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Protein

60S ribosomal protein L27a

Gene

RPL27A

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 L27a
Gene namesi
Name:RPL27A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:10329. RPL27A.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • cytosolic large ribosomal subunit Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34708.

Polymorphism and mutation databases

BioMutaiRPL27A.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 14814760S ribosomal protein L27aPRO_0000104879Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei39 – 391(3S)-3-hydroxyhistidine1 Publication
Modified residuei47 – 471N6-acetyllysine1 Publication
Modified residuei55 – 551N6-acetyllysine1 Publication
Modified residuei68 – 681Phosphoserine2 Publications
Modified residuei110 – 1101N6-acetyllysine1 Publication

Post-translational modificationi

Hydroxylated on His-39 by MINA.1 Publication

Keywords - PTMi

Acetylation, Hydroxylation, Phosphoprotein

Proteomic databases

MaxQBiP46776.
PaxDbiP46776.
PRIDEiP46776.

2D gel databases

SWISS-2DPAGEP46776.

PTM databases

PhosphoSiteiP46776.

Expressioni

Gene expression databases

BgeeiP46776.
CleanExiHS_RPL27A.
ExpressionAtlasiP46776. baseline and differential.
GenevestigatoriP46776.

Organism-specific databases

HPAiHPA060776.
HPA063379.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
GTF2F2P139842EBI-350581,EBI-1030560

Protein-protein interaction databases

BioGridi112076. 89 interactions.
DIPiDIP-33121N.
IntActiP46776. 15 interactions.
MINTiMINT-1150308.
STRINGi9606.ENSP00000346015.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BXFX-ray2.05C/D32-50[»]
4V6Xelectron microscopy5.00Ca1-148[»]
ProteinModelPortaliP46776.
SMRiP46776. Positions 3-148.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L15P family.Curated

Phylogenomic databases

eggNOGiCOG0200.
GeneTreeiENSGT00390000005534.
HOGENOMiHOG000231263.
HOVERGENiHBG054587.
InParanoidiP46776.
KOiK02900.
OMAiKKNQSYC.
OrthoDBiEOG78SQKP.
PhylomeDBiP46776.
TreeFamiTF313742.

Family and domain databases

HAMAPiMF_01341. Ribosomal_L15.
InterProiIPR030878. Ribosomal_L15.
IPR001196. Ribosomal_L15_CS.
IPR021131. Ribosomal_L18e/L15P.
[Graphical view]
PfamiPF00828. Ribosomal_L18e. 1 hit.
[Graphical view]
SUPFAMiSSF52080. SSF52080. 1 hit.
PROSITEiPS00475. RIBOSOMAL_L15. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P46776-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSRLRKTRK LRGHVSHGHG RIGKHRKHPG GRGNAGGLHH HRINFDKYHP
60 70 80 90 100
GYFGKVGMKH YHLKRNQSFC PTVNLDKLWT LVSEQTRVNA AKNKTGAAPI
110 120 130 140
IDVVRSGYYK VLGKGKLPKQ PVIVKAKFFS RRAEEKIKSV GGACVLVA
Length:148
Mass (Da):16,561
Last modified:January 23, 2007 - v2
Checksum:iCB5E09C91507798F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14968 mRNA. Translation: AAA85656.1.
AB020236 Genomic DNA. Translation: BAA77361.1.
AK311767 mRNA. Translation: BAG34710.1.
CH471064 Genomic DNA. Translation: EAW68619.1.
BC005326 mRNA. Translation: AAH05326.1.
BC020169 mRNA. Translation: AAH20169.1.
AB007178 Genomic DNA. Translation: BAA25837.1.
CCDSiCCDS7790.1.
PIRiS55914.
RefSeqiNP_000981.1. NM_000990.4.
UniGeneiHs.523463.

Genome annotation databases

EnsembliENST00000314138; ENSP00000346015; ENSG00000166441.
GeneIDi6157.
KEGGihsa:6157.
UCSCiuc001mgs.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14968 mRNA. Translation: AAA85656.1.
AB020236 Genomic DNA. Translation: BAA77361.1.
AK311767 mRNA. Translation: BAG34710.1.
CH471064 Genomic DNA. Translation: EAW68619.1.
BC005326 mRNA. Translation: AAH05326.1.
BC020169 mRNA. Translation: AAH20169.1.
AB007178 Genomic DNA. Translation: BAA25837.1.
CCDSiCCDS7790.1.
PIRiS55914.
RefSeqiNP_000981.1. NM_000990.4.
UniGeneiHs.523463.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BXFX-ray2.05C/D32-50[»]
4V6Xelectron microscopy5.00Ca1-148[»]
ProteinModelPortaliP46776.
SMRiP46776. Positions 3-148.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112076. 89 interactions.
DIPiDIP-33121N.
IntActiP46776. 15 interactions.
MINTiMINT-1150308.
STRINGi9606.ENSP00000346015.

PTM databases

PhosphoSiteiP46776.

Polymorphism and mutation databases

BioMutaiRPL27A.

2D gel databases

SWISS-2DPAGEP46776.

Proteomic databases

MaxQBiP46776.
PaxDbiP46776.
PRIDEiP46776.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000314138; ENSP00000346015; ENSG00000166441.
GeneIDi6157.
KEGGihsa:6157.
UCSCiuc001mgs.4. human.

Organism-specific databases

CTDi6157.
GeneCardsiGC11P008703.
HGNCiHGNC:10329. RPL27A.
HPAiHPA060776.
HPA063379.
MIMi603637. gene.
neXtProtiNX_P46776.
PharmGKBiPA34708.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0200.
GeneTreeiENSGT00390000005534.
HOGENOMiHOG000231263.
HOVERGENiHBG054587.
InParanoidiP46776.
KOiK02900.
OMAiKKNQSYC.
OrthoDBiEOG78SQKP.
PhylomeDBiP46776.
TreeFamiTF313742.

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

ChiTaRSiRPL27A. human.
GeneWikiiRPL27A.
GenomeRNAii6157.
NextBioi23911.
PROiP46776.
SOURCEiSearch...

Gene expression databases

BgeeiP46776.
CleanExiHS_RPL27A.
ExpressionAtlasiP46776. baseline and differential.
GenevestigatoriP46776.

Family and domain databases

HAMAPiMF_01341. Ribosomal_L15.
InterProiIPR030878. Ribosomal_L15.
IPR001196. Ribosomal_L15_CS.
IPR021131. Ribosomal_L18e/L15P.
[Graphical view]
PfamiPF00828. Ribosomal_L18e. 1 hit.
[Graphical view]
SUPFAMiSSF52080. SSF52080. 1 hit.
PROSITEiPS00475. RIBOSOMAL_L15. 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].
    Tissue: Colon.
  2. "Genomic structure and chromosome location of RPL27A/Rpl27a, the genes encoding human and mouse ribosomal protein L27A."
    Kusuda J., Hirai M., Tanuma R., Hirata M., Hashimoto K.
    Cytogenet. Cell Genet. 85:248-251(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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].
    Tissue: Tongue.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Kidney and Lymph.
  6. "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 73-106.
  7. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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-47; LYS-55 AND LYS-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: HYDROXYLATION AT HIS-39 BY MINA.
  12. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRL27A_HUMAN
AccessioniPrimary (citable) accession number: P46776
Secondary accession number(s): B2R4B3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: May 27, 2015
This is version 134 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, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Ribosomal proteins
    Ribosomal proteins families and list of entries
  5. 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.