UniProt Accession

 PMVK_HUMAN; Q15126; Q5TZW9 

Genbank Protein ID

 L77213; BT019976; BC006089; BC007694; AF026069 

Genbank Nucleotide ID

 AAC37593.1; AAV38779.1; AAH06089.1; AAH07694.1; AAC60791.1 

Protein Name

 Phosphomevalonate kinase 

Protein Synonyms/Alias

 PMKase; hPMK 

Gene Name

 PMVK 

Gene Synonyms/Alias

 PMKI 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
17	LVLLFSGKRKSGKDF	ubiquitination	[1]
19	LLFSGKRKSGKDFVT	ubiquitination	[2]
22	SGKRKSGKDFVTEAL	ubiquitination	[1, 2]
48	LRLSGPLKEQYAQEH	acetylation	[3]
48	LRLSGPLKEQYAQEH	ubiquitination	[1, 2, 4, 5, 6, 7]
69	LLDTSTYKEAFRKDM	ubiquitination	[1, 2, 4, 5, 6]
94	DPGFFCRKIVEGISQ	ubiquitination	[2]

Reference

 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 

Functional Description

  

Sequence Annotation

 NP_BIND 17 23 ATP (Probable).
 MOTIF 190 192 Microbody targeting signal (Potential).
 BINDING 141 141 ATP (Probable).
 BINDING 170 170 Substrate.
 BINDING 171 171 ATP (Probable).
 BINDING 176 176 ATP (Probable).
 BINDING 180 180 ATP (Probable).  

Keyword

 3D-structure; ATP-binding; Cholesterol biosynthesis; Cholesterol metabolism; Complete proteome; Kinase; Lipid biosynthesis; Lipid metabolism; Nucleotide-binding; Peroxisome; Polymorphism; Reference proteome; Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 192 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005777; C:peroxisome; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IDA:UniProtKB.
 GO:0004631; F:phosphomevalonate kinase activity; IDA:UniProtKB.
 GO:0006695; P:cholesterol biosynthetic process; IDA:UniProtKB.
 GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IEA:UniProtKB-UniPathway.
 GO:0070723; P:response to cholesterol; IEP:UniProtKB. 

Interpro

 IPR027417; P-loop_NTPase.
 IPR005919; Pmev_kin_anim. 

Pfam

 PF04275; P-mevalo_kinase 

SMART

  

PROSITE

  

PRINTS