NTAN1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NTAN1_HUMAN
• UniProt AC: Q96AB6
• Protein Name: Protein N-terminal asparagine amidohydrolase
• Gene Name: NTAN1
• Organism: Homo sapiens (Human).
• Sequence Length: 310
• Subcellular Localization: Cytoplasm .
• Protein Description: N-terminal asparagine deamidase that mediates deamidation of N-terminal asparagine residues to aspartate. Required for the ubiquitin-dependent turnover of intracellular proteins that initiate with Met-Asn. These proteins are acetylated on the retained initiator methionine and can subsequently be modified by the removal of N-acetyl methionine by acylaminoacid hydrolase (AAH). Conversion of the resulting N-terminal asparagine to aspartate by PNAD renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. This enzyme does not act on substrates with internal or C-terminal asparagines and does not act on glutamine residues in any position, nor on acetylated N-terminal peptidyl Asn..
• Protein Sequence: MPLLVEGRRVRLPQSAGDLVRAHPPLEERARLLRGQSVQQVGPQGLLYVQQRELAVTSPKDGSISILGSDDATTCHIVVLRHTGNGATCLTHCDGTDTKAEVPLIMNSIKSFSDHAQCGRLEVHLVGGFSDDRQLSQKLTHQLLSEFDRQEDDIHLVTLCVTELNDREENENHFPVIYGIAVNIKTAEIYRASFQDRGPEEQLRAARTLAGGPMISIYDAETEQLRIGPYSWTPFPHVDFWLHQDDKQILENLSTSPLAEPPHFVEHIRSTLMFLKKHPSPAHTLFSGNKALLYKKNEDGLWEKISSPGS

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
15	Phosphorylation	RRVRLPQSAGDLVRA CEEECCCCHHHHHHC	32.07	22210691
37	Phosphorylation	ARLLRGQSVQQVGPQ HHHHCCCCHHHHCCC	25.39	24043423
48	Phosphorylation	VGPQGLLYVQQRELA HCCCCEEEEEEEEEE	10.97	24043423
58	Phosphorylation	QRELAVTSPKDGSIS EEEEEEECCCCCCEE	24.29	22985185
63	Phosphorylation	VTSPKDGSISILGSD EECCCCCCEEEECCC	24.24	29759185
65	Phosphorylation	SPKDGSISILGSDDA CCCCCCEEEECCCCC	17.29	29759185
69	Phosphorylation	GSISILGSDDATTCH CCEEEECCCCCCEEE	28.95	29759185
280	Phosphorylation	MFLKKHPSPAHTLFS HHHHHCCCCHHHCCC	34.14	25159151
294	Phosphorylation	SGNKALLYKKNEDGL CCCEEEEEEECCCCC	22.29	27762562
295	Acetylation	GNKALLYKKNEDGLW CCEEEEEEECCCCCC	49.44	20167786

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

Oops, there are no upstream regulatory protein records of NTAN1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NTAN1_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
280	Phosphorylation	283 (3)	H ⇒ N;Y	rs1136001	Height	20189936 24823311

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RIPK1_HUMAN	RIPK1	physical	26186194
RIPK1_HUMAN	RIPK1	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.