40S ribosomal protein S11 - Homo sapiens (Human)

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P62280 (RS11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 92. 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 S11

Gene names

Name:

RPS11

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	158 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 S17P family.

Ontologies

Keywords
Ligand	RNA-binding rRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Acetylation Lipoprotein Palmitate 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 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
Molecular function	rRNA binding Inferred from electronic annotation. Source: UniProtKB-KW structural constituent of ribosome Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
DDX56	Q9NY93	1	EBI-1047710,EBI-372376
EIF1B	O60739	1	EBI-1047710,EBI-1043343
MAGEB2	O15479	1	EBI-1047710,EBI-1057615
NDN	Q99608	1	EBI-1047710,EBI-718177
RUVBL2	Q9Y230	1	EBI-1047710,EBI-352939

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.6

Chain

2 – 158

157

40S ribosomal protein S11

PRO_0000128509

Amino acid modifications

Modified residue

N-acetylalanine Ref.6 Ref.9

Modified residue

Phosphotyrosine Ref.10

Modified residue

Phosphotyrosine Ref.10

Modified residue

Phosphotyrosine Ref.10

Modified residue

N6-acetyllysine Ref.11

Modified residue

N6-acetyllysine Ref.11

Modified residue

Phosphotyrosine Ref.10

Lipidation

S-palmitoyl cysteine Probable

Experimental info

Mutagenesis

C → S: Abolishes S-acylation. Ref.13

Sequences

Sequence

Length

Mass (Da)

Tools

P62280 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 9FB75DC1D99614B0
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FASTA

158

18,431

        10         20         30         40         50         60 
MADIQTERAY QKQPTIFQNK KRVLLGETGK EKLPRYYKNI GLGFKTPKEA IEGTYIDKKC 

        70         80         90        100        110        120 
PFTGNVSIRG RILSGVVTKM KMQRTIVIRR DYLHYIRKYN RFEKRHKNMS VHLSPCFRDV 

       130        140        150 
QIGDIVTVGE CRPLSKTVRF NVLKVTKAAG TKKQFQKF

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of a cloned cDNA encoding human ribosomal protein S11." Lott J.B., Mackie G.A. Nucleic Acids Res. 16:1205-1205(1988) [PubMed: 3267208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Gene organization and sequence of the region containing the ribosomal protein genes RPL13A and RPS11 in the human genome and conserved features in the mouse genome." Higa S., Yoshihama M., Tanaka T., Kenmochi N. Gene 240:371-377(1999) [PubMed: 10580157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Thymus.
[4]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: B-cell, Eye, Lung and Prostate.
[6]	Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M. Submitted (MAY-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-11, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: T-cell.
[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 39-45 AND 137-143. Tissue: Placenta.
[8]	"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: 9582194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-158.
[9]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[10]	"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: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-10; TYR-36; TYR-37 AND TYR-55, MASS SPECTROMETRY.
[11]	"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-38 AND LYS-45, MASS SPECTROMETRY.
[12]	"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].
[13]	"Site-specific analysis of protein S-acylation by resin-assisted capture." Forrester M.T., Hess D.T., Thompson J.W., Hultman R., Moseley M.A., Stamler J.S., Casey P.J. J. Lipid Res. 52:393-398(2011) [PubMed: 21044946] [Abstract] Cited for: MUTAGENESIS OF CYS-60, PALMITOYLATION AT CYS-60.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X06617 mRNA. Translation: CAA29834.1. AB028893 Genomic DNA. Translation: BAA88215.1. AK311809 mRNA. Translation: BAG34752.1. CH471177 Genomic DNA. Translation: EAW52497.1. BC007283 mRNA. Translation: AAH07283.1. BC007603 mRNA. Translation: AAH07603.1. BC007945 mRNA. Translation: AAH07945.1. BC010028 mRNA. Translation: AAH10028.1. BC016378 mRNA. Translation: AAH16378.1. BC070224 mRNA. Translation: AAH70224.1. BC100025 mRNA. Translation: AAI00026.1. AB007152 Genomic DNA. Translation: BAA25818.1.
IPI	IPI00025091.
PIR	R3HU11. S02133.
RefSeq	NP_001006.1. NM_001015.3.
UniGene	Hs.433529.
3D structure databases
ProteinModelPortal	P62280.
SMR	P62280. Positions 3-158.
ModBase	Search...
Protein-protein interaction databases
IntAct	P62280. 8 interactions.
MINT	MINT-1154341.
STRING	P62280.
PTM databases
PhosphoSite	P62280.
Polymorphism databases
DMDM	50403609.
2D gel databases
SWISS-2DPAGE	P62280.
Proteomic databases
PeptideAtlas	P62280.
PRIDE	P62280.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000270625; ENSP00000270625; ENSG00000142534.
GeneID	6205.
KEGG	hsa:6205.
UCSC	uc002pob.1. human.
Organism-specific databases
CTD	6205.
GeneCards	GC19P049999.
H-InvDB	HIX0202820.
HGNC	HGNC:10384. RPS11.
MIM	180471. gene.
neXtProt	NX_P62280.
PharmGKB	PA34782.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG19414.
GeneTree	ENSGT00390000002732.
HOGENOM	HBG750455.
HOVERGEN	HBG004670.
InParanoid	P62280.
OMA	GAKKQFQ.
OrthoDB	EOG4MGS8N.
PhylomeDB	P62280.
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
ArrayExpress	P62280.
Bgee	P62280.
CleanEx	HS_RPS11.
Genevestigator	P62280.
GermOnline	ENSG00000142534. Homo sapiens.
Family and domain databases
InterPro	IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. IPR000266. Ribosomal_S17. IPR019978. Ribosomal_S17_archaeal. IPR019979. Ribosomal_S17_CS. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
KO	K02949.
PANTHER	PTHR10744. Ribosomal_S17. 1 hit.
Pfam	PF00366. Ribosomal_S17. 1 hit. [Graphical view]
PRINTS	PR00973. RIBOSOMALS17.
ProDom	PD001295. Ribosomal_S17. 1 hit. [Graphical view] [Entries sharing at least one domain]
SUPFAM	SSF50249. Nucleic_acid_OB. 1 hit.
TIGRFAMs	TIGR03630. Arch_S17P. 1 hit.
PROSITE	PS00056. RIBOSOMAL_S17. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	24099.
PMAP-CutDB	P62280.
SOURCE	Search...

Entry information

Entry name

RS11_HUMAN

Accession

Primary (citable) accession number: P62280
Secondary accession number(s): B2R4F5

Q6IRY0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 92 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.

Relevant documents

Ribosomal proteins

Ribosomal proteins families and list of entries

Human chromosome 19

Human chromosome 19: 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

2D gel 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