Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P26373 (RL13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length211 AA.
Sequence statusComplete.
Protein existenceEvidence 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 diversityAlternative splicing
Polymorphism
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

SRP-dependent cotranslational protein targeting to membrane

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Traceable author statement. Source: Reactome

translation

Non-traceable author statement PubMed 12962325. Source: UniProtKB

translational elongation

Traceable author statement. Source: Reactome

translational initiation

Traceable author statement. Source: Reactome

translational termination

Traceable author statement. Source: Reactome

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

viral transcription

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

cytosolic large ribosomal subunit

Inferred from direct assay PubMed 12962325. Source: UniProtKB

cytosolic ribosome

Traceable author statement PubMed 9582194. Source: ProtInc

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

   Molecular_functionRNA binding

Traceable author statement PubMed 9582194. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 17474147. Source: IntAct

structural constituent of ribosome

Non-traceable author statement PubMed 12962325. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NCK1P163332EBI-356849,EBI-389883
PIK3R1P279862EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 21121160S ribosomal protein L13
PRO_0000192919

Amino acid modifications

Modified residue161N6-acetyllysine Ref.8
Modified residue771Phosphoserine Ref.6
Modified residue1061Phosphoserine Ref.9
Modified residue1771N6-acetyllysine Ref.8

Natural variations

Alternative sequence88 – 13447Missing in isoform 2.
VSP_046028
Natural variant1121A → T. Ref.1 Ref.5
Corresponds to variant rs9930567 [ dbSNP | Ensembl ].
VAR_051801
Natural variant1701T → P.
Corresponds to variant rs16965839 [ dbSNP | Ensembl ].
VAR_051802

Experimental info

Sequence conflict91V → A in BAG59685. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: DB9FC57768E6BEDE

FASTA21124,261
        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 

« Hide

Isoform 2 [UniParc].

Checksum: F631C531204EEFAC
Show »

FASTA16418,845

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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].
[12]"Structures of the human and Drosophila 80S ribosome."
Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M., Wilson D.N., Beckmann R.
Nature 497:80-85(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
+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.
CCDSCCDS10979.1. [P26373-1]
CCDS58492.1. [P26373-2]
PIRS23753.
RefSeqNP_000968.2. NM_000977.3. [P26373-1]
NP_001230059.1. NM_001243130.1.
NP_001230060.1. NM_001243131.1. [P26373-2]
NP_150254.1. NM_033251.2. [P26373-1]
UniGeneHs.410817.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Belectron microscopy5.00L1-211[»]
ProteinModelPortalP26373.
SMRP26373. Positions 2-211.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112057. 117 interactions.
IntActP26373. 32 interactions.
MINTMINT-1148895.
STRING9606.ENSP00000307889.

PTM databases

PhosphoSiteP26373.

Polymorphism databases

DMDM21903462.

Proteomic databases

MaxQBP26373.
PaxDbP26373.
PeptideAtlasP26373.
PRIDEP26373.

Protocols and materials databases

DNASU6137.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000311528; ENSP00000307889; ENSG00000167526. [P26373-1]
ENST00000393099; ENSP00000376811; ENSG00000167526. [P26373-1]
ENST00000452368; ENSP00000438959; ENSG00000167526. [P26373-2]
ENST00000567815; ENSP00000455009; ENSG00000167526. [P26373-1]
GeneID6137.
KEGGhsa:6137.
UCSCuc002fnm.2. human. [P26373-1]

Organism-specific databases

CTD6137.
GeneCardsGC16P089659.
HGNCHGNC:10303. RPL13.
HPAHPA051702.
MIM113703. gene.
neXtProtNX_P26373.
PharmGKBPA34670.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4352.
HOGENOMHOG000170452.
HOVERGENHBG001156.
InParanoidP26373.
KOK02873.
OMAGKGNNMI.
OrthoDBEOG74TX1G.
PhylomeDBP26373.
TreeFamTF300073.

Enzyme and pathway databases

ReactomeREACT_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

ArrayExpressP26373.
BgeeP26373.
CleanExHS_RPL13.
GenevestigatorP26373.

Family and domain databases

InterProIPR001380. Ribosomal_L13e.
IPR018256. Ribosomal_L13e_CS.
[Graphical view]
PANTHERPTHR11722. PTHR11722. 1 hit.
PfamPF01294. Ribosomal_L13e. 1 hit.
[Graphical view]
PROSITEPS01104. RIBOSOMAL_L13E. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPL13. human.
GeneWikiRPL13.
GenomeRNAi6137.
NextBio23839.
PMAP-CutDBP26373.
PROP26373.
SOURCESearch...

Entry information

Entry nameRL13_HUMAN
AccessionPrimary (citable) accession number: P26373
Secondary accession number(s): B4DLX3 expand/collapse secondary AC list , F5H1S2, Q3KQT8, Q567Q8, Q9BPX0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 140 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM