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P23396

- RS3_HUMAN

UniProt

P23396 - RS3_HUMAN

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Protein
40S ribosomal protein S3
Gene
RPS3, OK/SW-cl.26
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. DNA-(apurinic or apyrimidinic site) lyase activity Source: UniProtKB
  2. NF-kappaB binding Source: UniProtKB
  3. damaged DNA binding Source: UniProtKB
  4. endonuclease activity Source: UniProtKB
  5. enzyme binding Source: UniProtKB
  6. iron-sulfur cluster binding Source: UniProtKB
  7. mRNA binding Source: UniProtKB
  8. poly(A) RNA binding Source: UniProtKB
  9. protein binding Source: UniProtKB
  10. protein kinase A binding Source: UniProtKB
  11. protein kinase binding Source: UniProtKB
  12. structural constituent of ribosome Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. DNA catabolic process, endonucleolytic Source: GOC
  2. RNA metabolic process Source: Reactome
  3. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  4. cellular protein metabolic process Source: Reactome
  5. cellular response to DNA damage stimulus Source: UniProtKB
  6. cytoplasmic translation Source: RefGenome
  7. gene expression Source: Reactome
  8. mRNA metabolic process Source: Reactome
  9. negative regulation of DNA repair Source: UniProtKB
  10. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  11. nucleic acid phosphodiester bond hydrolysis Source: GOC
  12. positive regulation of DNA N-glycosylase activity Source: UniProtKB
  13. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  14. positive regulation of apoptotic signaling pathway Source: UniProtKB
  15. translation Source: UniProtKB
  16. translational elongation Source: Reactome
  17. translational initiation Source: UniProtKB
  18. translational termination Source: Reactome
  19. viral life cycle Source: Reactome
  20. viral process Source: Reactome
  21. viral transcription Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding

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 S3
Gene namesi
Name:RPS3
ORF Names:OK/SW-cl.26
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:10420. RPS3.

Subcellular locationi

Cytoplasm
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. cytosolic small ribosomal subunit Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProt
  5. nucleus Source: UniProtKB
  6. ribonucleoprotein complex Source: UniProtKB
  7. ruffle membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34829.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 24324240S ribosomal protein S3
PRO_0000130320Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei62 – 621N6-acetyllysine1 Publication
Cross-linki90 – 90Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei132 – 1321N6-succinyllysine By similarity
Cross-linki202 – 202Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei221 – 2211Phosphothreonine6 Publications
Modified residuei224 – 2241Phosphoserine1 Publication
Modified residuei242 – 2421Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP23396.
PaxDbiP23396.
PeptideAtlasiP23396.
PRIDEiP23396.

PTM databases

PhosphoSiteiP23396.

Expressioni

Gene expression databases

ArrayExpressiP23396.
BgeeiP23396.
CleanExiHS_RPS3.
GenevestigatoriP23396.

Interactioni

Subunit structurei

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with HNRPD. Identified in a HCV IRES-mediated translation complex, at least composed of EIF3C, IGF2BP1, RPS3 and HCV RNA-replicon.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
IKBKBO149204EBI-351193,EBI-81266
LRRK2Q5S0072EBI-351193,EBI-5323863
NEDD8Q158432EBI-351193,EBI-716247
NFKB1P198382EBI-351193,EBI-300010
NFKBIAP259636EBI-351193,EBI-307386
PPIDQ087524EBI-351193,EBI-716596
RELAQ042067EBI-351193,EBI-73886
YWHAZP631042EBI-351193,EBI-347088

Protein-protein interaction databases

BioGridi112102. 178 interactions.
IntActiP23396. 44 interactions.
MINTiMINT-4999144.
STRINGi9606.ENSP00000278572.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi17 – 2812
Turni29 – 335
Beta strandi34 – 418
Beta strandi46 – 538
Helixi55 – 595
Helixi61 – 633
Helixi64 – 7714
Beta strandi83 – 908

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WH9NMR-A17-95[»]
3J3Aelectron microscopy5.00D1-243[»]
ProteinModelPortaliP23396.
SMRiP23396. Positions 1-227.

Miscellaneous databases

EvolutionaryTraceiP23396.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 9272KH type-2
Add
BLAST

Sequence similaritiesi

Contains 1 KH type-2 domain.

Phylogenomic databases

eggNOGiCOG0092.
HOGENOMiHOG000210611.
HOVERGENiHBG002195.
InParanoidiP23396.
KOiK02985.
OMAiVDYPEMI.
OrthoDBiEOG7F7W9M.
PhylomeDBiP23396.
TreeFamiTF300901.

Family and domain databases

Gene3Di3.30.1140.32. 1 hit.
3.30.300.20. 1 hit.
InterProiIPR004087. KH_dom.
IPR015946. KH_dom-like_a/b.
IPR004044. KH_dom_type_2.
IPR009019. KH_prok-type.
IPR001351. Ribosomal_S3_C.
IPR018280. Ribosomal_S3_CS.
IPR005703. Ribosomal_S3_euk/arc.
[Graphical view]
PfamiPF07650. KH_2. 1 hit.
PF00189. Ribosomal_S3_C. 1 hit.
[Graphical view]
SMARTiSM00322. KH. 1 hit.
[Graphical view]
SUPFAMiSSF54814. SSF54814. 1 hit.
SSF54821. SSF54821. 1 hit.
TIGRFAMsiTIGR01008. rpsC_E_A. 1 hit.
PROSITEiPS50823. KH_TYPE_2. 1 hit.
PS00548. RIBOSOMAL_S3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P23396-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MAVQISKKRK FVADGIFKAE LNEFLTRELA EDGYSGVEVR VTPTRTEIII    50
LATRTQNVLG EKGRRIRELT AVVQKRFGFP EGSVELYAEK VATRGLCAIA 100
QAESLRYKLL GGLAVRRACY GVLRFIMESG AKGCEVVVSG KLRGQRAKSM 150
KFVDGLMIHS GDPVNYYVDT AVRHVLLRQG VLGIKVKIML PWDPTGKIGP 200
KKPLPDHVSI VEPKDEILPT TPISEQKGGK PEPPAMPQPV PTA 243
Length:243
Mass (Da):26,688
Last modified:October 1, 1993 - v2
Checksum:i6ECBB34A8EE04AAF
GO
Isoform 2 (identifier: P23396-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     85-85: E → ELKIMVMVTGYPLLPLK

Note: No experimental confirmation available. Gene prediction based on EST data.

Show »
Length:259
Mass (Da):28,487
Checksum:i68FF5C2DF8769693
GO

Sequence cautioni

The sequence BAB93471.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei85 – 851E → ELKIMVMVTGYPLLPLK in isoform 2.
VSP_046667

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81K → R in AAB19349. 1 Publication
Sequence conflicti104 – 1041S → C in CAA39248. 1 Publication
Sequence conflicti233 – 2331P → L in CAA39248. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
AP000744 Genomic DNA. No translation available.
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.
CCDSiCCDS58161.1. [P23396-2]
CCDS8236.1. [P23396-1]
PIRiA41247. R3HUS3.
RefSeqiNP_000996.2. NM_001005.4. [P23396-1]
NP_001243731.1. NM_001256802.1. [P23396-1]
NP_001247435.1. NM_001260506.1. [P23396-2]
NP_001247436.1. NM_001260507.1.
UniGeneiHs.546286.
Hs.740358.

Genome annotation databases

EnsembliENST00000278572; ENSP00000278572; ENSG00000149273. [P23396-2]
ENST00000524851; ENSP00000433821; ENSG00000149273. [P23396-1]
ENST00000527446; ENSP00000436971; ENSG00000149273. [P23396-1]
ENST00000531188; ENSP00000434643; ENSG00000149273. [P23396-1]
GeneIDi6188.
KEGGihsa:6188.
UCSCiuc001owh.4. human. [P23396-1]

Polymorphism databases

DMDMi417719.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
AP000744 Genomic DNA. No translation available.
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.
CCDSi CCDS58161.1. [P23396-2 ]
CCDS8236.1. [P23396-1 ]
PIRi A41247. R3HUS3.
RefSeqi NP_000996.2. NM_001005.4. [P23396-1 ]
NP_001243731.1. NM_001256802.1. [P23396-1 ]
NP_001247435.1. NM_001260506.1. [P23396-2 ]
NP_001247436.1. NM_001260507.1.
UniGenei Hs.546286.
Hs.740358.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WH9 NMR - A 17-95 [» ]
3J3A electron microscopy 5.00 D 1-243 [» ]
ProteinModelPortali P23396.
SMRi P23396. Positions 1-227.
ModBasei Search...

Protein-protein interaction databases

BioGridi 112102. 178 interactions.
IntActi P23396. 44 interactions.
MINTi MINT-4999144.
STRINGi 9606.ENSP00000278572.

PTM databases

PhosphoSitei P23396.

Polymorphism databases

DMDMi 417719.

Proteomic databases

MaxQBi P23396.
PaxDbi P23396.
PeptideAtlasi P23396.
PRIDEi P23396.

Protocols and materials databases

DNASUi 6188.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000278572 ; ENSP00000278572 ; ENSG00000149273 . [P23396-2 ]
ENST00000524851 ; ENSP00000433821 ; ENSG00000149273 . [P23396-1 ]
ENST00000527446 ; ENSP00000436971 ; ENSG00000149273 . [P23396-1 ]
ENST00000531188 ; ENSP00000434643 ; ENSG00000149273 . [P23396-1 ]
GeneIDi 6188.
KEGGi hsa:6188.
UCSCi uc001owh.4. human. [P23396-1 ]

Organism-specific databases

CTDi 6188.
GeneCardsi GC11P075110.
HGNCi HGNC:10420. RPS3.
MIMi 600454. gene.
neXtProti NX_P23396.
PharmGKBi PA34829.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0092.
HOGENOMi HOG000210611.
HOVERGENi HBG002195.
InParanoidi P23396.
KOi K02985.
OMAi VDYPEMI.
OrthoDBi EOG7F7W9M.
PhylomeDBi P23396.
TreeFami TF300901.

Enzyme and pathway databases

Reactomei REACT_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

ChiTaRSi RpS3. human.
EvolutionaryTracei P23396.
GeneWikii RPS3.
GenomeRNAii 6188.
NextBioi 24029.
PROi P23396.
SOURCEi Search...

Gene expression databases

ArrayExpressi P23396.
Bgeei P23396.
CleanExi HS_RPS3.
Genevestigatori P23396.

Family and domain databases

Gene3Di 3.30.1140.32. 1 hit.
3.30.300.20. 1 hit.
InterProi IPR004087. KH_dom.
IPR015946. KH_dom-like_a/b.
IPR004044. KH_dom_type_2.
IPR009019. KH_prok-type.
IPR001351. Ribosomal_S3_C.
IPR018280. Ribosomal_S3_CS.
IPR005703. Ribosomal_S3_euk/arc.
[Graphical view ]
Pfami PF07650. KH_2. 1 hit.
PF00189. Ribosomal_S3_C. 1 hit.
[Graphical view ]
SMARTi SM00322. KH. 1 hit.
[Graphical view ]
SUPFAMi SSF54814. SSF54814. 1 hit.
SSF54821. SSF54821. 1 hit.
TIGRFAMsi TIGR01008. rpsC_E_A. 1 hit.
PROSITEi PS50823. KH_TYPE_2. 1 hit.
PS00548. RIBOSOMAL_S3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORM 1).
    Tissue: Adrenal cortex, Liver, Lymph, Skin and Testis.
  9. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 1-94 (ISOFORM 1).
  10. 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, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma and Colon adenocarcinoma.
  11. "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 (ISOFORM 1).
    Tissue: Colon adenocarcinoma.
  12. 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, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma.
  13. "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 188-197.
    Tissue: Placenta.
  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: 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 THR-221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Pituitary.
  17. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  18. "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 THR-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A HCV IRES-MEDIATED TRANSLATION COMPLEX.
  23. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  24. "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-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "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 THR-221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "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 THR-221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. "AUF1 contributes to Cryptochrome1 mRNA degradation and rhythmic translation."
    Lee K.H., Kim S.H., Kim H.J., Kim W., Lee H.R., Jung Y., Choi J.H., Hong K.Y., Jang S.K., Kim K.T.
    Nucleic Acids Res. 42:3590-3606(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HNRPD.
  30. "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.
  31. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.

Entry informationi

Entry nameiRS3_HUMAN
AccessioniPrimary (citable) accession number: P23396
Secondary accession number(s): B2R7N5
, J3KN86, Q498B5, Q8NI95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: October 1, 1993
Last modified: September 3, 2014
This is version 167 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 11
    Human chromosome 11: 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

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