P26373 (RL13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
60S ribosomal protein L13

Alternative name(s):
Breast basic conserved protein 1

Gene names

Name:	RPL13
Synonyms:	BBC1
ORF Names:	OK/SW-cl.46

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

General annotation (Comments)

Tissue specificity	Higher levels of expression in benign breast lesions than in carcinomas.
Sequence similarities	Belongs to the ribosomal protein L13e family.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Acetylation Phosphoprotein
Technical term	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 9582194. Source: ProtInc structural constituent of ribosome Non-traceable author statement PubMed 12962325. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NCK1	P16333	2	EBI-356849,EBI-389883
PIK3R1	P27986	2	EBI-356849,EBI-79464

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P26373-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P26373-2)

The sequence of this isoform differs from the canonical sequence as follows:
     88-134: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 211	211	60S ribosomal protein L13		PRO_0000192919
Amino acid modifications
	Modified residue	16	1	N6-acetyllysine Ref.8
	Modified residue	77	1	Phosphoserine Ref.6
	Modified residue	106	1	Phosphoserine Ref.9
	Modified residue	177	1	N6-acetyllysine Ref.8
Natural variations
	Alternative sequence	88 – 134	47	Missing in isoform 2.		VSP_046028
	Natural variant	112	1	A → T. Ref.1 Ref.5 Corresponds to variant rs9930567 [ dbSNP | Ensembl ].		VAR_051801
	Natural variant	170	1	T → P. Corresponds to variant rs16965839 [ dbSNP | Ensembl ].		VAR_051802
Experimental info
	Sequence conflict	9	1	V → A in BAG59685. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: DB9FC57768E6BEDE	FASTA	211	24,261
	10 20 30 40 50 60 MAPSRNGMVL KPHFHKDWQR RVATWFNQPA RKIRRRKARQ AKARRIAPRP ASGPIRPIVR 70 80 90 100 110 120 CPTVRYHTKV RAGRGFSLEE LRVAGIHKKV ARTIGISVDP RRRNKSTESL QANVQRLKEY 130 140 150 160 170 180 RSKLILFPRK PSAPKKGDSS AEELKLATQL TGPVMPVRNV YKKEKARVIT EEEKNFKAFA 190 200 210 SLRMARANAR LFGIRAKRAK EAAEQDVEKK K
	Isoform 2 [UniParc]. Checksum: F631C531204EEFAC	FASTA	164	18,845
	10 20 30 40 50 60 MAPSRNGMVL KPHFHKDWQR RVATWFNQPA RKIRRRKARQ AKARRIAPRP ASGPIRPIVR 70 80 90 100 110 120 CPTVRYHTKV RAGRGFSLEE LRVAGIHKKG DSSAEELKLA TQLTGPVMPV RNVYKKEKAR 130 140 150 160 VITEEEKNFK AFASLRMARA NARLFGIRAK RAKEAAEQDV EKKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of a novel gene with differential expression in benign and malignant human breast tumours." Adams S.M., Helps N.R., Sharp M.G.F., Brammar W.J., Walker R.A., Varley J.M. Hum. Mol. Genet. 1:91-96(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-112.
[2]	"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] (ISOFORM 1). Tissue: Colon adenocarcinoma.
[3]	"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] (ISOFORM 2). Tissue: Brain.
[4]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A. Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORM 1), VARIANT THR-112. Tissue: Blood vessel, Brain, Cervix, Lung, Lymph, Pancreas, Placenta and Uterus.
[6]	"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-77, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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-16 AND LYS-177, 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-106, 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X64707 mRNA. Translation: CAA45963.1. AB062392 mRNA. Translation: BAB93479.1. AK297198 mRNA. Translation: BAG59685.1. AC092123 Genomic DNA. No translation available. BC004954 mRNA. Translation: AAH04954.1. BC007345 mRNA. Translation: AAH07345.1. BC007563 mRNA. Translation: AAH07563.1. BC007805 mRNA. Translation: AAH07805.1. BC010994 mRNA. Translation: AAH10994.1. BC013078 mRNA. Translation: AAH13078.1. BC014167 mRNA. Translation: AAH14167.1. BC020804 mRNA. Translation: AAH20804.1. BC027463 mRNA. Translation: AAH27463.1. BC063378 mRNA. Translation: AAH63378.1. BC093063 mRNA. Translation: AAH93063.1. BC106058 mRNA. Translation: AAI06059.1.
IPI	IPI00465361. IPI00978971.
PIR	S23753.
RefSeq	NP_000968.2. NM_000977.3. NP_001230059.1. NM_001243130.1. NP_001230060.1. NM_001243131.1. NP_150254.1. NM_033251.2.
UniGene	Hs.410817.
3D structure databases
ProteinModelPortal	P26373.
ModBase	Search...
Protein-protein interaction databases
IntAct	P26373. 18 interactions.
MINT	MINT-1148895.
STRING	9606.ENSP00000307889.
PTM databases
PhosphoSite	P26373.
Polymorphism databases
DMDM	21903462.
Proteomic databases
PaxDb	P26373.
PeptideAtlas	P26373.
PRIDE	P26373.
Protocols and materials databases
DNASU	6137.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000311528; ENSP00000307889; ENSG00000167526. ENST00000393099; ENSP00000376811; ENSG00000167526. ENST00000452368; ENSP00000438959; ENSG00000167526. ENST00000567815; ENSP00000455009; ENSG00000167526.
GeneID	6137.
KEGG	hsa:6137.
UCSC	uc002fnm.2. human. uc010vpj.2. human.
Organism-specific databases
CTD	6137.
GeneCards	GC16P089637.
HGNC	HGNC:10303. RPL13.
HPA	HPA051702.
MIM	113703. gene.
neXtProt	NX_P26373.
PharmGKB	PA34670.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG4352.
HOGENOM	HOG000170452.
HOVERGEN	HBG001156.
InParanoid	P26373.
KO	K02873.
OMA	LNPHFHK.
OrthoDB	EOG4SJ5FX.
PhylomeDB	P26373.
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	P26373.
Bgee	P26373.
CleanEx	HS_RPL13.
Genevestigator	P26373.
GermOnline	ENSG00000167526. Homo sapiens.
Family and domain databases
InterPro	IPR001380. Ribosomal_L13e. IPR018256. Ribosomal_L13e_CS. [Graphical view]
PANTHER	PTHR11722. PTHR11722. 1 hit.
Pfam	PF01294. Ribosomal_L13e. 1 hit. [Graphical view]
PROSITE	PS01104. RIBOSOMAL_L13E. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	RPL13. human.
GenomeRNAi	6137.
NextBio	23839.
PMAP-CutDB	P26373.
SOURCE	Search...

Entry information

Entry name

RL13_HUMAN

Accession

Primary (citable) accession number: P26373
Secondary accession number(s): B4DLX3 , F5H1S2, Q3KQT8, Q567Q8, Q9BPX0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 128 of the entry and version 4 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.