P61247 (RS3A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
40S ribosomal protein S3a

Alternative name(s):
v-fos transformation effector protein
Short name=Fte-1

Gene names

Name:	RPS3A
Synonyms:	FTE1, MFTL

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	264 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)

Function	May play a role during erythropoiesis through regulation of transcription factor DDIT3 By similarity. HAMAP-Rule MF_03122
Subunit structure	Component of the small ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains about 33 different proteins and 1 molecule of RNA (18S). The 60S subunit contains about 49 different proteins and 3 molecules of RNA (28S, 5.8S and 5S). 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. Binds with high affinity to IPO4. Interacts with DDIT3 By similarity. Ref.12 Ref.16
Subcellular location	Cytoplasm. Nucleus By similarity. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.16
Sequence similarities	Belongs to the ribosomal protein S3Ae family.

Ontologies

Keywords
Biological process	Differentiation
Cellular component	Cytoplasm Nucleus
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	SRP-dependent cotranslational protein targeting to membrane Traceable author statement. Source: Reactome cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW induction of apoptosis Inferred from mutant phenotype PubMed 9566973. Source: UniProtKB nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Traceable author statement. Source: Reactome translational elongation Traceable author statement. Source: Reactome translational initiation Traceable author statement PubMed 9566973. 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 PubMed 15883184Ref.9. Source: UniProtKB nucleolus Inferred from direct assay PubMed 15572026. Source: UniProtKB
Molecular_function	RNA binding Non-traceable author statement Ref.1. Source: UniProtKB structural constituent of ribosome Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HSP90AA1	P07900	2	EBI-352378,EBI-296047

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.9
	Chain	2 – 264	263	40S ribosomal protein S3a HAMAP-Rule MF_03122		PRO_0000153524
Amino acid modifications
	Modified residue	34	1	N6-acetyllysine Ref.19
	Modified residue	249	1	N6-acetyllysine Ref.19
	Modified residue	256	1	Phosphotyrosine Ref.13
	Modified residue	263	1	Phosphoserine Ref.14 Ref.15 Ref.17 Ref.18 Ref.20 Ref.22

Sequences

	Sequence		Length	Mass (Da)
	P61247 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 000037AE195F7A9D	FASTA	264	29,945
	10 20 30 40 50 60 MAVGKNKRLT KGGKKGAKKK VVDPFSKKDW YDVKAPAMFN IRNIGKTLVT RTQGTKIASD 70 80 90 100 110 120 GLKGRVFEVS LADLQNDEVA FRKFKLITED VQGKNCLTNF HGMDLTRDKM CSMVKKWQTM 130 140 150 160 170 180 IEAHVDVKTT DGYLLRLFCV GFTKKRNNQI RKTSYAQHQQ VRQIRKKMME IMTREVQTND 190 200 210 220 230 240 LKEVVNKLIP DSIGKDIEKA CQSIYPLHDV FVRKVKMLKK PKFELGKLME LHGEGSSSGK 250 260 ATGDETGAKV ERADGYEPPV QESV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human ribosomal protein S3a: cloning of the cDNA and primary structure of the protein." Metspalu A., Rebane A., Hoth S., Pooga M., Stahl J., Kruppa J. Gene 119:313-316(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Fte-1, a v-fos transformation effector gene, encodes the mammalian homologue of a yeast gene involved in protein import into mitochondria." Kho C.J., Zarbl H. Proc. Natl. Acad. Sci. U.S.A. 89:2200-2204(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	Bonaldo M., Soares M.B. Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[4]	"The human S3a ribosomal protein: sequence, location and cell-free transcription of the functional gene." Nolte D., Taimor G., Kalff-Suske M., Seifart K.H. Gene 169:179-185(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[7]	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].
[8]	"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: B-cell, Eye, Muscle, Ovary, Skin and Uterus.
[9]	"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 2-13. Tissue: Placenta.
[10]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 206-262.
[11]	"The S3a ribosomal protein gene is identical to the Fte-1 (v-fos transformation effector) gene and the TNF-alpha-induced TU-11 gene, and its transcript level is altered in transformed and tumor cells." Lecomte F., Szpirer J., Szpirer C. Gene 186:271-277(1997) [PubMed] [Europe PMC] [Abstract] Cited for: GENE NOMENCLATURE.
[12]	"Importins fulfill a dual function as nuclear import receptors and cytoplasmic chaperones for exposed basic domains." Jaekel S., Mingot J.-M., Schwarzmaier P., Hartmann E., Goerlich D. EMBO J. 21:377-386(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH IPO4.
[13]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-256, MASS SPECTROMETRY.
[14]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[17]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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-263, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"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-34 AND LYS-249, MASS SPECTROMETRY.
[20]	"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-263, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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].
[22]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M77234 mRNA. Translation: AAA60290.1. M84711 mRNA. Translation: AAA58487.1. L13802 mRNA. Translation: AAA35682.1. X87373 Genomic DNA. Translation: CAA60827.1. AC095055 Genomic DNA. No translation available. AK311788 mRNA. Translation: BAG34731.1. CH471056 Genomic DNA. Translation: EAX04991.1. CH471056 Genomic DNA. Translation: EAX04995.1. BC000204 mRNA. Translation: AAH00204.1. BC001708 mRNA. Translation: AAH01708.1. BC004981 mRNA. Translation: AAH04981.1. BC006298 mRNA. Translation: AAH06298.1. BC009219 mRNA. Translation: AAH09219.1. BC009404 mRNA. Translation: AAH09404.1. BC017123 mRNA. Translation: AAH17123.1. BC019072 mRNA. Translation: AAH19072.1. BC030161 mRNA. Translation: AAH30161.1. BC070211 mRNA. Translation: AAH70211.1. BC071916 mRNA. Translation: AAH71916.1. AB007148 Genomic DNA. Translation: BAA25814.1.
IPI	IPI00419880.
PIR	JC4662.
RefSeq	NP_000997.1. NM_001006.4.
UniGene	Hs.356572.
3D structure databases
ProteinModelPortal	P61247.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29408N.
IntAct	P61247. 22 interactions.
MINT	MINT-1160853.
STRING	9606.ENSP00000346050.
PTM databases
PhosphoSite	P61247.
Polymorphism databases
DMDM	47117764.
2D gel databases
SWISS-2DPAGE	P61247.
Proteomic databases
PaxDb	P61247.
PRIDE	P61247.
Protocols and materials databases
DNASU	6189.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000274065; ENSP00000346050; ENSG00000145425.
GeneID	6189.
KEGG	hsa:6189.
UCSC	uc003ilz.3. human.
Organism-specific databases
CTD	6189.
GeneCards	GC04P152020.
HGNC	HGNC:10421. RPS3A.
HPA	HPA047100.
MIM	180478. gene.
neXtProt	NX_P61247.
PharmGKB	PA34830.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1890.
HOGENOM	HOG000105220.
HOVERGEN	HBG000783.
InParanoid	P61247.
KO	K02984.
OMA	GHDTTRE.
OrthoDB	EOG4HX51Q.
PhylomeDB	P61247.
Enzyme and pathway databases
Reactome	REACT_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
ArrayExpress	P61247.
Bgee	P61247.
CleanEx	HS_RPS3A.
Genevestigator	P61247.
GermOnline	ENSG00000145425. Homo sapiens.
Family and domain databases
HAMAP	MF_03122. Ribosomal_S3Ae_euk.
InterPro	IPR027500. Ribosomal_S1/3_euk. IPR001593. Ribosomal_S3Ae. IPR018281. Ribosomal_S3Ae_CS. [Graphical view]
Pfam	PF01015. Ribosomal_S3Ae. 1 hit. [Graphical view]
PROSITE	PS01191. RIBOSOMAL_S3AE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	6189.
NextBio	24033.
PMAP-CutDB	P61247.
SOURCE	Search...

Entry information

Entry name

RS3A_HUMAN

Accession

Primary (citable) accession number: P61247
Secondary accession number(s): B2R4D4 , D3DP05, P33443, P49241

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2004
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 100 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.