dbPTM

DPOD2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DPOD2_HUMAN
UniProt AC	P49005
Protein Name	DNA polymerase delta subunit 2
Gene Name	POLD2
Organism	Homo sapiens (Human).
Sequence Length	469
Subcellular Localization	Nucleus . Recruited to DNA damage sites within 2 hours following UV irradiation.
Protein Description	As a component of the trimeric and tetrameric DNA polymerase delta complexes (Pol-delta3 and Pol-delta4, respectively), plays a role in high fidelity genome replication, including in lagging strand synthesis, and repair. [PubMed: 12403614]
Protein Sequence	MFSEQAAQRAHTLLSPPSANNATFARVPVATYTNSSQPFRLGERSFSRQYAHIYATRLIQMRPFLENRAQQHWGSGVGVKKLCELQPEEKCCVVGTLFKAMPLQPSILREVSEEHNLLPQPPRSKYIHPDDELVLEDELQRIKLKGTIDVSKLVTGTVLAVFGSVRDDGKFLVEDYCFADLAPQKPAPPLDTDRFVLLVSGLGLGGGGGESLLGTQLLVDVVTGQLGDEGEQCSAAHVSRVILAGNLLSHSTQSRDSINKAKYLTKKTQAASVEAVKMLDEILLQLSASVPVDVMPGEFDPTNYTLPQQPLHPCMFPLATAYSTLQLVTNPYQATIDGVRFLGTSGQNVSDIFRYSSMEDHLEILEWTLRVRHISPTAPDTLGCYPFYKTDPFIFPECPHVYFCGNTPSFGSKIIRGPEDQTVLLVTVPDFSATQTACLVNLRSLACQPISFSGFGAEDDDLGGLGLGP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MFSEQAAQ -------CCCHHHHH	8.22	22223895
12	Phosphorylation	QAAQRAHTLLSPPSA HHHHHHHHHCCCCCC	28.54	30266825
15	O-linked_Glycosylation	QRAHTLLSPPSANNA HHHHHHCCCCCCCCC	37.57	30059200
15	Phosphorylation	QRAHTLLSPPSANNA HHHHHHCCCCCCCCC	37.57	30266825
18	Phosphorylation	HTLLSPPSANNATFA HHHCCCCCCCCCCEE	47.19	30266825
23	Phosphorylation	PPSANNATFARVPVA CCCCCCCCEEEEEEE	21.68	29396449
31	Phosphorylation	FARVPVATYTNSSQP EEEEEEEEECCCCCC	30.98	21945579
32	Phosphorylation	ARVPVATYTNSSQPF EEEEEEEECCCCCCC	8.32	21945579
33	Phosphorylation	RVPVATYTNSSQPFR EEEEEEECCCCCCCC	25.03	21945579
35	Phosphorylation	PVATYTNSSQPFRLG EEEEECCCCCCCCCC	23.66	28555341
36	Phosphorylation	VATYTNSSQPFRLGE EEEECCCCCCCCCCC	43.90	21945579
45	Phosphorylation	PFRLGERSFSRQYAH CCCCCCCCHHHHHHH	24.22	24719451
47	Phosphorylation	RLGERSFSRQYAHIY CCCCCCHHHHHHHHH	21.52	17081983
50	Phosphorylation	ERSFSRQYAHIYATR CCCHHHHHHHHHHHH	10.07	20068231
53	Phosphorylation	FSRQYAHIYATRLIQ HHHHHHHHHHHHHHH	1.58	-
68	Phosphorylation	MRPFLENRAQQHWGS HHHHHCHHHHHHCCC	25.13	-
75	Phosphorylation	RAQQHWGSGVGVKKL HHHHHCCCCCCHHHH	25.72	22210691
80	Acetylation	WGSGVGVKKLCELQP CCCCCCHHHHHHCCC	33.81	25953088
80	Phosphorylation	WGSGVGVKKLCELQP CCCCCCHHHHHHCCC	33.81	-
80	Ubiquitination	WGSGVGVKKLCELQP CCCCCCHHHHHHCCC	33.81	21906983
81	Ubiquitination	GSGVGVKKLCELQPE CCCCCHHHHHHCCCH	56.83	-
82	Phosphorylation	SGVGVKKLCELQPEE CCCCHHHHHHCCCHH	1.97	-
90	Ubiquitination	CELQPEEKCCVVGTL HHCCCHHCEEEEEHH	31.13	-
99	Ubiquitination	CVVGTLFKAMPLQPS EEEEHHHHHCCCCHH	47.06	-
106	Phosphorylation	KAMPLQPSILREVSE HHCCCCHHHHHHHHH	22.69	21964256
110	Phosphorylation	LQPSILREVSEEHNL CCHHHHHHHHHHCCC	47.12	-
112	Phosphorylation	PSILREVSEEHNLLP HHHHHHHHHHCCCCC	32.30	20873877
115	Ubiquitination	LREVSEEHNLLPQPP HHHHHHHCCCCCCCC	26.62	-
116	Ubiquitination	REVSEEHNLLPQPPR HHHHHHCCCCCCCCC	46.70	-
125	Acetylation	LPQPPRSKYIHPDDE CCCCCCHHCCCCCCC	49.88	25953088
125	Ubiquitination	LPQPPRSKYIHPDDE CCCCCCHHCCCCCCC	49.88	21906983
134	Ubiquitination	IHPDDELVLEDELQR CCCCCCEECHHHHHH	5.31	-
145	Ubiquitination	ELQRIKLKGTIDVSK HHHHHCCCCEECHHH	49.35	21906983
147	Phosphorylation	QRIKLKGTIDVSKLV HHHCCCCEECHHHCC	16.65	20068231
151	Phosphorylation	LKGTIDVSKLVTGTV CCCEECHHHCCCCCE	19.27	20068231
155	Phosphorylation	IDVSKLVTGTVLAVF ECHHHCCCCCEEEEE	37.26	20068231
157	Phosphorylation	VSKLVTGTVLAVFGS HHHCCCCCEEEEECE	11.72	20068231
160	Ubiquitination	LVTGTVLAVFGSVRD CCCCCEEEEECEECC	7.11	-
164	Phosphorylation	TVLAVFGSVRDDGKF CEEEEECEECCCCCE	11.52	20068231
178	Ubiquitination	FLVEDYCFADLAPQK EEEEEEEECCCCCCC	4.89	-
180	Ubiquitination	VEDYCFADLAPQKPA EEEEEECCCCCCCCC	24.10	-
182	Phosphorylation	DYCFADLAPQKPAPP EEEECCCCCCCCCCC	12.67	20068231
186	Phosphorylation	ADLAPQKPAPPLDTD CCCCCCCCCCCCCCC	44.76	20068231
192	Phosphorylation	KPAPPLDTDRFVLLV CCCCCCCCCCEEEEE	36.44	20068231
220	Ubiquitination	LGTQLLVDVVTGQLG HHHHEEEEECCCCCC	29.19	-
249	Phosphorylation	ILAGNLLSHSTQSRD HHHHHHHCCCCCCHH	20.68	30108239
251	Phosphorylation	AGNLLSHSTQSRDSI HHHHHCCCCCCHHHH	25.43	30108239
252	Phosphorylation	GNLLSHSTQSRDSIN HHHHCCCCCCHHHHH	25.74	30108239
254	Phosphorylation	LLSHSTQSRDSINKA HHCCCCCCHHHHHHH	37.84	30108239
257	Phosphorylation	HSTQSRDSINKAKYL CCCCCHHHHHHHHHH	27.27	26055452
263	Phosphorylation	DSINKAKYLTKKTQA HHHHHHHHHCHHHHC	25.18	-
265	Phosphorylation	INKAKYLTKKTQAAS HHHHHHHCHHHHCCH	27.66	-
267	Ubiquitination	KAKYLTKKTQAASVE HHHHHCHHHHCCHHH	40.40	21906983
267	Ubiquitination	KAKYLTKKTQAASVE HHHHHCHHHHCCHHH	40.40	21906983
268	Phosphorylation	AKYLTKKTQAASVEA HHHHCHHHHCCHHHH	25.62	29457462
272	Phosphorylation	TKKTQAASVEAVKML CHHHHCCHHHHHHHH	24.41	29457462
286	Phosphorylation	LDEILLQLSASVPVD HHHHHHHHHCCCCCC	4.69	27251275
292	Phosphorylation	QLSASVPVDVMPGEF HHHCCCCCCCCCCCC	8.97	20068231
298	Phosphorylation	PVDVMPGEFDPTNYT CCCCCCCCCCCCCCC	40.79	-
300	Phosphorylation	DVMPGEFDPTNYTLP CCCCCCCCCCCCCCC	44.82	-
302	Ubiquitination	MPGEFDPTNYTLPQQ CCCCCCCCCCCCCCC	42.58	-
345	Phosphorylation	GVRFLGTSGQNVSDI CEEEECCCCCCHHHH	36.26	20068231
384	Glutathionylation	TAPDTLGCYPFYKTD CCCCCCCCCCCCCCC	4.36	22555962
389	Ubiquitination	LGCYPFYKTDPFIFP CCCCCCCCCCCCCCC	46.99	-
413	Ubiquitination	NTPSFGSKIIRGPED CCCCCCCCCCCCCCC	42.40	-
424	Ubiquitination	GPEDQTVLLVTVPDF CCCCCEEEEEECCCC	3.46	-
448	Ubiquitination	NLRSLACQPISFSGF HHHHHCCEECCCCCC	32.52	-

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
33	T	Phosphorylation	Kinase	MAP3K7	O43318	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DPOD2_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 DPOD2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PCNA_HUMAN	PCNA	physical	11986310
DPOD1_HUMAN	POLD1	physical	16510448
DPOD4_HUMAN	POLD4	physical	16510448
SOX12_HUMAN	SOX12	physical	21988832
OSBL9_HUMAN	OSBPL9	physical	26344197
DPOA2_HUMAN	POLA2	physical	26344197
POLH_HUMAN	POLH	physical	25662213
REV3L_HUMAN	REV3L	physical	28514442
DPOD4_HUMAN	POLD4	physical	28514442
DPOD1_HUMAN	POLD1	physical	28514442
DPOD3_HUMAN	POLD3	physical	28514442
PPP5_HUMAN	PPP5C	physical	28514442
P4HA2_HUMAN	P4HA2	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of DPOD2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.	19413330 [Abstract]