CARNMT1
entrez
138199
canonical
uniprot
Q8N4J0
canonical
ensembl
ENSG00000156017
resolver
ensp
ENSP00000366030
resolver
ensp
ENSP00000649925
resolver
enst
ENST00000376834
resolver
genesymbol
CARNMT1
resolver
genesymbol_syn
C9orf41
resolver
hgnc
HGNC:23435
resolver
uniprot
Q7Z383
resolver
uniprot
Q8N7C5
resolver
uniprot_entry
CARME_HUMAN
resolver
uniprot_sec
Q7Z383
resolver
uniprot_sec
Q8N7C5
resolver
amino_acid_sequence
MQRRRRPPPPTSRLPEGCGGGGGGSEEVEVQFSAGRWGSAAAVSAAAAAATRSTEEEEERLEREHFWKIINAFRYYGTSMHERVNRTERQFRSLPANQQKLLPQFLLHLDKIRKCIDHNQEILLTIVNDCIHMFENKEYGEDGNGKIMPASTFDMDKLKSTLKQFVRDWSETGKAERDACYQPIIKEILKNFPKERWDPSKVNILVPGAGLGRLAWEIAMLGYACQGNEWSFFMLFSSNFVLNRCSEINKYKLYPWIHQFSNNRRSADQIRPIFFPDVDPHSLPPGSNFSMTAGDFQEIYSECNTWDCIATCFFIDTAHNVIDYIDTIWKILKPGGIWINLGPLLYHFENLANELSIELSYEDIKNVVLQYGFKVEVEKESVLSTYTVNDLSMMKYYYECVLFVVRKPQ
uniprot
proteins
ec_number
2.1.1.-
uniprot
proteins
ec_number
2.1.1.22
uniprot
proteins
function
FUNCTION: Protein-histidine N-methyltransferase that specifically catalyzes the N1-methylation (pros-methylation) of histidine residues in a wide range of proteins. It primarily monomethylates proteins containing RNA-binding C3H1 zinc finger motifs, such as U2AF1, ZC3H15, ZC3H18, PPP1R10, PRR3 and RNF113A, thereby modulating mRNA splicing and turnover (PubMed:37612136, PubMed:39198440, PubMed:40473212). Additionally, methylates the dipeptide carnosine (beta-alanyl-L-histidine) at the N1 position to generate anserine, an abundant component of vertebrate skeletal muscle. Acts also on other L-histidine-containing di- and tripeptides, such as Gly-Gly-His, Gly-His, and homocarnosine (GABA-His) (PubMed:26001783). {ECO:0000269|PubMed:26001783, ECO:0000269|PubMed:37612136, ECO:0000269|PubMed:39198440, ECO:0000269|PubMed:40473212}.
uniprot
proteins
mass_dalton
47186
uniprot
proteins
mutagenesis
MUTAGEN 229; /note="E->A: Abolishes N-methyltransferase activity."; /evidence="ECO:0000269|PubMed:40473212"; MUTAGEN 313; /note="F->A: Impairs N-methyltransferase activity."; /evidence="ECO:0000269|PubMed:29463897"; MUTAGEN 316; /note="D->A,E,N: Impairs N-methyltransferase activity."; /evidence="ECO:0000269|PubMed:29463897"; MUTAGEN 343; /note="P->A: Impairs N-methyltransferase activity."; /evidence="ECO:0000269|PubMed:29463897"; MUTAGEN 345; /note="L->A: Significantly reduces N-methyltransferase activity."; /evidence="ECO:0000269|PubMed:29463897"; MUTAGEN 347; /note="H->A,F: Impairs binding to S-adenosyl-L-methionine. Significantly reduces N-methyltransferase activity."; /evidence="ECO:0000269|PubMed:29463897"; MUTAGEN 386; /note="Y->A: Impairs N-methyltransferase activity."; /evidence="ECO:0000269|PubMed:29463897"; MUTAGEN 386; /note="Y->F,W: Reduces N-methyltransferase activity."; /evidence="ECO:0000269|PubMed:29463897"; MUTAGEN 396; /note="Y->A: Reduces N-methyltransferase activity."; /evidence="ECO:0000269|PubMed:29463897"; MUTAGEN 396; /note="Y->D: Impairs N-methyltransferase activity."; /evidence="ECO:0000269|PubMed:29463897"; MUTAGEN 398; /note="Y->A,F: Impairs N-methyltransferase activity."; /evidence="ECO:0000269|PubMed:29463897
uniprot
proteins
protein_family
Carnosine N-methyltransferase family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
26001783
uniprot
proteins
pubmed
29463897
uniprot
proteins
pubmed
37612136
uniprot
proteins
pubmed
39198440
uniprot
proteins
pubmed
40473212
uniprot
proteins
sequence_length
409
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:26001783, ECO:0000269|PubMed:40473212}. Nucleus {ECO:0000269|PubMed:26001783, ECO:0000269|PubMed:40473212}.
uniprot
proteins