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Protein

60S ribosomal protein L29

Gene

RPL29

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

Functioni

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • heparin binding Source: ProtInc
  • 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

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).
SignaLinkiP47914.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L29
Alternative name(s):
Cell surface heparin-binding protein HIP
Gene namesi
Name:RPL29
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:10331. RPL29.

Subcellular locationi

GO - Cellular componenti

  • cell-cell adherens junction Source: BHF-UCL
  • cytosol Source: Reactome
  • cytosolic large ribosomal subunit Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34711.

Polymorphism and mutation databases

BioMutaiRPL29.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 15915860S ribosomal protein L29PRO_0000219134Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51N6-methyllysine1 Publication
Modified residuei31 – 311PhosphoserineCombined sources
Modified residuei33 – 331N6-acetyllysineCombined sources
Cross-linki56 – 56Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki73 – 73Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei142 – 1421PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP47914.
MaxQBiP47914.
PaxDbiP47914.
PeptideAtlasiP47914.
PRIDEiP47914.
TopDownProteomicsiP47914.

PTM databases

iPTMnetiP47914.
PhosphoSiteiP47914.
SwissPalmiP47914.

Expressioni

Gene expression databases

BgeeiENSG00000162244.
CleanExiHS_RPL29.
ExpressionAtlasiP47914. baseline and differential.
GenevisibleiP47914. HS.

Organism-specific databases

HPAiHPA069064.

Interactioni

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL

Protein-protein interaction databases

BioGridi112078. 65 interactions.
IntActiP47914. 15 interactions.
MINTiMINT-1375294.
STRINGi9606.ENSP00000294189.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4UG0electron microscopy-Lb1-159[»]
4V6Xelectron microscopy5.00Cb1-159[»]
5AJ0electron microscopy3.50Ab1-159[»]
ProteinModelPortaliP47914.
SMRiP47914. Positions 2-76.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L29e family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3504. Eukaryota.
ENOG4112428. LUCA.
GeneTreeiENSGT00390000007084.
HOVERGENiHBG000386.
InParanoidiP47914.
KOiK02905.
OMAiCRPKSQA.
OrthoDBiEOG091G15LL.
PhylomeDBiP47914.
TreeFamiTF313858.

Family and domain databases

InterProiIPR002673. Ribosomal_L29e.
[Graphical view]
PANTHERiPTHR12884. PTHR12884. 1 hit.
PfamiPF01779. Ribosomal_L29e. 1 hit.
[Graphical view]
ProDomiPD010314. Ribosomal_L29e. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

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

P47914-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKSKNHTTH NQSRKWHRNG IKKPRSQRYE SLKGVDPKFL RNMRFAKKHN
60 70 80 90 100
KKGLKKMQAN NAKAMSARAE AIKALVKPKE VKPKIPKGVS RKLDRLAYIA
110 120 130 140 150
HPKLGKRARA RIAKGLRLCR PKAKAKAKAK DQTKAQAAAP ASVPAQAPKR

TQAPTKASE
Length:159
Mass (Da):17,752
Last modified:January 23, 2007 - v2
Checksum:i2A0C31984EF4FF95
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51K → R in BAF82227 (PubMed:14702039).Curated
Sequence conflicti120 – 1201R → A in CAA89008 (PubMed:8597591).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10248 mRNA. Translation: AAC50499.1.
Z49148 mRNA. Translation: CAA89008.1.
U49083 mRNA. Translation: AAC50647.1.
AK289538 mRNA. Translation: BAF82227.1.
AK311884 mRNA. Translation: BAG34825.1.
BC008926 mRNA. Translation: AAH08926.1.
BC070190 mRNA. Translation: AAH70190.1.
BC070481 mRNA. Translation: AAH70481.1.
BC071663 mRNA. Translation: AAH71663.1.
CCDSiCCDS2845.1.
PIRiS65784.
RefSeqiNP_000983.1. NM_000992.2.
UniGeneiHs.425125.

Genome annotation databases

EnsembliENST00000294189; ENSP00000294189; ENSG00000162244.
ENST00000466397; ENSP00000418868; ENSG00000162244.
ENST00000475248; ENSP00000417048; ENSG00000162244.
ENST00000479017; ENSP00000418153; ENSG00000162244.
ENST00000492277; ENSP00000418346; ENSG00000162244.
ENST00000495383; ENSP00000420673; ENSG00000162244.
GeneIDi6159.
KEGGihsa:6159.
UCSCiuc003dcs.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10248 mRNA. Translation: AAC50499.1.
Z49148 mRNA. Translation: CAA89008.1.
U49083 mRNA. Translation: AAC50647.1.
AK289538 mRNA. Translation: BAF82227.1.
AK311884 mRNA. Translation: BAG34825.1.
BC008926 mRNA. Translation: AAH08926.1.
BC070190 mRNA. Translation: AAH70190.1.
BC070481 mRNA. Translation: AAH70481.1.
BC071663 mRNA. Translation: AAH71663.1.
CCDSiCCDS2845.1.
PIRiS65784.
RefSeqiNP_000983.1. NM_000992.2.
UniGeneiHs.425125.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4UG0electron microscopy-Lb1-159[»]
4V6Xelectron microscopy5.00Cb1-159[»]
5AJ0electron microscopy3.50Ab1-159[»]
ProteinModelPortaliP47914.
SMRiP47914. Positions 2-76.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112078. 65 interactions.
IntActiP47914. 15 interactions.
MINTiMINT-1375294.
STRINGi9606.ENSP00000294189.

PTM databases

iPTMnetiP47914.
PhosphoSiteiP47914.
SwissPalmiP47914.

Polymorphism and mutation databases

BioMutaiRPL29.

Proteomic databases

EPDiP47914.
MaxQBiP47914.
PaxDbiP47914.
PeptideAtlasiP47914.
PRIDEiP47914.
TopDownProteomicsiP47914.

Protocols and materials databases

DNASUi6159.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000294189; ENSP00000294189; ENSG00000162244.
ENST00000466397; ENSP00000418868; ENSG00000162244.
ENST00000475248; ENSP00000417048; ENSG00000162244.
ENST00000479017; ENSP00000418153; ENSG00000162244.
ENST00000492277; ENSP00000418346; ENSG00000162244.
ENST00000495383; ENSP00000420673; ENSG00000162244.
GeneIDi6159.
KEGGihsa:6159.
UCSCiuc003dcs.4. human.

Organism-specific databases

CTDi6159.
GeneCardsiRPL29.
H-InvDBHIX0031209.
HGNCiHGNC:10331. RPL29.
HPAiHPA069064.
MIMi601832. gene.
neXtProtiNX_P47914.
PharmGKBiPA34711.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3504. Eukaryota.
ENOG4112428. LUCA.
GeneTreeiENSGT00390000007084.
HOVERGENiHBG000386.
InParanoidiP47914.
KOiK02905.
OMAiCRPKSQA.
OrthoDBiEOG091G15LL.
PhylomeDBiP47914.
TreeFamiTF313858.

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).
SignaLinkiP47914.

Miscellaneous databases

ChiTaRSiRPL29. human.
GeneWikiiRPL29.
GenomeRNAii6159.
PROiP47914.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000162244.
CleanExiHS_RPL29.
ExpressionAtlasiP47914. baseline and differential.
GenevisibleiP47914. HS.

Family and domain databases

InterProiIPR002673. Ribosomal_L29e.
[Graphical view]
PANTHERiPTHR12884. PTHR12884. 1 hit.
PfamiPF01779. Ribosomal_L29e. 1 hit.
[Graphical view]
ProDomiPD010314. Ribosomal_L29e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Entry informationi

Entry nameiRL29_HUMAN
AccessioniPrimary (citable) accession number: P47914
Secondary accession number(s): A8K0H3, B2R4M8, Q6IPY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 151 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

Keywords - Technical termi

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

Documents

  1. Human chromosome 3
    Human chromosome 3: 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.