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P39023 (RL3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
60S ribosomal protein L3
Alternative name(s):
HIV-1 TAR RNA-binding protein B
Short name=TARBP-B
Gene names
Name:RPL3
ORF Names:OK/SW-cl.32
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length403 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subcellular location

Nucleusnucleolus. Cytoplasm Ref.11.

Sequence similarities

Belongs to the ribosomal protein L3P family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 40340260S ribosomal protein L3
PRO_0000077227

Amino acid modifications

Modified residue131Phosphoserine Ref.13 Ref.15
Modified residue2941N6-acetyllysine Ref.14
Modified residue3041Phosphoserine Ref.17
Modified residue3661N6-acetyllysine Ref.14

Natural variations

Natural variant111H → R Rare variant found in a Diamond-Blackfan anemia patient; unknown pathological significance. Ref.18
VAR_069220
Natural variant781I → T.
Corresponds to variant rs11548004 [ dbSNP | Ensembl ].
VAR_052040

Experimental info

Sequence conflict221S → T in AAA91344. Ref.8
Sequence conflict2601A → V in AAA91344. Ref.8

Sequences

Sequence LengthMass (Da)Tools
P39023 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: A607CEE75CF62148

FASTA40346,109
        10         20         30         40         50         60 
MSHRKFSAPR HGSLGFLPRK RSSRHRGKVK SFPKDDPSKP VHLTAFLGYK AGMTHIVREV 

        70         80         90        100        110        120 
DRPGSKVNKK EVVEAVTIVE TPPMVVVGIV GYVETPRGLR TFKTVFAEHI SDECKRRFYK 

       130        140        150        160        170        180 
NWHKSKKKAF TKYCKKWQDE DGKKQLEKDF SSMKKYCQVI RVIAHTQMRL LPLRQKKAHL 

       190        200        210        220        230        240 
MEIQVNGGTV AEKLDWARER LEQQVPVNQV FGQDEMIDVI GVTKGKGYKG VTSRWHTKKL 

       250        260        270        280        290        300 
PRKTHRGLRK VACIGAWHPA RVAFSVARAG QKGYHHRTEI NKKIYKIGQG YLIKDGKLIK 

       310        320        330        340        350        360 
NNASTDYDLS DKSINPLGGF VHYGEVTNDF VMLKGCVVGT KKRVLTLRKS LLVQTKRRAL 

       370        380        390        400 
EKIDLKFIDT TSKFGHGRFQ TMEEKKAFMG PLKKDRIAKE EGA 

« Hide

References

« Hide 'large scale' references
[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]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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, 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]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[16]"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].
[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, MASS SPECTROMETRY.
[18]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
IPIIPI00550021.
PIRS34195.
RefSeqNP_000958.1. NM_000967.3.
UniGeneHs.119598.

3D structure databases

ProteinModelPortalP39023.
ModBaseSearch...

Protein-protein interaction databases

IntActP39023. 20 interactions.
MINTMINT-1145548.
STRING9606.ENSP00000346001.

PTM databases

PhosphoSiteP39023.

Polymorphism databases

DMDM730565.

2D gel databases

SWISS-2DPAGEP39023.

Proteomic databases

PaxDbP39023.
PRIDEP39023.

Protocols and materials databases

DNASU6122.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216146; ENSP00000346001; ENSG00000100316.
GeneID6122.
KEGGhsa:6122.
UCSCuc003axh.3. human.

Organism-specific databases

CTD6122.
GeneCardsGC22M039723.
H-InvDBHIX0172339.
HGNCHGNC:10332. RPL3.
HPAHPA003365.
MIM604163. gene.
neXtProtNX_P39023.
PharmGKBPA34713.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0087.
HOGENOMHOG000107319.
HOVERGENHBG001864.
InParanoidP39023.
KOK02925.
OMAGFHQRTE.
PhylomeDBP39023.

Enzyme and pathway databases

ReactomeREACT_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

ArrayExpressP39023.
BgeeP39023.
CleanExHS_RPL3.
GenevestigatorP39023.
GermOnlineENSG00000100316. Homo sapiens.

Family and domain databases

InterProIPR000597. Ribosomal_L3.
IPR019926. Ribosomal_L3_CS.
IPR009000. Transl_elong_init/rib_B-barrel.
[Graphical view]
PfamPF00297. Ribosomal_L3. 1 hit.
[Graphical view]
SUPFAMSSF50447. Translat_factor. 1 hit.
PROSITEPS00474. RIBOSOMAL_L3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPL3. human.
GenomeRNAi6122.
NextBio23777.
SOURCESearch...

Entry information

Entry nameRL3_HUMAN
AccessionPrimary (citable) accession number: P39023
Secondary accession number(s): B2RDV9, Q15548, Q5I0G0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Ribosomal proteins

Ribosomal proteins families and list of entries

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families