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E2QXF3

- RL15_CANFA

UniProt

E2QXF3 - RL15_CANFA

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Protein

60S ribosomal protein L15

Gene

RPL15

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. poly(A) RNA binding Source: Ensembl
  2. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. translation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_204671. SRP-dependent cotranslational protein targeting to membrane.
REACT_236501. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_236618. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_244619. Peptide chain elongation.
REACT_249312. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_256443. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_263476. Eukaryotic Translation Termination.
REACT_269652. Formation of a pool of free 40S subunits.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L15
Gene namesi
Name:RPL15
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254: Chromosome 23

Subcellular locationi

GO - Cellular componenti

  1. cytosolic large ribosomal subunit Source: Ensembl
  2. extracellular vesicular exosome Source: Ensembl
  3. nucleus Source: Ensembl
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20420460S ribosomal protein L15PRO_0000405588Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei97 – 971PhosphoserineBy similarity
Modified residuei100 – 1001PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiE2QXF3.

Interactioni

Subunit structurei

Interacts with IFIT1 (via TPR repeats 1-4).By similarity

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZKRelectron microscopy8.70m1-204[»]
ProteinModelPortaliE2QXF3.
SMRiE2QXF3. Positions 2-204.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiE2QXF3.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L15e family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000005092.
InParanoidiE2QXF3.
KOiK02877.
OMAiSRRAAWK.
OrthoDBiEOG7M3J1R.
TreeFamiTF300050.

Family and domain databases

Gene3Di3.40.1120.10. 1 hit.
InterProiIPR024794. Rbsml_L15e_core_dom.
IPR000439. Ribosomal_L15e.
IPR020925. Ribosomal_L15e_CS.
IPR012678. Ribosomal_L23/L15e_core_dom.
[Graphical view]
PANTHERiPTHR11847. PTHR11847. 1 hit.
PfamiPF00827. Ribosomal_L15e. 1 hit.
[Graphical view]
SUPFAMiSSF54189. SSF54189. 1 hit.
PROSITEiPS01194. RIBOSOMAL_L15E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

E2QXF3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGAYKYIQEL WRKKQSDVMR FLLRVRCWQY RQLSALHRAP RPTRPDKARR
60 70 80 90 100
LGYKAKQGYV IYRIRVRRGG RKRPVPKGAT YGKPVHHGVN QLKFARSLQS
110 120 130 140 150
VAEERAGRHC GALRVLNSYW VGEDSTYKFF EVILIDPFHK AIRRNPDTQW
160 170 180 190 200
ITKPVHKHRE MRGLTSAGRK SRGLGKGHKF HHTIGGSRRA AWRRRNTLQL

HRYR
Length:204
Mass (Da):24,146
Last modified:November 30, 2010 - v1
Checksum:iA6E3AD1A76C9506F
GO

Sequence databases

RefSeqiXP_005634418.1. XM_005634361.1.
XP_005634419.1. XM_005634362.1.
XP_862876.1. XM_857783.3.

Genome annotation databases

EnsembliENSCAFT00000009299; ENSCAFP00000008630; ENSCAFG00000005764.
GeneIDi477046.
KEGGicfa:477046.

Cross-referencesi

Sequence databases

RefSeqi XP_005634418.1. XM_005634361.1.
XP_005634419.1. XM_005634362.1.
XP_862876.1. XM_857783.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2ZKR electron microscopy 8.70 m 1-204 [» ]
ProteinModelPortali E2QXF3.
SMRi E2QXF3. Positions 2-204.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi E2QXF3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSCAFT00000009299 ; ENSCAFP00000008630 ; ENSCAFG00000005764 .
GeneIDi 477046.
KEGGi cfa:477046.

Organism-specific databases

CTDi 6138.

Phylogenomic databases

GeneTreei ENSGT00390000005092.
InParanoidi E2QXF3.
KOi K02877.
OMAi SRRAAWK.
OrthoDBi EOG7M3J1R.
TreeFami TF300050.

Enzyme and pathway databases

Reactomei REACT_204671. SRP-dependent cotranslational protein targeting to membrane.
REACT_236501. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_236618. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_244619. Peptide chain elongation.
REACT_249312. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_256443. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_263476. Eukaryotic Translation Termination.
REACT_269652. Formation of a pool of free 40S subunits.

Miscellaneous databases

EvolutionaryTracei E2QXF3.
NextBioi 20852595.

Family and domain databases

Gene3Di 3.40.1120.10. 1 hit.
InterProi IPR024794. Rbsml_L15e_core_dom.
IPR000439. Ribosomal_L15e.
IPR020925. Ribosomal_L15e_CS.
IPR012678. Ribosomal_L23/L15e_core_dom.
[Graphical view ]
PANTHERi PTHR11847. PTHR11847. 1 hit.
Pfami PF00827. Ribosomal_L15e. 1 hit.
[Graphical view ]
SUPFAMi SSF54189. SSF54189. 1 hit.
PROSITEi PS01194. RIBOSOMAL_L15E. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence, comparative analysis and haplotype structure of the domestic dog."
    Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F., Smith D.R.
    , deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S., Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.
    Nature 438:803-819(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Boxer.
  2. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (8.70 ANGSTROMS).

Entry informationi

Entry nameiRL15_CANFA
AccessioniPrimary (citable) accession number: E2QXF3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 8, 2011
Last sequence update: November 30, 2010
Last modified: November 26, 2014
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3