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Protein

60S ribosomal protein L10

Gene

RPL10

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
  • structural constituent of ribosome Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciZFISH:ENSG00000147403-MONOMER.
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 and cytosol.
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).
SIGNORiP27635.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L10
Alternative name(s):
Laminin receptor homolog
Protein QM
Tumor suppressor QM
Gene namesi
Name:RPL10
Synonyms:DXS648E, QM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:10298. RPL10.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • cytosolic large ribosomal subunit Source: UniProtKB
  • endoplasmic reticulum Source: LIFEdb
  • membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Autism, X-linked 5 (AUTSX5)2 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry. RPL10 is involved in autism only in rare cases. Two hypomorphic variants affecting the translation process have been found in families with autism spectrum disorders, suggesting that aberrant translation may play a role in disease mechanisms.
Disease descriptionA complex multifactorial, pervasive developmental disorder characterized by impairments in reciprocal social interaction and communication, restricted and stereotyped patterns of interests and activities, and the presence of developmental abnormalities by 3 years of age. Most individuals with autism also manifest moderate mental retardation.
See also OMIM:300847
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_027795206L → M in AUTSX5. 1 Publication1
Natural variantiVAR_027796213H → Q in AUTSX5. 2 Publications1

Keywords - Diseasei

Autism, Autism spectrum disorder, Disease mutation

Organism-specific databases

DisGeNETi6134.
MalaCardsiRPL10.
MIMi300847. phenotype.
Orphaneti106. Autism.
PharmGKBiPA34660.

Polymorphism and mutation databases

BioMutaiRPL10.
DMDMi148887414.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001471052 – 21460S ribosomal protein L10Add BLAST213

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei32CitrullineBy similarity1
Cross-linki188Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Post-translational modificationi

Citrullinated by PADI4.By similarity

Keywords - PTMi

Citrullination, Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiP27635.
MaxQBiP27635.
PaxDbiP27635.
PeptideAtlasiP27635.
PRIDEiP27635.
TopDownProteomicsiP27635.

PTM databases

iPTMnetiP27635.
PhosphoSitePlusiP27635.
SwissPalmiP27635.

Miscellaneous databases

PMAP-CutDBP27635.

Expressioni

Developmental stagei

Down-regulated during adipocyte, kidney, and heart differentiation.

Gene expression databases

BgeeiENSG00000147403.
CleanExiHS_RPL10.
ExpressionAtlasiP27635. baseline and differential.
GenevisibleiP27635. HS.

Organism-specific databases

HPAiCAB010339.
HPA011311.

Interactioni

Subunit structurei

Component of the large ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains about 33 different proteins and 1 molecule of RNA (18S). The 60S subunit contains about 49 different proteins and 3 molecules of RNA (28S, 5.8S and 5S).

Binary interactionsi

WithEntry#Exp.IntActNotes
SRCP129316EBI-352398,EBI-621482

Protein-protein interaction databases

BioGridi112054. 347 interactors.
DIPiDIP-1133N.
IntActiP27635. 291 interactors.
MINTiMINT-1153266.
STRINGi9606.ENSP00000341730.

Structurei

Secondary structure

1214
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni43 – 45Combined sources3
Beta strandi48 – 54Combined sources7
Beta strandi58 – 61Combined sources4
Helixi62 – 80Combined sources19
Beta strandi84 – 89Combined sources6
Beta strandi126 – 129Combined sources4
Beta strandi133 – 140Combined sources8
Helixi142 – 144Combined sources3
Helixi145 – 155Combined sources11
Helixi156 – 158Combined sources3
Beta strandi159 – 161Combined sources3
Beta strandi163 – 169Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2PA2X-ray2.50A/B34-182[»]
5AJ0electron microscopy3.50AI1-214[»]
ProteinModelPortaliP27635.
SMRiP27635.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27635.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L10e family.Curated

Phylogenomic databases

eggNOGiKOG0857. Eukaryota.
COG0197. LUCA.
HOVERGENiHBG002287.
InParanoidiP27635.
KOiK02866.
OrthoDBiEOG091G0H9M.
PhylomeDBiP27635.
TreeFamiTF300082.

Family and domain databases

CDDicd01433. Ribosomal_L16_L10e. 1 hit.
Gene3Di3.90.1170.10. 1 hit.
InterProiIPR001197. Ribosomal_L10e.
IPR016180. Ribosomal_L10e/L16.
IPR018255. Ribosomal_L10e_CS.
[Graphical view]
PfamiPF00252. Ribosomal_L16. 1 hit.
[Graphical view]
PIRSFiPIRSF005590. Ribosomal_L10. 1 hit.
SUPFAMiSSF54686. SSF54686. 1 hit.
TIGRFAMsiTIGR00279. uL16_euk_arch. 1 hit.
PROSITEiPS01257. RIBOSOMAL_L10E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P27635-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRRPARCYR YCKNKPYPKS RFCRGVPDAK IRIFDLGRKK AKVDEFPLCG
60 70 80 90 100
HMVSDEYEQL SSEALEAARI CANKYMVKSC GKDGFHIRVR LHPFHVIRIN
110 120 130 140 150
KMLSCAGADR LQTGMRGAFG KPQGTVARVH IGQVIMSIRT KLQNKEHVIE
160 170 180 190 200
ALRRAKFKFP GRQKIHISKK WGFTKFNADE FEDMVAEKRL IPDGCGVKYI
210
PNRGPLDKWR ALHS
Length:214
Mass (Da):24,604
Last modified:June 12, 2007 - v4
Checksum:i0860CECC91DF74FE
GO

Sequence cautioni

The sequence AAB22173 differs from that shown. Reason: Frameshift at position 124.Curated
The sequence CAM45852 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAM45853 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti23Missing in AAL88713 (PubMed:12138090).Curated1
Sequence conflicti157F → L in BAD97029 (Ref. 8) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_006922202N → S.10 PublicationsCorresponds to variant rs12012747dbSNPEnsembl.1
Natural variantiVAR_027795206L → M in AUTSX5. 1 Publication1
Natural variantiVAR_027796213H → Q in AUTSX5. 2 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64241 mRNA. Translation: AAA63253.1.
M81806 Genomic DNA. Translation: AAA36021.1.
M73791 mRNA. Translation: AAA36378.1.
S64169, S64168 Genomic DNA. Translation: AAB27665.1.
AF486812 mRNA. Translation: AAL88713.1.
DQ369703 mRNA. Translation: ABC88559.1.
DQ369704 mRNA. Translation: ABC88560.1.
DQ369705 mRNA. Translation: ABC88561.1.
DQ369706 mRNA. Translation: ABC88562.1.
DQ369707 mRNA. Translation: ABC88563.1.
DQ369708 mRNA. Translation: ABC88564.1.
DQ369709 mRNA. Translation: ABC88565.1.
DQ369710 mRNA. Translation: ABC88566.1.
DQ369711 mRNA. Translation: ABC88567.1.
DQ369712 mRNA. Translation: ABC88568.1.
DQ369713 mRNA. Translation: ABC88569.1.
DQ369714 mRNA. Translation: ABC88570.1.
DQ369715 mRNA. Translation: ABC88571.1.
DQ369716 mRNA. Translation: ABC88572.1.
CR456797 mRNA. Translation: CAG33078.1.
CR542069 mRNA. Translation: CAG46866.1.
AK223309 mRNA. Translation: BAD97029.1.
L44140 Genomic DNA. Translation: AAA92646.1.
BX936347, BX936346 Genomic DNA. Translation: CAI43214.1.
BX936346, BX936347 Genomic DNA. Translation: CAI43230.1.
BX936347, BX936346 Genomic DNA. Translation: CAM45852.1. Sequence problems.
BX936346, BX936347 Genomic DNA. Translation: CAM45853.1. Sequence problems.
CH471172 Genomic DNA. Translation: EAW72737.1.
CH471172 Genomic DNA. Translation: EAW72739.1.
BC003358 mRNA. Translation: AAH03358.1.
BC026276 mRNA. Translation: AAH26276.1.
BC071918 mRNA. Translation: AAH71918.1.
S35960 mRNA. Translation: AAB22173.1. Frameshift.
AB007170 Genomic DNA. Translation: BAA28595.1.
CCDSiCCDS14746.1.
PIRiA42735.
RefSeqiNP_001243506.2. NM_001256577.2.
NP_001243509.2. NM_001256580.2.
NP_001290553.1. NM_001303624.1.
NP_001290554.1. NM_001303625.1.
NP_001290555.1. NM_001303626.1.
NP_006004.3. NM_006013.4.
UniGeneiHs.534404.
Hs.739235.

Genome annotation databases

EnsembliENST00000344746; ENSP00000341730; ENSG00000147403.
ENST00000369817; ENSP00000358832; ENSG00000147403.
ENST00000424325; ENSP00000413436; ENSG00000147403.
GeneIDi6134.
KEGGihsa:6134.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64241 mRNA. Translation: AAA63253.1.
M81806 Genomic DNA. Translation: AAA36021.1.
M73791 mRNA. Translation: AAA36378.1.
S64169, S64168 Genomic DNA. Translation: AAB27665.1.
AF486812 mRNA. Translation: AAL88713.1.
DQ369703 mRNA. Translation: ABC88559.1.
DQ369704 mRNA. Translation: ABC88560.1.
DQ369705 mRNA. Translation: ABC88561.1.
DQ369706 mRNA. Translation: ABC88562.1.
DQ369707 mRNA. Translation: ABC88563.1.
DQ369708 mRNA. Translation: ABC88564.1.
DQ369709 mRNA. Translation: ABC88565.1.
DQ369710 mRNA. Translation: ABC88566.1.
DQ369711 mRNA. Translation: ABC88567.1.
DQ369712 mRNA. Translation: ABC88568.1.
DQ369713 mRNA. Translation: ABC88569.1.
DQ369714 mRNA. Translation: ABC88570.1.
DQ369715 mRNA. Translation: ABC88571.1.
DQ369716 mRNA. Translation: ABC88572.1.
CR456797 mRNA. Translation: CAG33078.1.
CR542069 mRNA. Translation: CAG46866.1.
AK223309 mRNA. Translation: BAD97029.1.
L44140 Genomic DNA. Translation: AAA92646.1.
BX936347, BX936346 Genomic DNA. Translation: CAI43214.1.
BX936346, BX936347 Genomic DNA. Translation: CAI43230.1.
BX936347, BX936346 Genomic DNA. Translation: CAM45852.1. Sequence problems.
BX936346, BX936347 Genomic DNA. Translation: CAM45853.1. Sequence problems.
CH471172 Genomic DNA. Translation: EAW72737.1.
CH471172 Genomic DNA. Translation: EAW72739.1.
BC003358 mRNA. Translation: AAH03358.1.
BC026276 mRNA. Translation: AAH26276.1.
BC071918 mRNA. Translation: AAH71918.1.
S35960 mRNA. Translation: AAB22173.1. Frameshift.
AB007170 Genomic DNA. Translation: BAA28595.1.
CCDSiCCDS14746.1.
PIRiA42735.
RefSeqiNP_001243506.2. NM_001256577.2.
NP_001243509.2. NM_001256580.2.
NP_001290553.1. NM_001303624.1.
NP_001290554.1. NM_001303625.1.
NP_001290555.1. NM_001303626.1.
NP_006004.3. NM_006013.4.
UniGeneiHs.534404.
Hs.739235.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2PA2X-ray2.50A/B34-182[»]
5AJ0electron microscopy3.50AI1-214[»]
ProteinModelPortaliP27635.
SMRiP27635.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112054. 347 interactors.
DIPiDIP-1133N.
IntActiP27635. 291 interactors.
MINTiMINT-1153266.
STRINGi9606.ENSP00000341730.

PTM databases

iPTMnetiP27635.
PhosphoSitePlusiP27635.
SwissPalmiP27635.

Polymorphism and mutation databases

BioMutaiRPL10.
DMDMi148887414.

Proteomic databases

EPDiP27635.
MaxQBiP27635.
PaxDbiP27635.
PeptideAtlasiP27635.
PRIDEiP27635.
TopDownProteomicsiP27635.

Protocols and materials databases

DNASUi6134.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000344746; ENSP00000341730; ENSG00000147403.
ENST00000369817; ENSP00000358832; ENSG00000147403.
ENST00000424325; ENSP00000413436; ENSG00000147403.
GeneIDi6134.
KEGGihsa:6134.

Organism-specific databases

CTDi6134.
DisGeNETi6134.
GeneCardsiRPL10.
GeneReviewsiRPL10.
H-InvDBHIX0017152.
HIX0202878.
HGNCiHGNC:10298. RPL10.
HPAiCAB010339.
HPA011311.
MalaCardsiRPL10.
MIMi300847. phenotype.
312173. gene.
neXtProtiNX_P27635.
Orphaneti106. Autism.
PharmGKBiPA34660.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0857. Eukaryota.
COG0197. LUCA.
HOVERGENiHBG002287.
InParanoidiP27635.
KOiK02866.
OrthoDBiEOG091G0H9M.
PhylomeDBiP27635.
TreeFamiTF300082.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000147403-MONOMER.
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 and cytosol.
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).
SIGNORiP27635.

Miscellaneous databases

ChiTaRSiRPL10. human.
EvolutionaryTraceiP27635.
GeneWikiiRPL10.
GenomeRNAii6134.
PMAP-CutDBP27635.
PROiP27635.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000147403.
CleanExiHS_RPL10.
ExpressionAtlasiP27635. baseline and differential.
GenevisibleiP27635. HS.

Family and domain databases

CDDicd01433. Ribosomal_L16_L10e. 1 hit.
Gene3Di3.90.1170.10. 1 hit.
InterProiIPR001197. Ribosomal_L10e.
IPR016180. Ribosomal_L10e/L16.
IPR018255. Ribosomal_L10e_CS.
[Graphical view]
PfamiPF00252. Ribosomal_L16. 1 hit.
[Graphical view]
PIRSFiPIRSF005590. Ribosomal_L10. 1 hit.
SUPFAMiSSF54686. SSF54686. 1 hit.
TIGRFAMsiTIGR00279. uL16_euk_arch. 1 hit.
PROSITEiPS01257. RIBOSOMAL_L10E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRL10_HUMAN
AccessioniPrimary (citable) accession number: P27635
Secondary accession number(s): A3KQT0
, D3DWW6, Q16470, Q2HXT7, Q53FH7, Q6FGN8, Q8TDA5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: June 12, 2007
Last modified: November 30, 2016
This is version 176 of the entry and version 4 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

Keywords - Technical termi

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

Documents

  1. Human chromosome X
    Human chromosome X: 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

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.