dbPTM

DPOLB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DPOLB_HUMAN
UniProt AC	P06746
Protein Name	DNA polymerase beta
Gene Name	POLB
Organism	Homo sapiens (Human).
Sequence Length	335
Subcellular Localization	Nucleus. Cytoplasm. Cytoplasmic in normal conditions. Translocates to the nucleus following DNA damage.
Protein Description	Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases..
Protein Sequence	MSKRKAPQETLNGGITDMLTELANFEKNVSQAIHKYNAYRKAASVIAKYPHKIKSGAEAKKLPGVGTKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVSGIGPSAARKFVDEGIKTLEDLRKNEDKLNHHQRIGLKYFGDFEKRIPREEMLQMQDIVLNEVKKVDSEYIATVCGSFRRGAESSGDMDVLLTHPSFTSESTKQPKLLHQVVEQLQKVHFITDTLSKGETKFMGVCQLPSKNDEKEYPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEKGFTINEYTIRPLGVTGVAGEPLPVDSEKDIFDYIQWKYREPKDRSE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
36	Phosphorylation	VSQAIHKYNAYRKAA HHHHHHHHHHHHHHH	7.29	-
39	Phosphorylation	AIHKYNAYRKAASVI HHHHHHHHHHHHHHH	14.70	-
41	Ubiquitination	HKYNAYRKAASVIAK HHHHHHHHHHHHHHH	35.31	19713937
44	Phosphorylation	NAYRKAASVIAKYPH HHHHHHHHHHHHCCC	20.93	2040602
49	Phosphorylation	AASVIAKYPHKIKSG HHHHHHHCCCCCCCH	11.10	-
55	Phosphorylation	KYPHKIKSGAEAKKL HCCCCCCCHHHHHCC	46.86	2040602
61	Ubiquitination	KSGAEAKKLPGVGTK CCHHHHHCCCCCCHH	67.95	21362556
67	Phosphorylation	KKLPGVGTKIAEKID HCCCCCCHHHHHHHH	19.51	23532336
72	Acetylation	VGTKIAEKIDEFLAT CCHHHHHHHHHHHHH	46.57	23954790
81	Ubiquitination	DEFLATGKLRKLEKI HHHHHHCHHHHHHHH	40.54	19713937
81	Acetylation	DEFLATGKLRKLEKI HHHHHHCHHHHHHHH	40.54	25953088
83	Methylation	FLATGKLRKLEKIRQ HHHHCHHHHHHHHHC	45.02	16600869
104	Phosphorylation	INFLTRVSGIGPSAA HHHHHHHCCCCHHHH	22.77	28555341
113	Ubiquitination	IGPSAARKFVDEGIK CCHHHHHHHHHHHHH	45.04	-
141	Ubiquitination	HHQRIGLKYFGDFEK HHHHHCHHHHCCHHH	33.06	-
141	Sumoylation	HHQRIGLKYFGDFEK HHHHHCHHHHCCHHH	33.06	-
141	Sumoylation	HHQRIGLKYFGDFEK HHHHHCHHHHCCHHH	33.06	-
148	2-Hydroxyisobutyrylation	KYFGDFEKRIPREEM HHHCCHHHHCCHHHH	56.47	-
148	Ubiquitination	KYFGDFEKRIPREEM HHHCCHHHHCCHHHH	56.47	-
152	Methylation	DFEKRIPREEMLQMQ CHHHHCCHHHHHHHH	50.57	16600869
176	Phosphorylation	VDSEYIATVCGSFRR CCHHHHHHHHHHHHC	13.53	28348404
180	Phosphorylation	YIATVCGSFRRGAES HHHHHHHHHHCCCCC	15.51	28348404
206	Ubiquitination	SFTSESTKQPKLLHQ CCCCCCCCCHHHHHH	74.09	-
230	Acetylation	FITDTLSKGETKFMG EEECCCCCCCCEEEE	64.97	25953088
230	Ubiquitination	FITDTLSKGETKFMG EEECCCCCCCCEEEE	64.97	-
243	Phosphorylation	MGVCQLPSKNDEKEY EEEEECCCCCCCCCC	53.32	24719451
244	Ubiquitination	GVCQLPSKNDEKEYP EEEECCCCCCCCCCC	67.49	-
250	Phosphorylation	SKNDEKEYPHRRIDI CCCCCCCCCCCEEEE	18.53	17360941
258	Methylation	PHRRIDIRLIPKDQY CCCEEEEEECCCCCE	23.87	115488043
297	Phosphorylation	GFTINEYTIRPLGVT CCEEEEEEEEECCEE	12.34	24719451
322	Phosphorylation	SEKDIFDYIQWKYRE CCCHHHHHHHHHHCC	5.58	29083192
327	Phosphorylation	FDYIQWKYREPKDRS HHHHHHHHCCCCCCC	19.76	29083192

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
-	K	Ubiquitination	E3 ubiquitin ligase	STUB1	Q9UNE7	PMID:19713937
-	K	Ubiquitination	E3 ubiquitin ligase	HUWE1	Q7Z6Z7	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
41	K	ubiquitylation	19713937
Ubiquitinated at Lys-41, Lys-61 and Lys-81: monoubiquitinated by HUWE1/ARF-BP1.
61	K	ubiquitylation	19713937
Ubiquitinated at Lys-41, Lys-61 and Lys-81: monoubiquitinated by HUWE1/ARF-BP1.
81	K	ubiquitylation	19713937
Ubiquitinated at Lys-41, Lys-61 and Lys-81: monoubiquitinated by HUWE1/ARF-BP1.

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 DPOLB_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TAF1D_HUMAN	TAF1D	physical	15520167
XRCC1_HUMAN	XRCC1	physical	15520167
TLE1_HUMAN	TLE1	physical	16169070
KAT7_HUMAN	KAT7	physical	16169070
XRCC1_HUMAN	XRCC1	physical	11467963
PNKP_HUMAN	PNKP	physical	11163244
WRN_HUMAN	WRN	physical	17173071
FEN1_YEAST	RAD27	genetic	23144716
TPP2_HUMAN	TPP2	physical	25416956
EP300_HUMAN	EP300	physical	12453427
XPC_HUMAN	XPC	physical	26186194
SP16H_HUMAN	SUPT16H	physical	26186194
XRCC1_HUMAN	XRCC1	physical	26186194
DNLI3_HUMAN	LIG3	physical	26186194
TYDP1_HUMAN	TDP1	physical	26186194
PARP2_HUMAN	PARP2	physical	26186194
PARP1_HUMAN	PARP1	physical	26186194
SSRP1_HUMAN	SSRP1	physical	26186194
APLF_HUMAN	APLF	physical	26186194
H2A2B_HUMAN	HIST2H2AB	physical	26186194
ODBB_HUMAN	BCKDHB	physical	26186194
CETN2_HUMAN	CETN2	physical	26186194
APTX_HUMAN	APTX	physical	26186194
ODBA_HUMAN	BCKDHA	physical	26186194
PNKP_HUMAN	PNKP	physical	26186194
XRCC1_HUMAN	XRCC1	physical	25423885
PCNA_HUMAN	PCNA	physical	25184665
APLF_HUMAN	APLF	physical	28514442
DNLI3_HUMAN	LIG3	physical	28514442
TYDP1_HUMAN	TDP1	physical	28514442
XRCC1_HUMAN	XRCC1	physical	28514442
PNKP_HUMAN	PNKP	physical	28514442
PARP2_HUMAN	PARP2	physical	28514442
ODBB_HUMAN	BCKDHB	physical	28514442
APTX_HUMAN	APTX	physical	28514442
XPC_HUMAN	XPC	physical	28514442
SP16H_HUMAN	SUPT16H	physical	28514442
ODBA_HUMAN	BCKDHA	physical	28514442
H2A2B_HUMAN	HIST2H2AB	physical	28514442
PARP1_HUMAN	PARP1	physical	28514442
SSRP1_HUMAN	SSRP1	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
DB00987	Cytarabine

Regulatory Network of DPOLB_HUMAN

Related Literatures of Post-Translational Modification

Methylation
Reference	PubMed
"Arginine methylation regulates DNA polymerase beta."; El-Andaloussi N., Valovka T., Toueille M., Steinacher R., Focke F.,Gehrig P., Covic M., Hassa P.O., Schaer P., Huebscher U.,Hottiger M.O.; Mol. Cell 22:51-62(2006). Cited for: METHYLATION AT ARG-83 AND ARG-152 BY PRMT6, AND MUTAGENESIS OF ARG-83AND ARG-152.	16600869 [Abstract]
Ubiquitylation
Reference	PubMed
"USP47 is a deubiquitylating enzyme that regulates base excisionrepair by controlling steady-state levels of DNA Polymerase beta."; Parsons J.L., Dianova I.I., Khoronenkova S.V., Edelmann M.J.,Kessler B.M., Dianov G.L.; Mol. Cell 41:609-615(2011). Cited for: FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-41; LYS-61 ANDLYS-81, DEUBIQUITINATION BY USP47, AND INTERACTION WITH USP47.	21362556 [Abstract]
"Ubiquitin ligase ARF-BP1/Mule modulates base excision repair."; Parsons J.L., Tait P.S., Finch D., Dianova I.I., Edelmann M.J.,Khoronenkova S.V., Kessler B.M., Sharma R.A., McKenna W.G.,Dianov G.L.; EMBO J. 28:3207-3215(2009). Cited for: SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-41; LYS-61 AND LYS-81, ANDMUTAGENESIS OF LYS-41; LYS-61 AND LYS-81.	19713937 [Abstract]

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