P62888 (RL30_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
60S ribosomal protein L30

Gene names

Name:

RPL30

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	115 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the ribosomal protein L30e family.

Ontologies

Keywords
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome 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 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 PubMed 12962325. Source: UniProtKB
Molecular_function	RNA binding Traceable author statement PubMed 1577483. Source: UniProtKB structural constituent of ribosome Non-traceable author statement PubMed 12962325. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 115

115

60S ribosomal protein L30

PRO_0000146120

Amino acid modifications

Modified residue

10

1

Phosphoserine Ref.7 Ref.9 Ref.11

Modified residue

26

1

N6-acetyllysine Ref.8

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

115

Helix Strand Turn

Details...

Helix

15 – 24

10

Beta strand

25 – 30

6

Helix

31 – 39

9

Beta strand

44 – 48

5

Helix

54 – 66

13

Beta strand

70 – 73

4

Helix

78 – 84

7

Beta strand

93 – 98

6

Sequences

	Sequence		Length	Mass (Da)
	P62888 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 95186B081E39748C	FASTA	115	12,784
	10 20 30 40 50 60 MVAAKKTKKS LESINSRLQL VMKSGKYVLG YKQTLKMIRQ GKAKLVILAN NCPALRKSEI 70 80 90 100 110 EYYAMLAKTG VHHYSGNNIE LGTACGKYYR VCTLAIIDPG DSDIIRSMPE QTGEK

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[12]	"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.

IPI

IPI00219156.

PIR

S45004.

RefSeq

NP_000980.1. NM_000989.3.

UniGene

Hs.400295.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3VI6	X-ray	1.59	A	1-115	[»]

ProteinModelPortal

P62888.

ModBase

Search...

Protein-protein interaction databases

IntAct

P62888. 19 interactions.

MINT

MINT-5000026.

STRING

9606.ENSP00000287038.

PTM databases

PhosphoSite

P62888.

Polymorphism databases

DMDM

51702805.

2D gel databases

SWISS-2DPAGE

P62888.

Proteomic databases

PaxDb

P62888.

PeptideAtlas

P62888.

PRIDE

P62888.

Protocols and materials databases

DNASU

6156.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000287038; ENSP00000287038; ENSG00000156482.
ENST00000521291; ENSP00000428085; ENSG00000156482.

GeneID

6156.

KEGG

hsa:6156.

UCSC

uc003yif.3. human.

Organism-specific databases

CTD

6156.

GeneCards

GC08M099037.

HGNC

HGNC:10333. RPL30.

HPA

HPA002651.

MIM

180467. gene.

neXtProt

NX_P62888.

PharmGKB

PA34714.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1911.

HOGENOM

HOG000055224.

HOVERGEN

HBG000449.

KO

K02908.

OMA

KYFRVCT.

PhylomeDB

P62888.

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

P62888.

Bgee

P62888.

CleanEx

HS_RPL30.

Genevestigator

P62888.

Family and domain databases

InterPro

IPR000231. Ribosomal_L30e.
IPR022991. Ribosomal_L30e_CS.
IPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45.
[Graphical view]

PANTHER

PTHR11449. PTHR11449. 1 hit.

Pfam

PF01248. Ribosomal_L7Ae. 1 hit.
[Graphical view]

PROSITE

PS00709. RIBOSOMAL_L30E_1. 1 hit.
PS00993. RIBOSOMAL_L30E_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

RPL30. human.

GenomeRNAi

6156.

NextBio

23907.

SOURCE

Search...

Entry information

Entry name

RL30_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 87 of the entry and version 2 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.