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Protein

60S ribosomal protein L22

Gene

RPL22

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

Functioni

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

Heparin-binding, RNA-binding

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-6791226. Major pathway of rRNA processing in the nucleolus.
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).
SIGNORiP35268.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L22
Alternative name(s):
EBER-associated protein
Short name:
EAP
Epstein-Barr virus small RNA-associated protein
Heparin-binding protein HBp15
Gene namesi
Name:RPL22
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:10315. RPL22.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: Reactome
  • cytosolic large ribosomal subunit Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: BHF-UCL
  • focal adhesion Source: UniProtKB
  • intracellular ribonucleoprotein complex Source: MGI
  • nucleus Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34688.

Polymorphism and mutation databases

BioMutaiRPL22.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 12812760S ribosomal protein L22PRO_0000215501Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei62 – 621PhosphothreonineBy similarity
Modified residuei66 – 661PhosphoserineCombined sources
Modified residuei69 – 691N6-succinyllysineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP35268.
MaxQBiP35268.
PaxDbiP35268.
PeptideAtlasiP35268.
PRIDEiP35268.
TopDownProteomicsiP35268.

2D gel databases

SWISS-2DPAGEP35268.

PTM databases

iPTMnetiP35268.
PhosphoSiteiP35268.
SwissPalmiP35268.

Expressioni

Gene expression databases

BgeeiENSG00000116251.
CleanExiHS_RPL22.
ExpressionAtlasiP35268. baseline and differential.
GenevisibleiP35268. HS.

Interactioni

Protein-protein interaction databases

BioGridi112066. 150 interactions.
IntActiP35268. 48 interactions.
MINTiMINT-1149755.
STRINGi9606.ENSP00000346088.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4UG0electron microscopy-LU1-128[»]
4V6Xelectron microscopy5.00CU1-128[»]
5AJ0electron microscopy3.50AU1-128[»]
ProteinModelPortaliP35268.
SMRiP35268. 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.
GeneTreeiENSGT00390000003719.
HOGENOMiHOG000198396.
HOVERGENiHBG004373.
InParanoidiP35268.
KOiK02891.
OMAiAPANDNI.
OrthoDBiEOG091G0POE.
PhylomeDBiP35268.
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.

P35268-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPVKKLVVK GGKKKKQVLK FTLDCTHPVE DGIMDAANFE QFLQERIKVN
60 70 80 90 100
GKAGNLGGGV VTIERSKSKI TVTSEVPFSK RYLKYLTKKY LKKNNLRDWL
110 120
RVVANSKESY ELRYFQINQD EEEEEDED
Length:128
Mass (Da):14,787
Last modified:January 23, 2007 - v2
Checksum:i0F3ED8BE70C9F962
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59357 mRNA. Translation: CAA42007.1.
D17652 mRNA. Translation: BAA04545.1.
AK311749 mRNA. Translation: BAG34692.1.
CR456873 mRNA. Translation: CAG33154.1.
AL031847 Genomic DNA. Translation: CAI19448.1.
CH471130 Genomic DNA. Translation: EAW71518.1.
BC035566 mRNA. Translation: AAH35566.1.
BC058887 mRNA. Translation: AAH58887.1.
BC066314 mRNA. Translation: AAH66314.1.
CCDSiCCDS58.1.
PIRiJC2120.
RefSeqiNP_000974.1. NM_000983.3.
UniGeneiHs.515329.
Hs.554762.

Genome annotation databases

EnsembliENST00000234875; ENSP00000346088; ENSG00000116251.
GeneIDi6146.
KEGGihsa:6146.
UCSCiuc001amd.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59357 mRNA. Translation: CAA42007.1.
D17652 mRNA. Translation: BAA04545.1.
AK311749 mRNA. Translation: BAG34692.1.
CR456873 mRNA. Translation: CAG33154.1.
AL031847 Genomic DNA. Translation: CAI19448.1.
CH471130 Genomic DNA. Translation: EAW71518.1.
BC035566 mRNA. Translation: AAH35566.1.
BC058887 mRNA. Translation: AAH58887.1.
BC066314 mRNA. Translation: AAH66314.1.
CCDSiCCDS58.1.
PIRiJC2120.
RefSeqiNP_000974.1. NM_000983.3.
UniGeneiHs.515329.
Hs.554762.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4UG0electron microscopy-LU1-128[»]
4V6Xelectron microscopy5.00CU1-128[»]
5AJ0electron microscopy3.50AU1-128[»]
ProteinModelPortaliP35268.
SMRiP35268. Positions 17-115.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112066. 150 interactions.
IntActiP35268. 48 interactions.
MINTiMINT-1149755.
STRINGi9606.ENSP00000346088.

PTM databases

iPTMnetiP35268.
PhosphoSiteiP35268.
SwissPalmiP35268.

Polymorphism and mutation databases

BioMutaiRPL22.

2D gel databases

SWISS-2DPAGEP35268.

Proteomic databases

EPDiP35268.
MaxQBiP35268.
PaxDbiP35268.
PeptideAtlasiP35268.
PRIDEiP35268.
TopDownProteomicsiP35268.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000234875; ENSP00000346088; ENSG00000116251.
GeneIDi6146.
KEGGihsa:6146.
UCSCiuc001amd.4. human.

Organism-specific databases

CTDi6146.
GeneCardsiRPL22.
HGNCiHGNC:10315. RPL22.
MIMi180474. gene.
neXtProtiNX_P35268.
PharmGKBiPA34688.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3434. Eukaryota.
ENOG4111UVJ. LUCA.
GeneTreeiENSGT00390000003719.
HOGENOMiHOG000198396.
HOVERGENiHBG004373.
InParanoidiP35268.
KOiK02891.
OMAiAPANDNI.
OrthoDBiEOG091G0POE.
PhylomeDBiP35268.
TreeFamiTF313018.

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-6791226. Major pathway of rRNA processing in the nucleolus.
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).
SIGNORiP35268.

Miscellaneous databases

ChiTaRSiRPL22. human.
GeneWikiiRPL22.
GenomeRNAii6146.
PROiP35268.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000116251.
CleanExiHS_RPL22.
ExpressionAtlasiP35268. baseline and differential.
GenevisibleiP35268. HS.

Family and domain databases

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

Entry informationi

Entry nameiRL22_HUMAN
AccessioniPrimary (citable) accession number: P35268
Secondary accession number(s): B2R495, Q6IBD1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 157 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

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

Keywords - Technical termi

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

Documents

  1. Human chromosome 1
    Human chromosome 1: 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.