P36578 (RL4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
60S ribosomal protein L4

Alternative name(s):
60S ribosomal protein L1

Gene names

Name:	RPL4
Synonyms:	RPL1

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	427 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)

Subunit structure	May bind IPO9 with low affinity. Interacts with RBM3 By similarity. Ref.9
Sequence similarities	Belongs to the ribosomal protein L4P 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 PubMed 12962325. Source: UniProtKB nucleolus Inferred from direct assay. Source: HPA
Molecular_function	RNA binding Traceable author statement Ref.1. Source: ProtInc structural constituent of ribosome Non-traceable author statement PubMed 12962325. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HTT	P42858	2	EBI-348313,EBI-466029

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.8
	Chain	2 – 427	426	60S ribosomal protein L4		PRO_0000129350
Regions
	Compositional bias	364 – 427	64	Lys-rich
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.8
	Modified residue	14	1	N6-acetyllysine Ref.12
	Modified residue	106	1	N6-acetyllysine Ref.12
	Modified residue	295	1	Phosphoserine Ref.10 Ref.13
	Modified residue	333	1	N6-acetyllysine Ref.12
	Modified residue	365	1	Phosphoserine Ref.10 Ref.13
Experimental info
	Sequence conflict	3	1	C → V in AAA60281. Ref.1
	Sequence conflict	36	1	I → M in AAA60281. Ref.1
	Sequence conflict	63	1	S → R in AAA60281. Ref.1
	Sequence conflict	147	1	V → F in AAA60281. Ref.1
	Sequence conflict	201	1	Missing in AAA60281. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P36578 [UniParc]. Last modified January 23, 2007. Version 5. Checksum: 4785ED31699CD792	FASTA	427	47,697
	10 20 30 40 50 60 MACARPLISV YSEKGESSGK NVTLPAVFKA PIRPDIVNFV HTNLRKNNRQ PYAVSELAGH 70 80 90 100 110 120 QTSAESWGTG RAVARIPRVR GGGTHRSGQG AFGNMCRGGR MFAPTKTWRR WHRRVNTTQK 130 140 150 160 170 180 RYAICSALAA SALPALVMSK GHRIEEVPEL PLVVEDKVEG YKKTKEAVLL LKKLKAWNDI 190 200 210 220 230 240 KKVYASQRMR AGKGKMRNRR RIQRRGPCII YNEDNGIIKA FRNIPGITLL NVSKLNILKL 250 260 270 280 290 300 APGGHVGRFC IWTESAFRKL DELYGTWRKA ASLKSNYNLP MHKMINTDLS RILKSPEIQR 310 320 330 340 350 360 ALRAPRKKIH RRVLKKNPLK NLRIMLKLNP YAKTMRRNTI LRQARNHKLR VDKAAAAAAA 370 380 390 400 410 420 LQAKSDEKAA VAGKKPVVGK KGKKAAVGVK KQKKPLVGKK AAATKKPAPE KKPAEKKPTT EEKKPAA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human ribosomal protein L4: cloning and sequencing of the cDNA and primary structure of the protein." Bagni C., Mariottini P., Annesi F., Amaldi F. Biochim. Biophys. Acta 1216:475-478(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	Bagni C. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	Kato S. Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lymphoma.
[4]	"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].
[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: Skeletal muscle.
[6]	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].
[7]	"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: Colon, Embryonic stem cell, Eye, Hippocampus, Muscle, Pancreas and Skin.
[8]	Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M. Submitted (MAY-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-13, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: T-cell.
[9]	"Importins fulfill a dual function as nuclear import receptors and cytoplasmic chaperones for exposed basic domains." Jaekel S., Mingot J.-M., Schwarzmaier P., Hartmann E., Goerlich D. EMBO J. 21:377-386(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH IPO9.
[10]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295 AND SER-365, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[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-14; LYS-106 AND LYS-333, MASS SPECTROMETRY.
[13]	"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-295 AND SER-365, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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	L20868 mRNA. Translation: AAA60281.2. D23660 mRNA. Translation: BAA04887.1. AB061820 Genomic DNA. Translation: BAB79458.1. AK291117 mRNA. Translation: BAF83806.1. AK291859 mRNA. Translation: BAF84548.1. CH471082 Genomic DNA. Translation: EAW77776.1. BC001365 mRNA. Translation: AAH01365.1. BC005817 mRNA. Translation: AAH05817.1. BC007748 mRNA. Translation: AAH07748.1. BC007996 mRNA. Translation: AAH07996.1. BC009888 mRNA. Translation: AAH09888.1. BC010151 mRNA. Translation: AAH10151.1. BC014653 mRNA. Translation: AAH14653.1. BC066925 mRNA. Translation: AAH66925.1. BC095427 mRNA. Translation: AAH95427.1.
IPI	IPI00003918.
PIR	T09551.
RefSeq	NP_000959.2. NM_000968.3.
UniGene	Hs.186350. Hs.644628.
3D structure databases
ProteinModelPortal	P36578.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-27559N.
IntAct	P36578. 25 interactions.
MINT	MINT-1034893.
STRING	9606.ENSP00000311430.
PTM databases
PhosphoSite	P36578.
Polymorphism databases
DMDM	22002063.
2D gel databases
SWISS-2DPAGE	P36578.
Proteomic databases
PaxDb	P36578.
PRIDE	P36578.
Protocols and materials databases
DNASU	6124.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000307961; ENSP00000311430; ENSG00000174444.
GeneID	6124.
KEGG	hsa:6124.
UCSC	uc002apv.3. human.
Organism-specific databases
CTD	6124.
GeneCards	GC15M066790.
HGNC	HGNC:10353. RPL4.
HPA	HPA034600.
MIM	180479. gene.
neXtProt	NX_P36578.
PharmGKB	PA34749.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0088.
HOVERGEN	HBG001453.
InParanoid	P36578.
KO	K02930.
OMA	HTNMRKN.
OrthoDB	EOG483D4X.
PhylomeDB	P36578.
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	P36578.
Bgee	P36578.
CleanEx	HS_RPL4.
Genevestigator	P36578.
GermOnline	ENSG00000174444. Homo sapiens.
Family and domain databases
Gene3D	3.40.1370.10. 1 hit.
InterPro	IPR025755. Ribos_L4_C_dom. IPR002136. Ribosomal_L4/L1e. IPR013000. Ribosomal_L4/L1e_euk/arc_CS. IPR023574. Ribosomal_L4_dom. [Graphical view]
Pfam	PF14374. Ribos_L4_asso_C. 1 hit. PF00573. Ribosomal_L4. 1 hit. [Graphical view]
SUPFAM	SSF52166. Ribosomal_L4/L1E. 1 hit.
PROSITE	PS00939. RIBOSOMAL_L1E. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	RPL4. human.
GenomeRNAi	6124.
NextBio	23787.
PMAP-CutDB	P36578.
SOURCE	Search...

Entry information

Entry name

RL4_HUMAN

Accession

Primary (citable) accession number: P36578
Secondary accession number(s): A8K502 , P39029, Q4VBR0, Q969Z9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 133 of the entry and version 5 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.