NAR3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NAR3_HUMAN
• UniProt AC: Q13508
• Protein Name: Ecto-ADP-ribosyltransferase 3
• Gene Name: ART3
• Organism: Homo sapiens (Human).
• Sequence Length: 389
• Subcellular Localization: Cell membrane; Lipid-anchor, GPI-anchor.
• Protein Sequence: MKTGHFEIVTMLLATMILVDIFQVKAEVLDMADNAFDDEYLKCTDRMEIKYVPQLLKEEKASHQQLDTVWENAKAKWAARKTQIFLPMNFKDNHGIALMAYISEAQEQTPFYHLFSEAVKMAGQSREDYIYGFQFKAFHFYLTRALQLLRKPCEASSKTVVYRTSQGTSFTFGGLNQARFGHFTLAYSAKPQAANDQLTVLSIYTCLGVDIENFLDKESERITLIPLNEVFQVSQEGAGNNLILQSINKTCSHYECAFLGGLKTENCIENLEYFQPIYVYNPGEKNQKLEDHSEKNWKLEDHGEKNQKLEDHGVKILEPTQIPGMKIPEPFPLPEDKSQGNINNPTPGPVPVPGPKSHPSASSGKLLLPQFGMVIILISVSAINLFVAL

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
50	Acetylation	CTDRMEIKYVPQLLK CCCCCHHCCHHHHHH	27.21	25038526
57	Sumoylation	KYVPQLLKEEKASHQ CCHHHHHHHHHHHHH	72.86	-
57	Sumoylation	KYVPQLLKEEKASHQ CCHHHHHHHHHHHHH	72.86	-
101	Phosphorylation	HGIALMAYISEAQEQ CEEEEEEECHHHHHC	7.33	-
103	Phosphorylation	IALMAYISEAQEQTP EEEEEECHHHHHCCC	17.76	-
248	N-linked_Glycosylation	NLILQSINKTCSHYE CEEEHHHHHHCCHHH	38.54	UniProtKB CARBOHYD
250	Phosphorylation	ILQSINKTCSHYECA EEHHHHHHCCHHHHH	18.11	-
252	Phosphorylation	QSINKTCSHYECAFL HHHHHHCCHHHHHHH	34.04	-
254	Phosphorylation	INKTCSHYECAFLGG HHHHCCHHHHHHHCC	9.08	-
320	Phosphorylation	GVKILEPTQIPGMKI CCEECCCCCCCCCCC	29.74	28787133
346	O-linked_Glycosylation	QGNINNPTPGPVPVP CCCCCCCCCCCCCCC	42.89	22171320
362	GPI-anchor	PKSHPSASSGKLLLP CCCCCCCCCCCCCCC	43.92	-

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

Oops, there are no upstream regulatory protein records of NAR3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NAR3_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 NAR3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MDN1_HUMAN	MDN1	physical	26186194
AT12A_HUMAN	ATP12A	physical	26186194
PIGO_HUMAN	PIGO	physical	26186194
RB39B_HUMAN	RAB39B	physical	26186194
DD19B_HUMAN	DDX19B	physical	26186194
CHD1L_HUMAN	CHD1L	physical	26186194
DC2L1_HUMAN	DYNC2LI1	physical	26186194
AMD_HUMAN	PAM	physical	26186194
ANAG_HUMAN	NAGLU	physical	26186194
ARSK_HUMAN	ARSK	physical	26186194
HS12A_HUMAN	HSPA12A	physical	26186194
GPD1L_HUMAN	GPD1L	physical	26186194
ITA7_HUMAN	ITGA7	physical	26186194
MGT5A_HUMAN	MGAT5	physical	26186194
PGLT1_HUMAN	POGLUT1	physical	26186194
SPG7_HUMAN	SPG7	physical	26186194
PSN2_HUMAN	PSEN2	physical	26186194
MP2K2_HUMAN	MAP2K2	physical	26186194
SCAM2_HUMAN	SCAMP2	physical	26186194
GALT7_HUMAN	GALNT7	physical	26186194
ITA8_HUMAN	ITGA8	physical	26186194
AT12A_HUMAN	ATP12A	physical	28514442
ITA8_HUMAN	ITGA8	physical	28514442
ARSK_HUMAN	ARSK	physical	28514442
ANAG_HUMAN	NAGLU	physical	28514442
PGLT1_HUMAN	POGLUT1	physical	28514442
HS12A_HUMAN	HSPA12A	physical	28514442
AMD_HUMAN	PAM	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.

Related Literatures of Post-Translational Modification

O-linked Glycosylation

"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD.";
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
Mol. Cell. Proteomics 0:0-0(2011).
Cited for: GLYCOSYLATION AT THR-346, STRUCTURE OF CARBOHYDRATES, AND MASSSPECTROMETRY.
PubMed: 22171320