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P47914

- RL29_HUMAN

UniProt

P47914 - RL29_HUMAN

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Protein
60S ribosomal protein L29
Gene
RPL29
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. RNA binding Source: ProtInc
  2. heparin binding Source: ProtInc
  3. poly(A) RNA binding Source: UniProtKB
  4. structural constituent of ribosome Source: UniProtKB

GO - Biological processi

  1. RNA metabolic process Source: Reactome
  2. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  3. cellular protein metabolic process Source: Reactome
  4. embryo implantation Source: ProtInc
  5. gene expression Source: Reactome
  6. mRNA metabolic process Source: Reactome
  7. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  8. translation Source: UniProtKB
  9. translational elongation Source: Reactome
  10. translational initiation Source: Reactome
  11. translational termination Source: Reactome
  12. viral life cycle Source: Reactome
  13. viral process Source: Reactome
  14. viral transcription Source: Reactome
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: Chromosome 3

Organism-specific databases

HGNCiHGNC:10331. RPL29.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. cytosolic large ribosomal subunit Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34711.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 15915860S ribosomal protein L29
PRO_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 – 1421Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP47914.
PaxDbiP47914.
PRIDEiP47914.

PTM databases

PhosphoSiteiP47914.

Expressioni

Gene expression databases

ArrayExpressiP47914.
BgeeiP47914.
CleanExiHS_RPL29.
GenevestigatoriP47914.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

BioGridi112078. 52 interactions.
IntActiP47914. 12 interactions.
MINTiMINT-1375294.
STRINGi9606.ENSP00000294189.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Belectron microscopy5.00b1-159[»]
ProteinModelPortaliP47914.
SMRiP47914. Positions 2-79.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG249125.
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

MAKSKNHTTH NQSRKWHRNG IKKPRSQRYE SLKGVDPKFL RNMRFAKKHN    50
KKGLKKMQAN NAKAMSARAE AIKALVKPKE VKPKIPKGVS RKLDRLAYIA 100
HPKLGKRARA RIAKGLRLCR PKAKAKAKAK DQTKAQAAAP ASVPAQAPKR 150
TQAPTKASE 159
Length:159
Mass (Da):17,752
Last modified:January 23, 2007 - v2
Checksum:i2A0C31984EF4FF95
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51K → R in BAF82227. 1 Publication
Sequence conflicti120 – 1201R → A in CAA89008. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS2845.1.
PIRi S65784.
RefSeqi NP_000983.1. NM_000992.2.
UniGenei Hs.425125.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3J3B electron microscopy 5.00 b 1-159 [» ]
ProteinModelPortali P47914.
SMRi P47914. Positions 2-79.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112078. 52 interactions.
IntActi P47914. 12 interactions.
MINTi MINT-1375294.
STRINGi 9606.ENSP00000294189.

PTM databases

PhosphoSitei P47914.

Proteomic databases

MaxQBi P47914.
PaxDbi P47914.
PRIDEi P47914.

Protocols and materials databases

DNASUi 6159.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000294189 ; ENSP00000294189 ; ENSG00000162244 .
ENST00000466397 ; ENSP00000418868 ; ENSG00000162244 .
ENST00000475248 ; ENSP00000417048 ; ENSG00000162244 .
ENST00000479017 ; ENSP00000418153 ; ENSG00000162244 .
ENST00000492277 ; ENSP00000418346 ; ENSG00000162244 .
ENST00000495383 ; ENSP00000420673 ; ENSG00000162244 .
GeneIDi 6159.
KEGGi hsa:6159.
UCSCi uc003dcs.3. human.

Organism-specific databases

CTDi 6159.
GeneCardsi GC03M052029.
H-InvDB HIX0031209.
HGNCi HGNC:10331. RPL29.
MIMi 601832. gene.
neXtProti NX_P47914.
PharmGKBi PA34711.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG249125.
HOVERGENi HBG000386.
InParanoidi P47914.
KOi K02905.
OMAi CRPKSQA.
OrthoDBi EOG7JT70C.
PhylomeDBi P47914.
TreeFami TF313858.

Enzyme and pathway databases

Reactomei REACT_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.
SignaLinki P47914.

Miscellaneous databases

ChiTaRSi RPL29. human.
GeneWikii RPL29.
GenomeRNAii 6159.
NextBioi 23919.
PROi P47914.
SOURCEi Search...

Gene expression databases

ArrayExpressi P47914.
Bgeei P47914.
CleanExi HS_RPL29.
Genevestigatori P47914.

Family and domain databases

InterProi IPR002673. Ribosomal_L29e.
[Graphical view ]
PANTHERi PTHR12884. PTHR12884. 1 hit.
Pfami PF01779. Ribosomal_L29e. 1 hit.
[Graphical view ]
ProDomi PD010314. Ribosomal_L29e. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
ProtoNeti Search...

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. 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: September 3, 2014
This is version 131 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

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