P15880 (RS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
40S ribosomal protein S2

Alternative name(s):
40S ribosomal protein S4
Protein LLRep3

Gene names

Name:	RPS2
Synonyms:	RPS4

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	293 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 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
Domain	Repeat
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 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.5. Source: UniProtKB nucleoplasm Inferred from direct assay. Source: UniProtKB
Molecular function	RNA binding Inferred from electronic annotation. Source: InterPro fibroblast growth factor 1 binding Inferred from physical interaction. Source: UniProtKB fibroblast growth factor 3 binding Inferred from physical interaction. Source: UniProtKB structural constituent of ribosome Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 293	292	40S ribosomal protein S2		PRO_0000131673
Regions
	Domain	102 – 165	64	S5 DRBM
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.12
	Modified residue	77	1	Phosphoserine By similarity
	Modified residue	82	1	Phosphotyrosine By similarity
	Modified residue	85	1	Phosphoserine By similarity
	Modified residue	133	1	Phosphotyrosine Ref.13
	Modified residue	263	1	N6-acetyllysine Ref.14
	Modified residue	264	1	Phosphoserine Ref.6 Ref.10 Ref.11
	Modified residue	275	1	N6-acetyllysine Ref.14
	Modified residue	278	1	Phosphothreonine Ref.8
	Modified residue	281	1	Phosphoserine Ref.6 Ref.12
	Modified residue	293	1	Phosphothreonine Ref.7 Ref.9

Sequences

	Sequence		Length	Mass (Da)
	P15880 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 66C0DB7ED393B036	FASTA	293	31,324
	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

References

	« Hide 'large scale' referencesShow '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: 2308862] [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. , 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: 14702039] [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. , 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: 15489334] [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: 8706699] [Abstract] Cited for: PROTEIN SEQUENCE OF 276-291. Tissue: Placenta.
[6]	"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 SER-264 AND SER-281, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-293, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-278, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[9]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-293, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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-264, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[13]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-133, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[14]	"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-263 AND LYS-275, MASS SPECTROMETRY.
[15]	"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	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.
IPI	IPI00013485.
PIR	S08228.
RefSeq	NP_002943.2. NM_002952.3.
UniGene	Hs.356366. Hs.381079. Hs.498569. Hs.506997.
3D structure databases
ProteinModelPortal	P15880.
SMR	P15880. Positions 1-279.
ModBase	Search...
Protein-protein interaction databases
IntAct	P15880. 11 interactions.
MINT	MINT-3008399.
STRING	P15880.
PTM databases
PhosphoSite	P15880.
Polymorphism databases
DMDM	1710756.
Proteomic databases
PRIDE	P15880.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000343262; ENSP00000341885; ENSG00000140988.
GeneID	6187.
KEGG	hsa:6187.
UCSC	uc002cnn.2. human.
Organism-specific databases
CTD	6187.
GeneCards	GC16M002012.
H-InvDB	HIX0012702. HIX0029256. HIX0202579.
HGNC	HGNC:10404. RPS2.
MIM	603624. gene.
neXtProt	NX_P15880.
PharmGKB	PA34806.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HBG299153.
HOVERGEN	HBG000437.
InParanoid	P15880.
OMA	GIKDVWT.
OrthoDB	EOG4SXND8.
PhylomeDB	P15880.
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
Bgee	P15880.
CleanEx	HS_RPS2.
Genevestigator	P15880.
GermOnline	ENSG00000140988. Homo sapiens.
Family and domain databases
InterPro	IPR014720. dsRNA-bd-like. 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]
Gene3D	G3DSA:3.30.160.20. dsRNA-bd-like. 1 hit. G3DSA:3.30.230.10. Ribosomal_S5_D2-type_fold. 1 hit.
KO	K02981.
PANTHER	PTHR13718. Ribosomal_S5. 1 hit.
Pfam	PF00333. Ribosomal_S5. 1 hit. PF03719. Ribosomal_S5_C. 1 hit. [Graphical view]
SUPFAM	SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.
TIGRFAMs	TIGR01020. RpsE_arch. 1 hit.
PROSITE	PS00585. RIBOSOMAL_S5. 1 hit. PS50881. S5_DSRBD. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	24025.
SOURCE	Search...

Entry information

Entry name

RS2_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 130 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.