40S ribosomal protein S13 - Homo sapiens (Human)

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P62277 (RS13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 87. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
40S ribosomal protein S13

Gene names

Name:

RPS13

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	151 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 S15P 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	endocrine pancreas development Traceable author statement. Source: Reactome mRNA metabolic process Traceable author statement. Source: Reactome negative regulation of RNA splicing Inferred from direct assay. Source: UniProtKB translational elongation Traceable author statement. Source: Reactome translational termination Traceable author statement. Source: Reactome viral transcription Traceable author statement. Source: Reactome
Cellular component	cytosolic small ribosomal subunit Inferred from direct assay Ref.7. Source: UniProtKB nucleolus Inferred from direct assay. Source: UniProtKB
Molecular function	mRNA binding Inferred from direct assay. Source: UniProtKB protein binding Inferred from physical interaction. Source: UniProtKB structural constituent of ribosome Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PDCD4	Q53EL6	2	EBI-351850,EBI-935824

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 151

150

40S ribosomal protein S13

PRO_0000115661

Amino acid modifications

Modified residue

Phosphoserine Ref.12

Modified residue

N6-acetyllysine Ref.13

Modified residue

Phosphoserine Ref.11

Modified residue

Phosphotyrosine Ref.9

Modified residue

N6-acetyllysine Ref.13

Modified residue

128

Phosphotyrosine Ref.10

Modified residue

129

Phosphotyrosine Ref.10

Experimental info

Sequence conflict

P → S in AAC15854. Ref.8

Sequences

Sequence

Length

Mass (Da)

Tools

P62277 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 23F94D38F87B8D53
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FASTA

151

17,222

        10         20         30         40         50         60 
MGRMHAPGKG LSQSALPYRR SVPTWLKLTS DDVKEQIYKL AKKGLTPSQI GVILRDSHGV 

        70         80         90        100        110        120 
AQVRFVTGNK ILRILKSKGL APDLPEDLYH LIKKAVAVRK HLERNRKDKD AKFRLILIES 

       130        140        150 
RIHRLARYYK TKRVLPPNWK YESSTASALV A

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and analysis of the human S13 ribosomal protein cDNA." Chadeneau C., Lemoullac B., Denis M.G. Nucleic Acids Res. 21:2945-2945(1993) [PubMed: 8332508] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Filipenko M.L. Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[3]	"U14 snoRNAs are encoded in introns of human ribosomal protein S13 gene." Kenmochi N., Higa S., Yoshihama M., Tanaka T. Biochem. Biophys. Res. Commun. 228:371-374(1996) [PubMed: 8920921] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Uterus.
[5]	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. Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Bone, Brain, Muscle, Pancreas and Placenta.
[7]	"Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry." Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A. Eur. J. Biochem. 239:144-149(1996) [PubMed: 8706699] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-8. Tissue: Placenta.
[8]	Bhat K.S. Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 12-127.
[9]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-38, MASS SPECTROMETRY.
[10]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-128 AND TYR-129, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-27 AND LYS-39, MASS SPECTROMETRY.
[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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L01124 mRNA. Translation: AAA60283.1. X79239 mRNA. Translation: CAA55821.1. D88010 Genomic DNA. Translation: BAA13528.1. AK312060 mRNA. Translation: BAG34996.1. CH471064 Genomic DNA. Translation: EAW68448.1. BC000475 mRNA. Translation: AAH00475.1. BC006772 mRNA. Translation: AAH06772.1. BC029732 mRNA. Translation: AAH29732.1. BC066322 mRNA. Translation: AAH66322.1. BC100032 mRNA. Translation: AAI00033.1. L05090 mRNA. Translation: AAC15854.1.
IPI	IPI00221089.
PIR	S34109.
RefSeq	NP_001008.1. NM_001017.2.
UniGene	Hs.446588.
3D structure databases
ProteinModelPortal	P62277.
SMR	P62277. Positions 3-151.
ModBase	Search...
Protein-protein interaction databases
IntAct	P62277. 11 interactions.
MINT	MINT-4999984.
STRING	P62277.
PTM databases
PhosphoSite	P62277.
Polymorphism databases
DMDM	50403608.
Proteomic databases
PeptideAtlas	P62277.
PRIDE	P62277.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000228140; ENSP00000228140; ENSG00000110700.
GeneID	6207.
KEGG	hsa:6207.
UCSC	uc001mmp.1. human.
Organism-specific databases
CTD	6207.
GeneCards	GC11M017055.
H-InvDB	HIX0201653.
HGNC	HGNC:10386. RPS13.
HPA	HPA005985.
MIM	180476. gene.
neXtProt	NX_P62277.
PharmGKB	PA34785.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG19195.
GeneTree	ENSGT00390000017491.
HOGENOM	HBG747651.
HOVERGEN	HBG000938.
InParanoid	P62277.
OMA	IRRLVKY.
OrthoDB	EOG4RJG2T.
PhylomeDB	P62277.
Enzyme and pathway databases
Reactome	REACT_111045. Developmental Biology. REACT_111217. Metabolism. REACT_15380. Diabetes pathways. REACT_17015. Metabolism of proteins. REACT_1762. 3' -UTR-mediated translational regulation. REACT_6167. Influenza Infection. REACT_71. Gene Expression.
Gene expression databases
CleanEx	HS_RPS13.
Genevestigator	P62277.
GermOnline	ENSG00000110700. Homo sapiens.
Family and domain databases
InterPro	IPR012606. Ribosomal_S13/S15_N. IPR000589. Ribosomal_S15. IPR023029. Ribosomal_S15P. IPR009068. S15_NS1_RNA-bd. [Graphical view]
KO	K02953.
Pfam	PF08069. Ribosomal_S13_N. 1 hit. PF00312. Ribosomal_S15. 1 hit. [Graphical view]
SUPFAM	SSF47060. S15/NS1_bind. 1 hit.
PROSITE	PS00362. RIBOSOMAL_S15. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	24107.
SOURCE	Search...

Entry information

Entry name

RS13_HUMAN

Accession

Primary (citable) accession number: P62277
Secondary accession number(s): B2R549

Q498Y0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2004
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 87 of the entry and version 2 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.

Relevant documents

Ribosomal proteins

Ribosomal proteins families and list of entries

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents