dbPTM

DPOG2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DPOG2_HUMAN
UniProt AC	Q9UHN1
Protein Name	DNA polymerase subunit gamma-2, mitochondrial
Gene Name	POLG2
Organism	Homo sapiens (Human).
Sequence Length	485
Subcellular Localization	Mitochondrion.
Protein Description	Mitochondrial polymerase processivity subunit. Stimulates the polymerase and exonuclease activities, and increases the processivity of the enzyme. Binds to ss-DNA..
Protein Sequence	MRSRVAVRACHKVCRCLLSGFGGRVDAGQPELLTERSSPKGGHVKSHAELEGNGEHPEAPGSGEGSEALLEICQRRHFLSGSKQQLSRDSLLSGCHPGFGPLGVELRKNLAAEWWTSVVVFREQVFPVDALHHKPGPLLPGDSAFRLVSAETLREILQDKELSKEQLVAFLENVLKTSGKLRENLLHGALEHYVNCLDLVNKRLPYGLAQIGVCFHPVFDTKQIRNGVKSIGEKTEASLVWFTPPRTSNQWLDFWLRHRLQWWRKFAMSPSNFSSSDCQDEEGRKGNKLYYNFPWGKELIETLWNLGDHELLHMYPGNVSKLHGRDGRKNVVPCVLSVNGDLDRGMLAYLYDSFQLTENSFTRKKNLHRKVLKLHPCLAPIKVALDVGRGPTLELRQVCQGLFNELLENGISVWPGYLETMQSSLEQLYSKYDEMSILFTVLVTETTLENGLIHLRSRDTTMKEMMHISKLKDFLIKYISSAKNV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
34	Phosphorylation	AGQPELLTERSSPKG CCCCHHHCCCCCCCC	41.81	25849741
37	Phosphorylation	PELLTERSSPKGGHV CHHHCCCCCCCCCCC	44.77	25627689
38	Phosphorylation	ELLTERSSPKGGHVK HHHCCCCCCCCCCCC	36.53	10666468
82	Phosphorylation	RRHFLSGSKQQLSRD HHHHCCCCHHHHCHH	24.74	24260401
83	Ubiquitination	RHFLSGSKQQLSRDS HHHCCCCHHHHCHHH	45.66	-
143	Phosphorylation	GPLLPGDSAFRLVSA CCCCCCCHHHHHCCH	34.91	22210691
149	Phosphorylation	DSAFRLVSAETLREI CHHHHHCCHHHHHHH	25.61	24505115
269	Phosphorylation	WWRKFAMSPSNFSSS HHHHHCCCCCCCCCC	23.03	23663014
271	Phosphorylation	RKFAMSPSNFSSSDC HHHCCCCCCCCCCCC	43.11	23663014
285	Acetylation	CQDEEGRKGNKLYYN CCCCCCCCCCEEEEC	77.13	25953088
288	Acetylation	EEGRKGNKLYYNFPW CCCCCCCEEEECCCC	46.68	19608861
315	Phosphorylation	DHELLHMYPGNVSKL CHHHHHCCCCCHHHH	9.39	29759185
320	Phosphorylation	HMYPGNVSKLHGRDG HCCCCCHHHHCCCCC	33.24	29759185
337	Phosphorylation	NVVPCVLSVNGDLDR CCEEEEEEECCCCCH	7.98	27251275
357	Phosphorylation	LYDSFQLTENSFTRK HHHHHHCCCCCCCCC	23.49	-
362	Phosphorylation	QLTENSFTRKKNLHR HCCCCCCCCCHHHHH	41.21	-
469	Phosphorylation	MKEMMHISKLKDFLI HHHHHHHHHHHHHHH	19.77	29759185
477	Acetylation	KLKDFLIKYISSAKN HHHHHHHHHHHHCCC	38.38	26051181
480	Phosphorylation	DFLIKYISSAKNV-- HHHHHHHHHCCCC--	22.58	-
481	Phosphorylation	FLIKYISSAKNV--- HHHHHHHHCCCC---	33.43	-

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 DPOG2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DPOG2_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 DPOG2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DPOG1_HUMAN	POLG	physical	26496610
RS3_HUMAN	RPS3	physical	26496610
STXB1_HUMAN	STXBP1	physical	26496610
CCDC6_HUMAN	CCDC6	physical	26496610
AP4E1_HUMAN	AP4E1	physical	26496610
WAP53_HUMAN	WRAP53	physical	26496610
OSBL1_HUMAN	OSBPL1A	physical	26496610
DPOG1_HUMAN	POLG	physical	28514442
MMSA_HUMAN	ALDH6A1	physical	28514442
ADNP_HUMAN	ADNP	physical	28514442
HOME3_HUMAN	HOMER3	physical	28514442
GCSP_HUMAN	GLDC	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
610131	Progressive external ophthalmoplegia with mitochondrial DNA deletions, autosomal dominant, 4 (PEOA4)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of DPOG2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-288, AND MASS SPECTROMETRY.	19608861 [Abstract]