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Protein

40S ribosomal protein S3a

Gene

RPS3A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May play a role during erythropoiesis through regulation of transcription factor DDIT3.UniRule annotation

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • structural constituent of ribosome Source: UniProtKB-HAMAP

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Differentiation

Enzyme and pathway databases

ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1979. Translation initiation complex formation.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.
REACT_9491. Viral mRNA Translation.

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S3aUniRule annotation
Alternative name(s):
v-fos transformation effector protein
Short name:
Fte-1
Gene namesi
Name:RPS3AUniRule annotation
Synonyms:FTE1, MFTL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:10421. RPS3A.

Subcellular locationi

  • Cytoplasm UniRule annotation1 Publication
  • Nucleus UniRule annotation

  • Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • cytosolic small ribosomal subunit Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleus Source: UniProtKB
  • ribonucleoprotein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34830.

Polymorphism and mutation databases

BioMutaiRPS3A.
DMDMi47117764.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedUniRule annotation1 Publication
Chaini2 – 26426340S ribosomal protein S3aPRO_0000153524Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei34 – 341N6-acetyllysine1 Publication
Modified residuei56 – 561N6-acetyllysineBy similarity
Modified residuei237 – 2371PhosphoserineBy similarity
Modified residuei249 – 2491N6-acetyllysine1 Publication
Modified residuei256 – 2561Phosphotyrosine1 Publication
Modified residuei263 – 2631Phosphoserine7 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP61247.
PaxDbiP61247.
PRIDEiP61247.

2D gel databases

SWISS-2DPAGEP61247.

PTM databases

PhosphoSiteiP61247.

Miscellaneous databases

PMAP-CutDBP61247.

Expressioni

Gene expression databases

BgeeiP61247.
CleanExiHS_RPS3A.
ExpressionAtlasiP61247. baseline.
GenevisibleiP61247. HS.

Organism-specific databases

HPAiHPA047100.
HPA053454.

Interactioni

Subunit structurei

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 IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Binds with high affinity to IPO4. Interacts with DDIT3.UniRule annotation2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HSP90AA1P079003EBI-352378,EBI-296047

Protein-protein interaction databases

BioGridi112103. 190 interactions.
DIPiDIP-29408N.
IntActiP61247. 29 interactions.
MINTiMINT-1160853.
STRINGi9606.ENSP00000346050.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00AB1-264[»]
5AJ0electron microscopy3.50BB1-264[»]
ProteinModelPortaliP61247.
SMRiP61247. Positions 21-233.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S3Ae family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1890.
GeneTreeiENSGT00390000018433.
HOGENOMiHOG000105220.
HOVERGENiHBG000783.
InParanoidiP61247.
KOiK02984.
OMAiGQNAYTK.
OrthoDBiEOG7Q5HDW.
PhylomeDBiP61247.
TreeFamiTF300037.

Family and domain databases

HAMAPiMF_03122. Ribosomal_S3Ae_euk.
InterProiIPR027500. Ribosomal_S1/3_euk.
IPR001593. Ribosomal_S3Ae.
IPR018281. Ribosomal_S3Ae_CS.
[Graphical view]
PfamiPF01015. Ribosomal_S3Ae. 1 hit.
[Graphical view]
PROSITEiPS01191. RIBOSOMAL_S3AE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P61247-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVGKNKRLT KGGKKGAKKK VVDPFSKKDW YDVKAPAMFN IRNIGKTLVT
60 70 80 90 100
RTQGTKIASD GLKGRVFEVS LADLQNDEVA FRKFKLITED VQGKNCLTNF
110 120 130 140 150
HGMDLTRDKM CSMVKKWQTM IEAHVDVKTT DGYLLRLFCV GFTKKRNNQI
160 170 180 190 200
RKTSYAQHQQ VRQIRKKMME IMTREVQTND LKEVVNKLIP DSIGKDIEKA
210 220 230 240 250
CQSIYPLHDV FVRKVKMLKK PKFELGKLME LHGEGSSSGK ATGDETGAKV
260
ERADGYEPPV QESV
Length:264
Mass (Da):29,945
Last modified:January 23, 2007 - v2
Checksum:i000037AE195F7A9D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3775.1.
PIRiJC4662.
RefSeqiNP_000997.1. NM_001006.4.
UniGeneiHs.356572.

Genome annotation databases

EnsembliENST00000274065; ENSP00000346050; ENSG00000145425.
GeneIDi6189.
KEGGihsa:6189.
UCSCiuc003ilz.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3775.1.
PIRiJC4662.
RefSeqiNP_000997.1. NM_001006.4.
UniGeneiHs.356572.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00AB1-264[»]
5AJ0electron microscopy3.50BB1-264[»]
ProteinModelPortaliP61247.
SMRiP61247. Positions 21-233.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112103. 190 interactions.
DIPiDIP-29408N.
IntActiP61247. 29 interactions.
MINTiMINT-1160853.
STRINGi9606.ENSP00000346050.

PTM databases

PhosphoSiteiP61247.

Polymorphism and mutation databases

BioMutaiRPS3A.
DMDMi47117764.

2D gel databases

SWISS-2DPAGEP61247.

Proteomic databases

MaxQBiP61247.
PaxDbiP61247.
PRIDEiP61247.

Protocols and materials databases

DNASUi6189.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000274065; ENSP00000346050; ENSG00000145425.
GeneIDi6189.
KEGGihsa:6189.
UCSCiuc003ilz.4. human.

Organism-specific databases

CTDi6189.
GeneCardsiGC04P152020.
HGNCiHGNC:10421. RPS3A.
HPAiHPA047100.
HPA053454.
MIMi180478. gene.
neXtProtiNX_P61247.
PharmGKBiPA34830.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1890.
GeneTreeiENSGT00390000018433.
HOGENOMiHOG000105220.
HOVERGENiHBG000783.
InParanoidiP61247.
KOiK02984.
OMAiGQNAYTK.
OrthoDBiEOG7Q5HDW.
PhylomeDBiP61247.
TreeFamiTF300037.

Enzyme and pathway databases

ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1979. Translation initiation complex formation.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.
REACT_9491. Viral mRNA Translation.

Miscellaneous databases

GeneWikiiRPS3A.
GenomeRNAii6189.
NextBioi24033.
PMAP-CutDBP61247.
PROiP61247.
SOURCEiSearch...

Gene expression databases

BgeeiP61247.
CleanExiHS_RPS3A.
ExpressionAtlasiP61247. baseline.
GenevisibleiP61247. HS.

Family and domain databases

HAMAPiMF_03122. Ribosomal_S3Ae_euk.
InterProiIPR027500. Ribosomal_S1/3_euk.
IPR001593. Ribosomal_S3Ae.
IPR018281. Ribosomal_S3Ae_CS.
[Graphical view]
PfamiPF01015. Ribosomal_S3Ae. 1 hit.
[Graphical view]
PROSITEiPS01191. RIBOSOMAL_S3AE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  26. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.

Entry informationi

Entry nameiRS3A_HUMAN
AccessioniPrimary (citable) accession number: P61247
Secondary accession number(s): B2R4D4
, D3DP05, P33443, P49241
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Ribosomal proteins
    Ribosomal proteins families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.