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Protein

39S ribosomal protein L12, mitochondrial

Gene

Mrpl12

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

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiR-MMU-5389840. Mitochondrial translation elongation.
R-MMU-5419276. Mitochondrial translation termination.

Names & Taxonomyi

Protein namesi
Recommended name:
39S ribosomal protein L12, mitochondrial
Short name:
L12mt
Short name:
MRP-L12
Gene namesi
Name:Mrpl12
Synonyms:Rpml12
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1926273. Mrpl12.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial large ribosomal subunit Source: UniProtKB
  • mitochondrial ribosome Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4646MitochondrionSequence analysisAdd
BLAST
Chaini47 – 20115539S ribosomal protein L12, mitochondrialPRO_0000030459Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei141 – 1411N6-acetyllysineCombined sources
Modified residuei153 – 1531N6-succinyllysineCombined sources
Modified residuei165 – 1651N6-succinyllysineCombined sources
Modified residuei181 – 1811N6-succinyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9DB15.
MaxQBiQ9DB15.
PaxDbiQ9DB15.
PRIDEiQ9DB15.

PTM databases

iPTMnetiQ9DB15.
PhosphoSiteiQ9DB15.

Expressioni

Gene expression databases

BgeeiQ9DB15.
CleanExiMM_MRPL12.
GenevisibleiQ9DB15. MM.

Interactioni

Subunit structurei

Interacts with NOA1.By similarity

Protein-protein interaction databases

BioGridi207875. 1 interaction.
IntActiQ9DB15. 4 interactions.
MINTiMINT-1861094.
STRINGi10090.ENSMUSP00000044417.

Structurei

3D structure databases

ProteinModelPortaliQ9DB15.
SMRiQ9DB15. Positions 64-201.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L7/L12P family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1715. Eukaryota.
COG0222. LUCA.
GeneTreeiENSGT00390000000190.
HOGENOMiHOG000248814.
HOVERGENiHBG001832.
InParanoidiQ9DB15.
KOiK02935.
OMAiRAKERTH.
OrthoDBiEOG7B5WXR.
PhylomeDBiQ9DB15.
TreeFamiTF105997.

Family and domain databases

Gene3Di3.30.1390.10. 1 hit.
HAMAPiMF_00368. Ribosomal_L7_L12.
InterProiIPR000206. Ribosomal_L7/12.
IPR014719. Ribosomal_L7/12_C/ClpS-like.
IPR013823. Ribosomal_L7/L12_C.
IPR008932. Ribosomal_L7/L12_oligo.
[Graphical view]
PfamiPF00542. Ribosomal_L12. 1 hit.
PF16320. Ribosomal_L12_N. 1 hit.
[Graphical view]
ProDomiPD001326. Ribosomal_L7/L12_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF48300. SSF48300. 1 hit.
SSF54736. SSF54736. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9DB15-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPVAASRCL WGPRLGLRGA ALRLARQQMP SVCAARQLRS SSHRRSEALA
60 70 80 90 100
GAPLDNAPKE YPPKIQQLVQ DIASLTLLEI SDLNELLKKT LKIQDVGLMP
110 120 130 140 150
MGGMVPGPVS AAAPASEAAE EEDVPKQKER THFTVRLTEA KPVDKVKLIK
160 170 180 190 200
EIKNYVQGIN LVQAKKLVES LPQEIKANVA KAEAEKIKAA LEAVGGTVVL

E
Length:201
Mass (Da):21,708
Last modified:December 13, 2001 - v2
Checksum:i893BEFB4F154076D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 1811RCLWGPRLGLR → AACGGHGLDSW in BAB23955 (PubMed:16141072).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005328 mRNA. Translation: BAB23955.1.
AK028168 mRNA. Translation: BAC25787.1.
AK134816 mRNA. Translation: BAE22297.1.
AK166969 mRNA. Translation: BAE39152.1.
AK168337 mRNA. Translation: BAE40275.1.
AL669855 Genomic DNA. Translation: CAM27051.1.
BC005712 mRNA. Translation: AAH05712.1.
BC019565 mRNA. Translation: AAH19565.1.
CCDSiCCDS25737.1.
RefSeqiNP_081480.2. NM_027204.2.
UniGeneiMm.133851.
Mm.491127.

Genome annotation databases

EnsembliENSMUST00000043627; ENSMUSP00000044417; ENSMUSG00000039640.
GeneIDi56282.
KEGGimmu:56282.
UCSCiuc007mta.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005328 mRNA. Translation: BAB23955.1.
AK028168 mRNA. Translation: BAC25787.1.
AK134816 mRNA. Translation: BAE22297.1.
AK166969 mRNA. Translation: BAE39152.1.
AK168337 mRNA. Translation: BAE40275.1.
AL669855 Genomic DNA. Translation: CAM27051.1.
BC005712 mRNA. Translation: AAH05712.1.
BC019565 mRNA. Translation: AAH19565.1.
CCDSiCCDS25737.1.
RefSeqiNP_081480.2. NM_027204.2.
UniGeneiMm.133851.
Mm.491127.

3D structure databases

ProteinModelPortaliQ9DB15.
SMRiQ9DB15. Positions 64-201.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207875. 1 interaction.
IntActiQ9DB15. 4 interactions.
MINTiMINT-1861094.
STRINGi10090.ENSMUSP00000044417.

PTM databases

iPTMnetiQ9DB15.
PhosphoSiteiQ9DB15.

Proteomic databases

EPDiQ9DB15.
MaxQBiQ9DB15.
PaxDbiQ9DB15.
PRIDEiQ9DB15.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000043627; ENSMUSP00000044417; ENSMUSG00000039640.
GeneIDi56282.
KEGGimmu:56282.
UCSCiuc007mta.1. mouse.

Organism-specific databases

CTDi6182.
MGIiMGI:1926273. Mrpl12.

Phylogenomic databases

eggNOGiKOG1715. Eukaryota.
COG0222. LUCA.
GeneTreeiENSGT00390000000190.
HOGENOMiHOG000248814.
HOVERGENiHBG001832.
InParanoidiQ9DB15.
KOiK02935.
OMAiRAKERTH.
OrthoDBiEOG7B5WXR.
PhylomeDBiQ9DB15.
TreeFamiTF105997.

Enzyme and pathway databases

ReactomeiR-MMU-5389840. Mitochondrial translation elongation.
R-MMU-5419276. Mitochondrial translation termination.

Miscellaneous databases

NextBioi312184.
PROiQ9DB15.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DB15.
CleanExiMM_MRPL12.
GenevisibleiQ9DB15. MM.

Family and domain databases

Gene3Di3.30.1390.10. 1 hit.
HAMAPiMF_00368. Ribosomal_L7_L12.
InterProiIPR000206. Ribosomal_L7/12.
IPR014719. Ribosomal_L7/12_C/ClpS-like.
IPR013823. Ribosomal_L7/L12_C.
IPR008932. Ribosomal_L7/L12_oligo.
[Graphical view]
PfamiPF00542. Ribosomal_L12. 1 hit.
PF16320. Ribosomal_L12_N. 1 hit.
[Graphical view]
ProDomiPD001326. Ribosomal_L7/L12_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF48300. SSF48300. 1 hit.
SSF54736. SSF54736. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: Cerebellum, Liver and Medulla oblongata.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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: FVB/N.
    Tissue: Colon.
  4. Lubec G., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 154-165.
    Tissue: Brain.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-153; LYS-165 AND LYS-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-141, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiRM12_MOUSE
AccessioniPrimary (citable) accession number: Q9DB15
Secondary accession number(s): B1ATZ3, Q3TKJ3, Q99JS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: December 13, 2001
Last modified: March 16, 2016
This is version 114 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. 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.