P49207 (RL34_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
60S ribosomal protein L34

Gene names

Name:

RPL34

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	117 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the ribosomal protein L34e family.

Ontologies

Keywords
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 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.6. Source: UniProtKB
Molecular_function	RNA binding Traceable author statement Ref.1. Source: ProtInc structural constituent of ribosome Non-traceable author statement Ref.6. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CNBP	P62633	1	EBI-1051893,EBI-1047529
DDX56	Q9NY93	1	EBI-1051893,EBI-372376
EIF6	P56537	1	EBI-1051893,EBI-372243
MAGEB2	O15479	1	EBI-1051893,EBI-1057615
PSTPIP1	O43586	1	EBI-1051893,EBI-1050964

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.6
	Chain	2 – 117	116	60S ribosomal protein L34		PRO_0000131831
Amino acid modifications
	Modified residue	12	1	Phosphoserine Ref.10 Ref.12
	Modified residue	36	1	N6-acetyllysine Ref.9
Experimental info
	Sequence conflict	52	1	R → K in AAC41916. Ref.1
	Sequence conflict	58	1	A → P in AAC41916. Ref.1
	Sequence conflict	103	1	V → I in AAC41916. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P49207 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: FC09D00B98CB770C	FASTA	117	13,293
	10 20 30 40 50 60 MVQRLTYRRR LSYNTASNKT RLSRTPGNRI VYLYTKKVGK APKSACGVCP GRLRGVRAVR 70 80 90 100 110 PKVLMRLSKT KKHVSRAYGG SMCAKCVRDR IKRAFLIEEQ KIVVKVLKAQ AQSQKAK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Generation of a transcription map at the HSD17B locus centromeric to BRCA1 at 17q21." Rommens J.M., Durocher F., McArthur J., Tonin P., Leblanc J.-F., Allen T., Samson C., Ferri L., Narod S., Morgan K., Simard J. Genomics 28:530-542(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Ovary.
[2]	"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].
[3]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"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 and Eye.
[5]	"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 4-48.
[6]	"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: PROTEIN SEQUENCE OF 2-12, MASS SPECTROMETRY.
[7]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[8]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]	"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-36, MASS SPECTROMETRY.
[10]	"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-12, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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].
[12]	"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-12, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L38941 mRNA. Translation: AAC41916.1. AB061832 Genomic DNA. Translation: BAB79470.1. CR542232 mRNA. Translation: CAG47028.1. CR542242 mRNA. Translation: CAG47038.1. BC001773 mRNA. Translation: AAH01773.1. BC070208 mRNA. Translation: AAH70208.1. BC106009 mRNA. Translation: AAI06010.1. AB007181 Genomic DNA. Translation: BAA25840.1.
IPI	IPI00219160.
PIR	I68524.
RefSeq	NP_000986.2. NM_000995.3. NP_296374.1. NM_033625.2.
UniGene	Hs.438227.
3D structure databases
ProteinModelPortal	P49207.
ModBase	Search...
Protein-protein interaction databases
IntAct	P49207. 6 interactions.
STRING	9606.ENSP00000378160.
PTM databases
PhosphoSite	P49207.
Polymorphism databases
DMDM	22002070.
Proteomic databases
PaxDb	P49207.
PeptideAtlas	P49207.
PRIDE	P49207.
Protocols and materials databases
DNASU	6164.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000394665; ENSP00000378160; ENSG00000109475. ENST00000394667; ENSP00000378162; ENSG00000109475. ENST00000394668; ENSP00000378163; ENSG00000109475. ENST00000502534; ENSP00000423983; ENSG00000109475. ENST00000506397; ENSP00000423316; ENSG00000109475.
GeneID	6164.
KEGG	hsa:6164.
UCSC	uc003hyz.3. human.
Organism-specific databases
CTD	6164.
GeneCards	GC04P109541.
H-InvDB	HIX0004432.
HGNC	HGNC:10340. RPL34.
HPA	HPA035139.
neXtProt	NX_P49207.
PharmGKB	PA34723.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2174.
HOGENOM	HOG000216922.
HOVERGEN	HBG024280.
InParanoid	P49207.
KO	K02915.
OMA	KKTVQRA.
OrthoDB	EOG4RNB9V.
PhylomeDB	P49207.
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
Bgee	P49207.
CleanEx	HS_RPL34.
Genevestigator	P49207.
Family and domain databases
InterPro	IPR008195. Ribosomal_L34Ae. IPR018065. Ribosomal_L34e_CS. [Graphical view]
PANTHER	PTHR10759. PTHR10759. 1 hit.
Pfam	PF01199. Ribosomal_L34e. 1 hit. [Graphical view]
PRINTS	PR01250. RIBOSOMALL34.
PROSITE	PS01145. RIBOSOMAL_L34E. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	RPL34. human.
GenomeRNAi	6164.
NextBio	23943.

Entry information

Entry name

RL34_HUMAN

Accession

Primary (citable) accession number: P49207
Secondary accession number(s): Q6FG66, Q9BUZ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 113 of the entry and version 3 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.