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E2RR58

- RL12_CANFA

UniProt

E2RR58 - RL12_CANFA

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Protein

60S ribosomal protein L12

Gene

RPL12

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

Functioni

Binds directly to 26S ribosomal RNA.By similarity

GO - Molecular functioni

  1. 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 L12
Gene namesi
Name:RPL12
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254: Chromosome 9

Subcellular locationi

GO - Cellular componenti

  1. ribosome Source: UniProtKB-KW
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16516560S ribosomal protein L12PRO_0000405586Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381PhosphoserineBy similarity
Modified residuei54 – 541N6-acetyllysineBy similarity
Modified residuei83 – 831N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiE2RR58.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZKRelectron microscopy8.70i1-165[»]
ProteinModelPortaliE2RR58.
SMRiE2RR58. Positions 1-163.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiE2RR58.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L11P family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000006922.
InParanoidiE2RR58.
KOiK02870.
OrthoDBiEOG7JMGG9.

Family and domain databases

Gene3Di1.10.10.250. 1 hit.
3.30.1550.10. 1 hit.
HAMAPiMF_00736. Ribosomal_L11.
InterProiIPR000911. Ribosomal_L11/L12.
IPR020783. Ribosomal_L11_C.
IPR020785. Ribosomal_L11_CS.
IPR020784. Ribosomal_L11_N.
[Graphical view]
PANTHERiPTHR11661. PTHR11661. 1 hit.
PfamiPF00298. Ribosomal_L11. 1 hit.
PF03946. Ribosomal_L11_N. 1 hit.
[Graphical view]
SMARTiSM00649. RL11. 1 hit.
[Graphical view]
SUPFAMiSSF46906. SSF46906. 1 hit.
SSF54747. SSF54747. 1 hit.
PROSITEiPS00359. RIBOSOMAL_L11. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

E2RR58-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPPKFDPNEI KVVYLRCTGG EVGATSALAP KIGPLGLSPK KVGDDIAKAT
60 70 80 90 100
GDWKGLRITV KLTIQNRQAQ IEVVPSASAL IIKALKEPPR DRKKQKNIKH
110 120 130 140 150
SGNITFDEIV NIARQMRHRS LARELSGTIK EILGTAQSVG CNVDGRHPHD
160
IIDDINSGAV ECPAS
Length:165
Mass (Da):17,819
Last modified:November 30, 2010 - v1
Checksum:i7EFD783A8ED350F9
GO

Sequence databases

RefSeqiNP_001238885.1. NM_001251956.1.
UniGeneiCfa.39098.

Genome annotation databases

EnsembliENSCAFT00000045165; ENSCAFP00000035849; ENSCAFG00000020136.
GeneIDi480716.
KEGGicfa:480716.

Cross-referencesi

Sequence databases

RefSeqi NP_001238885.1. NM_001251956.1.
UniGenei Cfa.39098.

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 i 1-165 [» ]
ProteinModelPortali E2RR58.
SMRi E2RR58. Positions 1-163.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi E2RR58.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSCAFT00000045165 ; ENSCAFP00000035849 ; ENSCAFG00000020136 .
GeneIDi 480716.
KEGGi cfa:480716.

Organism-specific databases

CTDi 6136.

Phylogenomic databases

GeneTreei ENSGT00390000006922.
InParanoidi E2RR58.
KOi K02870.
OrthoDBi EOG7JMGG9.

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 E2RR58.
NextBioi 20855696.

Family and domain databases

Gene3Di 1.10.10.250. 1 hit.
3.30.1550.10. 1 hit.
HAMAPi MF_00736. Ribosomal_L11.
InterProi IPR000911. Ribosomal_L11/L12.
IPR020783. Ribosomal_L11_C.
IPR020785. Ribosomal_L11_CS.
IPR020784. Ribosomal_L11_N.
[Graphical view ]
PANTHERi PTHR11661. PTHR11661. 1 hit.
Pfami PF00298. Ribosomal_L11. 1 hit.
PF03946. Ribosomal_L11_N. 1 hit.
[Graphical view ]
SMARTi SM00649. RL11. 1 hit.
[Graphical view ]
SUPFAMi SSF46906. SSF46906. 1 hit.
SSF54747. SSF54747. 1 hit.
PROSITEi PS00359. RIBOSOMAL_L11. 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 nameiRL12_CANFA
AccessioniPrimary (citable) accession number: E2RR58
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 8, 2011
Last sequence update: November 30, 2010
Last modified: November 26, 2014
This is version 29 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