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Protein

39S ribosomal protein L15, mitochondrial

Gene

MRPL15

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

Functioni

GO - Molecular functioni

  • RNA binding Source: UniProtKB
  • structural constituent of ribosome Source: GO_Central

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

HGNCiHGNC:14054. MRPL15.

Subcellular locationi

GO - Cellular componenti

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.

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. 76 interactors.
IntActiQ9P015. 16 interactors.
MINTiMINT-3066248.
STRINGi9606.ENSP00000260102.

Structurei

Secondary structure

1296
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi11 – 15Combined sources5
Turni24 – 26Combined sources3
Turni31 – 33Combined sources3
Turni43 – 45Combined sources3
Turni47 – 50Combined sources4
Turni55 – 59Combined sources5
Helixi74 – 77Combined sources4
Beta strandi83 – 86Combined sources4
Helixi87 – 89Combined sources3
Beta strandi92 – 97Combined sources6
Helixi98 – 107Combined sources10
Beta strandi108 – 110Combined sources3
Helixi118 – 124Combined sources7
Turni131 – 134Combined sources4
Beta strandi135 – 142Combined sources8
Beta strandi153 – 159Combined sources7
Helixi161 – 169Combined sources9
Beta strandi173 – 176Combined sources4
Helixi181 – 188Combined sources8
Helixi190 – 196Combined sources7
Beta strandi208 – 210Combined sources3
Helixi211 – 214Combined sources4
Helixi217 – 219Combined sources3
Helixi229 – 240Combined sources12
Turni247 – 249Combined sources3
Helixi253 – 256Combined sources4
Beta strandi266 – 268Combined sources3
Beta strandi274 – 276Combined sources3
Turni277 – 280Combined sources4
Beta strandi281 – 283Combined sources3
Helixi288 – 295Combined sources8

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[»]
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
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: August 30, 2017
This is version 130 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