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Protein

39S ribosomal protein L12, mitochondrial

Gene

MRPL12

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

Functioni

GO - Molecular functioni

  • RNA binding Source: ProtInc
  • structural constituent of ribosome Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciZFISH:G66-30949-MONOMER.
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 L12, mitochondrial
Short name:
L12mt
Short name:
MRP-L12
Alternative name(s):
5c5-2
Gene namesi
Name:MRPL12
Synonyms:RPML12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:10378. MRPL12.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: Reactome
  • mitochondrial large ribosomal subunit Source: UniProtKB
  • mitochondrion Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

OpenTargetsiENSG00000262814.
PharmGKBiPA30941.

Polymorphism and mutation databases

BioMutaiMRPL12.
DMDMi20981709.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 45MitochondrionSequence analysisAdd BLAST45
ChainiPRO_000003045846 – 19839S ribosomal protein L12, mitochondrialAdd BLAST153

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei138N6-acetyllysineBy similarity1
Modified residuei150N6-succinyllysineBy similarity1
Modified residuei162N6-succinyllysineBy similarity1
Modified residuei178N6-succinyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP52815.
MaxQBiP52815.
PaxDbiP52815.
PeptideAtlasiP52815.
PRIDEiP52815.
TopDownProteomicsiP52815.

2D gel databases

DOSAC-COBS-2DPAGEP52815.
SWISS-2DPAGEP52815.

PTM databases

iPTMnetiP52815.
PhosphoSitePlusiP52815.
SwissPalmiP52815.

Expressioni

Gene expression databases

BgeeiENSG00000262814.
CleanExiHS_MRPL12.
GenevisibleiP52815. HS.

Organism-specific databases

HPAiHPA022853.
HPA023043.

Interactioni

Subunit structurei

Interacts with NOA1.1 Publication

Protein-protein interaction databases

BioGridi112097. 150 interactors.
DIPiDIP-50865N.
IntActiP52815. 17 interactors.
MINTiMINT-1150069.
STRINGi9606.ENSP00000333837.

Structurei

3D structure databases

ProteinModelPortaliP52815.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L7/L12P family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1715. Eukaryota.
COG0222. LUCA.
GeneTreeiENSGT00390000000190.
HOGENOMiHOG000248814.
HOVERGENiHBG001832.
InParanoidiP52815.
KOiK02935.
OrthoDBiEOG091G0BQ7.
PhylomeDBiP52815.
TreeFamiTF105997.

Family and domain databases

CDDicd00387. Ribosomal_L7_L12. 1 hit.
Gene3Di3.30.1390.10. 1 hit.
HAMAPiMF_00368. Ribosomal_L7_L12. 1 hit.
InterProiIPR000206. Ribosomal_L7/12.
IPR014719. Ribosomal_L7/12_C/ClpS-like.
IPR013823. Ribosomal_L7/L12_C.
IPR008932. Ribosomal_L7/L12_oligo.
[Graphical view]
PfamiPF00542. Ribosomal_L12. 1 hit.
PF16320. Ribosomal_L12_N. 1 hit.
[Graphical view]
ProDomiPD001326. Ribosomal_L7/L12_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF48300. SSF48300. 1 hit.
SSF54736. SSF54736. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P52815-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPAAARPLW GPCLGLRAAA FRLARRQVPC VCAVRHMRSS GHQRCEALAG
60 70 80 90 100
APLDNAPKEY PPKIQQLVQD IASLTLLEIS DLNELLKKTL KIQDVGLVPM
110 120 130 140 150
GGVMSGAVPA AAAQEAVEED IPIAKERTHF TVRLTEAKPV DKVKLIKEIK
160 170 180 190
NYIQGINLVQ AKKLVESLPQ EIKANVAKAE AEKIKAALEA VGGTVVLE
Length:198
Mass (Da):21,348
Last modified:May 15, 2002 - v2
Checksum:i7F26BEDE9218CEF0
GO

Sequence cautioni

The sequence AAD16894 differs from that shown. Reason: Frameshift at several positions.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti33A → T in CAA56249 (PubMed:8626705).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_052001105S → P.Corresponds to variant rs11546280dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79865 mRNA. Translation: CAA56249.1.
AF059736 Genomic DNA. Translation: AAG32154.1.
BC002344 mRNA. Translation: AAH02344.1.
BC007497 mRNA. Translation: AAH07497.1.
AF105278 mRNA. Translation: AAD16894.1. Frameshift.
CCDSiCCDS11785.1.
RefSeqiNP_002940.2. NM_002949.3.
UniGeneiHs.109059.

Genome annotation databases

EnsembliENST00000333676; ENSP00000333837; ENSG00000262814.
GeneIDi6182.
KEGGihsa:6182.
UCSCiuc002kbh.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79865 mRNA. Translation: CAA56249.1.
AF059736 Genomic DNA. Translation: AAG32154.1.
BC002344 mRNA. Translation: AAH02344.1.
BC007497 mRNA. Translation: AAH07497.1.
AF105278 mRNA. Translation: AAD16894.1. Frameshift.
CCDSiCCDS11785.1.
RefSeqiNP_002940.2. NM_002949.3.
UniGeneiHs.109059.

3D structure databases

ProteinModelPortaliP52815.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112097. 150 interactors.
DIPiDIP-50865N.
IntActiP52815. 17 interactors.
MINTiMINT-1150069.
STRINGi9606.ENSP00000333837.

PTM databases

iPTMnetiP52815.
PhosphoSitePlusiP52815.
SwissPalmiP52815.

Polymorphism and mutation databases

BioMutaiMRPL12.
DMDMi20981709.

2D gel databases

DOSAC-COBS-2DPAGEP52815.
SWISS-2DPAGEP52815.

Proteomic databases

EPDiP52815.
MaxQBiP52815.
PaxDbiP52815.
PeptideAtlasiP52815.
PRIDEiP52815.
TopDownProteomicsiP52815.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000333676; ENSP00000333837; ENSG00000262814.
GeneIDi6182.
KEGGihsa:6182.
UCSCiuc002kbh.3. human.

Organism-specific databases

CTDi6182.
GeneCardsiMRPL12.
HGNCiHGNC:10378. MRPL12.
HPAiHPA022853.
HPA023043.
MIMi602375. gene.
neXtProtiNX_P52815.
OpenTargetsiENSG00000262814.
PharmGKBiPA30941.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1715. Eukaryota.
COG0222. LUCA.
GeneTreeiENSGT00390000000190.
HOGENOMiHOG000248814.
HOVERGENiHBG001832.
InParanoidiP52815.
KOiK02935.
OrthoDBiEOG091G0BQ7.
PhylomeDBiP52815.
TreeFamiTF105997.

Enzyme and pathway databases

BioCyciZFISH:G66-30949-MONOMER.
ReactomeiR-HSA-5368286. Mitochondrial translation initiation.
R-HSA-5389840. Mitochondrial translation elongation.
R-HSA-5419276. Mitochondrial translation termination.

Miscellaneous databases

ChiTaRSiMRPL12. human.
GeneWikiiMRPL12.
GenomeRNAii6182.
PROiP52815.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000262814.
CleanExiHS_MRPL12.
GenevisibleiP52815. HS.

Family and domain databases

CDDicd00387. Ribosomal_L7_L12. 1 hit.
Gene3Di3.30.1390.10. 1 hit.
HAMAPiMF_00368. Ribosomal_L7_L12. 1 hit.
InterProiIPR000206. Ribosomal_L7/12.
IPR014719. Ribosomal_L7/12_C/ClpS-like.
IPR013823. Ribosomal_L7/L12_C.
IPR008932. Ribosomal_L7/L12_oligo.
[Graphical view]
PfamiPF00542. Ribosomal_L12. 1 hit.
PF16320. Ribosomal_L12_N. 1 hit.
[Graphical view]
ProDomiPD001326. Ribosomal_L7/L12_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF48300. SSF48300. 1 hit.
SSF54736. SSF54736. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRM12_HUMAN
AccessioniPrimary (citable) accession number: P52815
Secondary accession number(s): Q969U0, Q9HCA2, Q9UQJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 15, 2002
Last modified: November 30, 2016
This is version 163 of the entry and version 2 of the sequence. [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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Ribosomal proteins
    Ribosomal proteins families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.