Q8IXM3 (RM41_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	137 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Apoptosis Cell cycle
Cellular component	Mitochondrion
Domain	Transit peptide
Molecular function	Ribonucleoprotein Ribosomal protein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic 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_component	mitochondrial large ribosomal subunit Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	structural constituent of ribosome Inferred from direct assay Ref.7. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 13	13	Mitochondrion By similarity
	Chain	14 – 137	124	39S ribosomal protein L41, mitochondrial		PRO_0000273228

Sequences

	Sequence		Length	Mass (Da)
	Q8IXM3 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 25A9F3105ABF1189	FASTA	137	15,383
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00217553.
RefSeq	NP_115866.1. NM_032477.2.
UniGene	Hs.44017.
3D structure databases
ProteinModelPortal	Q8IXM3.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8IXM3. 2 interactions.
MINT	MINT-6492237.
STRING	9606.ENSP00000360498.
Polymorphism databases
DMDM	74750734.
Proteomic databases
PaxDb	Q8IXM3.
PeptideAtlas	Q8IXM3.
PRIDE	Q8IXM3.
Protocols and materials databases
DNASU	64975.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000371443; ENSP00000360498; ENSG00000182154.
GeneID	64975.
KEGG	hsa:64975.
UCSC	uc004cnh.4. human.
Organism-specific databases
CTD	64975.
GeneCards	GC09P140445.
HGNC	HGNC:14492. MRPL41.
HPA	HPA024550. HPA027160.
MIM	611846. gene.
neXtProt	NX_Q8IXM3.
PharmGKB	PA30973.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG264900.
HOGENOM	HOG000231555.
HOVERGEN	HBG080323.
InParanoid	Q8IXM3.
OMA	GPRTFYK.
OrthoDB	EOG4C2HBW.
PhylomeDB	Q8IXM3.
Gene expression databases
Bgee	Q8IXM3.
CleanEx	HS_MRPL27. HS_MRPL41.
Genevestigator	Q8IXM3.
Family and domain databases
InterPro	IPR019189. Ribosomal_L27/L41_mit. [Graphical view]
Pfam	PF09809. MRP-L27. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	64975.
NextBio	67156.
SOURCE	Search...

Entry information

Entry name

RM41_HUMAN

Accession

Primary (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:	April 3, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.