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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

  • 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

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_9491. Viral mRNA Translation.
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
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:10331. RPL29.

Subcellular locationi

GO - Cellular componenti

  • 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 methioninei1 – 11Removed1 Publication
Chaini2 – 15915860S ribosomal protein L29PRO_0000219134Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51N6-methyllysine1 Publication
Modified residuei33 – 331N6-acetyllysine1 Publication
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 – 1421Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP47914.
PaxDbiP47914.
PRIDEiP47914.

PTM databases

PhosphoSiteiP47914.

Expressioni

Gene expression databases

BgeeiP47914.
CleanExiHS_RPL29.
ExpressionAtlasiP47914. baseline.
GenevestigatoriP47914.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
DDX56Q9NY931EBI-714039,EBI-372376
PSTPIP1O435861EBI-714039,EBI-1050964

Protein-protein interaction databases

BioGridi112078. 54 interactions.
IntActiP47914. 12 interactions.
MINTiMINT-1375294.
STRINGi9606.ENSP00000294189.

Structurei

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L29e family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG249125.
GeneTreeiENSGT00390000007084.
HOVERGENiHBG000386.
InParanoidiP47914.
KOiK02905.
OMAiCRPKSQA.
OrthoDBiEOG7JT70C.
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.3. 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
4V6Xelectron microscopy5.00Cb1-159[»]
ProteinModelPortaliP47914.
SMRiP47914. Positions 2-76.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112078. 54 interactions.
IntActiP47914. 12 interactions.
MINTiMINT-1375294.
STRINGi9606.ENSP00000294189.

PTM databases

PhosphoSiteiP47914.

Polymorphism and mutation databases

BioMutaiRPL29.

Proteomic databases

MaxQBiP47914.
PaxDbiP47914.
PRIDEiP47914.

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.3. human.

Organism-specific databases

CTDi6159.
GeneCardsiGC03M052029.
H-InvDBHIX0031209.
HGNCiHGNC:10331. RPL29.
MIMi601832. gene.
neXtProtiNX_P47914.
PharmGKBiPA34711.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG249125.
GeneTreeiENSGT00390000007084.
HOVERGENiHBG000386.
InParanoidiP47914.
KOiK02905.
OMAiCRPKSQA.
OrthoDBiEOG7JT70C.
PhylomeDBiP47914.
TreeFamiTF313858.

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_9491. Viral mRNA Translation.
SignaLinkiP47914.

Miscellaneous databases

ChiTaRSiRPL29. human.
GeneWikiiRPL29.
GenomeRNAii6159.
NextBioi23919.
PROiP47914.
SOURCEiSearch...

Gene expression databases

BgeeiP47914.
CleanExiHS_RPL29.
ExpressionAtlasiP47914. baseline.
GenevestigatoriP47914.

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...

Publicationsi

« Hide 'large scale' publications
  1. Law P.T., Tsui S.K., Lee C.Y., Waye M.M.
    Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "cDNA cloning and expression of HIP, a novel cell surface heparan sulfate/heparin-binding protein of human uterine epithelial cells and cell lines."
    Liu S., Smith S.E., Julian J., Rohde L.H., Karin N.J., Carson D.D.
    J. Biol. Chem. 271:11817-11823(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain and Cerebellum.
  5. "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: Ovary and Pancreas.
  6. "Characterization and analysis of posttranslational modifications of the human large cytoplasmic ribosomal subunit proteins by mass spectrometry and Edman sequencing."
    Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R., Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B., Karpova G.G.
    J. Protein Chem. 22:249-258(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-15, IDENTIFICATION BY MASS SPECTROMETRY, METHYLATION AT LYS-5.
  7. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
    Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
    Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-56 AND LYS-73.
    Tissue: Mammary cancer.
  8. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

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: April 29, 2015
This is version 137 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

External Data

Dasty 3

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 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.