P32969 (RL9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
60S ribosomal protein L9

Gene names

Name:	RPL9
ORF Names:	OK/SW-cl.103
AND
Name:	RPL9P7
AND
Name:	RPL9P8
AND
Name:	RPL9P9

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

General annotation (Comments)

Sequence similarities

Belongs to the ribosomal protein L6P family.

Ontologies

Keywords
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Acetylation
Technical term	3D-structure 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 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 nucleolus Inferred from direct assay. Source: HPA
Molecular_function	RNA binding Traceable author statement Ref.2. Source: ProtInc rRNA binding Inferred from electronic annotation. Source: InterPro 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 – 192

192

60S ribosomal protein L9

PRO_0000131097

Sites

Site

1

1

Not acetylated

Amino acid modifications

Modified residue

121

1

N6-acetyllysine Ref.8

Experimental info

Sequence conflict

11

1

D → E in AAB01040. Ref.2

Sequence conflict

11

1

D → E in AAB01041. Ref.2

Secondary structure

1

.

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.

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.

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192

Helix Strand Turn

Details...

Beta strand

8 – 10

3

Beta strand

17 – 21

5

Beta strand

24 – 29

6

Beta strand

32 – 37

6

Beta strand

44 – 48

5

Beta strand

50 – 52

3

Beta strand

54 – 58

5

Beta strand

61 – 63

3

Helix

65 – 85

21

Sequences

	Sequence		Length	Mass (Da)
	P32969 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 0249E6CA12F77934	FASTA	192	21,863
	10 20 30 40 50 60 MKTILSNQTV DIPENVDITL KGRTVIVKGP RGTLRRDFNH INVELSLLGK KKKRLRVDKW 70 80 90 100 110 120 WGNRKELATV RTICSHVQNM IKGVTLGFRY KMRSVYAHFP INVVIQENGS LVEIRNFLGE 130 140 150 160 170 180 KYIRRVRMRP GVACSVSQAQ KDELILEGND IELVSNSAAL IQQATTVKNK DIRKFLDGIY 190 VSEKGTVQQA DE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A new human ribosomal protein sequence, homologue of rat L9." Hori N., Murakawa K., Matoba R., Fukushima A., Okubo K., Matsubara K. Nucleic Acids Res. 21:4395-4395(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Structural organization and chromosomal localization of the human ribosomal protein L9 gene." Mazuruk K., Schoen T.J., Chader G.J., Iwata T., Rodriguez I.R. Biochim. Biophys. Acta 1305:151-162(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Retina.
[3]	"Human homolog of rat ribosomal protein L9." Williams J.H., Pearse M.J., Power D.A. Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients." Shichijo S., Itoh K. Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon adenocarcinoma.
[5]	"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: Brain, Muscle, Placenta and Uterus.
[6]	Bienvenut W.V., Bilsland A.E., Keith W.N. Submitted (JAN-2010) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-21; 36-51; 94-115; 142-168 AND 174-184, LACK OF N-TERMINAL ACETYLATION, MASS SPECTROMETRY. Tissue: Colon carcinoma.
[7]	"A map of 75 human ribosomal protein genes." Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J., Tanaka T., Page D.C. Genome Res. 8:509-523(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 146-192.
[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-121, MASS SPECTROMETRY.
[9]	"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].
[10]	"Solution structure of the N-terminal domain of human ribosomal protein L9." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 1-87.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D14531 mRNA. Translation: BAA03401.1.
U09953 mRNA. Translation: AAB01040.1.
U09954 Genomic DNA. Translation: AAB01041.1.
U21138 mRNA. Translation: AAA63752.1.
AB062431 mRNA. Translation: BAB93494.1.
BC000483 mRNA. Translation: AAH00483.1.
BC004156 mRNA. Translation: AAH04156.1.
BC004206 mRNA. Translation: AAH04206.1.
BC007967 mRNA. Translation: AAH07967.1.
BC012149 mRNA. Translation: AAH12149.1.
BC031906 mRNA. Translation: AAH31906.1.
BC066318 mRNA. Translation: AAH66318.1.
BC070214 mRNA. Translation: AAH70214.1.
AB007169 Genomic DNA. Translation: BAA25830.1.

IPI

IPI00031691.

PIR

S65792.

RefSeq

NP_000652.2. NM_000661.4.
NP_001020092.1. NM_001024921.2.

UniGene

Hs.412370.
Hs.513083.
Hs.730597.
Hs.741045.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CQL	NMR	-	A	1-87	[»]

ProteinModelPortal

P32969.

ModBase

Search...

Protein-protein interaction databases

IntAct

P32969. 13 interactions.

MINT

MINT-5000985.

STRING

9606.ENSP00000346022.

PTM databases

PhosphoSite

P32969.

Polymorphism databases

DMDM

417677.

2D gel databases

SWISS-2DPAGE

P32969.

Proteomic databases

PaxDb

P32969.

PeptideAtlas

P32969.

PRIDE

P32969.

Protocols and materials databases

DNASU

6133.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000295955; ENSP00000346022; ENSG00000163682.
ENST00000449470; ENSP00000400467; ENSG00000163682.

GeneID

6133.

KEGG

hsa:6133.

UCSC

uc003gub.3. human.

Organism-specific databases

CTD

6133.

HGNC

HGNC:10369. RPL9.

HPA

HPA003372.

MIM

603686. gene.

neXtProt

NX_P32969.

PharmGKB

PA34769.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0097.

HOGENOM

HOG000039905.

HOVERGEN

HBG000942.

InParanoid

P32969.

KO

K02940.

OMA

AVRTVCS.

OrthoDB

EOG4T4CWJ.

PhylomeDB

P32969.

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

P32969.

Bgee

P32969.

CleanEx

HS_RPL9.

Genevestigator

P32969.

GermOnline

ENSG00000163682. Homo sapiens.
ENSG00000169653. Homo sapiens.
ENSG00000182754. Homo sapiens.
ENSG00000185078. Homo sapiens.

Family and domain databases

Gene3D

3.90.930.12. 2 hits.

InterPro

IPR000702. Ribosomal_L6.
IPR020040. Ribosomal_L6_a/b-dom.
IPR002359. Ribosomal_L6_CS2.
[Graphical view]

PANTHER

PTHR11655. PTHR11655. 1 hit.

Pfam

PF00347. Ribosomal_L6. 2 hits.
[Graphical view]

PIRSF

PIRSF002162. Ribosomal_L6. 1 hit.

SUPFAM

SSF56053. Ribosomal_L6. 2 hits.

PROSITE

PS00700. RIBOSOMAL_L6_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P32969.

GenomeRNAi

6133.

NextBio

23821.

SOURCE

Search...

Entry information

Entry name

RL9_HUMAN

Accession

Primary (citable) accession number: P32969

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	May 1, 2013
This is version 139 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.