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Protein

39S ribosomal protein L33, mitochondrial

Gene

Mrpl33

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

GO - Molecular functioni

  1. structural constituent of ribosome Source: GO_Central

GO - Biological processi

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

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_270125. Mitochondrial translation elongation.
REACT_270158. Mitochondrial translation termination.
REACT_271096. Mitochondrial translation initiation.

Names & Taxonomyi

Protein namesi
Recommended name:
39S ribosomal protein L33, mitochondrial
Short name:
L33mt
Short name:
MRP-L33
Gene namesi
Name:Mrpl33
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:2137225. Mrpl33.

Subcellular locationi

Mitochondrion 1 Publication

GO - Cellular componenti

  1. mitochondrial large ribosomal subunit Source: GO_Central
  2. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 656539S ribosomal protein L33, mitochondrialPRO_0000238626Add
BLAST

Proteomic databases

MaxQBiQ9CQP0.
PaxDbiQ9CQP0.
PRIDEiQ9CQP0.

Expressioni

Gene expression databases

BgeeiQ9CQP0.
CleanExiMM_MRPL33.
ExpressionAtlasiQ9CQP0. baseline.
GenevestigatoriQ9CQP0.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000116693.

Structurei

3D structure databases

ProteinModelPortaliQ9CQP0.
SMRiQ9CQP0. Positions 13-60.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L33P family.Curated

Phylogenomic databases

eggNOGiNOG48156.
GeneTreeiENSGT00390000010130.
HOGENOMiHOG000004840.
HOVERGENiHBG053140.
InParanoidiQ9CQP0.
KOiK02913.
OMAiAVKYDPR.
OrthoDBiEOG7J9VSQ.
TreeFamiTF300279.

Family and domain databases

InterProiIPR001705. Ribosomal_L33.
IPR011332. Ribosomal_zn-bd.
[Graphical view]
PfamiPF00471. Ribosomal_L33. 1 hit.
[Graphical view]
SUPFAMiSSF57829. SSF57829. 1 hit.
TIGRFAMsiTIGR01023. rpmG_bact. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9CQP0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLLSAVSFAK SKSKTILVKL VSQAGTGFSF NHKRSRLREK LSLLHYDPIV
60
NKKVLFVEQK KIRSL
Length:65
Mass (Da):7,416
Last modified:June 1, 2001 - v1
Checksum:i6F8E69CA0359BE6F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti58 – 581E → G in BAB25665. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB049651 mRNA. Translation: BAB40856.1.
AK002421 mRNA. Translation: BAB22088.1.
AK008431 mRNA. Translation: BAB25665.1.
AK021173 mRNA. Translation: BAB32314.1.
AK167883 mRNA. Translation: BAE39896.1.
BC037363 mRNA. Translation: AAH37363.1.
BC051471 mRNA. Translation: AAH51471.1.
BC055724 mRNA. Translation: AAH55724.1.
BC059722 mRNA. Translation: AAH59722.1.
CCDSiCCDS39056.1.
RefSeqiNP_080072.2. NM_025796.3.
UniGeneiMm.120763.

Genome annotation databases

EnsembliENSMUST00000031024; ENSMUSP00000031024; ENSMUSG00000029142.
GeneIDi66845.
KEGGimmu:66845.
UCSCiuc008wyt.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB049651 mRNA. Translation: BAB40856.1.
AK002421 mRNA. Translation: BAB22088.1.
AK008431 mRNA. Translation: BAB25665.1.
AK021173 mRNA. Translation: BAB32314.1.
AK167883 mRNA. Translation: BAE39896.1.
BC037363 mRNA. Translation: AAH37363.1.
BC051471 mRNA. Translation: AAH51471.1.
BC055724 mRNA. Translation: AAH55724.1.
BC059722 mRNA. Translation: AAH59722.1.
CCDSiCCDS39056.1.
RefSeqiNP_080072.2. NM_025796.3.
UniGeneiMm.120763.

3D structure databases

ProteinModelPortaliQ9CQP0.
SMRiQ9CQP0. Positions 13-60.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000116693.

Proteomic databases

MaxQBiQ9CQP0.
PaxDbiQ9CQP0.
PRIDEiQ9CQP0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031024; ENSMUSP00000031024; ENSMUSG00000029142.
GeneIDi66845.
KEGGimmu:66845.
UCSCiuc008wyt.2. mouse.

Organism-specific databases

CTDi9553.
MGIiMGI:2137225. Mrpl33.

Phylogenomic databases

eggNOGiNOG48156.
GeneTreeiENSGT00390000010130.
HOGENOMiHOG000004840.
HOVERGENiHBG053140.
InParanoidiQ9CQP0.
KOiK02913.
OMAiAVKYDPR.
OrthoDBiEOG7J9VSQ.
TreeFamiTF300279.

Enzyme and pathway databases

ReactomeiREACT_270125. Mitochondrial translation elongation.
REACT_270158. Mitochondrial translation termination.
REACT_271096. Mitochondrial translation initiation.

Miscellaneous databases

ChiTaRSiMrpl33. mouse.
NextBioi322803.
PROiQ9CQP0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQP0.
CleanExiMM_MRPL33.
ExpressionAtlasiQ9CQP0. baseline.
GenevestigatoriQ9CQP0.

Family and domain databases

InterProiIPR001705. Ribosomal_L33.
IPR011332. Ribosomal_zn-bd.
[Graphical view]
PfamiPF00471. Ribosomal_L33. 1 hit.
[Graphical view]
SUPFAMiSSF57829. SSF57829. 1 hit.
TIGRFAMsiTIGR01023. rpmG_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], SUBCELLULAR LOCATION.
  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 and DBA/2.
    Tissue: Kidney 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/6.
    Tissue: Brain, Mammary gland and Testis.

Entry informationi

Entry nameiRM33_MOUSE
AccessioniPrimary (citable) accession number: Q9CQP0
Secondary accession number(s): Q9D860
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: June 1, 2001
Last modified: February 4, 2015
This is version 87 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

External Data

Dasty 3

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 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.