P18124 (RL7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
60S ribosomal protein L7

Gene names

Name:

RPL7

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	248 AA.
Sequence status	Complete.
Protein existence	Evidence 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
Domain	Repeat
Ligand	RNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	SRP-dependent cotranslational protein targeting to membrane 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 translational elongation Traceable author statement. Source: Reactome translational initiation Traceable author statement. Source: Reactome translational termination Traceable author statement. Source: Reactome viral transcription Traceable author statement. Source: Reactome
Cellular_component	cytosolic large ribosomal subunit Inferred from direct assay Ref.9. Source: UniProtKB
Molecular_function	DNA binding Inferred from direct assay Ref.1. Source: MGI mRNA binding Inferred from direct assay Ref.1. Source: MGI structural constituent of ribosome Non-traceable author statement Ref.9. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 248	248	60S ribosomal protein L7		PRO_0000104633
Regions
	Repeat	7 – 18	12	1
	Repeat	19 – 30	12	2
	Repeat	31 – 42	12	3
	Repeat	43 – 54	12	4
	Region	7 – 54	48	4 X 12 AA tandem repeats
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine Ref.7 Ref.9
	Modified residue	124	1	N6-acetyllysine Ref.11
	Modified residue	139	1	Phosphotyrosine Ref.10
Experimental info
	Sequence conflict	48	1	K → E in CAG33054. Ref.4
	Sequence conflict	157	1	R → L in CAA41026. Ref.1
	Sequence conflict	157	1	R → L in CAA41027. Ref.1
	Sequence conflict	160	1	G → A in CAA41026. Ref.1
	Sequence conflict	166	1	R → Q in CAA41026. Ref.1
	Sequence conflict	173	1	A → S in AAA03081. Ref.2
	Sequence conflict	192	1	H → R in CAG33054. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P18124 [UniParc]. Last modified November 1, 1990. Version 1. Checksum: 070EB4C904E6795A	FASTA	248	29,226
	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

References

	« Hide 'large scale' referencesShow '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. , 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, 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: MASS SPECTROMETRY, PROBABLE ACETYLATION AT MET-1.
[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, MASS SPECTROMETRY.
[11]	"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, MASS SPECTROMETRY.
[12]	"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].
+	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.
IPI	IPI00030179.
PIR	R5HU7. S11709.
RefSeq	NP_000962.2. NM_000971.3.
UniGene	Hs.421257. Hs.571841.
3D structure databases
ProteinModelPortal	P18124.
ModBase	Search...
Protein-protein interaction databases
IntAct	P18124. 20 interactions.
MINT	MINT-1152474.
STRING	9606.ENSP00000339795.
PTM databases
PhosphoSite	P18124.
Polymorphism databases
DMDM	133021.
2D gel databases
SWISS-2DPAGE	P18124.
Proteomic databases
PaxDb	P18124.
PRIDE	P18124.
Protocols and materials databases
DNASU	6129.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000352983; ENSP00000339795; ENSG00000147604.
GeneID	6129.
KEGG	hsa:6129.
UCSC	uc003xzg.3. human.
Organism-specific databases
CTD	6129.
GeneCards	GC08M074202.
H-InvDB	HIX0058339.
HGNC	HGNC:10363. RPL7.
MIM	604166. gene.
neXtProt	NX_P18124.
PharmGKB	PA34759.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1841.
HOGENOM	HOG000170917.
HOVERGEN	HBG003280.
KO	K02937.
OMA	MEDVIHE.
OrthoDB	EOG42Z4R0.
Enzyme and pathway databases
Reactome	REACT_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
ArrayExpress	P18124.
Bgee	P18124.
CleanEx	HS_RPL7.
Genevestigator	P18124.
GermOnline	ENSG00000147604. Homo sapiens.
Family and domain databases
Gene3D	3.30.1390.20. 2 hits.
InterPro	IPR018038. Ribosomal_L30_CS. IPR016082. Ribosomal_L30_ferredoxin-like. IPR012988. Ribosomal_L30_N. IPR005998. Ribosomal_L7_euk. [Graphical view]
Pfam	PF00327. Ribosomal_L30. 1 hit. PF08079. Ribosomal_L30_N. 1 hit. [Graphical view]
SUPFAM	SSF55129. Ribosomal_L30. 1 hit.
TIGRFAMs	TIGR01310. L7. 1 hit.
PROSITE	PS00634. RIBOSOMAL_L30. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	RPL7. human.
GenomeRNAi	6129.
NextBio	23805.
SOURCE	Search...

Entry information

Entry name

RL7_HUMAN

Accession

Primary (citable) accession number: P18124
Secondary accession number(s): A8K504 , Q15289, Q3KQU0, Q5I0X1, Q6IBM9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	May 29, 2013
This is version 142 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.