MVK
entrez
4598
canonical
uniprot
Q03426
canonical
ensembl
ENSG00000110921
resolver
ensp
ENSP00000228510
resolver
ensp
ENSP00000376487
resolver
ensp
ENSP00000438153
resolver
ensp
ENSP00000548364
resolver
ensp
ENSP00000548365
resolver
ensp
ENSP00000548366
resolver
ensp
ENSP00000548368
resolver
ensp
ENSP00000591033
resolver
ensp
ENSP00000635159
resolver
ensp
ENSP00000789099
resolver
enst
ENST00000228510
resolver
enst
ENST00000392727
resolver
enst
ENST00000546277
resolver
enst
ENST00000878305
resolver
enst
ENST00000878306
resolver
enst
ENST00000878307
resolver
enst
ENST00000878309
resolver
enst
ENST00000920974
resolver
enst
ENST00000965100
resolver
genesymbol
MVK
resolver
hgnc
HGNC:7530
resolver
uniprot
A0A0S2Z468
resolver
uniprot
B2RDU6
resolver
uniprot
B7Z1C2
resolver
uniprot
B7Z301
resolver
uniprot
F5H8H2
resolver
uniprot_entry
A0A0S2Z468_HUMAN
resolver
uniprot_entry
B2RDU6_HUMAN
resolver
uniprot_entry
B7Z1C2_HUMAN
resolver
uniprot_entry
B7Z301_HUMAN
resolver
uniprot_entry
F5H8H2_HUMAN
resolver
uniprot_entry
KIME_HUMAN
resolver
activity_regulation
ACTIVITY REGULATION: Farnesyl pyrophosphate and geranyl pyrophosphate inhibit mevalonate kinase activity by binding competitively at the ATP-binding sites. {ECO:0000269|PubMed:18302342, ECO:0000269|PubMed:9392419}.
uniprot
proteins
amino_acid_sequence
MLSEVLLVSAPGKVILHGEHAVVHGKVALAVSLNLRTFLRLQPHSNGKVDLSLPNIGIKRAWDVARLQSLDTSFLEQGDVTTPTSEQVEKLKEVAGLPDDCAVTERLAVLAFLYLYLSICRKQRALPSLDIVVWSELPPGAGLGSSAAYSVCLAAALLTVCEEIPNPLKDGDCVNRWTKEDLELINKWAFQGERMIHGNPSGVDNAVSTWGGALRYHQGKISSLKRSPALQILLTNTKVPRNTRALVAGVRNRLLKFPEIVAPLLTSIDAISLECERVLGEMGEAPAPEQYLVLEELIDMNQHHLNALGVGHASLDQLCQVTRARGLHSKLTGAGGGGCGITLLKPGLEQPEVEATKQALTSCGFDCLETSIGAPGVSIHSATSLDSRVQQALDGL
uniprot
proteins
disease_involvement
DISEASE: Mevalonic aciduria (MEVA) [MIM:610377]: Accumulation of mevalonic acid which causes a variety of symptoms such as psychomotor retardation, dysmorphic features, cataracts, hepatosplenomegaly, lymphadenopathy, anemia, hypotonia, myopathy, and ataxia. {ECO:0000269|PubMed:10401001, ECO:0000269|PubMed:10417275, ECO:0000269|PubMed:11313768, ECO:0000269|PubMed:11313769, ECO:0000269|PubMed:1377680}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Hyperimmunoglobulinemia D and periodic fever syndrome (HIDS) [MIM:260920]: Autosomal recessive disease characterized by recurrent episodes of unexplained high fever associated with skin rash, diarrhea, adenopathy (swollen, tender lymph nodes), arthralgias and/or arthritis. Concentration of IgD, and often IgA, are above normal. {ECO:0000269|PubMed:10369261, ECO:0000269|PubMed:10369262, ECO:0000269|PubMed:11313768, ECO:0000269|PubMed:11313769, ECO:0000269|PubMed:15536479}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Porokeratosis 3, multiple types (POROK3) [MIM:175900]: A form of porokeratosis, a disorder of faulty keratinization characterized by one or more atrophic patches surrounded by a distinctive hyperkeratotic ridgelike border called the cornoid lamella. The keratotic lesions can progress to overt cutaneous neoplasms, typically squamous cell carcinomas. Multiple clinical variants of porokeratosis are recognized, including porokeratosis of Mibelli, linear porokeratosis, disseminated superficial actinic porokeratosis, palmoplantar porokeratosis, and punctate porokeratosis. Different clinical presentations can be observed among members of the same family. Individuals expressing more than one variant have also been reported. {ECO:0000269|PubMed:22983302, ECO:0000269|PubMed:24781643}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.1.36
uniprot
proteins
function
FUNCTION: Catalyzes the phosphorylation of mevalonate to mevalonate 5-phosphate, a key step in isoprenoid and cholesterol biosynthesis (PubMed:11278915, PubMed:18302342, PubMed:9325256, PubMed:9392419). {ECO:0000269|PubMed:11278915, ECO:0000269|PubMed:18302342, ECO:0000269|PubMed:9325256, ECO:0000269|PubMed:9392419}.
uniprot
proteins
mass_dalton
42451
uniprot
proteins
mutagenesis
MUTAGEN 19; /note="E->D: No change in protein stability. Weak decrease in kinase activity. Approximately 2-fold decrease in Vmax. Approximately 2-fold decrease affinity for ATP and mevalonate."; /evidence="ECO:0000269|PubMed:9325256"; MUTAGEN 56; /note="I->A: No effect on kinase activity. Approximately 4- and 5-fold decrease affinities for ATP and mevalonate, respectively."; /evidence="ECO:0000269|PubMed:18302342"; MUTAGEN 104; /note="T->A: No effect on kinase activity. Approximately 4-fold increase affinity for ATP. Normal affinity for mevalonate."; /evidence="ECO:0000269|PubMed:18302342"; MUTAGEN 145; /note="S->A: Modest changes in KM for ATP. 20-fold increase in KM for mevalonate. Approximately 2-fold decrease in Vmax."; /evidence="ECO:0000269|PubMed:11278915"; MUTAGEN 146; /note="S->A: Modest changes in KM for ATP. 20-fold increase in KM for mevalonate. 4000-fold decrease in Vmax."; /evidence="ECO:0000269|PubMed:11278915"; MUTAGEN 149; /note="Y->A: No effect on kinase activity. Approximately 4- and 8-fold decrease affinities for ATP and mevalonate, respectively."; /evidence="ECO:0000269|PubMed:18302342"; MUTAGEN 193; /note="E->Q: No change in protein stability. Decreased kinase activity. Approximately 50-fold decrease in Vmax. Approximately 20- and 40-fold decrease affinities for ATP and mevalonate, respectively."; /evidence="ECO:0000269|PubMed:9325256"; MUTAGEN 196; /note="I->A: No effect on kinase activity. Approximately 2- and 3-fold decrease affinities for ATP and mevalonate, respectively."; /evidence="ECO:0000269|PubMed:18302342"; MUTAGEN 201; /note="S->A: Modest changes in KM for ATP. 100-fold increase in KM for mevalonate. Approximately 2-fold increase in Vmax."; /evidence="ECO:0000269|PubMed:11278915"; MUTAGEN 204; /note="D->A: No change in protein stability. Loss of kinase activity. Normal affinities for ATP and mevalonate."; /evidence="ECO:0000269|PubMed:9325256"; MUTAGEN 204; /note="D->N: No change in protein stability. Loss of kinase activity. Normal affinities for ATP and mevalonate."; /evidence="ECO:0000269|PubMed:9325256"; MUTAGEN 243; /note="T->A: Modest changes in KM for ATP. 40-fold increase in KM for mevalonate. Approximately 2-fold decrease in Vmax."; /evidence="ECO:0000269|PubMed:11278915"; MUTAGEN 296; /note="E->Q: No change in protein stability. No effect on kinase activity."; /evidence="ECO:0000269|PubMed:9325256
uniprot
proteins
pathway_participation
PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 1/3. {ECO:0000305}.
uniprot
proteins
protein_family
GHMP kinase family
uniprot
proteins
protein_family
Mevalonate kinase subfamily
uniprot
proteins
pubmed
10369261
uniprot
proteins
pubmed
10369262
uniprot
proteins
pubmed
10401001
uniprot
proteins
pubmed
10417275
uniprot
proteins
pubmed
11278915
uniprot
proteins
pubmed
11313768
uniprot
proteins
pubmed
11313769
uniprot
proteins
pubmed
1377680
uniprot
proteins
pubmed
14730012
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15536479
uniprot
proteins
pubmed
18302342
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22983302
uniprot
proteins
pubmed
24781643
uniprot
proteins
pubmed
8302606
uniprot
proteins
pubmed
9325256
uniprot
proteins
pubmed
9392419
uniprot
proteins
sequence_length
396
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14730012}. Peroxisome {ECO:0000250|UniProtKB:P17256}.
uniprot
proteins