Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

39S ribosomal protein L15, mitochondrial

Gene

MRPL15

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

Functioni

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiR-HSA-5368286 Mitochondrial translation initiation
R-HSA-5389840 Mitochondrial translation elongation
R-HSA-5419276 Mitochondrial translation termination

Names & Taxonomyi

Protein namesi
Recommended name:
39S ribosomal protein L15, mitochondrial
Short name:
L15mt
Short name:
MRP-L15
Alternative name(s):
Mitochondrial large ribosomal subunit protein uL15m1 Publication
Gene namesi
Name:MRPL15
ORF Names:HSPC145
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

EuPathDBiHostDB:ENSG00000137547.8
HGNCiHGNC:14054 MRPL15
MIMi611828 gene
neXtProtiNX_Q9P015

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

OpenTargetsiENSG00000137547
PharmGKBiPA30944

Polymorphism and mutation databases

BioMutaiMRPL15
DMDMi74734761

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 21MitochondrionBy similarityAdd BLAST21
ChainiPRO_000025783822 – 29639S ribosomal protein L15, mitochondrialAdd BLAST275

Proteomic databases

EPDiQ9P015
MaxQBiQ9P015
PaxDbiQ9P015
PeptideAtlasiQ9P015
PRIDEiQ9P015
ProteomicsDBi83533

PTM databases

iPTMnetiQ9P015
PhosphoSitePlusiQ9P015
SwissPalmiQ9P015

Expressioni

Gene expression databases

BgeeiENSG00000137547
CleanExiHS_MRPL15
ExpressionAtlasiQ9P015 baseline and differential
GenevisibleiQ9P015 HS

Organism-specific databases

HPAiHPA044425

Interactioni

Subunit structurei

Component of the mitochondrial large ribosomal subunit (mt-LSU). Mature mammalian 55S mitochondrial ribosomes consist of a small (28S) and a large (39S) subunit. The 28S small subunit contains a 12S ribosomal RNA (12S mt-rRNA) and 30 different proteins. The 39S large subunit contains a 16S rRNA (16S mt-rRNA), a copy of mitochondrial valine transfer RNA (mt-tRNA(Val)), which plays an integral structural role, and 52 different proteins.2 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi118857, 77 interactors
CORUMiQ9P015
IntActiQ9P015, 21 interactors
MINTiQ9P015
STRINGi9606.ENSP00000260102

Structurei

Secondary structure

1296
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi12 – 18Combined sources7
Turni24 – 26Combined sources3
Turni31 – 33Combined sources3
Beta strandi42 – 45Combined sources4
Turni47 – 50Combined sources4
Beta strandi53 – 56Combined sources4
Turni57 – 60Combined sources4
Turni74 – 76Combined sources3
Turni85 – 89Combined sources5
Beta strandi92 – 97Combined sources6
Helixi98 – 106Combined sources9
Beta strandi108 – 110Combined sources3
Helixi118 – 123Combined sources6
Turni131 – 134Combined sources4
Beta strandi135 – 141Combined sources7
Beta strandi153 – 155Combined sources3
Beta strandi157 – 159Combined sources3
Helixi161 – 169Combined sources9
Beta strandi173 – 176Combined sources4
Helixi181 – 188Combined sources8
Turni191 – 195Combined sources5
Turni208 – 210Combined sources3
Helixi211 – 214Combined sources4
Turni217 – 220Combined sources4
Beta strandi226 – 228Combined sources3
Helixi229 – 239Combined sources11
Turni247 – 249Combined sources3
Turni251 – 257Combined sources7
Beta strandi266 – 268Combined sources3
Beta strandi274 – 276Combined sources3
Turni277 – 280Combined sources4
Beta strandi281 – 285Combined sources5
Helixi288 – 294Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J7Yelectron microscopy3.40M1-296[»]
3J9Melectron microscopy3.50M1-296[»]
5OOLelectron microscopy3.06M1-296[»]
5OOMelectron microscopy3.03M1-296[»]
ProteinModelPortaliQ9P015
SMRiQ9P015
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi38 – 64Arg-richAdd BLAST27

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0846 Eukaryota
COG0200 LUCA
GeneTreeiENSGT00390000009040
HOGENOMiHOG000231264
HOVERGENiHBG088294
InParanoidiQ9P015
KOiK02876
OMAiYEPYYKG
OrthoDBiEOG091G0VT9
PhylomeDBiQ9P015
TreeFamiTF105918

Family and domain databases

HAMAPiMF_01341 Ribosomal_L15, 1 hit
InterProiView protein in InterPro
IPR036227 L18e/L15P_sf
IPR030878 Ribosomal_L15
IPR005749 Ribosomal_L15_bac-type
IPR021131 Ribosomal_L18e/L15P
PANTHERiPTHR12934 PTHR12934, 1 hit
PfamiView protein in Pfam
PF00828 Ribosomal_L27A, 1 hit
SUPFAMiSSF52080 SSF52080, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q9P015-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGPLQGGGA RALDLLRGLP RVSLANLKPN PGSKKPERRP RGRRRGRKCG
60 70 80 90 100
RGHKGERQRG TRPRLGFEGG QTPFYIRIPK YGFNEGHSFR RQYKPLSLNR
110 120 130 140 150
LQYLIDLGRV DPSQPIDLTQ LVNGRGVTIQ PLKRDYGVQL VEEGADTFTA
160 170 180 190 200
KVNIEVQLAS ELAIAAIEKN GGVVTTAFYD PRSLDIVCKP VPFFLRGQPI
210 220 230 240 250
PKRMLPPEEL VPYYTDAKNR GYLADPAKFP EARLELARKY GYILPDITKD
260 270 280 290
ELFKMLCTRK DPRQIFFGLA PGWVVNMADK KILKPTDENL LKYYTS
Length:296
Mass (Da):33,420
Last modified:October 1, 2000 - v1
Checksum:iD7396086F808A72C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti96L → M in CAB66600 (PubMed:11230166).Curated1
Sequence conflicti96L → M in CAG38562 (Ref. 3) Curated1
Sequence conflicti137G → D in CAB66600 (PubMed:11230166).Curated1
Sequence conflicti137G → D in CAG38562 (Ref. 3) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF161494 mRNA Translation: AAF29109.1
AL136665 mRNA Translation: CAB66600.1
CR533531 mRNA Translation: CAG38562.1
BC000891 mRNA Translation: AAH00891.1
AB051619 Genomic DNA Translation: BAB54947.1
CCDSiCCDS6158.1
RefSeqiNP_054894.1, NM_014175.3
UniGeneiHs.18349

Genome annotation databases

EnsembliENST00000260102; ENSP00000260102; ENSG00000137547
GeneIDi29088
KEGGihsa:29088
UCSCiuc003xsa.3 human

Similar proteinsi

Entry informationi

Entry nameiRM15_HUMAN
AccessioniPrimary (citable) accession number: Q9P015
Secondary accession number(s): Q96Q54, Q9H0Y1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 1, 2000
Last modified: June 20, 2018
This is version 136 of the entry and version 1 of the sequence. See 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 8
    Human chromosome 8: 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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health