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P46779 (RL28_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
60S ribosomal protein L28
Gene names
Name:RPL28
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length137 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the ribosomal protein L28e family.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

SRP-dependent cotranslational protein targeting to membrane

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Traceable author statement. Source: Reactome

translation

Non-traceable author statement Ref.8. Source: UniProtKB

translational elongation

Traceable author statement. Source: Reactome

translational initiation

Traceable author statement. Source: Reactome

translational termination

Traceable author statement. Source: Reactome

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

viral transcription

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

cytosolic large ribosomal subunit

Inferred from direct assay Ref.8. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

   Molecular_functionRNA binding

Traceable author statement Ref.1. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 20434207. Source: IntAct

structural constituent of ribosome

Non-traceable author statement Ref.8. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DCCP431463EBI-366357,EBI-1222919

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P46779-1)

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.
Isoform 2 (identifier: P46779-2)

The sequence of this isoform differs from the canonical sequence as follows:
     109-137: AAIRRASAILRSQKPVMVKRKRTRPTKSS → VSWGLGIRLG...PRGRLVECMG
Note: No experimental confirmation available.
Isoform 3 (identifier: P46779-3)

The sequence of this isoform differs from the canonical sequence as follows:
     109-137: AAIRRASAILRSQKPVMVKRKRTRPTKSS → DMLASTGSGL...QNLLDCAHKS
Note: No experimental confirmation available.
Isoform 4 (identifier: P46779-4)

The sequence of this isoform differs from the canonical sequence as follows:
     69-137: GQRKPATSYVRTTINKNARATLSSIRHMIRKNKYRPDLRMAAIRRASAILRSQKPVMVKRKRTRPTKSS → E
Note: No experimental confirmation available. Gene prediction based on EST data.
Isoform 5 (identifier: P46779-5)

The sequence of this isoform differs from the canonical sequence as follows:
     70-137: QRKPATSYVR...RKRTRPTKSS → EFCLVWARERPLSRVWEL
Note: No experimental confirmation available. Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 13713660S ribosomal protein L28
PRO_0000122389

Amino acid modifications

Modified residue21N-acetylserine Ref.7 Ref.8 Ref.9 Ref.12
Modified residue1151Phosphoserine Ref.10

Natural variations

Alternative sequence69 – 13769GQRKP…PTKSS → E in isoform 4.
VSP_047026
Alternative sequence70 – 13768QRKPA…PTKSS → EFCLVWARERPLSRVWEL in isoform 5.
VSP_047027
Alternative sequence109 – 13729AAIRR…PTKSS → VSWGLGIRLGETGQCCGEGP PTTGCNMGWRGMDSCFQPTP HTQHWPRGRLVECMG in isoform 2.
VSP_043026
Alternative sequence109 – 13729AAIRR…PTKSS → DMLASTGSGLCCSVAVQPWA SSSTSLCLRTLICNMRVDRP YYSGLMRRLNVQNLLDCAHK S in isoform 3.
VSP_046173
Natural variant661R → L.
Corresponds to variant rs13502 [ dbSNP | Ensembl ].
VAR_034460

Experimental info

Sequence conflict841K → R in AAH10182. Ref.6
Sequence conflict1201S → T in AAA85657. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 44DCDE45473D7C7B

FASTA13715,748
        10         20         30         40         50         60 
MSAHLQWMVV RNCSSFLIKR NKQTYSTEPN NLKARNSFRY NGLIHRKTVG VEPAADGKGV 

        70         80         90        100        110        120 
VVVIKRRSGQ RKPATSYVRT TINKNARATL SSIRHMIRKN KYRPDLRMAA IRRASAILRS 

       130 
QKPVMVKRKR TRPTKSS 

« Hide

Isoform 2 [UniParc].

Checksum: 1C9BD1FA0A0E14EE
Show »

FASTA16318,430
Isoform 3 [UniParc].

Checksum: D4D6E5C7F4116D16
Show »

FASTA16919,148
Isoform 4 [UniParc].

Checksum: EDE20EE54DFE31FE
Show »

FASTA697,888
Isoform 5 [UniParc].

Checksum: 791604CE95F509E2
Show »

FASTA8710,088

References

« Hide 'large scale' references
[1]"Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9, S10 and S29 human ribosomal protein mRNAs."
Frigerio J.-M., Dagorn J.-C., Iovanna J.L.
Biochim. Biophys. Acta 1262:64-68(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Colon.
[2]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"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] (ISOFORMS 1 AND 2).
Tissue: Cerebellum and Hippocampus.
[4]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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. expand/collapse author list , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
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] (ISOFORMS 1 AND 3).
Tissue: B-cell, Kidney, Prostatic adenocarcinoma and Uterus.
[7]Bienvenut W.V., Boldt K., von Kriegsheim A., Lilla S., Lempens A., Kolch W.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-11; 23-33; 40-58; 72-79 AND 120-127, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Hepatoma and Ovarian carcinoma.
[8]"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: ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
[9]"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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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-115, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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].
[12]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Structures of the human and Drosophila 80S ribosome."
Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M., Wilson D.N., Beckmann R.
Nature 497:80-85(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U14969 mRNA. Translation: AAA85657.1.
CR457024 mRNA. Translation: CAG33305.1.
AK311760 mRNA. Translation: BAG34703.1.
AK293736 mRNA. Translation: BAG57160.1.
AC020922 Genomic DNA. No translation available.
CH471135 Genomic DNA. Translation: EAW72374.1.
CH471135 Genomic DNA. Translation: EAW72375.1.
CH471135 Genomic DNA. Translation: EAW72376.1.
BC010173 mRNA. Translation: AAH10173.1.
BC010182 mRNA. Translation: AAH10182.1.
BC011582 mRNA. Translation: AAH11582.1.
BG777550 mRNA. No translation available.
CCDSCCDS12924.1. [P46779-1]
CCDS46189.1. [P46779-3]
CCDS46190.1. [P46779-2]
CCDS46191.1. [P46779-4]
CCDS46192.1. [P46779-5]
PIRS55915.
RefSeqNP_000982.2. NM_000991.4. [P46779-1]
NP_001129606.1. NM_001136134.1. [P46779-2]
NP_001129607.1. NM_001136135.1. [P46779-3]
NP_001129608.1. NM_001136136.1. [P46779-5]
NP_001129609.1. NM_001136137.1. [P46779-4]
UniGeneHs.652114.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Belectron microscopy5.00r1-137[»]
ProteinModelPortalP46779.
SMRP46779. Positions 1-137.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112077. 45 interactions.
IntActP46779. 23 interactions.
MINTMINT-5004261.
STRING9606.ENSP00000401450.

PTM databases

PhosphoSiteP46779.

Proteomic databases

MaxQBP46779.
PaxDbP46779.
PeptideAtlasP46779.
PRIDEP46779.

Protocols and materials databases

DNASU6158.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000344063; ENSP00000342787; ENSG00000108107. [P46779-1]
ENST00000428193; ENSP00000391665; ENSG00000108107. [P46779-4]
ENST00000431533; ENSP00000400596; ENSG00000108107. [P46779-5]
ENST00000458349; ENSP00000401450; ENSG00000108107. [P46779-3]
ENST00000558815; ENSP00000452909; ENSG00000108107. [P46779-3]
ENST00000559463; ENSP00000453319; ENSG00000108107. [P46779-1]
ENST00000560583; ENSP00000453029; ENSG00000108107. [P46779-2]
GeneID6158.
KEGGhsa:6158.
UCSCuc002qkv.3. human. [P46779-1]
uc010yfz.2. human.
uc010yga.2. human.
uc010ygb.2. human. [P46779-2]

Organism-specific databases

CTD6158.
GeneCardsGC19P055897.
HGNCHGNC:10330. RPL28.
HPAHPA050459.
MIM603638. gene.
neXtProtNX_P46779.
PharmGKBPA34710.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG148062.
HOGENOMHOG000200513.
HOVERGENHBG000701.
InParanoidP46779.
KOK02903.
OMAWLIIRNN.
OrthoDBEOG74N5JT.
PhylomeDBP46779.
TreeFamTF300173.

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

ArrayExpressP46779.
BgeeP46779.
CleanExHS_RPL28.
GenevestigatorP46779.

Family and domain databases

InterProIPR029004. L28e/Mak16.
IPR002672. Ribosomal_L28e.
[Graphical view]
PANTHERPTHR10544. PTHR10544. 1 hit.
PfamPF01778. Ribosomal_L28e. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPL28. human.
GeneWiki60S_ribosomal_protein_L28.
GenomeRNAi6158.
NextBio23915.
PMAP-CutDBP46779.
PROP46779.
SOURCESearch...

Entry information

Entry nameRL28_HUMAN
AccessionPrimary (citable) accession number: P46779
Secondary accession number(s): B2R4A6 expand/collapse secondary AC list , B4DEP9, C9JB50, E9PB24, G5E9L2, Q6IAY0, Q96FX1, Q9BWQ0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 134 of the entry and version 3 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

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM