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P46776

- RL27A_HUMAN

UniProt

P46776 - RL27A_HUMAN

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Protein

60S ribosomal protein L27a

Gene

RPL27A

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

Functioni

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. RNA binding Source: ProtInc
  3. structural constituent of ribosome Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. gene expression Source: Reactome
  3. mRNA metabolic process Source: Reactome
  4. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  5. RNA metabolic process Source: Reactome
  6. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  7. translation Source: UniProtKB
  8. translational elongation Source: Reactome
  9. translational initiation Source: Reactome
  10. translational termination Source: Reactome
  11. viral life cycle Source: Reactome
  12. viral process Source: Reactome
  13. viral transcription Source: Reactome
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: Chromosome 11

Organism-specific databases

HGNCiHGNC:10329. RPL27A.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. cytosolic large ribosomal subunit Source: UniProtKB
  3. membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34708.

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.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

BioGridi112076. 85 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
3J3Belectron microscopy5.00a1-148[»]
4BXFX-ray2.05C/D32-50[»]
ProteinModelPortaliP46776.
SMRiP46776. Positions 6-147.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L15P family.Curated

Phylogenomic databases

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

Family and domain databases

HAMAPiMF_01341. Ribosomal_L15.
InterProiIPR001196. 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 .
CCDSi CCDS7790.1.
PIRi S55914.
RefSeqi NP_000981.1. NM_000990.4.
UniGenei Hs.523463.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3J3B electron microscopy 5.00 a 1-148 [» ]
4BXF X-ray 2.05 C/D 32-50 [» ]
ProteinModelPortali P46776.
SMRi P46776. Positions 6-147.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112076. 85 interactions.
DIPi DIP-33121N.
IntActi P46776. 15 interactions.
MINTi MINT-1150308.
STRINGi 9606.ENSP00000346015.

PTM databases

PhosphoSitei P46776.

2D gel databases

SWISS-2DPAGE P46776.

Proteomic databases

MaxQBi P46776.
PaxDbi P46776.
PRIDEi P46776.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000314138 ; ENSP00000346015 ; ENSG00000166441 .
GeneIDi 6157.
KEGGi hsa:6157.
UCSCi uc001mgs.4. human.

Organism-specific databases

CTDi 6157.
GeneCardsi GC11P008703.
HGNCi HGNC:10329. RPL27A.
MIMi 603637. gene.
neXtProti NX_P46776.
PharmGKBi PA34708.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0200.
GeneTreei ENSGT00390000005534.
HOGENOMi HOG000231263.
HOVERGENi HBG054587.
InParanoidi P46776.
KOi K02900.
OMAi DKAPVID.
OrthoDBi EOG78SQKP.
PhylomeDBi P46776.
TreeFami TF313742.

Enzyme and pathway databases

Reactomei REACT_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

ChiTaRSi RPL27A. human.
GeneWikii RPL27A.
GenomeRNAii 6157.
NextBioi 23911.
PROi P46776.
SOURCEi Search...

Gene expression databases

Bgeei P46776.
CleanExi HS_RPL27A.
ExpressionAtlasi P46776. baseline and differential.
Genevestigatori P46776.

Family and domain databases

HAMAPi MF_01341. Ribosomal_L15.
InterProi IPR001196. Ribosomal_L15_CS.
IPR021131. Ribosomal_L18e/L15P.
[Graphical view ]
Pfami PF00828. Ribosomal_L18e. 1 hit.
[Graphical view ]
SUPFAMi SSF52080. SSF52080. 1 hit.
PROSITEi PS00475. RIBOSOMAL_L15. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: November 26, 2014
This is version 129 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