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Protein

60S ribosomal protein L28

Gene

RPL28

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

Functioni

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: ProtInc
  • structural constituent of ribosome Source: UniProtKB

GO - Biological processi

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 L28
Gene namesi
Name:RPL28
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:10330. RPL28.

Subcellular locationi

GO - Cellular componenti

  • cell body Source: ParkinsonsUK-UCL
  • cytoplasm Source: HPA
  • cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
  • cytosol Source: Reactome
  • cytosolic large ribosomal subunit Source: UniProtKB
  • dendrite Source: ParkinsonsUK-UCL
  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34710.

Polymorphism and mutation databases

BioMutaiRPL28.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 13713660S ribosomal protein L28PRO_0000122389Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine4 Publications
Modified residuei115 – 1151Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP46779.
PaxDbiP46779.
PeptideAtlasiP46779.
PRIDEiP46779.

PTM databases

PhosphoSiteiP46779.

Miscellaneous databases

PMAP-CutDBP46779.

Expressioni

Gene expression databases

BgeeiP46779.
CleanExiHS_RPL28.
ExpressionAtlasiP46779. baseline and differential.
GenevestigatoriP46779.

Organism-specific databases

HPAiHPA050459.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CCNDBP1O952734EBI-366357,EBI-748961
DCCP431463EBI-366357,EBI-1222919

Protein-protein interaction databases

BioGridi112077. 41 interactions.
IntActiP46779. 23 interactions.
MINTiMINT-5004261.
STRINGi9606.ENSP00000401450.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00Cr1-137[»]
ProteinModelPortaliP46779.
SMRiP46779. Positions 1-137.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L28e family.Curated

Phylogenomic databases

eggNOGiNOG148062.
GeneTreeiENSGT00390000008732.
HOGENOMiHOG000186171.
HOVERGENiHBG000701.
InParanoidiP46779.
KOiK02903.
OMAiNKPFSTE.
OrthoDBiEOG74N5JT.
PhylomeDBiP46779.
TreeFamiTF300173.

Family and domain databases

InterProiIPR029004. L28e/Mak16.
IPR002672. Ribosomal_L28e.
[Graphical view]
PANTHERiPTHR10544. PTHR10544. 1 hit.
PfamiPF01778. Ribosomal_L28e. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P46779-1) [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

        10         20         30         40         50
MSAHLQWMVV RNCSSFLIKR NKQTYSTEPN NLKARNSFRY NGLIHRKTVG
60 70 80 90 100
VEPAADGKGV VVVIKRRSGQ RKPATSYVRT TINKNARATL SSIRHMIRKN
110 120 130
KYRPDLRMAA IRRASAILRS QKPVMVKRKR TRPTKSS
Length:137
Mass (Da):15,748
Last modified:January 23, 2007 - v3
Checksum:i44DCDE45473D7C7B
GO
Isoform 2 (identifier: P46779-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     109-137: AAIRRASAILRSQKPVMVKRKRTRPTKSS → VSWGLGIRLG...PRGRLVECMG

Note: No experimental confirmation available.

Show »
Length:163
Mass (Da):18,430
Checksum:i1C9BD1FA0A0E14EE
GO
Isoform 3 (identifier: P46779-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     109-137: AAIRRASAILRSQKPVMVKRKRTRPTKSS → DMLASTGSGL...QNLLDCAHKS

Note: No experimental confirmation available.

Show »
Length:169
Mass (Da):19,148
Checksum:iD4D6E5C7F4116D16
GO
Isoform 4 (identifier: P46779-4) [UniParc]FASTAAdd to basket

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.

Show »
Length:69
Mass (Da):7,888
Checksum:iEDE20EE54DFE31FE
GO
Isoform 5 (identifier: P46779-5) [UniParc]FASTAAdd to basket

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.

Show »
Length:87
Mass (Da):10,088
Checksum:i791604CE95F509E2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841K → R in AAH10182 (PubMed:15489334).Curated
Sequence conflicti120 – 1201S → T in AAA85657 (PubMed:7772601).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti66 – 661R → L.
Corresponds to variant rs13502 [ dbSNP | Ensembl ].
VAR_034460

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei69 – 13769GQRKP…PTKSS → E in isoform 4. CuratedVSP_047026Add
BLAST
Alternative sequencei70 – 13768QRKPA…PTKSS → EFCLVWARERPLSRVWEL in isoform 5. CuratedVSP_047027Add
BLAST
Alternative sequencei109 – 13729AAIRR…PTKSS → VSWGLGIRLGETGQCCGEGP PTTGCNMGWRGMDSCFQPTP HTQHWPRGRLVECMG in isoform 2. 1 PublicationVSP_043026Add
BLAST
Alternative sequencei109 – 13729AAIRR…PTKSS → DMLASTGSGLCCSVAVQPWA SSSTSLCLRTLICNMRVDRP YYSGLMRRLNVQNLLDCAHK S in isoform 3. 1 PublicationVSP_046173Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS12924.1. [P46779-1]
CCDS46189.1. [P46779-3]
CCDS46190.1. [P46779-2]
CCDS46191.1. [P46779-4]
CCDS46192.1. [P46779-5]
PIRiS55915.
RefSeqiNP_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]
UniGeneiHs.652114.

Genome annotation databases

EnsembliENST00000344063; ENSP00000342787; ENSG00000108107. [P46779-1]
ENST00000428193; ENSP00000391665; ENSG00000108107. [P46779-4]
ENST00000431533; ENSP00000400596; ENSG00000108107. [P46779-5]
ENST00000558815; ENSP00000452909; ENSG00000108107. [P46779-3]
ENST00000559463; ENSP00000453319; ENSG00000108107. [P46779-1]
ENST00000560583; ENSP00000453029; ENSG00000108107. [P46779-2]
GeneIDi6158.
KEGGihsa:6158.
UCSCiuc002qkv.3. human. [P46779-1]
uc010yfy.1. human.
uc010yfz.2. human.
uc010yga.2. human.
uc010ygb.2. human. [P46779-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS12924.1. [P46779-1]
CCDS46189.1. [P46779-3]
CCDS46190.1. [P46779-2]
CCDS46191.1. [P46779-4]
CCDS46192.1. [P46779-5]
PIRiS55915.
RefSeqiNP_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]
UniGeneiHs.652114.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00Cr1-137[»]
ProteinModelPortaliP46779.
SMRiP46779. Positions 1-137.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112077. 41 interactions.
IntActiP46779. 23 interactions.
MINTiMINT-5004261.
STRINGi9606.ENSP00000401450.

PTM databases

PhosphoSiteiP46779.

Polymorphism and mutation databases

BioMutaiRPL28.

Proteomic databases

MaxQBiP46779.
PaxDbiP46779.
PeptideAtlasiP46779.
PRIDEiP46779.

Protocols and materials databases

DNASUi6158.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000344063; ENSP00000342787; ENSG00000108107. [P46779-1]
ENST00000428193; ENSP00000391665; ENSG00000108107. [P46779-4]
ENST00000431533; ENSP00000400596; ENSG00000108107. [P46779-5]
ENST00000558815; ENSP00000452909; ENSG00000108107. [P46779-3]
ENST00000559463; ENSP00000453319; ENSG00000108107. [P46779-1]
ENST00000560583; ENSP00000453029; ENSG00000108107. [P46779-2]
GeneIDi6158.
KEGGihsa:6158.
UCSCiuc002qkv.3. human. [P46779-1]
uc010yfy.1. human.
uc010yfz.2. human.
uc010yga.2. human.
uc010ygb.2. human. [P46779-2]

Organism-specific databases

CTDi6158.
GeneCardsiGC19P055897.
HGNCiHGNC:10330. RPL28.
HPAiHPA050459.
MIMi603638. gene.
neXtProtiNX_P46779.
PharmGKBiPA34710.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG148062.
GeneTreeiENSGT00390000008732.
HOGENOMiHOG000186171.
HOVERGENiHBG000701.
InParanoidiP46779.
KOiK02903.
OMAiNKPFSTE.
OrthoDBiEOG74N5JT.
PhylomeDBiP46779.
TreeFamiTF300173.

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.

Miscellaneous databases

ChiTaRSiRPL28. human.
GeneWikii60S_ribosomal_protein_L28.
GenomeRNAii6158.
NextBioi23915.
PMAP-CutDBP46779.
PROiP46779.
SOURCEiSearch...

Gene expression databases

BgeeiP46779.
CleanExiHS_RPL28.
ExpressionAtlasiP46779. baseline and differential.
GenevestigatoriP46779.

Family and domain databases

InterProiIPR029004. L28e/Mak16.
IPR002672. Ribosomal_L28e.
[Graphical view]
PANTHERiPTHR10544. PTHR10544. 1 hit.
PfamiPF01778. Ribosomal_L28e. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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], CLEAVAGE OF INITIATOR METHIONINE [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. 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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  13. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRL28_HUMAN
AccessioniPrimary (citable) accession number: P46779
Secondary accession number(s): B2R4A6
, B4DEP9, C9JB50, E9PB24, G5E9L2, Q6IAY0, Q96FX1, Q9BWQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: May 27, 2015
This is version 143 of the entry and version 3 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 19
    Human chromosome 19: 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

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.