MVD

Functionⁱ

Performs the first committed step in the biosynthesis of isoprenes.

Catalytic activityⁱ

ATP + (R)-5-diphosphomevalonate = ADP + phosphate + isopentenyl diphosphate + CO₂.1 Publication

Kineticsⁱ

K_M=
7.4 µM for (R)-5-diphosphomevalonate
1 Publication
Manual assertion based on experiment inⁱ
- Ref.5
  "Post-translational regulation of mevalonate kinase by intermediates of the cholesterol and nonsterol isoprene biosynthetic pathways."
  Hinson D.D., Chambliss K.L., Toth M.J., Tanaka R.D., Gibson K.M.
  J. Lipid Res. 38:2216-2223(1997) [PubMed] [Europe PMC] [Abstract]
  Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
K_M=
0.32 mM for ATP
1 Publication
Manual assertion based on experiment inⁱ
- Ref.5
  "Post-translational regulation of mevalonate kinase by intermediates of the cholesterol and nonsterol isoprene biosynthetic pathways."
  Hinson D.D., Chambliss K.L., Toth M.J., Tanaka R.D., Gibson K.M.
  J. Lipid Res. 38:2216-2223(1997) [PubMed] [Europe PMC] [Abstract]
  Cited for: BIOPHYSICOCHEMICAL PROPERTIES.

Pathwayⁱ: cholesterol biosynthesis

This protein is involved in the pathway cholesterol biosynthesis, which is part of Steroid biosynthesis.
View all proteins of this organism that are known to be involved in the pathway cholesterol biosynthesis and in Steroid biosynthesis.

GO - Molecular functionⁱ

ATP binding Source: UniProtKB-KW
diphosphomevalonate decarboxylase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 11792727
- 14680974
Hsp70 protein binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 12646231
protein homodimerization activity
Source: UniProtKB
Inferred from direct assayⁱ
- 8626466

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cholesterol biosynthetic process Source: Reactome
dolichyl diphosphate biosynthetic process Source: Reactome
isopentenyl diphosphate biosynthetic process, mevalonate pathway
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
isoprenoid biosynthetic process
Source: UniProtKB
Inferred from direct assayⁱ
- 11792727
- 14680974
positive regulation of cell proliferation
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 9270019
regulation of cholesterol biosynthetic process Source: Reactome

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Lyase
Biological process	Cholesterol biosynthesis, Cholesterol metabolism, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism
Ligand	ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCycⁱ	MetaCyc:ENSG00000167508-MONOMER
BRENDAⁱ	4.1.1.33 2681
Reactomeⁱ	R-HSA-191273 Cholesterol biosynthesis R-HSA-2426168 Activation of gene expression by SREBF (SREBP) R-HSA-446199 Synthesis of Dolichyl-phosphate
SABIO-RKⁱ	P53602
UniPathwayⁱ	UPA00063

Chemistry databases

SwissLipidsⁱ	SLP:000001242

SwissLipidsⁱ

SLP:000001242

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Diphosphomevalonate decarboxylase (EC:4.1.1.33) Alternative name(s): Mevalonate (diphospho)decarboxylase Short name: MDDase Mevalonate pyrophosphate decarboxylase
Gene namesⁱ	Name:MVD Synonyms:MPD
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 16

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000167508.10
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:7529 MVD
MIMⁱ	603236 gene
neXtProtⁱ	NX_P53602

Subcellular locationⁱ

GO - Cellular component

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Porokeratosis 7, multiple types (POROK7)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	17	N → A: 15-fold inflation in K(m) for mevalonate diphosphate. 1 Publication		1

Keywords - Diseaseⁱ

Disease mutation

Organism-specific databases

DisGeNET More...DisGeNETⁱ	4597
MalaCards human disease database More...MalaCardsⁱ	MVD
MIMⁱ	614714 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000167508
Orphanetⁱ	79152 Disseminated superficial actinic porokeratosis
PharmGKBⁱ	PA31330

Chemistry databases

ChEMBLⁱ	CHEMBL4340
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	642

Polymorphism and mutation databases

BioMutaⁱ	MVD
DMDMⁱ	1706681

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		RemovedCombined sources
ChainⁱPRO_0000087012	2 – 400	Diphosphomevalonate decarboxylaseAdd BLAST		399

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	2	N-acetylalanineCombined sources		1
Modified residueⁱ	96	PhosphoserineCombined sources		1

Keywords - PTMⁱ

Acetylation, Phosphoprotein

Proteomic databases

EPDⁱ	P53602
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P53602
PaxDbⁱ	P53602
PeptideAtlas More...PeptideAtlasⁱ	P53602
PRIDEⁱ	P53602
ProteomicsDBⁱ	56588

PTM databases

iPTMnetⁱ	P53602
PhosphoSitePlusⁱ	P53602

Expressionⁱ

Tissue specificityⁱ

Expressed in heart, skeletal muscle, lung, liver, brain, pancreas, kidney and placenta.1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000167508 Expressed in 130 organ(s), highest expression level in right adrenal gland cortex
CleanExⁱ	HS_MVD
ExpressionAtlasⁱ	P53602 baseline and differential
Genevisibleⁱ	P53602 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA041404 HPA048250

HPAⁱ

HPA041404
HPA048250

Interactionⁱ

Subunit structureⁱ

Homodimer.1 Publication

GO - Molecular functionⁱ

Hsp70 protein binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 12646231
protein homodimerization activity
Source: UniProtKB
Inferred from direct assayⁱ
- 8626466

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	110682, 37 interactors
IntActⁱ	P53602, 9 interactors
STRINGⁱ	9606.ENSP00000301012

Chemistry databases

BindingDBⁱ

P53602

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	10 – 14	Combined sources	5
Beta strandⁱ	17 – 21	Combined sources	5
Beta strandⁱ	26 – 28	Combined sources	3
Turnⁱ	29 – 32	Combined sources	4
Beta strandⁱ	33 – 36	Combined sources	4
Beta strandⁱ	38 – 43	Combined sources	6
Turnⁱ	45 – 47	Combined sources	3
Beta strandⁱ	50 – 56	Combined sources	7
Beta strandⁱ	64 – 67	Combined sources	4
Helixⁱ	77 – 88	Combined sources	12
Beta strandⁱ	110 – 118	Combined sources	9
Turnⁱ	120 – 122	Combined sources	3
Helixⁱ	126 – 139	Combined sources	14
Turnⁱ	140 – 143	Combined sources	4
Helixⁱ	149 – 155	Combined sources	7
Helixⁱ	157 – 163	Combined sources	7
Beta strandⁱ	164 – 170	Combined sources	7
Beta strandⁱ	178 – 180	Combined sources	3
Beta strandⁱ	183 – 187	Combined sources	5
Helixⁱ	189 – 191	Combined sources	3
Beta strandⁱ	195 – 202	Combined sources	8
Helixⁱ	211 – 221	Combined sources	11
Helixⁱ	223 – 231	Combined sources	9
Helixⁱ	233 – 245	Combined sources	13
Helixⁱ	249 – 268	Combined sources	20
Beta strandⁱ	270 – 272	Combined sources	3
Helixⁱ	279 – 295	Combined sources	17
Beta strandⁱ	300 – 303	Combined sources	4
Beta strandⁱ	306 – 308	Combined sources	3
Beta strandⁱ	310 – 315	Combined sources	6
Helixⁱ	316 – 318	Combined sources	3
Helixⁱ	319 – 329	Combined sources	11
Turnⁱ	337 – 339	Combined sources	3
Beta strandⁱ	340 – 343	Combined sources	4
Helixⁱ	352 – 358	Combined sources	7
Beta strandⁱ	366 – 375	Combined sources	10
Helixⁱ	385 – 387	Combined sources	3
Beta strandⁱ	392 – 394	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	P53602
SMRⁱ	P53602
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P53602

EvolutionaryTraceⁱ

P53602

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the diphosphomevalonate decarboxylase family.Curated

Phylogenomic databases

eggNOGⁱ	KOG2833 Eukaryota COG3407 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000015359
HOVERGENⁱ	HBG051503
InParanoidⁱ	P53602
KEGG Orthology (KO) More...KOⁱ	K01597
OMAⁱ	LTLHAMM
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0EUU
PhylomeDBⁱ	P53602
TreeFamⁱ	TF105952

Family and domain databases

Gene3Dⁱ	3.30.230.10, 1 hit 3.30.70.890, 1 hit
InterProⁱ	View protein in InterPro IPR036554 GHMP_kinase_C_sf IPR006204 GHMP_kinase_N_dom IPR005935 Mev_decarb IPR029765 Mev_diP_decarb IPR020568 Ribosomal_S5_D2-typ_fold IPR014721 Ribosomal_S5_D2-typ_fold_subgr
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00288 GHMP_kinases_N, 1 hit
PIRSFⁱ	PIRSF015950 Mev_P_decrbx, 1 hit
SUPFAMⁱ	SSF54211 SSF54211, 1 hit SSF55060 SSF55060, 1 hit
TIGRFAMsⁱ	TIGR01240 mevDPdecarb, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

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

This entry has 1 described isoform and 4 potential isoforms that are computationally mapped.Show all Align All

P53602-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MASEKPLAAV TCTAPVNIAV IKYWGKRDEE LVLPINSSLS VTLHQDQLKT 
        60         70         80         90        100
TTTAVISKDF TEDRIWLNGR EEDVGQPRLQ ACLREIRCLA RKRRNSRDGD 
       110        120        130        140        150
PLPSSLSCKV HVASVNNFPT AAGLASSAAG YACLAYTLAR VYGVESDLSE 
       160        170        180        190        200
VARRGSGSAC RSLYGGFVEW QMGEQADGKD SIARQVAPES HWPELRVLIL 
       210        220        230        240        250
VVSAEKKLTG STVGMRASVE TSPLLRFRAE SVVPARMAEM ARCIRERDFP 
       260        270        280        290        300
SFAQLTMKDS NQFHATCLDT FPPISYLNAI SWRIIHLVHR FNAHHGDTKV 
       310        320        330        340        350
AYTFDAGPNA VIFTLDDTVA EFVAAVWHGF PPGSNGDTFL KGLQVRPAPL 
       360        370        380        390        400
SAELQAALAM EPTPGGVKYI IVTQVGPGPQ ILDDPCAHLL GPDGLPKPAA

Length:400

Mass (Da):43,405

Last modified:October 1, 1996 - v1

Checksum:ⁱ3FD4741BCC4B68D8

GO

Computationally mapped potential isoform sequencesⁱ

There are 4 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

H3BP35	H3BP35_HUMAN	Diphosphomevalonate decarboxylase Diphosphomevalonate decarboxylase	MVD	271	Annotation score:
H3BQ47	H3BQ47_HUMAN	Diphosphomevalonate decarboxylase Diphosphomevalonate decarboxylase	MVD	91	Annotation score:
H3BVC4	H3BVC4_HUMAN	Diphosphomevalonate decarboxylase Diphosphomevalonate decarboxylase	MVD	51	Annotation score:
H3BRZ1	H3BRZ1_HUMAN	Diphosphomevalonate decarboxylase Diphosphomevalonate decarboxylase	MVD	41	Annotation score:

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_075052	101	P → R in POROK7; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs200033380Ensembl.	1
Natural variantⁱVAR_075053	128	A → V in POROK7; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs776358937Ensembl.	1
Natural variantⁱVAR_075054	161	R → L in POROK7; unknown pathological significance. 1 Publication	1
Natural variantⁱVAR_075055	161	R → Q in POROK7; 1000-fold diminution in specific activity. 2 PublicationsCorresponds to variant dbSNP:rs144010349Ensembl.	1
Natural variantⁱVAR_075056	228	R → Q in POROK7; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs770939767Ensembl.	1
Natural variantⁱVAR_075057	228	R → W in POROK7; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs776684503Ensembl.	1
Natural variantⁱVAR_075058	249	F → S in POROK7. 1 PublicationCorresponds to variant dbSNP:rs761991070EnsemblClinVar.	1
Natural variantⁱVAR_051605	278	N → H. Corresponds to variant dbSNP:rs34519538Ensembl.	1
Natural variantⁱVAR_075059	292	N → S in POROK7. 1 PublicationCorresponds to variant dbSNP:rs755948940EnsemblClinVar.	1
Natural variantⁱVAR_075060	371	Missing in POROK7; unknown pathological significance. 1 Publication	1
Natural variantⁱVAR_075061	376	G → R in POROK7; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs546127665Ensembl.	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U49260 mRNA Translation: AAC50440.1 BT006930 mRNA Translation: AAP35576.1 CH471184 Genomic DNA Translation: EAW66792.1 BC000011 mRNA Translation: AAH00011.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS10968.1
NCBI Reference Sequences More...RefSeqⁱ	NP_002452.1, NM_002461.2
UniGeneⁱ	Hs.252457

Genome annotation databases

Ensemblⁱ	ENST00000301012; ENSP00000301012; ENSG00000167508
GeneIDⁱ	4597
KEGGⁱ	hsa:4597
UCSC genome browser More...UCSCⁱ	uc002flg.2 human

Keywords - Coding sequence diversityⁱ

Polymorphism

Protein	Similar proteins		Species	Score	Length	Source
P53602	Diphosphomevalonate decarboxylase		COLAP		450	UniRef90_P53602
Diphosphomevalonate decarboxylase		MACMU		401
Diphosphomevalonate decarboxylase		MACFA		401
Diphosphomevalonate decarboxylase		CERAT		401
Diphosphomevalonate decarboxylase		RHIRO		401
+24

Protein	Similar proteins		Species	Score	Length	Source
P53602	Diphosphomevalonate decarboxylase		RAT		401	UniRef50_P53602
Diphosphomevalonate decarboxylase	)	MOUSE		401
Diphosphomevalonate decarboxylase		DANRE		400
Diphosphomevalonate decarboxylase		BOVIN		400
Diphosphomevalonate decarboxylase		COLAP		450
+352

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U49260 mRNA Translation: AAC50440.1 BT006930 mRNA Translation: AAP35576.1 CH471184 Genomic DNA Translation: EAW66792.1 BC000011 mRNA Translation: AAH00011.1
CCDSⁱ	CCDS10968.1
RefSeqⁱ	NP_002452.1, NM_002461.2
UniGeneⁱ	Hs.252457

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	3D4J	X-ray	2.40	A/B	1-400	[»]
ProteinModelPortalⁱ	P53602
SMRⁱ	P53602
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	110682, 37 interactors
IntActⁱ	P53602, 9 interactors
STRINGⁱ	9606.ENSP00000301012

Chemistry databases

BindingDBⁱ	P53602
ChEMBLⁱ	CHEMBL4340
GuidetoPHARMACOLOGYⁱ	642
SwissLipidsⁱ	SLP:000001242

PTM databases

iPTMnetⁱ	P53602
PhosphoSitePlusⁱ	P53602

Polymorphism and mutation databases

BioMutaⁱ	MVD
DMDMⁱ	1706681

Proteomic databases

EPDⁱ	P53602
MaxQBⁱ	P53602
PaxDbⁱ	P53602
PeptideAtlasⁱ	P53602
PRIDEⁱ	P53602
ProteomicsDBⁱ	56588

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	4597
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000301012; ENSP00000301012; ENSG00000167508
GeneIDⁱ	4597
KEGGⁱ	hsa:4597
UCSCⁱ	uc002flg.2 human

Organism-specific databases

CTDⁱ	4597
DisGeNETⁱ	4597
EuPathDBⁱ	HostDB:ENSG00000167508.10
GeneCardsⁱ	MVD
HGNCⁱ	HGNC:7529 MVD
HPAⁱ	HPA041404 HPA048250
MalaCardsⁱ	MVD
MIMⁱ	603236 gene 614714 phenotype
neXtProtⁱ	NX_P53602
OpenTargetsⁱ	ENSG00000167508
Orphanetⁱ	79152 Disseminated superficial actinic porokeratosis
PharmGKBⁱ	PA31330
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG2833 Eukaryota COG3407 LUCA
GeneTreeⁱ	ENSGT00390000015359
HOVERGENⁱ	HBG051503
InParanoidⁱ	P53602
KOⁱ	K01597
OMAⁱ	LTLHAMM
OrthoDBⁱ	EOG091G0EUU
PhylomeDBⁱ	P53602
TreeFamⁱ	TF105952

Enzyme and pathway databases

UniPathwayⁱ	UPA00063
BioCycⁱ	MetaCyc:ENSG00000167508-MONOMER
BRENDAⁱ	4.1.1.33 2681
Reactomeⁱ	R-HSA-191273 Cholesterol biosynthesis R-HSA-2426168 Activation of gene expression by SREBF (SREBP) R-HSA-446199 Synthesis of Dolichyl-phosphate
SABIO-RKⁱ	P53602

Miscellaneous databases

ChiTaRSⁱ	MVD human
EvolutionaryTraceⁱ	P53602
GenomeRNAiⁱ	4597
Protein Ontology More...PROⁱ	PR:P53602
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000167508 Expressed in 130 organ(s), highest expression level in right adrenal gland cortex
CleanExⁱ	HS_MVD
ExpressionAtlasⁱ	P53602 baseline and differential
Genevisibleⁱ	P53602 HS

Family and domain databases

Gene3Dⁱ	3.30.230.10, 1 hit 3.30.70.890, 1 hit
InterProⁱ	View protein in InterPro IPR036554 GHMP_kinase_C_sf IPR006204 GHMP_kinase_N_dom IPR005935 Mev_decarb IPR029765 Mev_diP_decarb IPR020568 Ribosomal_S5_D2-typ_fold IPR014721 Ribosomal_S5_D2-typ_fold_subgr
Pfamⁱ	View protein in Pfam PF00288 GHMP_kinases_N, 1 hit
PIRSFⁱ	PIRSF015950 Mev_P_decrbx, 1 hit
SUPFAMⁱ	SSF54211 SSF54211, 1 hit SSF55060 SSF55060, 1 hit
TIGRFAMsⁱ	TIGR01240 mevDPdecarb, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	MVD1_HUMAN
Accessionⁱ	P53602Primary (citable) accession number: P53602 Secondary accession number(s): Q53Y65
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
	Last sequence update:	October 1, 1996
	Last modified:	November 7, 2018
	This is version 161 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

SIMILARITY comments
Index of protein domains and families
Human chromosome 16
Human chromosome 16: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PATHWAY comments
Index of metabolic and biosynthesis pathways
PDB cross-references
Index of Protein Data Bank (PDB) cross-references

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P53602 (MVD1_HUMAN)

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Diphosphomevalonate decarboxylase

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: cholesterol biosynthesis

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Chemistry databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Cytosol

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Keywords - Diseasei

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Natural variant

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

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Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

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Keywords - Technical termi

Documents

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Functionⁱ

Kineticsⁱ

Pathwayⁱ: cholesterol biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ