DGUOK_HUMAN - dbPTM
DGUOK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DGUOK_HUMAN
UniProt AC Q16854
Protein Name Deoxyguanosine kinase, mitochondrial
Gene Name DGUOK
Organism Homo sapiens (Human).
Sequence Length 277
Subcellular Localization Mitochondrion.
Protein Description Phosphorylates deoxyguanosine and deoxyadenosine in the mitochondrial matrix, with the highest efficiency for deoxyguanosine. In non-replicating cells, where cytosolic dNTP synthesis is down-regulated, mtDNA synthesis depends solely on DGUOK and TK2. Phosphorylates certain nucleoside analogs. Widely used as target of antiviral and chemotherapeutic agents..
Protein Sequence MAAGRLFLSRLRAPFSSMAKSPLEGVSSSRGLHAGRGPRRLSIEGNIAVGKSTFVKLLTKTYPEWHVATEPVATWQNIQAAGTQKACTAQSLGNLLDMMYREPARWSYTFQTFSFLSRLKVQLEPFPEKLLQARKPVQIFERSVYSDRYIFAKNLFENGSLSDIEWHIYQDWHSFLLWEFASRITLHGFIYLQASPQVCLKRLYQRAREEEKGIELAYLEQLHGQHEAWLIHKTTKLHFEALMNIPVLVLDVNDDFSEEVTKQEDLMREVNTFVKNL
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
21PhosphorylationPFSSMAKSPLEGVSS
CCHHHCCCCCCCCCC		25.7721815630
42PhosphorylationGRGPRRLSIEGNIAV
CCCCCCEEEECCEEE		19.4424719451
56AcetylationVGKSTFVKLLTKTYP
ECHHHHHHHHHCCCC		33.3223236377
60UbiquitinationTFVKLLTKTYPEWHV
HHHHHHHCCCCCCEE		46.13-
60AcetylationTFVKLLTKTYPEWHV
HHHHHHHCCCCCCEE		46.1325038526
69 (in isoform 5)Phosphorylation-39.4722210691
91 (in isoform 4)Ubiquitination-35.4621890473
91 (in isoform 3)Ubiquitination-35.4621890473
97 (in isoform 4)Ubiquitination-23.9921890473
97 (in isoform 3)Ubiquitination-23.9921890473
107 (in isoform 5)Ubiquitination-14.5621890473
113 (in isoform 5)Ubiquitination-3.1921890473
117PhosphorylationFQTFSFLSRLKVQLE
EEHHHHHHHCCEECC		33.2924719451
120UbiquitinationFSFLSRLKVQLEPFP
HHHHHHCCEECCCCC		27.16-
129UbiquitinationQLEPFPEKLLQARKP
ECCCCCHHHHHCCCC		55.5221890473
129 (in isoform 2)Ubiquitination-55.5221890473
129 (in isoform 1)Ubiquitination-55.5221890473
129UbiquitinationQLEPFPEKLLQARKP
ECCCCCHHHHHCCCC		55.5221890473
135 (in isoform 1)Ubiquitination-53.1821890473
135 (in isoform 2)Ubiquitination-53.1821890473
135AcetylationEKLLQARKPVQIFER
HHHHHCCCCEEEEEC		53.1823236377
135MalonylationEKLLQARKPVQIFER
HHHHHCCCCEEEEEC		53.1826320211
135UbiquitinationEKLLQARKPVQIFER
HHHHHCCCCEEEEEC		53.18-
149 (in isoform 4)Ubiquitination-12.8421890473
187 (in isoform 2)Ubiquitination-22.0721890473
237 (in isoform 3)Ubiquitination-5.4121890473
253 (in isoform 5)Ubiquitination-42.6821890473
275 (in isoform 1)Ubiquitination-48.6321890473
275MalonylationREVNTFVKNL-----
HHHHHHHHCC-----		48.6332601280
275UbiquitinationREVNTFVKNL-----
HHHHHHHHCC-----		48.6319608861
275AcetylationREVNTFVKNL-----
HHHHHHHHCC-----		48.6319608861
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 DGUOK_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DGUOK_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 DGUOK_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DGUOK_HUMANDGUOKphysical
11427893
A4_HUMANAPPphysical
21832049
PAXI_HUMANPXNphysical
21988832
NCAM1_HUMANNCAM1physical
26186194
DPYL5_HUMANDPYSL5physical
26186194
STXB1_HUMANSTXBP1physical
26186194
ATP4A_HUMANATP4Aphysical
26186194
AT2B2_HUMANATP2B2physical
26186194
AT2B3_HUMANATP2B3physical
26186194
ELAV4_HUMANELAVL4physical
26186194
GPM6B_HUMANGPM6Bphysical
26186194
H15_HUMANHIST1H1Bphysical
26186194
H2B1L_HUMANHIST1H2BLphysical
26186194
CNTN1_HUMANCNTN1physical
26186194
DCLK1_HUMANDCLK1physical
26186194
AP180_HUMANSNAP91physical
26186194
SYT1_HUMANSYT1physical
26186194
HPCL4_HUMANHPCAL4physical
26186194
VISL1_HUMANVSNL1physical
26186194
SYN2_HUMANSYN2physical
26186194
SYN1_HUMANSYN1physical
26186194
DPYL1_HUMANCRMP1physical
26186194
DPYL3_HUMANDPYSL3physical
26186194
DPYL2_HUMANDPYSL2physical
26186194
DYN1_HUMANDNM1physical
26186194
DCK_HUMANDCKphysical
26186194
E41L1_HUMANEPB41L1physical
26186194
GNAQ_HUMANGNAQphysical
26186194
GBG2_HUMANGNG2physical
26186194
SYUB_HUMANSNCBphysical
26186194
SYUA_HUMANSNCAphysical
26186194
SYPH_HUMANSYPphysical
26186194
RAB3A_HUMANRAB3Aphysical
26186194
S12A5_HUMANSLC12A5physical
26186194
HPCL1_HUMANHPCAL1physical
26186194
NCALD_HUMANNCALDphysical
26186194
HPCA_HUMANHPCAphysical
26186194
STX1A_HUMANSTX1Aphysical
26186194
STX1B_HUMANSTX1Bphysical
26186194
KCC2B_HUMANCAMK2Bphysical
26186194
KCC2A_HUMANCAMK2Aphysical
26186194
CAD13_HUMANCDH13physical
26186194
ANK2_HUMANANK2physical
26186194
AMPH_HUMANAMPHphysical
26186194
BIN1_HUMANBIN1physical
26186194
NTRI_HUMANNTMphysical
26186194
GRIA2_HUMANGRIA2physical
26186194
SNAB_HUMANNAPBphysical
26186194
TAU_HUMANMAPTphysical
26186194
DPYL4_HUMANDPYSL4physical
26186194
EF1A2_HUMANEEF1A2physical
26186194
GNAO_HUMANGNAO1physical
26186194
CAMKV_HUMANCAMKVphysical
26186194
MP2K1_HUMANMAP2K1physical
26186194
DNM1L_HUMANDNM1Lphysical
26186194
VAMP2_HUMANVAMP2physical
26186194
RAB6B_HUMANRAB6Bphysical
26186194
ARL8B_HUMANARL8Bphysical
26186194
EDIL3_HUMANEDIL3physical
26186194
RAB14_HUMANRAB14physical
26186194
MTAP2_HUMANMAP2physical
26186194
L1CAM_HUMANL1CAMphysical
26186194
ERC2_HUMANERC2physical
26186194
SNP25_HUMANSNAP25physical
26186194
CALB2_HUMANCALB2physical
26186194
DCK_HUMANDCKphysical
28514442
SYN1_HUMANSYN1physical
28514442
STX1B_HUMANSTX1Bphysical
28514442
H2B1L_HUMANHIST1H2BLphysical
28514442
L1CAM_HUMANL1CAMphysical
28514442
SNP25_HUMANSNAP25physical
28514442
HPCA_HUMANHPCAphysical
28514442
SYN2_HUMANSYN2physical
28514442
VISL1_HUMANVSNL1physical
28514442
SNAB_HUMANNAPBphysical
28514442
DCLK1_HUMANDCLK1physical
28514442
STX1A_HUMANSTX1Aphysical
28514442
SYT1_HUMANSYT1physical
28514442
ATP4A_HUMANATP4Aphysical
28514442
HPCL4_HUMANHPCAL4physical
28514442
KCC2A_HUMANCAMK2Aphysical
28514442
S12A5_HUMANSLC12A5physical
28514442
SYPH_HUMANSYPphysical
28514442
TAU_HUMANMAPTphysical
28514442
DPYL1_HUMANCRMP1physical
28514442
MTAP2_HUMANMAP2physical
28514442
DPYL3_HUMANDPYSL3physical
28514442
STXB1_HUMANSTXBP1physical
28514442
SYUB_HUMANSNCBphysical
28514442
ELAV4_HUMANELAVL4physical
28514442
HPCL1_HUMANHPCAL1physical
28514442
AP180_HUMANSNAP91physical
28514442
CALB2_HUMANCALB2physical
28514442
GRIA2_HUMANGRIA2physical
28514442
DCX_HUMANDCXphysical
28514442
NTRI_HUMANNTMphysical
28514442
CNTN1_HUMANCNTN1physical
28514442
CAMKV_HUMANCAMKVphysical
28514442
DNM1L_HUMANDNM1Lphysical
28514442
AT2B3_HUMANATP2B3physical
28514442
RAB3A_HUMANRAB3Aphysical
28514442
H15_HUMANHIST1H1Bphysical
28514442
DYN1_HUMANDNM1physical
28514442
GBG2_HUMANGNG2physical
28514442
DPYL2_HUMANDPYSL2physical
28514442
E41L1_HUMANEPB41L1physical
28514442
VATC1_HUMANATP6V1C1physical
28514442
NCAM1_HUMANNCAM1physical
28514442
NCALD_HUMANNCALDphysical
28514442
GNAO_HUMANGNAO1physical
28514442
DPYL5_HUMANDPYSL5physical
28514442
BIN1_HUMANBIN1physical
28514442
GNAQ_HUMANGNAQphysical
28514442
CAD13_HUMANCDH13physical
28514442
MARE3_HUMANMAPRE3physical
28514442
ERC2_HUMANERC2physical
28514442
ANK2_HUMANANK2physical
28514442
ARL8B_HUMANARL8Bphysical
28514442
CANB1_HUMANPPP3R1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
251880Mitochondrial DNA depletion syndrome 3 (MTDPS3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB01280Nelarabine
Regulatory Network of DGUOK_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-56 AND LYS-275, AND MASSSPECTROMETRY.

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