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Protein

60S ribosomal protein L31

Gene

RPL31

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
  • structural constituent of ribosome Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

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).

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L31
Gene namesi
Name:RPL31
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:10334. RPL31.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • cytosolic large ribosomal subunit Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34715.

Polymorphism and mutation databases

BioMutaiRPL31.
DMDMi51702807.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12512560S ribosomal protein L31PRO_0000153763Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei15 – 151PhosphoserineBy similarity
Modified residuei55 – 551N6-succinyllysineBy similarity
Modified residuei70 – 701N6-succinyllysineBy similarity
Modified residuei75 – 751N6-acetyllysine; alternateCombined sources
Modified residuei75 – 751N6-succinyllysine; alternateBy similarity
Modified residuei98 – 981PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP62899.
MaxQBiP62899.
PaxDbiP62899.
PeptideAtlasiP62899.
PRIDEiP62899.
TopDownProteomicsiP62899-1. [P62899-1]

2D gel databases

SWISS-2DPAGEP62899.

PTM databases

iPTMnetiP62899.
PhosphoSiteiP62899.
SwissPalmiP62899.

Expressioni

Gene expression databases

BgeeiENSG00000071082.
CleanExiHS_RPL31.
ExpressionAtlasiP62899. baseline and differential.
GenevisibleiP62899. HS.

Interactioni

Protein-protein interaction databases

BioGridi112079. 154 interactions.
IntActiP62899. 33 interactions.
MINTiMINT-5000327.
STRINGi9606.ENSP00000386717.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4UG0electron microscopy-Ld1-125[»]
4V6Xelectron microscopy5.00Cd1-125[»]
5AJ0electron microscopy3.50Ad1-125[»]
ProteinModelPortaliP62899.
SMRiP62899. Positions 22-102.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L31e family.Curated

Phylogenomic databases

eggNOGiKOG0893. Eukaryota.
COG2097. LUCA.
GeneTreeiENSGT00390000005200.
HOGENOMiHOG000216660.
HOVERGENiHBG001549.
InParanoidiP62899.
KOiK02910.
OMAiEMGTNDV.
PhylomeDBiP62899.
TreeFamiTF314858.

Family and domain databases

CDDicd00463. Ribosomal_L31e. 1 hit.
Gene3Di3.10.440.10. 1 hit.
InterProiIPR000054. Ribosomal_L31e.
IPR020052. Ribosomal_L31e_CS.
IPR023621. Ribosomal_L31e_dom.
[Graphical view]
PANTHERiPTHR10956. PTHR10956. 1 hit.
PfamiPF01198. Ribosomal_L31e. 1 hit.
[Graphical view]
ProDomiPD006030. Ribosomal_L31e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM01380. Ribosomal_L31e. 1 hit.
[Graphical view]
SUPFAMiSSF54575. SSF54575. 1 hit.
PROSITEiPS01144. RIBOSOMAL_L31E. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P62899-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAPAKKGGEK KKGRSAINEV VTREYTINIH KRIHGVGFKK RAPRALKEIR
60 70 80 90 100
KFAMKEMGTP DVRIDTRLNK AVWAKGIRNV PYRIRVRLSR KRNEDEDSPN
110 120
KLYTLVTYVP VTTFKNLQTV NVDEN
Length:125
Mass (Da):14,463
Last modified:August 31, 2004 - v1
Checksum:iBA9DBE79B9E1C071
GO
Isoform 2 (identifier: P62899-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     116-125: NLQTVNVDEN → ISVLNSVTVAKSP

Note: No experimental confirmation available.
Show »
Length:128
Mass (Da):14,632
Checksum:i73178D90B1AE79A8
GO
Isoform 3 (identifier: P62899-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     116-125: NLQTVNVDEN → SKFSIP

Note: No experimental confirmation available.
Show »
Length:121
Mass (Da):13,995
Checksum:iBAD3547E9019CF61
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei116 – 12510NLQTVNVDEN → ISVLNSVTVAKSP in isoform 2. 1 PublicationVSP_042572
Alternative sequencei116 – 12510NLQTVNVDEN → SKFSIP in isoform 3. 1 PublicationVSP_043224

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15940 mRNA. Translation: CAA34066.1.
AB061830 Genomic DNA. Translation: BAB79468.1.
AK297483 mRNA. Translation: BAH12588.1.
AC016738 Genomic DNA. Translation: AAY14823.1.
CH471127 Genomic DNA. Translation: EAX01826.1.
CH471127 Genomic DNA. Translation: EAX01827.1.
CH471127 Genomic DNA. Translation: EAX01829.1.
BC017343 mRNA. Translation: AAH17343.1.
BC070210 mRNA. Translation: AAH70210.1.
BC070373 mRNA. Translation: AAH70373.1.
X69181 mRNA. Translation: CAA48925.1.
CCDSiCCDS2049.1. [P62899-1]
CCDS46373.1. [P62899-2]
CCDS46374.1. [P62899-3]
PIRiS05576. R5HU31.
RefSeqiNP_000984.1. NM_000993.4. [P62899-1]
NP_001092047.1. NM_001098577.2. [P62899-2]
NP_001093163.1. NM_001099693.1. [P62899-3]
UniGeneiHs.469473.

Genome annotation databases

EnsembliENST00000264258; ENSP00000264258; ENSG00000071082. [P62899-1]
ENST00000409028; ENSP00000386717; ENSG00000071082. [P62899-2]
ENST00000409320; ENSP00000387163; ENSG00000071082. [P62899-3]
ENST00000409733; ENSP00000386681; ENSG00000071082. [P62899-1]
GeneIDi6160.
KEGGihsa:6160.
UCSCiuc002taq.5. human. [P62899-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15940 mRNA. Translation: CAA34066.1.
AB061830 Genomic DNA. Translation: BAB79468.1.
AK297483 mRNA. Translation: BAH12588.1.
AC016738 Genomic DNA. Translation: AAY14823.1.
CH471127 Genomic DNA. Translation: EAX01826.1.
CH471127 Genomic DNA. Translation: EAX01827.1.
CH471127 Genomic DNA. Translation: EAX01829.1.
BC017343 mRNA. Translation: AAH17343.1.
BC070210 mRNA. Translation: AAH70210.1.
BC070373 mRNA. Translation: AAH70373.1.
X69181 mRNA. Translation: CAA48925.1.
CCDSiCCDS2049.1. [P62899-1]
CCDS46373.1. [P62899-2]
CCDS46374.1. [P62899-3]
PIRiS05576. R5HU31.
RefSeqiNP_000984.1. NM_000993.4. [P62899-1]
NP_001092047.1. NM_001098577.2. [P62899-2]
NP_001093163.1. NM_001099693.1. [P62899-3]
UniGeneiHs.469473.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4UG0electron microscopy-Ld1-125[»]
4V6Xelectron microscopy5.00Cd1-125[»]
5AJ0electron microscopy3.50Ad1-125[»]
ProteinModelPortaliP62899.
SMRiP62899. Positions 22-102.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112079. 154 interactions.
IntActiP62899. 33 interactions.
MINTiMINT-5000327.
STRINGi9606.ENSP00000386717.

PTM databases

iPTMnetiP62899.
PhosphoSiteiP62899.
SwissPalmiP62899.

Polymorphism and mutation databases

BioMutaiRPL31.
DMDMi51702807.

2D gel databases

SWISS-2DPAGEP62899.

Proteomic databases

EPDiP62899.
MaxQBiP62899.
PaxDbiP62899.
PeptideAtlasiP62899.
PRIDEiP62899.
TopDownProteomicsiP62899-1. [P62899-1]

Protocols and materials databases

DNASUi6160.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264258; ENSP00000264258; ENSG00000071082. [P62899-1]
ENST00000409028; ENSP00000386717; ENSG00000071082. [P62899-2]
ENST00000409320; ENSP00000387163; ENSG00000071082. [P62899-3]
ENST00000409733; ENSP00000386681; ENSG00000071082. [P62899-1]
GeneIDi6160.
KEGGihsa:6160.
UCSCiuc002taq.5. human. [P62899-1]

Organism-specific databases

CTDi6160.
GeneCardsiRPL31.
H-InvDBHIX0017577.
HGNCiHGNC:10334. RPL31.
neXtProtiNX_P62899.
PharmGKBiPA34715.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0893. Eukaryota.
COG2097. LUCA.
GeneTreeiENSGT00390000005200.
HOGENOMiHOG000216660.
HOVERGENiHBG001549.
InParanoidiP62899.
KOiK02910.
OMAiEMGTNDV.
PhylomeDBiP62899.
TreeFamiTF314858.

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).

Miscellaneous databases

ChiTaRSiRPL31. human.
GeneWikii60S_ribosomal_protein_L31.
GenomeRNAii6160.
PROiP62899.

Gene expression databases

BgeeiENSG00000071082.
CleanExiHS_RPL31.
ExpressionAtlasiP62899. baseline and differential.
GenevisibleiP62899. HS.

Family and domain databases

CDDicd00463. Ribosomal_L31e. 1 hit.
Gene3Di3.10.440.10. 1 hit.
InterProiIPR000054. Ribosomal_L31e.
IPR020052. Ribosomal_L31e_CS.
IPR023621. Ribosomal_L31e_dom.
[Graphical view]
PANTHERiPTHR10956. PTHR10956. 1 hit.
PfamiPF01198. Ribosomal_L31e. 1 hit.
[Graphical view]
ProDomiPD006030. Ribosomal_L31e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM01380. Ribosomal_L31e. 1 hit.
[Graphical view]
SUPFAMiSSF54575. SSF54575. 1 hit.
PROSITEiPS01144. RIBOSOMAL_L31E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRL31_HUMAN
AccessioniPrimary (citable) accession number: P62899
Secondary accession number(s): B7Z4K2
, D3DVJ4, P12947, Q53SQ5, Q6IRZ0, Q6LBJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: September 7, 2016
This is version 129 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. 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.