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

P15880 (RS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
40S ribosomal protein S2
Alternative name(s):
40S ribosomal protein S4
Protein LLRep3
Gene names
Name:RPS2
Synonyms:RPS4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length293 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Post-translational modification

Citrullinated by PADI4 in the Arg/Gly-rich region.

Asymmetric arginine dimethylation by PRMT3 occurs at multiple sites in the Arg/Gly-rich region.

Sequence similarities

Belongs to the ribosomal protein S5P family.

Contains 1 S5 DRBM domain.

Sequence caution

The sequence CAA35078.1 differs from that shown. Reason: Frameshift at positions 14, 27, 40, 46, 48 and 52.

Ontologies

Keywords
   DomainRepeat
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMAcetylation
Citrullination
Methylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
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

positive regulation of transferase activity

Inferred from direct assay PubMed 18573314. Source: UniProtKB

translation

Inferred by curator PubMed 15883184Ref.5. 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_componentcytosol

Traceable author statement. Source: Reactome

cytosolic small ribosomal subunit

Inferred from direct assay PubMed 15883184Ref.5. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

nucleoplasm

Inferred from direct assay PubMed 16061210PubMed 16263090. Source: UniProtKB

   Molecular_functionenzyme binding

Inferred from physical interaction PubMed 18573314Ref.12. Source: UniProtKB

fibroblast growth factor binding

Inferred from physical interaction PubMed 16263090. Source: UniProtKB

mRNA binding

Inferred from direct assay PubMed 18464793. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

structural constituent of ribosome

Inferred from direct assay PubMed 15883184. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.13
Chain2 – 29329240S ribosomal protein S2
PRO_0000131673

Regions

Domain102 – 16564S5 DRBM
Compositional bias22 – 5332Arg/Gly-rich

Amino acid modifications

Modified residue21N-acetylalanine Ref.13
Modified residue2631N6-acetyllysine Ref.9
Modified residue2641Phosphoserine Ref.7 Ref.10
Modified residue2751N6-acetyllysine Ref.9
Modified residue2811Phosphoserine Ref.10

Sequences

Sequence LengthMass (Da)Tools
P15880 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 66C0DB7ED393B036

FASTA29331,324
        10         20         30         40         50         60 
MADDAGAAGG PGGPGGPGMG NRGGFRGGFG SGIRGRGRGR GRGRGRGRGA RGGKAEDKEW 

        70         80         90        100        110        120 
MPVTKLGRLV KDMKIKSLEE IYLFSLPIKE SEIIDFFLGA SLKDEVLKIM PVQKQTRAGQ 

       130        140        150        160        170        180 
RTRFKAFVAI GDYNGHVGLG VKCSKEVATA IRGAIILAKL SIVPVRRGYW GNKIGKPHTV 

       190        200        210        220        230        240 
PCKVTGRCGS VLVRLIPAPR GTGIVSAPVP KKLLMMAGID DCYTSARGCT ATLGNFAKAT 

       250        260        270        280        290 
FDAISKTYSY LTPDLWKETV FTKSPYQEFT DHLVKTHTRV SVQRTQAPAV ATT 

« Hide

References

« Hide 'large scale' references
[1]"Human cDNA sequence homologous to the mouse LLRep3 gene family."
Slynn G., Jenner D., Potts W., Elvin P., Morten J.E.N., Markham A.F.
Nucleic Acids Res. 18:681-681(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Colon.
[2]"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].
Tissue: Brain.
[3]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. expand/collapse author list , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: Brain, Cervix, Colon, Eye, Kidney, Lung, Mammary gland, Muscle, Placenta, Skin, Testis and Uterus.
[5]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 276-291.
Tissue: Placenta.
[6]"Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3)."
Swiercz R., Person M.D., Bedford M.T.
Biochem. J. 386:85-91(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION BY PRMT3.
[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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"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-263 AND LYS-275, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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-264 AND SER-281, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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].
[12]"Discovery of peptidylarginine deiminase-4 substrates by protein array: antagonistic citrullination and methylation of human ribosomal protein S2."
Guo Q., Bedford M.T., Fast W.
Mol. Biosyst. 7:2286-2295(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: CITRULLINATION.
[13]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[14]"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
X17206 mRNA. Translation: CAA35078.1. Frameshift.
AK312173 mRNA. Translation: BAG35107.1.
CH471112 Genomic DNA. Translation: EAW85592.1.
CH471112 Genomic DNA. Translation: EAW85595.1.
BC001795 mRNA. Translation: AAH01795.1.
BC006559 mRNA. Translation: AAH06559.1.
BC008862 mRNA. Translation: AAH08862.1.
BC010165 mRNA. Translation: AAH10165.1.
BC012354 mRNA. Translation: AAH12354.1.
BC016178 mRNA. Translation: AAH16178.1.
BC016951 mRNA. Translation: AAH16951.1.
BC018993 mRNA. Translation: AAH18993.1.
BC021545 mRNA. Translation: AAH21545.1.
BC023541 mRNA. Translation: AAH23541.1.
BC025677 mRNA. Translation: AAH25677.1.
BC066321 mRNA. Translation: AAH66321.1.
BC068051 mRNA. Translation: AAH68051.1.
BC071922 mRNA. Translation: AAH71922.1.
BC071923 mRNA. Translation: AAH71923.1.
BC071924 mRNA. Translation: AAH71924.1.
BC073966 mRNA. Translation: AAH73966.1.
BC075830 mRNA. Translation: AAH75830.1.
BC103756 mRNA. Translation: AAI03757.1.
BC105985 mRNA. Translation: AAI05986.1.
PIRS08228.
RefSeqNP_002943.2. NM_002952.3.
UniGeneHs.356366.
Hs.381079.
Hs.498569.
Hs.506997.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Aelectron microscopy5.00C1-293[»]
ProteinModelPortalP15880.
SMRP15880. Positions 1-279.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112101. 188 interactions.
IntActP15880. 31 interactions.
MINTMINT-3008399.
STRING9606.ENSP00000341885.

PTM databases

PhosphoSiteP15880.

Polymorphism databases

DMDM1710756.

Proteomic databases

PaxDbP15880.
PRIDEP15880.

Protocols and materials databases

DNASU6187.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000343262; ENSP00000341885; ENSG00000140988.
GeneID6187.
KEGGhsa:6187.
UCSCuc002cnn.2. human.

Organism-specific databases

CTD6187.
GeneCardsGC16M002012.
H-InvDBHIX0029256.
HIX0039223.
HIX0202579.
HGNCHGNC:10404. RPS2.
HPAHPA055133.
MIM603624. gene.
neXtProtNX_P15880.
PharmGKBPA34806.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0098.
HOGENOMHOG000072596.
HOVERGENHBG000437.
InParanoidP15880.
KOK02981.
OMAGIKDVWT.
OrthoDBEOG7P5T1Q.
PhylomeDBP15880.
TreeFamTF300806.

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

BgeeP15880.
CleanExHS_RPS2.
GenevestigatorP15880.

Family and domain databases

Gene3D3.30.160.20. 1 hit.
3.30.230.10. 1 hit.
InterProIPR014720. dsRNA-bd_dom.
IPR000851. Ribosomal_S5.
IPR005324. Ribosomal_S5_C.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR005711. Ribosomal_S5_euk/arc.
IPR013810. Ribosomal_S5_N.
IPR018192. Ribosomal_S5_N_CS.
[Graphical view]
PANTHERPTHR13718. PTHR13718. 1 hit.
PfamPF00333. Ribosomal_S5. 1 hit.
PF03719. Ribosomal_S5_C. 1 hit.
[Graphical view]
SUPFAMSSF54211. SSF54211. 1 hit.
TIGRFAMsTIGR01020. rpsE_arch. 1 hit.
PROSITEPS00585. RIBOSOMAL_S5. 1 hit.
PS50881. S5_DSRBD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRPS2.
GenomeRNAi6187.
NextBio24025.
PROP15880.
SOURCESearch...

Entry information

Entry nameRS2_HUMAN
AccessionPrimary (citable) accession number: P15880
Secondary accession number(s): B2R5G0, D3DU82, Q3MIB1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 154 of the entry and version 2 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 chromosome 16

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