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Protein

39S ribosomal protein L20, mitochondrial

Gene

MRPL20

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • rRNA binding Source: InterPro
  • structural constituent of ribosome Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_267634. Mitochondrial translation initiation.
REACT_268133. Mitochondrial translation elongation.
REACT_268261. Mitochondrial translation termination.

Names & Taxonomyi

Protein namesi
Recommended name:
39S ribosomal protein L20, mitochondrial
Short name:
L20mt
Short name:
MRP-L20
Gene namesi
Name:MRPL20
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:14478. MRPL20.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: Reactome
  • mitochondrial ribosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30950.

Polymorphism and mutation databases

BioMutaiMRPL20.
DMDMi74752447.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4545MitochondrionSequence AnalysisAdd
BLAST
Chaini46 – 14910439S ribosomal protein L20, mitochondrialPRO_0000248279Add
BLAST

Proteomic databases

MaxQBiQ9BYC9.
PaxDbiQ9BYC9.
PeptideAtlasiQ9BYC9.
PRIDEiQ9BYC9.

PTM databases

PhosphoSiteiQ9BYC9.

Expressioni

Gene expression databases

BgeeiQ9BYC9.
CleanExiHS_MRPL20.
ExpressionAtlasiQ9BYC9. baseline and differential.
GenevisibleiQ9BYC9. HS.

Organism-specific databases

HPAiHPA047074.

Interactioni

Subunit structurei

Interacts with OXA1L.By similarity

Protein-protein interaction databases

BioGridi120374. 26 interactions.
IntActiQ9BYC9. 12 interactions.
MINTiMINT-1419302.
STRINGi9606.ENSP00000341082.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J7Yelectron microscopy3.40R1-149[»]
3J9Melectron microscopy3.50R1-149[»]
ProteinModelPortaliQ9BYC9.
SMRiQ9BYC9. Positions 10-149.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L20P family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0292.
GeneTreeiENSGT00390000015823.
HOGENOMiHOG000035046.
HOVERGENiHBG058971.
InParanoidiQ9BYC9.
KOiK02887.
OMAiRKNRCYS.
OrthoDBiEOG7PZS00.
PhylomeDBiQ9BYC9.
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.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BYC9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVFLTAQLWL RNRVTDRYFR IQEVLKHARH FRGRKNRCYR LAVRTVIRAF
60 70 80 90 100
VKCTKARYLK KKNMRTLWIN RITAASQEHG LKYPALIGNL VKCQVELNRK
110 120 130 140
VLADLAIYEP KTFKSLAALA SRRRHEGFAA ALGDGKEPEG IFSRVVQYH
Length:149
Mass (Da):17,443
Last modified:June 1, 2001 - v1
Checksum:i53AD05B3BBD9AE6B
GO
Isoform 2 (identifier: Q9BYC9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     93-149: CQVELNRKVL...GIFSRVVQYH → VWVSMWVPLK...VSMLSVVSIW

Note: No experimental confirmation available.
Show »
Length:155
Mass (Da):18,099
Checksum:iDCB0C378CF4DF3B1
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei93 – 14957CQVEL…VVQYH → VWVSMWVPLKFWTSAETIMR GVVVLPVVPANQEAEARGSL ETDFWAVVCYADGVSMLSVV SIW in isoform 2. 1 PublicationVSP_056084Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB049644 mRNA. Translation: BAB40849.1.
AK301440 mRNA. Translation: BAH13482.1.
AK315794 mRNA. Translation: BAG38138.1.
AL391244 Genomic DNA. Translation: CAI22658.1.
CH471183 Genomic DNA. Translation: EAW56207.1.
BC009515 mRNA. Translation: AAH09515.1.
BC014316 mRNA. Translation: AAH14316.1.
BC059945 mRNA. Translation: AAH59945.1.
CCDSiCCDS26.1. [Q9BYC9-1]
RefSeqiNP_060441.2. NM_017971.3. [Q9BYC9-1]
XP_005244824.1. XM_005244767.2. [Q9BYC9-2]
UniGeneiHs.182698.

Genome annotation databases

EnsembliENST00000344843; ENSP00000341082; ENSG00000242485. [Q9BYC9-1]
ENST00000482352; ENSP00000460924; ENSG00000242485. [Q9BYC9-2]
GeneIDi55052.
KEGGihsa:55052.
UCSCiuc001afo.4. human. [Q9BYC9-1]
uc010nyn.1. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB049644 mRNA. Translation: BAB40849.1.
AK301440 mRNA. Translation: BAH13482.1.
AK315794 mRNA. Translation: BAG38138.1.
AL391244 Genomic DNA. Translation: CAI22658.1.
CH471183 Genomic DNA. Translation: EAW56207.1.
BC009515 mRNA. Translation: AAH09515.1.
BC014316 mRNA. Translation: AAH14316.1.
BC059945 mRNA. Translation: AAH59945.1.
CCDSiCCDS26.1. [Q9BYC9-1]
RefSeqiNP_060441.2. NM_017971.3. [Q9BYC9-1]
XP_005244824.1. XM_005244767.2. [Q9BYC9-2]
UniGeneiHs.182698.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J7Yelectron microscopy3.40R1-149[»]
3J9Melectron microscopy3.50R1-149[»]
ProteinModelPortaliQ9BYC9.
SMRiQ9BYC9. Positions 10-149.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120374. 26 interactions.
IntActiQ9BYC9. 12 interactions.
MINTiMINT-1419302.
STRINGi9606.ENSP00000341082.

PTM databases

PhosphoSiteiQ9BYC9.

Polymorphism and mutation databases

BioMutaiMRPL20.
DMDMi74752447.

Proteomic databases

MaxQBiQ9BYC9.
PaxDbiQ9BYC9.
PeptideAtlasiQ9BYC9.
PRIDEiQ9BYC9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000344843; ENSP00000341082; ENSG00000242485. [Q9BYC9-1]
ENST00000482352; ENSP00000460924; ENSG00000242485. [Q9BYC9-2]
GeneIDi55052.
KEGGihsa:55052.
UCSCiuc001afo.4. human. [Q9BYC9-1]
uc010nyn.1. human.

Organism-specific databases

CTDi55052.
GeneCardsiGC01M001329.
H-InvDBHIX0000027.
HGNCiHGNC:14478. MRPL20.
HPAiHPA047074.
MIMi611833. gene.
neXtProtiNX_Q9BYC9.
PharmGKBiPA30950.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0292.
GeneTreeiENSGT00390000015823.
HOGENOMiHOG000035046.
HOVERGENiHBG058971.
InParanoidiQ9BYC9.
KOiK02887.
OMAiRKNRCYS.
OrthoDBiEOG7PZS00.
PhylomeDBiQ9BYC9.
TreeFamiTF324702.

Enzyme and pathway databases

ReactomeiREACT_267634. Mitochondrial translation initiation.
REACT_268133. Mitochondrial translation elongation.
REACT_268261. Mitochondrial translation termination.

Miscellaneous databases

GeneWikiiMRPL20.
GenomeRNAii55052.
NextBioi35480142.
PROiQ9BYC9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BYC9.
CleanExiHS_MRPL20.
ExpressionAtlasiQ9BYC9. baseline and differential.
GenevisibleiQ9BYC9. HS.

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.
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] (ISOFORM 1), SUBCELLULAR LOCATION.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Synovium and Uterus.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1).
    Tissue: Bone marrow, Lymph and Mammary gland.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRM20_HUMAN
AccessioniPrimary (citable) accession number: Q9BYC9
Secondary accession number(s): B2RE41, B7Z746
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: June 1, 2001
Last modified: June 24, 2015
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Ribosomal proteins
    Ribosomal proteins families and list of entries
  5. 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.