NEIL2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NEIL2_HUMAN
• UniProt AC: Q969S2
• Protein Name: Endonuclease 8-like 2
• Gene Name: NEIL2
• Organism: Homo sapiens (Human).
• Sequence Length: 332
• Subcellular Localization: Nucleus .
• Protein Description: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Has DNA glycosylase activity towards 5-hydroxyuracil and other oxidized derivatives of cytosine with a preference for mismatched double-stranded DNA (DNA bubbles). Has low or no DNA glycosylase activity towards thymine glycol, 2-hydroxyadenine, hypoxanthine and 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates..
• Protein Sequence: MPEGPLVRKFHHLVSPFVGQQVVKTGGSSKKLQPASLQSLWLQDTQVHGKKLFLRFDLDEEMGPPGSSPTPEPPQKEVQKEGAADPKQVGEPSGQKTLDGSSRSAELVPQGEDDSEYLERDAPAGDAGRWLRVSFGLFGSVWVNDFSRAKKANKRGDWRDPSPRLVLHFGGGGFLAFYNCQLSWSSSPVVTPTCDILSEKFHRGQALEALGQAQPVCYTLLDQRYFSGLGNIIKNEALYRAGIHPLSLGSVLSASRREVLVDHVVEFSTAWLQGKFQGRPQHTQVYQKEQCPAGHQVMKEAFGPEDGLQRLTWWCPQCQPQLSEEPEQCQFS

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
6 (in isoform 3)	Phosphorylation	-	9.52	26425664
25	Phosphorylation	VGQQVVKTGGSSKKL CCCCEECCCCCCCCC	34.85	23403867
28	Phosphorylation	QVVKTGGSSKKLQPA CEECCCCCCCCCCCC	40.09	23403867
29	Phosphorylation	VVKTGGSSKKLQPAS EECCCCCCCCCCCCC	36.76	23403867
35 (in isoform 3)	Ubiquitination	-	15.20	21906983
50	Acetylation	QDTQVHGKKLFLRFD ECCEECCEEEEEEEE	31.27	15175427
67	Phosphorylation	EEMGPPGSSPTPEPP HHHCCCCCCCCCCCC	38.63	29255136
67 (in isoform 2)	Phosphorylation	-	38.63	25849741
68	Phosphorylation	EMGPPGSSPTPEPPQ HHCCCCCCCCCCCCC	38.41	29255136
68 (in isoform 2)	Phosphorylation	-	38.41	29507054
70 (in isoform 2)	Phosphorylation	-	42.08	29507054
70	Phosphorylation	GPPGSSPTPEPPQKE CCCCCCCCCCCCCHH	42.08	29255136
93	Acetylation	PKQVGEPSGQKTLDG HHHCCCCCCCCCCCC	49.94	15175427
96 (in isoform 1)	Ubiquitination	-	55.36	21906983
96	Ubiquitination	VGEPSGQKTLDGSSR CCCCCCCCCCCCCCC	55.36	21906983
150	Acetylation	VNDFSRAKKANKRGD CCCHHHHHHHCCCCC	51.84	15175427
151	Acetylation	NDFSRAKKANKRGDW CCHHHHHHHCCCCCC	57.09	15175427
154	Acetylation	SRAKKANKRGDWRDP HHHHHHCCCCCCCCC	63.72	15175427
173 (in isoform 3)	Ubiquitination	-	20.05	21906983
198	Phosphorylation	TPTCDILSEKFHRGQ CCCCHHHHHHCHHHH	38.79	24719451
218 (in isoform 2)	Ubiquitination	-	10.72	21906983
225	Phosphorylation	YTLLDQRYFSGLGNI HHHHCCCHHCCCCHH	9.10	30622161
227	Phosphorylation	LLDQRYFSGLGNIIK HHCCCHHCCCCHHHH	24.95	30622161
234	Ubiquitination	SGLGNIIKNEALYRA CCCCHHHHHHHHHHC	44.96	2190698
234 (in isoform 1)	Ubiquitination	-	44.96	21906983
288	Ubiquitination	QHTQVYQKEQCPAGH CCCEEEEHHCCCCHH	31.87	-
299	Ubiquitination	PAGHQVMKEAFGPED CCHHHHHHHHHCCCC	47.21	-

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

Oops, there are no upstream regulatory protein records of NEIL2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NEIL2_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 NEIL2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KEAP1_HUMAN	KEAP1	physical	20534351
EP300_HUMAN	EP300	physical	15175427

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.

Related Literatures of Post-Translational Modification

Acetylation

"Acetylation of the human DNA glycosylase NEIL2 and inhibition of itsactivity.";
Bhakat K.K., Hazra T.K., Mitra S.;
Nucleic Acids Res. 32:3033-3039(2004).
Cited for: PROTEIN SEQUENCE OF 40-57 AND 142-161, FUNCTION, MUTAGENESIS OF LYS-50AND LYS-154, INTERACTION WITH EP300, AND ACETYLATION AT LYS-50 ANDLYS-154.
PubMed: 15175427