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Protein

60S ribosomal protein L12

Gene

Rpl12

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Binds directly to 26S ribosomal RNA.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-MMU-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-MMU-72689. Formation of a pool of free 40S subunits.
R-MMU-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-MMU-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-MMU-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L12
Gene namesi
Name:Rpl12
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:98002. Rpl12.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosolic large ribosomal subunit Source: MGI
  • extracellular exosome Source: MGI
  • focal adhesion Source: MGI
  • membrane Source: MGI
  • nucleolus Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16516560S ribosomal protein L12PRO_0000104457Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381PhosphoserineCombined sources
Modified residuei54 – 541N6-acetyllysineBy similarity
Modified residuei165 – 1651PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP35979.
PaxDbiP35979.
PRIDEiP35979.

PTM databases

iPTMnetiP35979.
PhosphoSiteiP35979.
SwissPalmiP35979.

Expressioni

Gene expression databases

BgeeiP35979.
CleanExiMM_RPL12.
ExpressionAtlasiP35979. baseline and differential.
GenevisibleiP35979. MM.

Interactioni

Protein-protein interaction databases

BioGridi234630. 3 interactions.
IntActiP35979. 6 interactions.
MINTiMINT-1870314.
STRINGi10090.ENSMUSP00000136144.

Structurei

Secondary structure

1
165
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 93Combined sources
Beta strandi11 – 188Combined sources
Helixi29 – 324Combined sources
Turni33 – 353Combined sources
Helixi39 – 4911Combined sources
Turni50 – 556Combined sources
Beta strandi56 – 6510Combined sources
Beta strandi68 – 703Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WIBNMR-A2-79[»]
ProteinModelPortaliP35979.
SMRiP35979. Positions 2-80.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35979.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L11P family.Curated

Phylogenomic databases

eggNOGiKOG0886. Eukaryota.
COG0080. LUCA.
HOGENOMiHOG000082125.
HOVERGENiHBG007231.
InParanoidiP35979.
KOiK02870.
OMAiAYSVGCQ.
OrthoDBiEOG7JMGG9.
PhylomeDBiP35979.
TreeFamiTF300123.

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.

P35979-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPKFDPNEV 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):17,805
Last modified:June 16, 2003 - v2
Checksum:i7EEEC00C57193116
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti79 – 791A → G in AAA40066 (PubMed:8359697).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04280 mRNA. Translation: AAA40066.1.
AK002973 mRNA. Translation: BAB22488.1.
AK008347 mRNA. Translation: BAB25619.1.
AK012349 mRNA. Translation: BAB28180.1.
AK012428 mRNA. Translation: BAB28232.1.
BC018321 mRNA. Translation: AAH18321.1.
BC081469 mRNA. Translation: AAH81469.1.
CCDSiCCDS15936.1.
PIRiJN0778.
RefSeqiNP_033102.2. NM_009076.3.
UniGeneiMm.250030.
Mm.381297.

Genome annotation databases

EnsembliENSMUST00000126610; ENSMUSP00000117461; ENSMUSG00000038900.
GeneIDi269261.
KEGGimmu:269261.
UCSCiuc008jhe.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04280 mRNA. Translation: AAA40066.1.
AK002973 mRNA. Translation: BAB22488.1.
AK008347 mRNA. Translation: BAB25619.1.
AK012349 mRNA. Translation: BAB28180.1.
AK012428 mRNA. Translation: BAB28232.1.
BC018321 mRNA. Translation: AAH18321.1.
BC081469 mRNA. Translation: AAH81469.1.
CCDSiCCDS15936.1.
PIRiJN0778.
RefSeqiNP_033102.2. NM_009076.3.
UniGeneiMm.250030.
Mm.381297.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WIBNMR-A2-79[»]
ProteinModelPortaliP35979.
SMRiP35979. Positions 2-80.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi234630. 3 interactions.
IntActiP35979. 6 interactions.
MINTiMINT-1870314.
STRINGi10090.ENSMUSP00000136144.

PTM databases

iPTMnetiP35979.
PhosphoSiteiP35979.
SwissPalmiP35979.

Proteomic databases

EPDiP35979.
PaxDbiP35979.
PRIDEiP35979.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000126610; ENSMUSP00000117461; ENSMUSG00000038900.
GeneIDi269261.
KEGGimmu:269261.
UCSCiuc008jhe.2. mouse.

Organism-specific databases

CTDi6136.
MGIiMGI:98002. Rpl12.

Phylogenomic databases

eggNOGiKOG0886. Eukaryota.
COG0080. LUCA.
HOGENOMiHOG000082125.
HOVERGENiHBG007231.
InParanoidiP35979.
KOiK02870.
OMAiAYSVGCQ.
OrthoDBiEOG7JMGG9.
PhylomeDBiP35979.
TreeFamiTF300123.

Enzyme and pathway databases

ReactomeiR-MMU-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-MMU-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-MMU-72689. Formation of a pool of free 40S subunits.
R-MMU-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-MMU-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-MMU-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

EvolutionaryTraceiP35979.
NextBioi392764.
PROiP35979.
SOURCEiSearch...

Gene expression databases

BgeeiP35979.
CleanExiMM_RPL12.
ExpressionAtlasiP35979. baseline and differential.
GenevisibleiP35979. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of mouse cDNAs encoding ribosomal proteins L12 and L18."
    Hou E.W., Li S.S.L.
    Gene 130:287-290(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6 X CBA.
    Tissue: Lung.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain, Embryo and Small intestine.
  3. "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].
    Strain: C57BL/6J.
    Tissue: Brain and Mammary gland.
  4. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  6. "Solution structure of the N-terminal domain from mouse hypothetical protein BAB22488."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 2-80.

Entry informationi

Entry nameiRL12_MOUSE
AccessioniPrimary (citable) accession number: P35979
Secondary accession number(s): Q9CQK4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 16, 2003
Last modified: May 11, 2016
This is version 138 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.