Mitochondrial ribosomal protein L41

Protein-coding gene in the species Homo sapiens

MRPL41

| Available structures

PDB| Ortholog search: PDBe RCSB
| List of PDB id codes

3J7Y, 3J9M

Identifiers
Aliases| MRPL41, BMRP, MRP-L27, MRPL27, RPML27, PIG3, Mitochondrial ribosomal protein L41
External IDs| OMIM: 611846; MGI: 1333816; HomoloGene: 13036; GeneCards: MRPL41; OMA:MRPL41 - orthologs
| Gene location (Human)

Chr.| Chromosome 9 (human)[1]

Band| 9q34.3| Start| 137,551,879 bp[1]
End| 137,552,555 bp[1]
| Gene location (Mouse)

Chr.| Chromosome 2 (mouse)[2]

Band| 2|2 A3| Start| 24,864,129 bp[2]
End| 24,865,110 bp[2]
| RNA expression pattern

Bgee| | Human| Mouse (ortholog)

|

| Top expressed in

* apex of heart

* myocardium of left ventricle

* right auricle of heart

* right ventricle

* mucosa of transverse colon

* cingulate gyrus

* anterior cingulate cortex

* caudate nucleus

* putamen

* muscle of thigh

| Top expressed in

* facial motor nucleus

* fossa

* condyle

* motor neuron

* epithelium of lens

* endocardial cushion

* external carotid artery

* internal carotid artery

* renal corpuscle

* atrioventricular junction

More reference expression data
BioGPS| |

More reference expression data
| Gene ontology

Molecular function|

* structural constituent of ribosome
* protein binding
* RNA binding

Cellular component|

* mitochondrial inner membrane
* ribosome
* mitochondrion
* mitochondrial large ribosomal subunit
* ribonucleoprotein complex

Biological process|

* cell cycle
* mitochondrial translational elongation
* mitochondrial translational termination
* protein biosynthesis
* apoptotic process

Sources:Amigo / QuickGO
| Orthologs

Species| Human| Mouse
Entrez| |

64975

107733

Ensembl| |

ENSG00000182154

ENSMUSG00000036850

UniProt| |

Q8IXM3

Q9CQN7

RefSeq (mRNA)| |

NM_032477

NM_001031808

RefSeq (protein)| |

NP_115866

NP_001026978

Location (UCSC)| Chr 9: 137.55 – 137.55 Mb| Chr 2: 24.86 – 24.87 Mb
PubMed search| [3]| [4]
Wikidata
| View/Edit Human| View/Edit Mouse

|

39S ribosomal protein L41, mitochondrial is a protein that in humans is encoded by the MRPL41 gene.[5][6]

Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. They have an estimated 75% protein to rRNA composition compared to prokaryotic ribosomes, where this ratio is reversed. Another difference between mammalian mitoribosomes and prokaryotic ribosomes is that the latter contain a 5S rRNA. Among different species, the proteins comprising the mitoribosome differ greatly in sequence, and sometimes in biochemical properties, which prevents easy recognition by sequence homology. This gene encodes a 39S subunit protein that belongs to the YmL27 ribosomal protein family.[6]

## References

[edit]

1. ^ a b c GRCh38: Ensembl release 89: ENSG00000182154 - Ensembl, May 2017
2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000036850 - Ensembl, May 2017
3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. ^ Kenmochi N, Suzuki T, Uechi T, Magoori M, Kuniba M, Higa S, Watanabe K, Tanaka T (Sep 2001). "The human mitochondrial ribosomal protein genes: mapping of 54 genes to the chromosomes and implications for human disorders". Genomics. 77 (1–2): 65–70\. doi:10.1006/geno.2001.6622. PMID 11543634.1–2&rft.pages=65-70&rft.date=2001-09&rft_id=info:doi/10.1006/geno.2001.6622&rft_id=info:pmid/11543634&rft.aulast=Kenmochi&rft.aufirst=N&rft.au=Suzuki,+T&rft.au=Uechi,+T&rft.au=Magoori,+M&rft.au=Kuniba,+M&rft.au=Higa,+S&rft.au=Watanabe,+K&rft.au=Tanaka,+T&rfr_id=info:sid/en.wikipedia.org:Mitochondrial+ribosomal+protein+L41" class="Z3988">
6. ^ a b "Entrez Gene: MRPL41 mitochondrial ribosomal protein L41".

## Further reading

[edit]

* Goldschmidt-Reisin S, Kitakawa M, Herfurth E, et al. (1999). "Mammalian mitochondrial ribosomal proteins. N-terminal amino acid sequencing, characterization, and identification of corresponding gene sequences". J. Biol. Chem. 273 (52): 34828–36\. doi:10.1074/jbc.273.52.34828. PMID 9857009.34828-36&rft.date=1999&rft_id=info:doi/10.1074/jbc.273.52.34828&rft_id=info:pmid/9857009&rft.aulast=Goldschmidt-Reisin&rft.aufirst=S&rft.au=Kitakawa,+M&rft.au=Herfurth,+E&rft_id=https://doi.org/10.1074%2Fjbc.273.52.34828&rfr_id=info:sid/en.wikipedia.org:Mitochondrial+ribosomal+protein+L41" class="Z3988">
* Koc EC, Burkhart W, Blackburn K, et al. (2001). "The large subunit of the mammalian mitochondrial ribosome. Analysis of the complement of ribosomal proteins present". J. Biol. Chem. 276 (47): 43958–69\. doi:10.1074/jbc.M106510200. PMID 11551941.43958-69&rft.date=2001&rft_id=info:doi/10.1074/jbc.M106510200&rft_id=info:pmid/11551941&rft.aulast=Koc&rft.aufirst=EC&rft.au=Burkhart,+W&rft.au=Blackburn,+K&rft_id=https://doi.org/10.1074%2Fjbc.M106510200&rfr_id=info:sid/en.wikipedia.org:Mitochondrial+ribosomal+protein+L41" class="Z3988">
* Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903\. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.16899-903&rft.date=2003&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC139241#id-name=PMC&rft_id=info:pmid/12477932&rft_id=info:doi/10.1073/pnas.242603899&rft_id=info:bibcode/2002PNAS...9916899M&rft.aulast=Strausberg&rft.aufirst=RL&rft.au=Feingold,+EA&rft.au=Grouse,+LH&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC139241&rfr_id=info:sid/en.wikipedia.org:Mitochondrial+ribosomal+protein+L41" class="Z3988">
* Zhang Z, Gerstein M (2003). "Identification and characterization of over 100 mitochondrial ribosomal protein pseudogenes in the human genome". Genomics. 81 (5): 468–80\. doi:10.1016/S0888-7543(03)00004-1. PMID 12706105.468-80&rft.date=2003&rft_id=info:doi/10.1016/S0888-7543(03)00004-1&rft_id=info:pmid/12706105&rft.aulast=Zhang&rft.aufirst=Z&rft.au=Gerstein,+M&rfr_id=info:sid/en.wikipedia.org:Mitochondrial+ribosomal+protein+L41" class="Z3988">
* Humphray SJ, Oliver K, Hunt AR, et al. (2004). "DNA sequence and analysis of human chromosome 9". Nature. 429 (6990): 369–74\. Bibcode:2004Natur.429..369H. doi:10.1038/nature02465. PMC 2734081. PMID 15164053.369-74&rft.date=2004&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2734081#id-name=PMC&rft_id=info:pmid/15164053&rft_id=info:doi/10.1038/nature02465&rft_id=info:bibcode/2004Natur.429..369H&rft.aulast=Humphray&rft.aufirst=SJ&rft.au=Oliver,+K&rft.au=Hunt,+AR&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2734081&rfr_id=info:sid/en.wikipedia.org:Mitochondrial+ribosomal+protein+L41" class="Z3988">
* Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7\. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.2121-7&rft.date=2004&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC528928#id-name=PMC&rft_id=info:pmid/15489334&rft_id=info:doi/10.1101/gr.2596504&rft.aulast=Gerhard&rft.aufirst=DS&rft.au=Wagner,+L&rft.au=Feingold,+EA&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC528928&rfr_id=info:sid/en.wikipedia.org:Mitochondrial+ribosomal+protein+L41" class="Z3988">
* Chintharlapalli SR, Jasti M, Malladi S, et al. (2005). "BMRP is a Bcl-2 binding protein that induces apoptosis". J. Cell. Biochem. 94 (3): 611–26\. doi:10.1002/jcb.20292. PMID 15547950. S2CID 23940695.611-26&rft.date=2005&rft_id=https://api.semanticscholar.org/CorpusID:23940695#id-name=S2CID&rft_id=info:pmid/15547950&rft_id=info:doi/10.1002/jcb.20292&rft.aulast=Chintharlapalli&rft.aufirst=SR&rft.au=Jasti,+M&rft.au=Malladi,+S&rfr_id=info:sid/en.wikipedia.org:Mitochondrial+ribosomal+protein+L41" class="Z3988">
* Yoo YA, Kim MJ, Park JK, et al. (2005). "Mitochondrial ribosomal protein L41 suppresses cell growth in association with p53 and p27Kip1". Mol. Cell. Biol. 25 (15): 6603–16\. doi:10.1128/MCB.25.15.6603-6616.2005. PMC 1190350. PMID 16024796.6603-16&rft.date=2005&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1190350#id-name=PMC&rft_id=info:pmid/16024796&rft_id=info:doi/10.1128/MCB.25.15.6603-6616.2005&rft.aulast=Yoo&rft.aufirst=YA&rft.au=Kim,+MJ&rft.au=Park,+JK&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1190350&rfr_id=info:sid/en.wikipedia.org:Mitochondrial+ribosomal+protein+L41" class="Z3988">
* Kim MJ, Yoo YA, Kim HJ, et al. (2006). "Mitochondrial ribosomal protein L41 mediates serum starvation-induced cell-cycle arrest through an increase of p21(WAF1/CIP1)". Biochem. Biophys. Res. Commun. 338 (2): 1179–84\. doi:10.1016/j.bbrc.2005.10.064. PMID 16256947.1179-84&rft.date=2006&rft_id=info:doi/10.1016/j.bbrc.2005.10.064&rft_id=info:pmid/16256947&rft.aulast=Kim&rft.aufirst=MJ&rft.au=Yoo,+YA&rft.au=Kim,+HJ&rfr_id=info:sid/en.wikipedia.org:Mitochondrial+ribosomal+protein+L41" class="Z3988">

* v
* t
* e

Protein biosynthesis: translation (bacterial, archaeal, eukaryotic)

Proteins|

| Initiation factor|

| Bacterial|

* IF1
* IF2
* IF3

|

Mitochondrial|

* MTIF1
* MTIF2
* MTIF3

Archaeal|

* aIF1
* aIF2
* aIF5
* aIF6

Eukaryotic|

| eIF1|

* eIF1
* B
* SUI1 family
* eIF1A
* Y

|

eIF2|

* α
* kinase
* β
* γ
* eIF2A
* eIF2B
* 1
* 2
* 3
* 4
* 5
* eIF2D

eIF3|

* A
* B
* C
* D
* E
* F
* G
* H
* I
* J
* K
* L
* M

eIF4|

* A
* 1
* 2
* 3
* E1
* 2
* 3
* G
* 1
* 2
* 3
* B
* H

eIF5|

* EIF5
* EIF5A
* 2
* 5B

eIF6|

* EIF6

Elongation factor|

| Bacterial/Mitochondrial|

* EF-Tu
* EF-Ts
* EF-G
* EF-4
* EF-P
* TSFM
* GFM1
* GFM2

|

Archaeal/Eukaryotic|

* a/eEF-1
* A1
* 2
* 3
* B
* P1
* P2
* P3
* D
* E
* G
* a/eEF-2

Release factor|

* Class 1
* eRF1
* Class 2/RF3
* GSPT1
* GSPT2

Ribosomal Proteins|

| Cytoplasmic|

| 60S subunit|

* RPL3
* RPL4
* RPL5
* RPL6
* RPL7
* RPL7A
* RPL8
* RPL9
* RPL10
* RPL10A
* RPL10-like
* RPL11
* RPL12
* RPL13
* RPL13A
* RPL14
* RPL15
* RPL17
* RPL18
* RPL18A
* RPL19
* RPL21
* RPL22
* RPL23
* RPL23A
* RPL24
* RPL26
* RPL27
* RPL27A
* RPL28
* RPL29
* RPL30
* RPL31
* RPL32
* RPL34
* RPL35
* RPL35A
* RPL36
* RPL36A
* RPL37
* RPL37A
* RPL38
* RPL39
* RPL40
* RPL41
* RPLP0
* RPLP1
* RPLP2
* RRP15-like
* RSL24D1

|

40S subunit|

* RPSA
* RPS2
* RPS3
* RPS3A
* RPS4 (RPS4X, RPS4Y1, RPS4Y2)
* RPS5
* RPS6
* RPS7
* RPS8
* RPS9
* RPS10
* RPS11
* RPS12
* RPS13
* RPS14
* RPS15
* RPS15A
* RPS16
* RPS17
* RPS18
* RPS19
* RPS20
* RPS21
* RPS23
* RPS24
* RPS25
* RPS26
* RPS27
* RPS27A
* RPS28
* RPS29
* RPS30
* RACK1

Mitochondrial|

| 39S subunit|

* MRPL1
* 2
* 3
* 4
* 5
* 6
* 7
* 8
* 9
* 10
* 11
* 12
* 13
* 14
* 15
* 16
* 17
* 18
* 19
* 20
* 21
* 22
* 23
* 24
* 25
* 26
* 27
* 28
* 29
* 30
* 31
* 32
* 33
* 34
* 35
* 36
* 37
* 38
* 39
* 40
* 41
* 42

|

28S subunit|

* MRPS1
* 2
* 3
* 4
* 5
* 6
* 7
* 8
* 9
* 10
* 11
* 12
* 13
* 14
* 15
* 16
* 17
* 18
* 19
* 20
* 21
* 22
* 23
* 24
* 25
* 26
* 27
* 28
* 29
* 30
* 31
* 32
* 33
* 34
* 35

Other concepts|

* Aminoacyl tRNA synthetase
* Reading frame
* Start codon
* Stop codon
* Shine-Dalgarno sequence/Kozak consensus sequence

* v
* t
* e

Ribosomal RNA / ribosome subunits

Archaea
(70S)|

Large (50S):

* 5S
* 23S

Small (30S):

* 16S

Bacteria
(70S)|

Large (50S):

* 5S
* 23S

Small (30S):

* 16S

Eukaryotes|

| Cytoplasmic (80S)|

Large (60S):

* 5S
* 5.8S
* 28S

Small (40S):

* 18S

|

Mitochondrial (55S)|

Large (28S):

* MT-RNR2, 16S
* MT-tRNAVal

Small (39S):

* MT-RNR1, 12S

Chloroplast (70S)|

Large (50S):

* 5S
* 4.5S
* 23S

Small (30S):

* 16S

Ribosomal proteins|

(See article table)

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