MRPL12
entrez
6182
canonical
uniprot
P52815
canonical
ensembl
ENSG00000262814
resolver
ensp
ENSP00000333837
resolver
enst
ENST00000333676
resolver
genesymbol
MRPL12
resolver
genesymbol_syn
MRPL7
resolver
genesymbol_syn
RPML12
resolver
hgnc
HGNC:10378
resolver
uniprot
Q969U0
resolver
uniprot
Q9HCA2
resolver
uniprot
Q9UQJ3
resolver
uniprot_entry
RM12_HUMAN
resolver
uniprot_sec
Q969U0
resolver
uniprot_sec
Q9HCA2
resolver
uniprot_sec
Q9UQJ3
resolver
amino_acid_sequence
MLPAAARPLWGPCLGLRAAAFRLARRQVPCVCAVRHMRSSGHQRCEALAGAPLDNAPKEYPPKIQQLVQDIASLTLLEISDLNELLKKTLKIQDVGLVPMGGVMSGAVPAAAAQEAVEEDIPIAKERTHFTVRLTEAKPVDKVKLIKEIKNYIQGINLVQAKKLVESLPQEIKANVAKAEAEKIKAALEAVGGTVVLE
uniprot
proteins
disease_involvement
DISEASE: Combined oxidative phosphorylation deficiency 45 (COXPD45) [MIM:618951]: An autosomal recessive mitochondrial disorder with onset in utero and characterized by poor overall growth, failure to thrive, global developmental delay, poor or absent speech, seizures, hypotonia, loss of walking, acute progressive neurologic deterioration, brain lesions, and facial dysmorphism. Laboratory studies show increased serum lactate and decreased mitochondrial respiratory chain enzyme activity in patient tissues. {ECO:0000269|PubMed:23603806}. Note=The disease may be caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: As a component of the mitochondrial large ribosomal subunit, plays a role in mitochondrial translation (PubMed:23603806). When present in mitochondria as a free protein not associated with the ribosome, associates with mitochondrial RNA polymerase POLRMT to activate transcription (PubMed:22003127). Required for POLRMT stability (PubMed:26586915). {ECO:0000269|PubMed:22003127, ECO:0000269|PubMed:23603806, ECO:0000269|PubMed:26586915}.
uniprot
proteins
mass_dalton
21348
uniprot
proteins
mutagenesis
MUTAGEN 138; /note="K->Q,R: No effect on promoter binding activity of POLRMT."; /evidence="ECO:0000269|PubMed:38146092"; MUTAGEN 142; /note="K->Q,R: No effect on promoter binding activity of POLRMT."; /evidence="ECO:0000269|PubMed:38146092"; MUTAGEN 144; /note="K->Q,R: No effect on promoter binding activity of POLRMT."; /evidence="ECO:0000269|PubMed:38146092"; MUTAGEN 144; /note="K->R: No effect on ubiquitination."; /evidence="ECO:0000269|PubMed:37526061"; MUTAGEN 147; /note="K->R: No effect on ubiquitination."; /evidence="ECO:0000269|PubMed:37526061"; MUTAGEN 150; /note="K->R: Reduced ubiquitination."; /evidence="ECO:0000269|PubMed:37526061"; MUTAGEN 163; /note="K->Q,R: No effect on promoter binding activity of POLRMT."; /evidence="ECO:0000269|PubMed:38146092"; MUTAGEN 173; /note="K->Q: No effect on promoter binding activity of POLRMT."; /evidence="ECO:0000269|PubMed:38146092"; MUTAGEN 173; /note="K->R: Reduced promoter binding activity of POLRMT."; /evidence="ECO:0000269|PubMed:38146092
uniprot
proteins
post_translational_modification
PTM: Two mature forms are produced by differential two-step proteolytic cleavage (PubMed:26586915). Cleaved by the mitochondrial processing protease to produce the long mature form and subsequently by the mitochondrial intermediate protease to produce the short mature form (PubMed:26586915). {ECO:0000269|PubMed:26586915}.; PTM: In the presence of CUL3, undergoes 'Lys-63'-linked ubiquitination at Lys-150 which results in proteasomal degradation. {ECO:0000269|PubMed:37526061}.
uniprot
proteins
protein_family
Bacterial ribosomal protein bL12 family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19103604
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22003127
uniprot
proteins
pubmed
23603806
uniprot
proteins
pubmed
25278503
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26586915
uniprot
proteins
pubmed
27184847
uniprot
proteins
pubmed
37526061
uniprot
proteins
pubmed
38146092
uniprot
proteins
pubmed
8626705
uniprot
proteins
sequence_length
198
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:27184847, ECO:0000269|PubMed:8626705}.
uniprot
proteins