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Q8IXM3 (RM41_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
39S ribosomal protein L41, mitochondrial

Short name=L41mt
Short name=MRP-L41
Alternative name(s):
39S ribosomal protein L27 homolog
Bcl-2-interacting mitochondrial ribosomal protein L41
Cell proliferation-inducing gene 3 protein
MRP-L27 homolog
Gene names
Name:MRPL41
Synonyms:BMRP, MRPL27, RPML27
ORF Names:PIG3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length137 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the mitochondrial ribosome large subunit. Also involved in apoptosis and cell cycle. Enhances p53/TP53 stability, thereby contributing to p53/TP53-induced apoptosis in response to growth-inhibitory condition. Enhances p53/TP53 translocation to the mitochondria. Has the ability to arrest the cell cycle at the G1 phase, possibly by stabilizing the CDKN1A and CDKN1B (p27Kip1) proteins. Ref.7 Ref.8

Subunit structure

Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins. Interacts with BCL2. Ref.6

Subcellular location

Mitochondrion Ref.7.

Tissue specificity

Present in kidney, liver, thymus and testis, and at lower level in brain and spleen (at protein level). Ref.6

Sequence similarities

Belongs to the ribosomal protein L41 family.

Ontologies

Keywords
   Biological processApoptosis
Cell cycle
   Cellular componentMitochondrion
   DomainTransit peptide
   Molecular functionRibonucleoprotein
Ribosomal protein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

translation

Inferred from direct assay Ref.7. Source: UniProtKB

   Cellular_componentmitochondrial large ribosomal subunit

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_functionstructural constituent of ribosome

Inferred from direct assay Ref.7. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TRIM63Q969Q12EBI-912501,EBI-5661333

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1313Mitochondrion By similarity
Chain14 – 13712439S ribosomal protein L41, mitochondrial
PRO_0000273228

Sequences

Sequence LengthMass (Da)Tools
Q8IXM3 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 25A9F3105ABF1189

FASTA13715,383
        10         20         30         40         50         60 
MGVLAAAARC LVRGADRMSK WTSKRGPRSF RGRKGRGAKG IGFLTSGWRF VQIKEMVPEF 

        70         80         90        100        110        120 
VVPDLTGFKL KPYVSYLAPE SEETPLTAAQ LFSEAVAPAI EKDFKDGTFD PDNLEKYGFE 

       130 
PTQEGKLFQL YPRNFLR 

« Hide

References

« Hide 'large scale' references
[1]Kim J.W.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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 gland.
[4]"The human mitochondrial ribosomal protein genes: mapping of 54 genes to the chromosomes and implications for human disorders."
Kenmochi N., Suzuki T., Uechi T., Magoori M., Kuniba M., Higa S., Watanabe K., Tanaka T.
Genomics 77:65-70(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 90-135.
[5]"The large subunit of the mammalian mitochondrial ribosome. Analysis of the complement of ribosomal proteins present."
Koc E.C., Burkhart W., Blackburn K., Moyer M.B., Schlatzer D.M., Moseley A., Spremulli L.L.
J. Biol. Chem. 276:43958-43969(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[6]"BMRP is a Bcl-2 binding protein that induces apoptosis."
Chintharlapalli S.R., Jasti M., Malladi S., Parsa K.V.L., Ballestero R.P., Gonzalez-Garcia M.
J. Cell. Biochem. 94:611-626(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BCL2, TISSUE SPECIFICITY.
[7]"Mitochondrial ribosomal protein L41 suppresses cell growth in association with p53 and p27Kip1."
Yoo Y.A., Kim M.J., Park J.K., Chung Y.M., Lee J.H., Chi S.-G., Kim J.S., Yoo Y.D.
Mol. Cell. Biol. 25:6603-6616(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]"Mitochondrial ribosomal protein L41 mediates serum starvation-induced cell-cycle arrest through an increase of p21(WAF1/CIP1)."
Kim M.J., Yoo Y.A., Kim H.J., Kang S., Kim Y.G., Kim J.S., Yoo Y.D.
Biochem. Biophys. Res. Commun. 338:1179-1184(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY232291 mRNA. Translation: AAP69986.1.
AL365502 Genomic DNA. Translation: CAI14583.1.
BC040035 mRNA. Translation: AAH40035.1.
AB051625 Genomic DNA. Translation: BAB54952.1.
RefSeqNP_115866.1. NM_032477.2.
UniGeneHs.44017.

3D structure databases

ProteinModelPortalQ8IXM3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122363. 27 interactions.
IntActQ8IXM3. 5 interactions.
MINTMINT-6492237.
STRING9606.ENSP00000360498.

Polymorphism databases

DMDM74750734.

Proteomic databases

PaxDbQ8IXM3.
PeptideAtlasQ8IXM3.
PRIDEQ8IXM3.

Protocols and materials databases

DNASU64975.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371443; ENSP00000360498; ENSG00000182154.
GeneID64975.
KEGGhsa:64975.
UCSCuc004cnh.4. human.

Organism-specific databases

CTD64975.
GeneCardsGC09P140445.
HGNCHGNC:14492. MRPL41.
HPAHPA024550.
HPA027160.
MIM611846. gene.
neXtProtNX_Q8IXM3.
PharmGKBPA30973.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG264900.
HOGENOMHOG000231555.
HOVERGENHBG080323.
InParanoidQ8IXM3.
KOK17422.
OMAPRTFYKS.
OrthoDBEOG708W17.
PhylomeDBQ8IXM3.
TreeFamTF325007.

Gene expression databases

BgeeQ8IXM3.
CleanExHS_MRPL27.
HS_MRPL41.
GenevestigatorQ8IXM3.

Family and domain databases

InterProIPR019189. Ribosomal_L27/L41_mit.
[Graphical view]
PfamPF09809. MRP-L27. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiMitochondrial_ribosomal_protein_L41.
GenomeRNAi64975.
NextBio67156.
PROQ8IXM3.
SOURCESearch...

Entry information

Entry nameRM41_HUMAN
AccessionPrimary (citable) accession number: Q8IXM3
Secondary accession number(s): Q96Q49
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: March 1, 2003
Last modified: February 19, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM