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P18124 (RL7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. 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 L7
Gene names
Name:RPL7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length248 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to G-rich structures in 28S rRNA and in mRNAs. Plays a regulatory role in the translation apparatus; inhibits cell-free translation of mRNAs.

Subunit structure

Homodimer.

Sequence similarities

Belongs to the ribosomal protein L30P family.

Sequence caution

The sequence CAA41026.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   DomainRepeat
   LigandRNA-binding
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMAcetylation
Phosphoprotein
   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

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

rRNA processing

Inferred from mutant phenotype PubMed 18697920. Source: UniProtKB

ribosomal large subunit biogenesis

Inferred from mutant phenotype PubMed 18697920. Source: UniProtKB

translation

Non-traceable author statement Ref.9. 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.9. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

ribonucleoprotein complex

Inferred from direct assay PubMed 18809582. Source: MGI

   Molecular_functionDNA binding

Inferred from direct assay Ref.1. Source: MGI

RNA binding

Traceable author statement Ref.1. Source: ProtInc

mRNA binding

Inferred from direct assay Ref.1. Source: MGI

poly(A) RNA binding

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

protein binding

Inferred from physical interaction PubMed 18274552PubMed 20828572. Source: IntAct

protein homodimerization activity

Inferred from physical interaction Ref.1. Source: MGI

structural constituent of ribosome

Non-traceable author statement Ref.9. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

IPO5O004104EBI-350806,EBI-356424
NEDD8Q158432EBI-350806,EBI-716247

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 24824860S ribosomal protein L7
PRO_0000104633

Regions

Repeat7 – 18121
Repeat19 – 30122
Repeat31 – 42123
Repeat43 – 54124
Region7 – 54484 X 12 AA tandem repeats

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7 Ref.9 Ref.11 Ref.14
Modified residue1241N6-acetyllysine Ref.12
Modified residue1271N6-succinyllysine By similarity
Modified residue1391Phosphotyrosine Ref.10

Experimental info

Sequence conflict481K → E in CAG33054. Ref.4
Sequence conflict1571R → L in CAA41026. Ref.1
Sequence conflict1571R → L in CAA41027. Ref.1
Sequence conflict1601G → A in CAA41026. Ref.1
Sequence conflict1661R → Q in CAA41026. Ref.1
Sequence conflict1731A → S in AAA03081. Ref.2
Sequence conflict1921H → R in CAG33054. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P18124 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 070EB4C904E6795A

FASTA24829,226
        10         20         30         40         50         60 
MEGVEEKKKE VPAVPETLKK KRRNFAELKI KRLRKKFAQK MLRKARRKLI YEKAKHYHKE 

        70         80         90        100        110        120 
YRQMYRTEIR MARMARKAGN FYVPAEPKLA FVIRIRGING VSPKVRKVLQ LLRLRQIFNG 

       130        140        150        160        170        180 
TFVKLNKASI NMLRIVEPYI AWGYPNLKSV NELIYKRGYG KINKKRIALT DNALIARSLG 

       190        200        210        220        230        240 
KYGIICMEDL IHEIYTVGKR FKEANNFLWP FKLSSPRGGM KKKTTHFVEG GDAGNREDQI 


NRLIRRMN 

« Hide

References

« Hide 'large scale' references
[1]"Structural and functional properties of ribosomal protein L7 from humans and rodents."
Hemmerich P., von Mikecz A., Neumann F., Soezen O., Wolff-Vorbeck G., Zoebelein R., Krawinkel U.
Nucleic Acids Res. 21:223-231(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[2]"Identification of a transcript that is down-regulated in senescent human fibroblasts. Cloning, sequence analysis, and regulation of the human L7 ribosomal protein gene."
Seshadri T., Uzman J.A., Oshima J., Campisi J.
J. Biol. Chem. 268:18474-18480(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fibroblast.
[3]Schneider R., Herzog H., Hfferer L., Schweiger M.
Submitted (MAY-1990) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"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: Thymus.
[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: Bone marrow, Eye, Lung, Mammary gland, Muscle and Skin.
[7]Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-7; 10-20; 48-53; 77-88; 107-113; 128-156; 167-177; 201-212 AND 224-242, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Hepatoma.
[8]"Human ribosomal protein L7 inhibits cell-free translation in reticulocyte lysates and affects the expression of nuclear proteins upon stable transfection into Jurkat T-lymphoma cells."
Neumann F., Hemmerich P., von Mikecz A., Peter H.-H., Krawinkel U.
Nucleic Acids Res. 23:195-202(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[9]"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: ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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].
[14]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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) OF 80S RIBOSOME.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X57958 mRNA. Translation: CAA41026.1. Different initiation.
X57959 mRNA. Translation: CAA41027.1.
L16558 mRNA. Translation: AAA03081.1.
X52967 mRNA. Translation: CAA37139.1.
CR456773 mRNA. Translation: CAG33054.1.
AK291119 mRNA. Translation: BAF83808.1.
AK313365 mRNA. Translation: BAG36165.1.
BC006095 mRNA. Translation: AAH06095.1.
BC008850 mRNA. Translation: AAH08850.1.
BC009599 mRNA. Translation: AAH09599.1.
BC071671 mRNA. Translation: AAH71671.1.
BC071894 mRNA. Translation: AAH71894.1.
BC071895 mRNA. Translation: AAH71895.1.
BC087837 mRNA. Translation: AAH87837.1.
CCDSCCDS6212.1.
PIRR5HU7. S11709.
RefSeqNP_000962.2. NM_000971.3.
UniGeneHs.421257.
Hs.571841.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Belectron microscopy5.00F1-248[»]
ProteinModelPortalP18124.
SMRP18124. Positions 20-248.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112049. 134 interactions.
IntActP18124. 28 interactions.
MINTMINT-1152474.
STRING9606.ENSP00000339795.

PTM databases

PhosphoSiteP18124.

Polymorphism databases

DMDM133021.

2D gel databases

SWISS-2DPAGEP18124.

Proteomic databases

MaxQBP18124.
PaxDbP18124.
PRIDEP18124.

Protocols and materials databases

DNASU6129.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000352983; ENSP00000339795; ENSG00000147604.
GeneID6129.
KEGGhsa:6129.
UCSCuc003xzg.3. human.

Organism-specific databases

CTD6129.
GeneCardsGC08M074202.
H-InvDBHIX0058339.
HGNCHGNC:10363. RPL7.
HPAHPA058373.
MIM604166. gene.
neXtProtNX_P18124.
PharmGKBPA34759.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1841.
HOGENOMHOG000170917.
HOVERGENHBG003280.
KOK02937.
OMAKATQQML.
OrthoDBEOG7K9K3X.
PhylomeDBP18124.
TreeFamTF300740.

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

ArrayExpressP18124.
BgeeP18124.
CleanExHS_RPL7.
GenevestigatorP18124.

Family and domain databases

Gene3D3.30.1390.20. 2 hits.
InterProIPR018038. Ribosomal_L30_CS.
IPR016082. Ribosomal_L30_ferredoxin-like.
IPR012988. Ribosomal_L30_N.
IPR005998. Ribosomal_L7_euk.
[Graphical view]
PfamPF00327. Ribosomal_L30. 1 hit.
PF08079. Ribosomal_L30_N. 1 hit.
[Graphical view]
SUPFAMSSF55129. SSF55129. 1 hit.
TIGRFAMsTIGR01310. L7. 1 hit.
PROSITEPS00634. RIBOSOMAL_L30. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPL7. human.
GeneWikiRPL7.
GenomeRNAi6129.
NextBio23805.
PROP18124.
SOURCESearch...

Entry information

Entry nameRL7_HUMAN
AccessionPrimary (citable) accession number: P18124
Secondary accession number(s): A8K504 expand/collapse secondary AC list , Q15289, Q3KQU0, Q5I0X1, Q6IBM9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: July 9, 2014
This is version 154 of the entry and version 1 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