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P39023

- RL3_HUMAN

UniProt

P39023 - RL3_HUMAN

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Protein

60S ribosomal protein L3

Gene

RPL3

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

Functioni

The L3 protein is a component of the large subunit of cytoplasmic ribosomes.

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. RNA binding Source: ProtInc
  3. structural constituent of ribosome Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. cellular response to interleukin-4 Source: Ensembl
  3. gene expression Source: Reactome
  4. mRNA metabolic process Source: Reactome
  5. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  6. RNA metabolic process Source: Reactome
  7. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  8. translation Source: UniProtKB
  9. translational elongation Source: Reactome
  10. translational initiation Source: Reactome
  11. translational termination Source: Reactome
  12. viral life cycle Source: Reactome
  13. viral process Source: Reactome
  14. viral transcription Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
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_9491. Viral mRNA Translation.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L3
Alternative name(s):
HIV-1 TAR RNA-binding protein B
Short name:
TARBP-B
Gene namesi
Name:RPL3
ORF Names:OK/SW-cl.32
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:10332. RPL3.

Subcellular locationi

Nucleusnucleolus 1 Publication. Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. cytosolic large ribosomal subunit Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProt
  5. focal adhesion Source: UniProtKB
  6. nucleolus Source: UniProtKB
  7. nucleus Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34713.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 40340260S ribosomal protein L3PRO_0000077227Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131Phosphoserine2 Publications
Modified residuei136 – 1361N6-acetyllysineBy similarity
Modified residuei286 – 2861N6-acetyllysineBy similarity
Modified residuei294 – 2941N6-acetyllysine1 Publication
Modified residuei304 – 3041Phosphoserine1 Publication
Modified residuei366 – 3661N6-acetyllysine1 Publication
Modified residuei373 – 3731N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP39023.
PaxDbiP39023.
PRIDEiP39023.

2D gel databases

SWISS-2DPAGEP39023.

PTM databases

PhosphoSiteiP39023.

Expressioni

Gene expression databases

BgeeiP39023.
CleanExiHS_RPL3.
ExpressionAtlasiP39023. baseline and differential.
GenevestigatoriP39023.

Organism-specific databases

HPAiHPA003365.
HPA055361.

Interactioni

Subunit structurei

Interacts with METTL18.1 Publication

Protein-protein interaction databases

BioGridi112042. 114 interactions.
IntActiP39023. 25 interactions.
MINTiMINT-1145548.
STRINGi9606.ENSP00000346001.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Belectron microscopy5.00B1-403[»]
ProteinModelPortaliP39023.
SMRiP39023. Positions 2-398.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L3P family.Curated

Phylogenomic databases

eggNOGiCOG0087.
GeneTreeiENSGT00390000017606.
HOGENOMiHOG000107319.
HOVERGENiHBG001864.
InParanoidiP39023.
KOiK02925.
OMAiFQTFEEK.
PhylomeDBiP39023.
TreeFamiTF300555.

Family and domain databases

InterProiIPR000597. Ribosomal_L3.
IPR019926. Ribosomal_L3_CS.
IPR009000. Transl_B-barrel.
[Graphical view]
PfamiPF00297. Ribosomal_L3. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
PROSITEiPS00474. RIBOSOMAL_L3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P39023-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSHRKFSAPR HGSLGFLPRK RSSRHRGKVK SFPKDDPSKP VHLTAFLGYK
60 70 80 90 100
AGMTHIVREV DRPGSKVNKK EVVEAVTIVE TPPMVVVGIV GYVETPRGLR
110 120 130 140 150
TFKTVFAEHI SDECKRRFYK NWHKSKKKAF TKYCKKWQDE DGKKQLEKDF
160 170 180 190 200
SSMKKYCQVI RVIAHTQMRL LPLRQKKAHL MEIQVNGGTV AEKLDWARER
210 220 230 240 250
LEQQVPVNQV FGQDEMIDVI GVTKGKGYKG VTSRWHTKKL PRKTHRGLRK
260 270 280 290 300
VACIGAWHPA RVAFSVARAG QKGYHHRTEI NKKIYKIGQG YLIKDGKLIK
310 320 330 340 350
NNASTDYDLS DKSINPLGGF VHYGEVTNDF VMLKGCVVGT KKRVLTLRKS
360 370 380 390 400
LLVQTKRRAL EKIDLKFIDT TSKFGHGRFQ TMEEKKAFMG PLKKDRIAKE

EGA
Length:403
Mass (Da):46,109
Last modified:January 23, 2007 - v2
Checksum:iA607CEE75CF62148
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221S → T in AAA91344. (PubMed:7576925)Curated
Sequence conflicti260 – 2601A → V in AAA91344. (PubMed:7576925)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111H → R Rare variant found in a Diamond-Blackfan anemia patient; unknown pathological significance. 1 Publication
VAR_069220
Natural varianti78 – 781I → T.
Corresponds to variant rs11548004 [ dbSNP | Ensembl ].
VAR_052040

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X73460 mRNA. Translation: CAA51839.1.
AB062291 mRNA. Translation: BAB93474.1.
CR456566 mRNA. Translation: CAG30452.1.
AK315693 mRNA. Translation: BAG38056.1.
AL022326 Genomic DNA. Translation: CAA18450.1.
BC002408 mRNA. Translation: AAH02408.1.
BC006483 mRNA. Translation: AAH06483.1.
BC008003 mRNA. Translation: AAH08003.1.
BC012146 mRNA. Translation: AAH12146.1.
BC012786 mRNA. Translation: AAH12786.1.
BC013674 mRNA. Translation: AAH13674.1.
BC014017 mRNA. Translation: AAH14017.1.
BC015032 mRNA. Translation: AAH15032.1.
BC015767 mRNA. Translation: AAH15767.1.
BC063662 mRNA. Translation: AAH63662.1.
BC088373 mRNA. Translation: AAH88373.1.
BC107711 mRNA. Translation: AAI07712.1.
M90054 mRNA. Translation: AAA60291.1.
L22453 mRNA. Translation: AAA91344.1.
AB007166 Genomic DNA. Translation: BAA25828.1.
CCDSiCCDS13988.1.
PIRiS34195.
RefSeqiNP_000958.1. NM_000967.3.
UniGeneiHs.119598.

Genome annotation databases

EnsembliENST00000216146; ENSP00000346001; ENSG00000100316.
GeneIDi6122.
KEGGihsa:6122.
UCSCiuc003axh.3. human.

Polymorphism databases

DMDMi730565.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X73460 mRNA. Translation: CAA51839.1 .
AB062291 mRNA. Translation: BAB93474.1 .
CR456566 mRNA. Translation: CAG30452.1 .
AK315693 mRNA. Translation: BAG38056.1 .
AL022326 Genomic DNA. Translation: CAA18450.1 .
BC002408 mRNA. Translation: AAH02408.1 .
BC006483 mRNA. Translation: AAH06483.1 .
BC008003 mRNA. Translation: AAH08003.1 .
BC012146 mRNA. Translation: AAH12146.1 .
BC012786 mRNA. Translation: AAH12786.1 .
BC013674 mRNA. Translation: AAH13674.1 .
BC014017 mRNA. Translation: AAH14017.1 .
BC015032 mRNA. Translation: AAH15032.1 .
BC015767 mRNA. Translation: AAH15767.1 .
BC063662 mRNA. Translation: AAH63662.1 .
BC088373 mRNA. Translation: AAH88373.1 .
BC107711 mRNA. Translation: AAI07712.1 .
M90054 mRNA. Translation: AAA60291.1 .
L22453 mRNA. Translation: AAA91344.1 .
AB007166 Genomic DNA. Translation: BAA25828.1 .
CCDSi CCDS13988.1.
PIRi S34195.
RefSeqi NP_000958.1. NM_000967.3.
UniGenei Hs.119598.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3J3B electron microscopy 5.00 B 1-403 [» ]
ProteinModelPortali P39023.
SMRi P39023. Positions 2-398.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112042. 114 interactions.
IntActi P39023. 25 interactions.
MINTi MINT-1145548.
STRINGi 9606.ENSP00000346001.

Chemistry

DrugBanki DB04865. Homoharringtonine.

PTM databases

PhosphoSitei P39023.

Polymorphism databases

DMDMi 730565.

2D gel databases

SWISS-2DPAGE P39023.

Proteomic databases

MaxQBi P39023.
PaxDbi P39023.
PRIDEi P39023.

Protocols and materials databases

DNASUi 6122.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000216146 ; ENSP00000346001 ; ENSG00000100316 .
GeneIDi 6122.
KEGGi hsa:6122.
UCSCi uc003axh.3. human.

Organism-specific databases

CTDi 6122.
GeneCardsi GC22M040108.
H-InvDB HIX0172339.
HGNCi HGNC:10332. RPL3.
HPAi HPA003365.
HPA055361.
MIMi 604163. gene.
neXtProti NX_P39023.
PharmGKBi PA34713.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0087.
GeneTreei ENSGT00390000017606.
HOGENOMi HOG000107319.
HOVERGENi HBG001864.
InParanoidi P39023.
KOi K02925.
OMAi FQTFEEK.
PhylomeDBi P39023.
TreeFami TF300555.

Enzyme and pathway databases

Reactomei 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_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_9491. Viral mRNA Translation.

Miscellaneous databases

ChiTaRSi RPL3. human.
GeneWikii RPL3.
GenomeRNAii 6122.
NextBioi 23777.
PROi P39023.
SOURCEi Search...

Gene expression databases

Bgeei P39023.
CleanExi HS_RPL3.
ExpressionAtlasi P39023. baseline and differential.
Genevestigatori P39023.

Family and domain databases

InterProi IPR000597. Ribosomal_L3.
IPR019926. Ribosomal_L3_CS.
IPR009000. Transl_B-barrel.
[Graphical view ]
Pfami PF00297. Ribosomal_L3. 1 hit.
[Graphical view ]
SUPFAMi SSF50447. SSF50447. 1 hit.
PROSITEi PS00474. RIBOSOMAL_L3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complete coding sequence of human ribosomal protein L3 mRNA."
    Leffers H.
    Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
    Shichijo S., Itoh K.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon adenocarcinoma.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "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: Testis.
  5. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Brain, Colon, Lung, Muscle, Ovary, PNS, Skin and Uterus.
  7. Still I.H.
    Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-403.
  8. "Molecular cloning and characterization of a TAR-binding nuclear factor from T cells."
    Reddy T.R., Suhasini M., Rappaport J., Looney D.J., Kraus G., Wong-Staal F.
    AIDS Res. Hum. Retroviruses 11:663-669(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-277.
  9. "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 328-398.
  10. "Characterization and analysis of posttranslational modifications of the human large cytoplasmic ribosomal subunit proteins by mass spectrometry and Edman sequencing."
    Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R., Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B., Karpova G.G.
    J. Protein Chem. 22:249-258(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13, IDENTIFICATION BY MASS SPECTROMETRY.
  11. "NOP132 is required for proper nucleolus localization of DEAD-box RNA helicase DDX47."
    Sekiguchi T., Hayano T., Yanagida M., Takahashi N., Nishimoto T.
    Nucleic Acids Res. 34:4593-4608(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-294 AND LYS-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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-304, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity."
    Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.
    PLoS Genet. 9:E1003210-E1003210(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH METTL18.
  19. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.
  20. "Frameshift mutation in p53 regulator RPL26 is associated with multiple physical abnormalities and a specific pre-ribosomal RNA processing defect in diamond-blackfan anemia."
    Gazda H.T., Preti M., Sheen M.R., O'Donohue M.F., Vlachos A., Davies S.M., Kattamis A., Doherty L., Landowski M., Buros C., Ghazvinian R., Sieff C.A., Newburger P.E., Niewiadomska E., Matysiak M., Glader B., Atsidaftos E., Lipton J.M., Gleizes P.E., Beggs A.H.
    Hum. Mutat. 33:1037-1044(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ARG-11.

Entry informationi

Entry nameiRL3_HUMAN
AccessioniPrimary (citable) accession number: P39023
Secondary accession number(s): B2RDV9, Q15548, Q5I0G0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 155 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 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Ribosomal proteins
    Ribosomal proteins families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

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