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P46779 (RL28_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 121. 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·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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DCCP431463EBI-366357,EBI-1222919

Alternative products

This entry describes 3 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.

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
Modified residue1151Phosphoserine Ref.9

Natural variations

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

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, 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: MASS SPECTROMETRY, PROBABLE ACETYLATION AT SER-2.
[9]"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, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[10]"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].
+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.
BC010173 mRNA. Translation: AAH10173.1.
BC010182 mRNA. Translation: AAH10182.1.
BC011582 mRNA. Translation: AAH11582.1.
BG777550 mRNA. No translation available.
IPIIPI00182533.
IPI00910727.
IPI00914529.
PIRS55915.
RefSeqNP_000982.2. NM_000991.4.
NP_001129606.1. NM_001136134.1.
NP_001129607.1. NM_001136135.1.
UniGeneHs.652114.

3D structure databases

ProteinModelPortalP46779.
SMRP46779. Positions 1-124.
ModBaseSearch...

Protein-protein interaction databases

IntActP46779. 16 interactions.
MINTMINT-5004261.
STRING9606.ENSP00000401450.

PTM databases

PhosphoSiteP46779.

Polymorphism databases

DMDM22002069.

Proteomic databases

PaxDbP46779.
PeptideAtlasP46779.
PRIDEP46779.

Protocols and materials databases

DNASU6158.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000344063; ENSP00000342787; ENSG00000108107.
ENST00000458349; ENSP00000401450; ENSG00000108107.
ENST00000558815; ENSP00000452909; ENSG00000108107.
ENST00000559463; ENSP00000453319; ENSG00000108107.
ENST00000560583; ENSP00000453029; ENSG00000108107.
GeneID6158.
KEGGhsa:6158.
UCSCuc002qkv.3. human.

Organism-specific databases

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

Phylogenomic databases

eggNOGNOG148062.
HOGENOMHOG000200513.
HOVERGENHBG000701.
InParanoidP46779.
KOK02903.
OMAKPFSTEP.
OrthoDBEOG4W9J5C.
PhylomeDBP46779.

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.
GermOnlineENSG00000108107. Homo sapiens.

Family and domain databases

InterProIPR002672. Ribosomal_L28e.
[Graphical view]
PANTHERPTHR10544. PTHR10544. 1 hit.
ProtoNetSearch...

Other

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

Entry information

Entry nameRL28_HUMAN
AccessionPrimary (citable) accession number: P46779
Secondary accession number(s): B2R4A6 expand/collapse secondary AC list , B4DEP9, E9PB24, Q6IAY0, Q96FX1, Q9BWQ0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 121 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

Ribosomal proteins

Ribosomal proteins families and list of entries

Human chromosome 19

Human chromosome 19: 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