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Protein

60S ribosomal protein L30

Gene

RPL30

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

Functioni

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • structural constituent of ribosome Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

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.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L30
Gene namesi
Name:RPL30
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:10333. RPL30.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • cytosolic large ribosomal subunit Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34714.

Polymorphism and mutation databases

BioMutaiRPL30.
DMDMi51702805.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11511560S ribosomal protein L30PRO_0000146120Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei10 – 101Phosphoserine3 Publications
Modified residuei26 – 261N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP62888.
PaxDbiP62888.
PeptideAtlasiP62888.
PRIDEiP62888.

2D gel databases

SWISS-2DPAGEP62888.

PTM databases

PhosphoSiteiP62888.

Expressioni

Gene expression databases

BgeeiP62888.
CleanExiHS_RPL30.
ExpressionAtlasiP62888. baseline and differential.
GenevisibleiP62888. HS.

Organism-specific databases

HPAiHPA002651.

Interactioni

Protein-protein interaction databases

BioGridi112075. 106 interactions.
IntActiP62888. 28 interactions.
MINTiMINT-5000026.
STRINGi9606.ENSP00000287038.

Structurei

Secondary structure

1
115
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 2410Combined sources
Beta strandi25 – 306Combined sources
Helixi31 – 399Combined sources
Beta strandi44 – 485Combined sources
Helixi54 – 6613Combined sources
Beta strandi70 – 734Combined sources
Helixi78 – 847Combined sources
Beta strandi93 – 986Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VI6X-ray1.59A1-115[»]
4V6Xelectron microscopy5.00Cc1-115[»]
5AJ0electron microscopy3.50Ac1-115[»]
ProteinModelPortaliP62888.
SMRiP62888. Positions 9-105.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L30e family.Curated

Phylogenomic databases

eggNOGiCOG1911.
GeneTreeiENSGT00390000012138.
HOGENOMiHOG000055224.
HOVERGENiHBG000449.
InParanoidiP62888.
KOiK02908.
OMAiNIPVYQH.
OrthoDBiEOG70CR8V.
PhylomeDBiP62888.
TreeFamiTF300252.

Family and domain databases

Gene3Di3.30.1330.30. 1 hit.
HAMAPiMF_00481. Ribosomal_L30e.
InterProiIPR029064. L30e-like.
IPR000231. Ribosomal_L30e.
IPR022991. Ribosomal_L30e_CS.
IPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45.
[Graphical view]
PANTHERiPTHR11449. PTHR11449. 1 hit.
PfamiPF01248. Ribosomal_L7Ae. 1 hit.
[Graphical view]
SUPFAMiSSF55315. SSF55315. 1 hit.
PROSITEiPS00709. RIBOSOMAL_L30E_1. 1 hit.
PS00993. RIBOSOMAL_L30E_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P62888-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVAAKKTKKS LESINSRLQL VMKSGKYVLG YKQTLKMIRQ GKAKLVILAN
60 70 80 90 100
NCPALRKSEI EYYAMLAKTG VHHYSGNNIE LGTACGKYYR VCTLAIIDPG
110
DSDIIRSMPE QTGEK
Length:115
Mass (Da):12,784
Last modified:January 23, 2007 - v2
Checksum:i95186B081E39748C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34928.1.
PIRiS45004.
RefSeqiNP_000980.1. NM_000989.3.
UniGeneiHs.400295.

Genome annotation databases

EnsembliENST00000287038; ENSP00000287038; ENSG00000156482.
ENST00000521291; ENSP00000428085; ENSG00000156482.
GeneIDi6156.
KEGGihsa:6156.
UCSCiuc003yif.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34928.1.
PIRiS45004.
RefSeqiNP_000980.1. NM_000989.3.
UniGeneiHs.400295.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VI6X-ray1.59A1-115[»]
4V6Xelectron microscopy5.00Cc1-115[»]
5AJ0electron microscopy3.50Ac1-115[»]
ProteinModelPortaliP62888.
SMRiP62888. Positions 9-105.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112075. 106 interactions.
IntActiP62888. 28 interactions.
MINTiMINT-5000026.
STRINGi9606.ENSP00000287038.

PTM databases

PhosphoSiteiP62888.

Polymorphism and mutation databases

BioMutaiRPL30.
DMDMi51702805.

2D gel databases

SWISS-2DPAGEP62888.

Proteomic databases

MaxQBiP62888.
PaxDbiP62888.
PeptideAtlasiP62888.
PRIDEiP62888.

Protocols and materials databases

DNASUi6156.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000287038; ENSP00000287038; ENSG00000156482.
ENST00000521291; ENSP00000428085; ENSG00000156482.
GeneIDi6156.
KEGGihsa:6156.
UCSCiuc003yif.3. human.

Organism-specific databases

CTDi6156.
GeneCardsiGC08M099037.
HGNCiHGNC:10333. RPL30.
HPAiHPA002651.
MIMi180467. gene.
neXtProtiNX_P62888.
PharmGKBiPA34714.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1911.
GeneTreeiENSGT00390000012138.
HOGENOMiHOG000055224.
HOVERGENiHBG000449.
InParanoidiP62888.
KOiK02908.
OMAiNIPVYQH.
OrthoDBiEOG70CR8V.
PhylomeDBiP62888.
TreeFamiTF300252.

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.

Miscellaneous databases

ChiTaRSiRPL30. human.
GeneWikiiRPL30.
GenomeRNAii6156.
NextBioi23907.
PROiP62888.
SOURCEiSearch...

Gene expression databases

BgeeiP62888.
CleanExiHS_RPL30.
ExpressionAtlasiP62888. baseline and differential.
GenevisibleiP62888. HS.

Family and domain databases

Gene3Di3.30.1330.30. 1 hit.
HAMAPiMF_00481. Ribosomal_L30e.
InterProiIPR029064. L30e-like.
IPR000231. Ribosomal_L30e.
IPR022991. Ribosomal_L30e_CS.
IPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45.
[Graphical view]
PANTHERiPTHR11449. PTHR11449. 1 hit.
PfamiPF01248. Ribosomal_L7Ae. 1 hit.
[Graphical view]
SUPFAMiSSF55315. SSF55315. 1 hit.
PROSITEiPS00709. RIBOSOMAL_L30E_1. 1 hit.
PS00993. RIBOSOMAL_L30E_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "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).

Entry informationi

Entry nameiRL30_HUMAN
AccessioniPrimary (citable) accession number: P62888
Secondary accession number(s): B2R591, P04645, Q502Z6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 108 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, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: 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.