DPOE4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DPOE4_HUMAN
• UniProt AC: Q9NR33
• Protein Name: DNA polymerase epsilon subunit 4
• Gene Name: POLE4
• Organism: Homo sapiens (Human).
• Sequence Length: 117
• Subcellular Localization: Nucleus .
• Protein Description: May play a role in allowing polymerase epsilon to carry out its replication and/or repair function..
• Protein Sequence: MAAAAAAGSGTPREEEGPAGEAAASQPQAPTSVPGARLSRLPLARVKALVKADPDVTLAGQEAIFILARAAELFVETIAKDAYCCAQQGKRKTLQRRDLDNAIEAVDEFAFLEGTLD

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
2	Acetylation	------MAAAAAAGS ------CHHHHHCCC	13.05	22814378
9	Phosphorylation	AAAAAAGSGTPREEE HHHHHCCCCCCCCCC	34.46	23401153
11	Phosphorylation	AAAAGSGTPREEEGP HHHCCCCCCCCCCCC	22.37	29255136
25	Phosphorylation	PAGEAAASQPQAPTS CCHHHHHCCCCCCCC	37.35	17525332
31	Phosphorylation	ASQPQAPTSVPGARL HCCCCCCCCCCCCCH	45.43	25159151
32	Phosphorylation	SQPQAPTSVPGARLS CCCCCCCCCCCCCHH	25.84	25159151
51	Sumoylation	ARVKALVKADPDVTL HHHHHHHHCCCCCCC	48.17	-
51	Ubiquitination	ARVKALVKADPDVTL HHHHHHHHCCCCCCC	48.17	22053931
57	Phosphorylation	VKADPDVTLAGQEAI HHCCCCCCCCHHHHH	20.47	20860994
77	Phosphorylation	AAELFVETIAKDAYC HHHHHHHHHHHHHHH	22.42	26852163
84	S-nitrosocysteine	TIAKDAYCCAQQGKR HHHHHHHHHHHHCCC	1.34	-
84	S-nitrosylation	TIAKDAYCCAQQGKR HHHHHHHHHHHHCCC	1.34	19483679
85	S-nitrosocysteine	IAKDAYCCAQQGKRK HHHHHHHHHHHCCCC	2.20	-
85	S-nitrosylation	IAKDAYCCAQQGKRK HHHHHHHHHHHCCCC	2.20	19483679
90	Ubiquitination	YCCAQQGKRKTLQRR HHHHHHCCCCCCHHH	46.51	29967540
90	2-Hydroxyisobutyrylation	YCCAQQGKRKTLQRR HHHHHHCCCCCCHHH	46.51	-
90	Acetylation	YCCAQQGKRKTLQRR HHHHHHCCCCCCHHH	46.51	25953088

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of DPOE4_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DPOE4_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of DPOE4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DPOE4_HUMAN	POLE4	physical	10801849
M3K7_HUMAN	MAP3K7	physical	22939629
NU133_HUMAN	NUP133	physical	22939629
ISY1_HUMAN	ISY1	physical	26344197
DPOE1_HUMAN	POLE	physical	26344197
DPOE3_HUMAN	POLE3	physical	26344197

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
• DB00242: Cladribine

Related Literatures of Post-Translational Modification

Acetylation

"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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-11, AND MASS SPECTROMETRY.
PubMed: 19413330

Phosphorylation

"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASSSPECTROMETRY.
PubMed: 17525332

"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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-11, AND MASS SPECTROMETRY.
PubMed: 19413330