P23396 (RS3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
40S ribosomal protein S3

Gene names

Name:	RPS3
ORF Names:	OK/SW-cl.26

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	243 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)

Subunit structure	Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Identified in a HCV IRES-mediated translation complex, at least composed of EIF3C, IGF2BP1, RPS3 and HCV RNA-replicon.
Subcellular location	Cytoplasm. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.18
Sequence similarities	Belongs to the ribosomal protein S3P family. Contains 1 KH type-2 domain.
Sequence caution	The sequence BAB93471.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	RNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	activation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from direct assay. Source: UniProtKB endocrine pancreas development Traceable author statement. Source: Reactome induction of apoptosis Inferred from direct assay. Source: UniProtKB mRNA metabolic process Traceable author statement. Source: Reactome negative regulation of DNA repair Inferred from mutant phenotype. Source: UniProtKB negative regulation of NF-kappaB transcription factor activity Inferred from mutant phenotype. Source: UniProtKB response to DNA damage stimulus Inferred from expression pattern. Source: UniProtKB translational elongation Traceable author statement. Source: Reactome translational initiation Non-traceable author statement. Source: UniProtKB 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.12. Source: UniProtKB nucleus Inferred from direct assay. Source: UniProtKB ruffle membrane Inferred from direct assay. Source: UniProtKB
Molecular function	DNA-(apurinic or apyrimidinic site) lyase activity Inferred from direct assay. Source: UniProtKB NF-kappaB binding Inferred from physical interaction. Source: UniProtKB damaged DNA binding Inferred from direct assay. Source: UniProtKB endonuclease activity Inferred from mutant phenotype. Source: UniProtKB iron-sulfur cluster binding Non-traceable author statement. Source: UniProtKB mRNA binding Inferred from direct assay. Source: UniProtKB protein kinase binding Inferred from physical interaction. Source: UniProtKB structural constituent of ribosome Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
IKBKB	O14920	4	EBI-351193,EBI-81266
NFKB1	P19838	2	EBI-351193,EBI-300010
RELA	Q04206	6	EBI-351193,EBI-73886

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.9

Chain

2 – 243

242

40S ribosomal protein S3

PRO_0000130320

Regions

Domain

21 – 92

72

KH type-2

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.9 Ref.24

Modified residue

62

1

N6-acetyllysine Ref.29

Modified residue

166

1

Phosphotyrosine Ref.27

Modified residue

220

1

Phosphothreonine Ref.20 Ref.24 Ref.25

Modified residue

221

1

Phosphothreonine Ref.11 Ref.13 Ref.14 Ref.16 Ref.17 Ref.19 Ref.20 Ref.22 Ref.23 Ref.24 Ref.25 Ref.28

Modified residue

224

1

Phosphoserine Ref.15 Ref.20 Ref.22

Modified residue

242

1

Phosphothreonine Ref.22 Ref.23

Cross-link

90

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.21

Cross-link

202

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.21

Experimental info

Sequence conflict

8

1

K → R in AAB19349. Ref.2

Sequence conflict

104

1

S → C in CAA39248. Ref.1

Sequence conflict

233

1

P → L in CAA39248. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

243

Helix Strand Turn

Details...

Helix

17 – 28

12

Turn

29 – 33

5

Beta strand

34 – 41

8

Beta strand

46 – 53

8

Helix

55 – 59

5

Helix

61 – 63

3

Helix

64 – 77

14

Beta strand

83 – 90

8

Sequences

	Sequence		Length	Mass (Da)
	P23396 [UniParc]. Last modified October 1, 1993. Version 2. Checksum: 6ECBB34A8EE04AAF	FASTA	243	26,688
	10 20 30 40 50 60 MAVQISKKRK FVADGIFKAE LNEFLTRELA EDGYSGVEVR VTPTRTEIII LATRTQNVLG 70 80 90 100 110 120 EKGRRIRELT AVVQKRFGFP EGSVELYAEK VATRGLCAIA QAESLRYKLL GGLAVRRACY 130 140 150 160 170 180 GVLRFIMESG AKGCEVVVSG KLRGQRAKSM KFVDGLMIHS GDPVNYYVDT AVRHVLLRQG 190 200 210 220 230 240 VLGIKVKIML PWDPTGKIGP KKPLPDHVSI VEPKDEILPT TPISEQKGGK PEPPAMPQPV PTA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of a cDNA encoding human 40S ribosomal protein s3." Zhang X.T., Tan Y.M., Tan Y.H. Nucleic Acids Res. 18:6689-6689(1990) [PubMed: 2129557] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Ribosomal protein genes are overexpressed in colorectal cancer: isolation of a cDNA clone encoding the human S3 ribosomal protein." Pogue-Geile K., Geiser J.R., Shu M., Miller C., Wool I.G., Meisler A.I., Pipas J.M. Mol. Cell. Biol. 11:3842-3849(1991) [PubMed: 1712897] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The human ribosomal protein genes: sequencing and comparative analysis of 73 genes." Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N. Genome Res. 12:379-390(2002) [PubMed: 11875025] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	NIEHS SNPs program Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"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.
[6]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: Adrenal cortex, Liver, Lymph, Skin and Testis.
[8]	"A small nucleolar RNA is processed from an intron of the human gene encoding ribosomal protein S3." Tycowski K.T., Shu M.D., Steitz J.A. Genes Dev. 7:1176-1190(1993) [PubMed: 8319909] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1-94.
[9]	Bienvenut W.V., Murray L., Brunton V.G., Frame M.C., Calvo F., Kolch W. Submitted (FEB-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-8; 10-64; 68-116; 118-141; 152-173; 186-197 AND 202-243, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Cervix carcinoma and Colon adenocarcinoma.
[10]	"Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients." Shichijo S., Itoh K. Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-243. Tissue: Colon adenocarcinoma.
[11]	Bienvenut W.V., Waridel P., Quadroni M. Submitted (MAR-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 10-40; 46-54; 76-90; 95-106; 109-116; 118-132; 152-173; 179-185; 188-197 AND 202-243, PHOSPHORYLATION AT THR-221, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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 188-197. Tissue: Placenta.
[13]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, MASS SPECTROMETRY. Tissue: Cervix adenocarcinoma.
[15]	"Phosphoproteomic analysis of the human pituitary." Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F. Pituitary 9:109-120(2006) [PubMed: 16807684] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, MASS SPECTROMETRY. Tissue: Pituitary.
[16]	"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-221, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[17]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Molecular composition of IMP1 ribonucleoprotein granules." Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C. Mol. Cell. Proteomics 6:798-811(2007) [PubMed: 17289661] [Abstract] Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[19]	"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-221, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"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 THR-220; THR-221 AND SER-224, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry." Meierhofer D., Wang X., Huang L., Kaiser P. J. Proteome Res. 7:4566-4576(2008) [PubMed: 18781797] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-90 AND LYS-202, MASS SPECTROMETRY.
[22]	"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 THR-221; SER-224 AND THR-242, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"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 THR-221 AND THR-242, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[24]	"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 THR-220 AND THR-221, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[25]	"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 THR-220 AND THR-221, MASS SPECTROMETRY.
[26]	"IGF2BP1 enhances HCV IRES-mediated translation initiation via the 3'UTR." Weinlich S., Huettelmaier S., Schierhorn A., Behrens S.-E., Ostareck-Lederer A., Ostareck D.H. RNA 15:1528-1542(2009) [PubMed: 19541769] [Abstract] Cited for: IDENTIFICATION IN A HCV IRES-MEDIATED TRANSLATION COMPLEX.
[27]	"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-166, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[28]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[29]	"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-62, MASS SPECTROMETRY.
[30]	"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].
[31]	"Solution structure of the KH domain of human ribosomal protein S3." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2004) to the PDB data bank Cited for: STRUCTURE BY NMR OF 17-95.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U14990 mRNA. Translation: AAB60336.1.
U14991 mRNA. Translation: AAB60337.1.
U14992 mRNA. Translation: AAB60338.1.
X55715 mRNA. Translation: CAA39248.1.
S42658 mRNA. Translation: AAB19349.2.
AB061838 Genomic DNA. Translation: BAB79476.1.
AY791291 Genomic DNA. Translation: AAV40835.1.
AK313051 mRNA. Translation: BAG35882.1.
CH471076 Genomic DNA. Translation: EAW74963.1.
BC003137 mRNA. Translation: AAH03137.1.
BC003577 mRNA. Translation: AAH03577.1.
BC013196 mRNA. Translation: AAH13196.1.
BC034149 mRNA. Translation: AAH34149.1.
BC071917 mRNA. Translation: AAH71917.1.
BC100284 mRNA. Translation: AAI00285.1.
L16016 Genomic DNA. Translation: AAA18095.1.
AB062288 mRNA. Translation: BAB93471.1. Different initiation.

IPI

IPI00011253.

PIR

R3HUS3. A41247.

RefSeq

NP_000996.2. NM_001005.3.

UniGene

Hs.546286.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WH9	NMR	-	A	17-95	[»]

ProteinModelPortal

P23396.

SMR

P23396. Positions 2-193.

ModBase

Search...

Protein-protein interaction databases

IntAct

P23396. 20 interactions.

MINT

MINT-4999144.

STRING

P23396.

PTM databases

PhosphoSite

P23396.

Polymorphism databases

DMDM

417719.

Proteomic databases

PeptideAtlas

P23396.

PRIDE

P23396.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000278572; ENSP00000278572; ENSG00000149273.
ENST00000405680; ENSP00000385909; ENSG00000149273.

GeneID

6188.

KEGG

hsa:6188.

NMPDR

fig|9606.3.peg.6308.

UCSC

uc001owh.1. human.

Organism-specific databases

CTD

6188.

GeneCards

GC11P075110.

H-InvDB

HIX0009946.

HGNC

HGNC:10420. RPS3.

MIM

600454. gene.

neXtProt

NX_P23396.

PharmGKB

PA34829.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG13875.

HOGENOM

HBG748975.

HOVERGEN

HBG002195.

InParanoid

P23396.

OMA

RGMHFRR.

OrthoDB

EOG4GXFNJ.

PhylomeDB

P23396.

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

P23396.

Bgee

P23396.

CleanEx

HS_RPS3.

Genevestigator

P23396.

GermOnline

ENSG00000149273. Homo sapiens.

Family and domain databases

InterPro

IPR004087. KH.
IPR015946. KH_dom-like_a/b.
IPR009019. KH_prok-type.
IPR004044. KH_type_2.
IPR001351. Ribosomal_S3_C.
IPR018280. Ribosomal_S3_CS.
IPR005703. Ribosomal_S3_euk/arc.
[Graphical view]

Gene3D

G3DSA:3.30.300.20. KH_prok. 1 hit.
G3DSA:3.30.1140.32. Ribosomal_S3_C. 1 hit.

KO

K02985.

Pfam

PF07650. KH_2. 1 hit.
PF00189. Ribosomal_S3_C. 1 hit.
[Graphical view]

SMART

SM00322. KH. 1 hit.
[Graphical view]

SUPFAM

SSF54814. KH_prok. 1 hit.
SSF54821. Ribosomal_S3_C. 1 hit.

TIGRFAMs

TIGR01008. RpsC_E_A. 1 hit.

PROSITE

PS50823. KH_TYPE_2. 1 hit.
PS00548. RIBOSOMAL_S3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

24029.

SOURCE

Search...

Entry information

Entry name

RS3_HUMAN

Accession

Primary (citable) accession number: P23396
Secondary accession number(s): B2R7N5, Q498B5, Q8NI95

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	October 1, 1993
Last modified:	January 25, 2012
This is version 139 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.