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Protein

39S ribosomal protein L9, mitochondrial

Gene

MRPL9

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

Functioni

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. structural constituent of ribosome Source: UniProtKB

GO - Biological processi

  1. mitochondrial translation Source: Reactome
  2. mitochondrial translational elongation Source: Reactome
  3. mitochondrial translational initiation Source: Reactome
  4. mitochondrial translational termination Source: Reactome
  5. organelle organization Source: Reactome
  6. translation Source: UniProtKB
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 L9, mitochondrial
Short name:
L9mt
Short name:
MRP-L9
Gene namesi
Name:MRPL9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:14277. MRPL9.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial inner membrane Source: Reactome
  2. mitochondrial ribosome Source: UniProtKB
  3. mitochondrion Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30991.

Polymorphism and mutation databases

BioMutaiMRPL9.
DMDMi209572671.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 26739S ribosomal protein L9, mitochondrialPRO_0000030550
Transit peptidei1 – ?MitochondrionSequence Analysis

Proteomic databases

MaxQBiQ9BYD2.
PaxDbiQ9BYD2.
PRIDEiQ9BYD2.

PTM databases

PhosphoSiteiQ9BYD2.

Expressioni

Gene expression databases

BgeeiQ9BYD2.
CleanExiHS_MRPL9.
ExpressionAtlasiQ9BYD2. baseline and differential.
GenevestigatoriQ9BYD2.

Organism-specific databases

HPAiHPA008579.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
FAM9BQ8IZU03EBI-726059,EBI-10175124

Protein-protein interaction databases

BioGridi122370. 39 interactions.
IntActiQ9BYD2. 6 interactions.
MINTiMINT-1392474.
STRINGi9606.ENSP00000357823.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J7Yelectron microscopy3.40H1-267[»]
ProteinModelPortaliQ9BYD2.
SMRiQ9BYD2. Positions 94-219.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L9P family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiNOG311734.
GeneTreeiENSGT00390000008281.
HOGENOMiHOG000247066.
HOVERGENiHBG002704.
InParanoidiQ9BYD2.
KOiK02939.
OMAiVKFLKSC.
OrthoDBiEOG76DTTG.
PhylomeDBiQ9BYD2.
TreeFamiTF300170.

Family and domain databases

Gene3Di3.40.5.10. 1 hit.
InterProiIPR000244. Ribosomal_L9.
IPR009027. Ribosomal_L9/RNase_H1_N.
IPR020070. Ribosomal_L9_N.
[Graphical view]
PANTHERiPTHR21368. PTHR21368. 1 hit.
PfamiPF01281. Ribosomal_L9_N. 1 hit.
[Graphical view]
SUPFAMiSSF55658. SSF55658. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9BYD2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPVVTAPG RALLRAGAGR LLRGGVQELL RPRHEGNAPD LACNFSLSQN
60 70 80 90 100
RGTVIVERWW KVPLAGEGRK PRLHRRHRVY KLVEDTKHRP KENLELILTQ
110 120 130 140 150
SVENVGVRGD LVSVKKSLGR NRLLPQGLAV YASPENKKLF EEEKLLRQEG
160 170 180 190 200
KLEKIQTKAG EATVKFLKSC RLEVGMKNNV KWELNPEIVA RHFFKNLGVV
210 220 230 240 250
VAPHTLKLPE EPITRWGEYW CEVTVNGLDT VRVPMSVVNF EKPKTKRYKY
260
WLAQQAAKAM APTSPQI
Length:267
Mass (Da):30,243
Last modified:October 14, 2008 - v2
Checksum:i3468214224FBD1B4
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti67 – 671E → G.
Corresponds to variant rs7007 [ dbSNP | Ensembl ].
VAR_028136
Natural varianti210 – 2101E → A.1 Publication
Corresponds to variant rs8480 [ dbSNP | Ensembl ].
VAR_028137

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB049636 mRNA. Translation: BAB40841.1.
AK315459 mRNA. Translation: BAG37846.1.
AL589765 Genomic DNA. Translation: CAI17171.1.
CH471121 Genomic DNA. Translation: EAW53415.1.
BC004517 mRNA. Translation: AAH04517.1.
CCDSiCCDS1003.1.
RefSeqiNP_001287662.1. NM_001300733.1.
NP_113608.1. NM_031420.3.
UniGeneiHs.288936.

Genome annotation databases

EnsembliENST00000368830; ENSP00000357823; ENSG00000143436.
GeneIDi65005.
KEGGihsa:65005.
UCSCiuc001eyv.3. human.

Polymorphism and mutation databases

BioMutaiMRPL9.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB049636 mRNA. Translation: BAB40841.1.
AK315459 mRNA. Translation: BAG37846.1.
AL589765 Genomic DNA. Translation: CAI17171.1.
CH471121 Genomic DNA. Translation: EAW53415.1.
BC004517 mRNA. Translation: AAH04517.1.
CCDSiCCDS1003.1.
RefSeqiNP_001287662.1. NM_001300733.1.
NP_113608.1. NM_031420.3.
UniGeneiHs.288936.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J7Yelectron microscopy3.40H1-267[»]
ProteinModelPortaliQ9BYD2.
SMRiQ9BYD2. Positions 94-219.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122370. 39 interactions.
IntActiQ9BYD2. 6 interactions.
MINTiMINT-1392474.
STRINGi9606.ENSP00000357823.

PTM databases

PhosphoSiteiQ9BYD2.

Polymorphism and mutation databases

BioMutaiMRPL9.
DMDMi209572671.

Proteomic databases

MaxQBiQ9BYD2.
PaxDbiQ9BYD2.
PRIDEiQ9BYD2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368830; ENSP00000357823; ENSG00000143436.
GeneIDi65005.
KEGGihsa:65005.
UCSCiuc001eyv.3. human.

Organism-specific databases

CTDi65005.
GeneCardsiGC01M151732.
HGNCiHGNC:14277. MRPL9.
HPAiHPA008579.
MIMi611824. gene.
neXtProtiNX_Q9BYD2.
PharmGKBiPA30991.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG311734.
GeneTreeiENSGT00390000008281.
HOGENOMiHOG000247066.
HOVERGENiHBG002704.
InParanoidiQ9BYD2.
KOiK02939.
OMAiVKFLKSC.
OrthoDBiEOG76DTTG.
PhylomeDBiQ9BYD2.
TreeFamiTF300170.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiMRPL9. human.
GenomeRNAii65005.
NextBioi67188.
PROiQ9BYD2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BYD2.
CleanExiHS_MRPL9.
ExpressionAtlasiQ9BYD2. baseline and differential.
GenevestigatoriQ9BYD2.

Family and domain databases

Gene3Di3.40.5.10. 1 hit.
InterProiIPR000244. Ribosomal_L9.
IPR009027. Ribosomal_L9/RNase_H1_N.
IPR020070. Ribosomal_L9_N.
[Graphical view]
PANTHERiPTHR21368. PTHR21368. 1 hit.
PfamiPF01281. Ribosomal_L9_N. 1 hit.
[Graphical view]
SUPFAMiSSF55658. SSF55658. 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], VARIANT ALA-210.
  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].
  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].
    Tissue: Lung.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRM09_HUMAN
AccessioniPrimary (citable) accession number: Q9BYD2
Secondary accession number(s): B2RD99, Q5SZR2, Q9BSW8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: October 14, 2008
Last modified: April 29, 2015
This is version 118 of the entry and version 2 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. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Ribosomal proteins
    Ribosomal proteins families and list of entries
  7. 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.