104
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Binds to Epstein-Barr virus small RNAs and to heparin.

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

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.