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P47914 (RL29_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
60S ribosomal protein L29
Alternative name(s):
Cell surface heparin-binding protein HIP
Gene names
Name:RPL29
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length159 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the ribosomal protein L29e family.

Ontologies

Keywords
   DomainRepeat
   LigandHeparin-binding
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMAcetylation
Isopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

SRP-dependent cotranslational protein targeting to membrane

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

embryo implantation

Traceable author statement Ref.3. Source: ProtInc

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Traceable author statement. Source: Reactome

translation

Non-traceable author statement Ref.6. Source: UniProtKB

translational elongation

Traceable author statement. Source: Reactome

translational initiation

Traceable author statement. Source: Reactome

translational termination

Traceable author statement. Source: Reactome

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

viral transcription

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

cytosolic large ribosomal subunit

Inferred from direct assay Ref.6. Source: UniProtKB

   Molecular_functionRNA binding

Traceable author statement Ref.2. Source: ProtInc

heparin binding

Traceable author statement Ref.3. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

structural constituent of ribosome

Non-traceable author statement Ref.6. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DDX56Q9NY931EBI-714039,EBI-372376
PSTPIP1O435861EBI-714039,EBI-1050964

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 15915860S ribosomal protein L29
PRO_0000219134

Amino acid modifications

Modified residue51N6-methyllysine Ref.6
Modified residue331N6-acetyllysine Ref.8
Modified residue1421Phosphoserine Ref.9
Cross-link56Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7
Cross-link73Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7

Experimental info

Sequence conflict51K → R in BAF82227. Ref.4
Sequence conflict1201R → A in CAA89008. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P47914 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 2A0C31984EF4FF95

FASTA15917,752
        10         20         30         40         50         60 
MAKSKNHTTH NQSRKWHRNG IKKPRSQRYE SLKGVDPKFL RNMRFAKKHN KKGLKKMQAN 

        70         80         90        100        110        120 
NAKAMSARAE AIKALVKPKE VKPKIPKGVS RKLDRLAYIA HPKLGKRARA RIAKGLRLCR 

       130        140        150 
PKAKAKAKAK DQTKAQAAAP ASVPAQAPKR TQAPTKASE 

« Hide

References

« Hide 'large scale' references
[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]"A novel cDNA encoding a human homologue of ribosomal protein L29."
Law P.T., Tsui S.K.W., Lam W.Y., Luk S.C., Hwang D.M., Liew C.C., Lee C.-Y., Fung K.-P., Waye M.M.Y.
Biochim. Biophys. Acta 1305:105-108(1996) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Structures of the human and Drosophila 80S ribosome."
Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M., Wilson D.N., Beckmann R.
Nature 497:80-85(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS2845.1.
PIRS65784.
RefSeqNP_000983.1. NM_000992.2.
UniGeneHs.425125.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Belectron microscopy5.00b1-159[»]
ProteinModelPortalP47914.
SMRP47914. Positions 2-79.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112078. 75 interactions.
IntActP47914. 12 interactions.
MINTMINT-1375294.
STRING9606.ENSP00000294189.

PTM databases

PhosphoSiteP47914.

Proteomic databases

MaxQBP47914.
PaxDbP47914.
PRIDEP47914.

Protocols and materials databases

DNASU6159.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000294189; ENSP00000294189; ENSG00000162244.
ENST00000466397; ENSP00000418868; ENSG00000162244.
ENST00000475248; ENSP00000417048; ENSG00000162244.
ENST00000479017; ENSP00000418153; ENSG00000162244.
ENST00000492277; ENSP00000418346; ENSG00000162244.
ENST00000495383; ENSP00000420673; ENSG00000162244.
GeneID6159.
KEGGhsa:6159.
UCSCuc003dcs.3. human.

Organism-specific databases

CTD6159.
GeneCardsGC03M052029.
H-InvDBHIX0031209.
HGNCHGNC:10331. RPL29.
MIM601832. gene.
neXtProtNX_P47914.
PharmGKBPA34711.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG249125.
HOVERGENHBG000386.
InParanoidP47914.
KOK02905.
OMACRPKSQA.
OrthoDBEOG7JT70C.
PhylomeDBP47914.
TreeFamTF313858.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.
SignaLinkP47914.

Gene expression databases

ArrayExpressP47914.
BgeeP47914.
CleanExHS_RPL29.
GenevestigatorP47914.

Family and domain databases

InterProIPR002673. Ribosomal_L29e.
[Graphical view]
PANTHERPTHR12884. PTHR12884. 1 hit.
PfamPF01779. Ribosomal_L29e. 1 hit.
[Graphical view]
ProDomPD010314. Ribosomal_L29e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Other

ChiTaRSRPL29. human.
GeneWikiRPL29.
GenomeRNAi6159.
NextBio23919.
PROP47914.
SOURCESearch...

Entry information

Entry nameRL29_HUMAN
AccessionPrimary (citable) accession number: P47914
Secondary accession number(s): A8K0H3, B2R4M8, Q6IPY3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM