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P62888 (RL30_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 98. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
60S ribosomal protein L30
Gene names
Name:RPL30
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length115 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the ribosomal protein L30e family.

Ontologies

Keywords
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
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

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 PubMed 12962325. 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_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

cytosolic large ribosomal subunit

Inferred from direct assay PubMed 12962325. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337PubMed 23376485. Source: UniProt

nucleus

Inferred from direct assay PubMed 22720776. Source: UniProt

   Molecular_functionRNA binding

Traceable author statement PubMed 1577483. Source: UniProtKB

poly(A) RNA binding

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

protein binding

Inferred from physical interaction PubMed 22720776. Source: UniProt

structural constituent of ribosome

Non-traceable author statement PubMed 12962325. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11511560S ribosomal protein L30 HAMAP-Rule MF_00481
PRO_0000146120

Amino acid modifications

Modified residue101Phosphoserine Ref.7 Ref.9 Ref.11
Modified residue261N6-acetyllysine Ref.8

Secondary structure

............... 115
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P62888 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 95186B081E39748C

FASTA11512,784
        10         20         30         40         50         60 
MVAAKKTKKS LESINSRLQL VMKSGKYVLG YKQTLKMIRQ GKAKLVILAN NCPALRKSEI 

        70         80         90        100        110 
EYYAMLAKTG VHHYSGNNIE LGTACGKYYR VCTLAIIDPG DSDIIRSMPE QTGEK 

« Hide

References

« Hide 'large scale' references
[1]Filipenko M.L., Karpova G.G.
Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[2]Bhat K.S.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The human ribosomal protein genes: sequencing and comparative analysis of 73 genes."
Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.
Genome Res. 12:379-390(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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: Embryonic stem cell and Mammary gland.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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-26, 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-10, 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]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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].
[13]"Crystallization and preliminary X-ray structure analysis of human ribosomal protein L30e."
Kawaguchi A., Ose T., Yao M., Tanaka I.
Acta Crystallogr. F 67:1516-1518(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L05095 mRNA. Translation: AAC15858.1.
X79238 mRNA. Translation: CAA55820.1.
AB070559 Genomic DNA. Translation: BAB79491.1.
AK312102 mRNA. Translation: BAG35038.1.
CH471060 Genomic DNA. Translation: EAW91770.1.
BC032700 mRNA. Translation: AAH32700.1.
BC095426 mRNA. Translation: AAH95426.1.
CCDSCCDS34928.1.
PIRS45004.
RefSeqNP_000980.1. NM_000989.3.
UniGeneHs.400295.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Belectron microscopy5.00c1-115[»]
3VI6X-ray1.59A1-115[»]
ProteinModelPortalP62888.
SMRP62888. Positions 9-105.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112075. 100 interactions.
IntActP62888. 27 interactions.
MINTMINT-5000026.
STRING9606.ENSP00000287038.

PTM databases

PhosphoSiteP62888.

Polymorphism databases

DMDM51702805.

2D gel databases

SWISS-2DPAGEP62888.

Proteomic databases

MaxQBP62888.
PaxDbP62888.
PeptideAtlasP62888.
PRIDEP62888.

Protocols and materials databases

DNASU6156.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000287038; ENSP00000287038; ENSG00000156482.
ENST00000521291; ENSP00000428085; ENSG00000156482.
GeneID6156.
KEGGhsa:6156.
UCSCuc003yif.3. human.

Organism-specific databases

CTD6156.
GeneCardsGC08M099037.
HGNCHGNC:10333. RPL30.
HPAHPA002651.
MIM180467. gene.
neXtProtNX_P62888.
PharmGKBPA34714.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1911.
HOGENOMHOG000055224.
HOVERGENHBG000449.
KOK02908.
OMAMRNGKAK.
OrthoDBEOG70CR8V.
PhylomeDBP62888.
TreeFamTF300252.

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.

Gene expression databases

ArrayExpressP62888.
BgeeP62888.
CleanExHS_RPL30.
GenevestigatorP62888.

Family and domain databases

Gene3D3.30.1330.30. 1 hit.
HAMAPMF_00481. Ribosomal_L30e.
InterProIPR029064. L30e-like.
IPR000231. Ribosomal_L30e.
IPR022991. Ribosomal_L30e_CS.
IPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45.
[Graphical view]
PANTHERPTHR11449. PTHR11449. 1 hit.
PfamPF01248. Ribosomal_L7Ae. 1 hit.
[Graphical view]
SUPFAMSSF55315. SSF55315. 1 hit.
PROSITEPS00709. RIBOSOMAL_L30E_1. 1 hit.
PS00993. RIBOSOMAL_L30E_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPL30. human.
GeneWikiRPL30.
GenomeRNAi6156.
NextBio23907.
PROP62888.
SOURCESearch...

Entry information

Entry nameRL30_HUMAN
AccessionPrimary (citable) accession number: P62888
Secondary accession number(s): B2R591, P04645, Q502Z6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 98 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 8

Human chromosome 8: entries, gene names and cross-references to MIM