NEIL1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NEIL1_HUMAN
• UniProt AC: Q96FI4
• Protein Name: Endonuclease 8-like 1
• Gene Name: NEIL1
• Organism: Homo sapiens (Human).
• Sequence Length: 390
• Subcellular Localization: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Nucleus . Chromosome . During mitosis, associates with centrosomes and condensed chromatin.
• Protein Description: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, formamidopyrimidine (Fapy) and 5-hydroxyuracil. Has marginal activity towards 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. Has DNA glycosylase/lyase activity towards mismatched uracil and thymine, in particular in U:C and T:C mismatches. Specifically binds 5-hydroxymethylcytosine (5hmC), suggesting that it acts as a specific reader of 5hmC..
• Protein Sequence: MPEGPELHLASQFVNEACRALVFGGCVEKSSVSRNPEVPFESSAYRISASARGKELRLILSPLPGAQPQQEPLALVFRFGMSGSFQLVPREELPRHAHLRFYTAPPGPRLALCFVDIRRFGRWDLGGKWQPGRGPCVLQEYQQFRENVLRNLADKAFDRPICEALLDQRFFNGIGNYLRAEILYRLKIPPFEKARSVLEALQQHRPSPELTLSQKIRTKLQNPDLLELCHSVPKEVVQLGGKGYGSESGEEDFAAFRAWLRCYGMPGMSSLQDRHGRTIWFQGDPGPLAPKGRKSRKKKSKATQLSPEDRVEDALPPSKAPSRTRRAKRDLPKRTATQRPEGTSLQQDPEAPTVPKKGRRKGRQAASGHCRPRKVKADIPSLEPEGTSAS

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
61	Phosphorylation	KELRLILSPLPGAQP CEEEEEEECCCCCCC	19.87	-
147	Phosphorylation	EYQQFRENVLRNLAD HHHHHHHHHHHHHHH	33.59	-
207	Phosphorylation	ALQQHRPSPELTLSQ HHHHHCCCCCCCHHH	30.85	24719451
263	Phosphorylation	FRAWLRCYGMPGMSS HHHHHHHHCCCCCCC	15.27	18491316
269	Phosphorylation	CYGMPGMSSLQDRHG HHCCCCCCCCCCCCC	33.54	18491316
293	Phosphorylation	GPLAPKGRKSRKKKS CCCCCCCCHHCCCCC	39.64	27251275
303	Phosphorylation	RKKKSKATQLSPEDR CCCCCCCCCCCHHHH	33.50	27050516
306	Phosphorylation	KSKATQLSPEDRVED CCCCCCCCHHHHHHH	19.20	21815630
349	Phosphorylation	GTSLQQDPEAPTVPK CCCCCCCCCCCCCCC	35.00	18491316
355	Phosphorylation	DPEAPTVPKKGRRKG CCCCCCCCCCCCCCC	34.81	18491316
392	Phosphorylation	EGTSAS--------- CCCCCC---------		27251275

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
61	S	Phosphorylation	Kinase	MAPK8	P45983	GPS
207	S	Phosphorylation	Kinase	MAPK8	P45983	GPS
306	S	Phosphorylation	Kinase	MAPK8	P45983	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NEIL1_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 NEIL1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DNLI3_HUMAN	LIG3	physical	15260972
DPOLB_HUMAN	POLB	physical	15260972
A4_HUMAN	APP	physical	21832049

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.