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Q9CQL4

- RM20_MOUSE

UniProt

Q9CQL4 - RM20_MOUSE

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Protein

39S ribosomal protein L20, mitochondrial

Gene
Mrpl20
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 2 out of 5 - Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. rRNA binding Source: InterPro
  2. structural constituent of ribosome Source: InterPro

GO - Biological processi

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

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Names & Taxonomyi

Protein namesi
Recommended name:
39S ribosomal protein L20, mitochondrial
Short name:
L20mt
Short name:
MRP-L20
Gene namesi
Name:Mrpl20
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:2137221. Mrpl20.

Subcellular locationi

Mitochondrion 1 Publication

GO - Cellular componenti

  1. mitochondrial ribosome Source: UniProtKB
  2. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4545Mitochondrion Reviewed predictionAdd
BLAST
Chaini46 – 14910439S ribosomal protein L20, mitochondrialPRO_0000248280Add
BLAST

Proteomic databases

MaxQBiQ9CQL4.
PaxDbiQ9CQL4.
PRIDEiQ9CQL4.

PTM databases

PhosphoSiteiQ9CQL4.

Expressioni

Gene expression databases

BgeeiQ9CQL4.
CleanExiMM_MRPL20.
GenevestigatoriQ9CQL4.

Interactioni

Subunit structurei

Interacts with OXA1L By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ9CQL4.
SMRiQ9CQL4. Positions 10-124.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0292.
GeneTreeiENSGT00390000015823.
HOGENOMiHOG000035046.
HOVERGENiHBG058971.
InParanoidiQ9CQL4.
KOiK02887.
OMAiINAEARN.
OrthoDBiEOG7PZS00.
PhylomeDBiQ9CQL4.
TreeFamiTF324702.

Family and domain databases

InterProiIPR005813. Ribosomal_L20.
[Graphical view]
PANTHERiPTHR10986. PTHR10986. 1 hit.
PfamiPF00453. Ribosomal_L20. 1 hit.
[Graphical view]
PRINTSiPR00062. RIBOSOMALL20.
TIGRFAMsiTIGR01032. rplT_bact. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9CQL4-1 [UniParc]FASTAAdd to Basket

« Hide

MVFLTTRLWL RNRLTDRYWR VQEVLKHAQH FRGRKNRCYR LAVRAVTRAF    50
VKCTKARRLK KRNLRTLWIN RITAASQEHG LKYPAFIVNL IKCQVELNRK 100
VLVDLAIYEP KTFKSLAALA KRRQQEGFAA ALGDGKEPEG IFSRVVQYH 149
Length:149
Mass (Da):17,595
Last modified:June 1, 2001 - v1
Checksum:i7B86D8C568B633AE
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti62 – 621R → L in BAB29744. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB049645 mRNA. Translation: BAB40850.1.
AK004053 mRNA. Translation: BAB23143.1.
AK011341 mRNA. Translation: BAB27555.1.
AK015199 mRNA. Translation: BAB29744.1.
AK168665 mRNA. Translation: BAE40517.1.
BC039985 mRNA. Translation: AAH39985.1.
CCDSiCCDS19041.1.
RefSeqiNP_079846.1. NM_025570.2.
XP_006539167.1. XM_006539104.1.
UniGeneiMm.23825.

Genome annotation databases

EnsembliENSMUST00000030942; ENSMUSP00000030942; ENSMUSG00000029066.
ENSMUST00000137487; ENSMUSP00000139122; ENSMUSG00000029066.
GeneIDi66448.
KEGGimmu:66448.
UCSCiuc008weu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB049645 mRNA. Translation: BAB40850.1 .
AK004053 mRNA. Translation: BAB23143.1 .
AK011341 mRNA. Translation: BAB27555.1 .
AK015199 mRNA. Translation: BAB29744.1 .
AK168665 mRNA. Translation: BAE40517.1 .
BC039985 mRNA. Translation: AAH39985.1 .
CCDSi CCDS19041.1.
RefSeqi NP_079846.1. NM_025570.2.
XP_006539167.1. XM_006539104.1.
UniGenei Mm.23825.

3D structure databases

ProteinModelPortali Q9CQL4.
SMRi Q9CQL4. Positions 10-124.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q9CQL4.

Proteomic databases

MaxQBi Q9CQL4.
PaxDbi Q9CQL4.
PRIDEi Q9CQL4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000030942 ; ENSMUSP00000030942 ; ENSMUSG00000029066 .
ENSMUST00000137487 ; ENSMUSP00000139122 ; ENSMUSG00000029066 .
GeneIDi 66448.
KEGGi mmu:66448.
UCSCi uc008weu.1. mouse.

Organism-specific databases

CTDi 55052.
MGIi MGI:2137221. Mrpl20.

Phylogenomic databases

eggNOGi COG0292.
GeneTreei ENSGT00390000015823.
HOGENOMi HOG000035046.
HOVERGENi HBG058971.
InParanoidi Q9CQL4.
KOi K02887.
OMAi INAEARN.
OrthoDBi EOG7PZS00.
PhylomeDBi Q9CQL4.
TreeFami TF324702.

Miscellaneous databases

NextBioi 321725.
PROi Q9CQL4.
SOURCEi Search...

Gene expression databases

Bgeei Q9CQL4.
CleanExi MM_MRPL20.
Genevestigatori Q9CQL4.

Family and domain databases

InterProi IPR005813. Ribosomal_L20.
[Graphical view ]
PANTHERi PTHR10986. PTHR10986. 1 hit.
Pfami PF00453. Ribosomal_L20. 1 hit.
[Graphical view ]
PRINTSi PR00062. RIBOSOMALL20.
TIGRFAMsi TIGR01032. rplT_bact. 1 hit.
ProtoNeti Search...

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.
    Tissue: Stomach and Testis.
  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: Mammary gland.
  4. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 83-92, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.

Entry informationi

Entry nameiRM20_MOUSE
AccessioniPrimary (citable) accession number: Q9CQL4
Secondary accession number(s): Q9D5L3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 96 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, 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

External Data

Dasty 3

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