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Protein

39S ribosomal protein L36, mitochondrial

Gene

Mrpl36

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Component of the large subunit of the mitochondrial ribosome.Curated

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 L36, mitochondrial
Short name:
L36mt
Short name:
MRP-L36
Gene namesi
Name:Mrpl36
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:2137228. Mrpl36.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 10239S ribosomal protein L36, mitochondrialPRO_0000030530
Transit peptidei1 – ?MitochondrionSequence analysis

Proteomic databases

PaxDbiQ99N90.
PRIDEiQ99N90.

Expressioni

Gene expression databases

BgeeiQ99N90.
CleanExiMM_MRPL36.
GenevisibleiQ99N90. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022098.

Structurei

3D structure databases

ProteinModelPortaliQ99N90.
SMRiQ99N90. Positions 65-102.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L36P family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG4122. Eukaryota.
COG0257. LUCA.
GeneTreeiENSGT00390000010866.
HOGENOMiHOG000111586.
HOVERGENiHBG029144.
InParanoidiQ99N90.
KOiK02919.
OMAiYVYCKTN.
OrthoDBiEOG79CZ1X.
PhylomeDBiQ99N90.
TreeFamiTF300275.

Family and domain databases

HAMAPiMF_00251. Ribosomal_L36.
InterProiIPR000473. Ribosomal_L36.
[Graphical view]
PANTHERiPTHR18804. PTHR18804. 1 hit.
PfamiPF00444. Ribosomal_L36. 1 hit.
[Graphical view]
SUPFAMiSSF57840. SSF57840. 1 hit.
TIGRFAMsiTIGR01022. rpmJ_bact. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q99N90-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAALLVRSVV ASVVDPFLHL SRLAVKPRVF SSFLLGTLPR AKPCAEVRSV
60 70 80 90 100
LCGRPLPTLL PSLGFKTKGV IKKRCKDCYK VKRRGRWFIL CKTNPKHKQR

QM
Length:102
Mass (Da):11,545
Last modified:June 1, 2001 - v1
Checksum:i28D6116D5FFCDEAC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB049655 mRNA. Translation: BAB40860.1.
AK075780 mRNA. Translation: BAC35954.1.
AK131597 mRNA. Translation: BAE20708.1.
AK131601 mRNA. Translation: BAE20711.1.
AK131604 mRNA. Translation: BAE20714.1.
AK160778 mRNA. Translation: BAE36002.1.
BC009166 mRNA. Translation: AAH09166.1.
CCDSiCCDS26631.1.
RefSeqiNP_444393.1. NM_053163.1.
UniGeneiMm.26775.

Genome annotation databases

EnsembliENSMUST00000022098; ENSMUSP00000022098; ENSMUSG00000021607.
GeneIDi94066.
KEGGimmu:94066.
UCSCiuc007rdi.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB049655 mRNA. Translation: BAB40860.1.
AK075780 mRNA. Translation: BAC35954.1.
AK131597 mRNA. Translation: BAE20708.1.
AK131601 mRNA. Translation: BAE20711.1.
AK131604 mRNA. Translation: BAE20714.1.
AK160778 mRNA. Translation: BAE36002.1.
BC009166 mRNA. Translation: AAH09166.1.
CCDSiCCDS26631.1.
RefSeqiNP_444393.1. NM_053163.1.
UniGeneiMm.26775.

3D structure databases

ProteinModelPortaliQ99N90.
SMRiQ99N90. Positions 65-102.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022098.

Proteomic databases

PaxDbiQ99N90.
PRIDEiQ99N90.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022098; ENSMUSP00000022098; ENSMUSG00000021607.
GeneIDi94066.
KEGGimmu:94066.
UCSCiuc007rdi.1. mouse.

Organism-specific databases

CTDi64979.
MGIiMGI:2137228. Mrpl36.

Phylogenomic databases

eggNOGiKOG4122. Eukaryota.
COG0257. LUCA.
GeneTreeiENSGT00390000010866.
HOGENOMiHOG000111586.
HOVERGENiHBG029144.
InParanoidiQ99N90.
KOiK02919.
OMAiYVYCKTN.
OrthoDBiEOG79CZ1X.
PhylomeDBiQ99N90.
TreeFamiTF300275.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ99N90.
SOURCEiSearch...

Gene expression databases

BgeeiQ99N90.
CleanExiMM_MRPL36.
GenevisibleiQ99N90. MM.

Family and domain databases

HAMAPiMF_00251. Ribosomal_L36.
InterProiIPR000473. Ribosomal_L36.
[Graphical view]
PANTHERiPTHR18804. PTHR18804. 1 hit.
PfamiPF00444. Ribosomal_L36. 1 hit.
[Graphical view]
SUPFAMiSSF57840. SSF57840. 1 hit.
TIGRFAMsiTIGR01022. rpmJ_bact. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structural compensation for the deficit of rRNA with proteins in the mammalian mitochondrial ribosome. Systematic analysis of protein components of the large ribosomal subunit from mammalian mitochondria."
    Suzuki T., Terasaki M., Takemoto-Hori C., Hanada T., Ueda T., Wada A., Watanabe K.
    J. Biol. Chem. 276:21724-21736(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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: Head, Heart and Pancreas.
  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].
    Tissue: Mammary tumor.

Entry informationi

Entry nameiRM36_MOUSE
AccessioniPrimary (citable) accession number: Q99N90
Secondary accession number(s): Q3V2T6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 108 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

Complete proteome, 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.