KIME_HUMAN - dbPTM
KIME_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KIME_HUMAN
UniProt AC Q03426
Protein Name Mevalonate kinase {ECO:0000305}
Gene Name MVK {ECO:0000312|HGNC:HGNC:7530}
Organism Homo sapiens (Human).
Sequence Length 396
Subcellular Localization Cytoplasm . Peroxisome .
Protein Description Catalyzes the phosphorylation of mevalonate to mevalonate 5-phosphate, a key step in isoprenoid and cholesterol biosynthesis. [PubMed: 9325256]
Protein Sequence MLSEVLLVSAPGKVILHGEHAVVHGKVALAVSLNLRTFLRLQPHSNGKVDLSLPNIGIKRAWDVARLQSLDTSFLEQGDVTTPTSEQVEKLKEVAGLPDDCAVTERLAVLAFLYLYLSICRKQRALPSLDIVVWSELPPGAGLGSSAAYSVCLAAALLTVCEEIPNPLKDGDCVNRWTKEDLELINKWAFQGERMIHGNPSGVDNAVSTWGGALRYHQGKISSLKRSPALQILLTNTKVPRNTRALVAGVRNRLLKFPEIVAPLLTSIDAISLECERVLGEMGEAPAPEQYLVLEELIDMNQHHLNALGVGHASLDQLCQVTRARGLHSKLTGAGGGGCGITLLKPGLEQPEVEATKQALTSCGFDCLETSIGAPGVSIHSATSLDSRVQQALDGL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
32PhosphorylationGKVALAVSLNLRTFL
CEEEEEEECCCHHHH
13.1122210691
37PhosphorylationAVSLNLRTFLRLQPH
EEECCCHHHHHCCCC
30.1322210691
45PhosphorylationFLRLQPHSNGKVDLS
HHHCCCCCCCCCCEE
54.70-
59UbiquitinationSLPNIGIKRAWDVAR
ECCCCCCCHHHHHHH
30.74-
90UbiquitinationPTSEQVEKLKEVAGL
CCHHHHHHHHHHCCC
67.03-
92AcetylationSEQVEKLKEVAGLPD
HHHHHHHHHHCCCCC
62.3027452117
179UbiquitinationDCVNRWTKEDLELIN
CCCCCCCHHHHHHHH
42.12-
187UbiquitinationEDLELINKWAFQGER
HHHHHHHHHHHCCCC
32.67-
208PhosphorylationSGVDNAVSTWGGALR
CCHHHHHHHCCHHHH
18.9428857561
220UbiquitinationALRYHQGKISSLKRS
HHHHCCCCCHHCCCC
32.61-
222PhosphorylationRYHQGKISSLKRSPA
HHCCCCCHHCCCCCH
32.8624719451
227PhosphorylationKISSLKRSPALQILL
CCHHCCCCCHHHHHH
16.97-
235PhosphorylationPALQILLTNTKVPRN
CHHHHHHHCCCCCCC
37.0828857561
237PhosphorylationLQILLTNTKVPRNTR
HHHHHHCCCCCCCHH
28.3428857561
238UbiquitinationQILLTNTKVPRNTRA
HHHHHCCCCCCCHHH
52.92-
256SumoylationGVRNRLLKFPEIVAP
HHHHHHHCCHHHHHH
64.56-
330UbiquitinationRARGLHSKLTGAGGG
HHCCCCCCCCCCCCC
39.04-
345UbiquitinationGCGITLLKPGLEQPE
CCCEEEECCCCCCCC
39.90-
345SumoylationGCGITLLKPGLEQPE
CCCEEEECCCCCCCC
39.90-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of KIME_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KIME_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of KIME_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KIME_HUMANMVKphysical
16189514
METK1_HUMANMAT1Aphysical
22939629
KIME_HUMANMVKphysical
25416956
CCD91_HUMANCCDC91physical
26186194
CCD91_HUMANCCDC91physical
28514442
TACC3_HUMANTACC3physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KIME_HUMAN

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Related Literatures of Post-Translational Modification

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