NALD2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NALD2_HUMAN
• UniProt AC: Q9Y3Q0
• Protein Name: N-acetylated-alpha-linked acidic dipeptidase 2
• Gene Name: NAALAD2
• Organism: Homo sapiens (Human).
• Sequence Length: 740
• Subcellular Localization: Cell membrane ; Single-pass type II membrane protein .
• Protein Description: Has N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Also exhibits a dipeptidyl-peptidase IV type activity. Inactivate the peptide neurotransmitter N-acetylaspartylglutamate..
• Protein Sequence: MAESRGRLYLWMCLAAALASFLMGFMVGWFIKPLKETTTSVRYHQSIRWKLVSEMKAENIKSFLRSFTKLPHLAGTEQNFLLAKKIQTQWKKFGLDSAKLVHYDVLLSYPNETNANYISIVDEHETEIFKTSYLEPPPDGYENVTNIVPPYNAFSAQGMPEGDLVYVNYARTEDFFKLEREMGINCTGKIVIARYGKIFRGNKVKNAMLAGAIGIILYSDPADYFAPEVQPYPKGWNLPGTAAQRGNVLNLNGAGDPLTPGYPAKEYTFRLDVEEGVGIPRIPVHPIGYNDAEILLRYLGGIAPPDKSWKGALNVSYSIGPGFTGSDSFRKVRMHVYNINKITRIYNVVGTIRGSVEPDRYVILGGHRDSWVFGAIDPTSGVAVLQEIARSFGKLMSKGWRPRRTIIFASWDAEEFGLLGSTEWAEENVKILQERSIAYINSDSSIEGNYTLRVDCTPLLYQLVYKLTKEIPSPDDGFESKSLYESWLEKDPSPENKNLPRINKLGSGSDFEAYFQRLGIASGRARYTKNKKTDKYSSYPVYHTIYETFELVEKFYDPTFKKQLSVAQLRGALVYELVDSKIIPFNIQDYAEALKNYAASIYNLSKKHDQQLTDHGVSFDSLFSAVKNFSEAASDFHKRLIQVDLNNPIAVRMMNDQLMLLERAFIDPLGLPGKLFYRHIIFAPSSHNKYAGESFPGIYDAIFDIENKANSRLAWKEVKKHISIAAFTIQAAAGTLKEVL

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
43	Phosphorylation	ETTTSVRYHQSIRWK CCCCHHHHHHHHHHH	11.31	-
62	Phosphorylation	MKAENIKSFLRSFTK HHHHHHHHHHHHHCC	26.22	24719451
66	Phosphorylation	NIKSFLRSFTKLPHL HHHHHHHHHCCCHHH	39.14	24719451
111	N-linked_Glycosylation	DVLLSYPNETNANYI EEEECCCCCCCCCEE	61.56	19678840
143	N-linked_Glycosylation	PPPDGYENVTNIVPP CCCCCCCCCCCCCCC	37.11	UniProtKB CARBOHYD
185	N-linked_Glycosylation	LEREMGINCTGKIVI HHHHHCCCCCCEEEE	16.15	19678840
314	N-linked_Glycosylation	KSWKGALNVSYSIGP CCCCCCEEEEEEECC	21.83	UniProtKB CARBOHYD
328	Phosphorylation	PGFTGSDSFRKVRMH CCCCCCHHHHEEEEE	28.75	-
341	Acetylation	MHVYNINKITRIYNV EEEEEHHHHHEEEEE	41.48	12430273
449	N-linked_Glycosylation	SDSSIEGNYTLRVDC CCCCCCCCEEEEEEC	17.52	19678840
451	Phosphorylation	SSIEGNYTLRVDCTP CCCCCCEEEEEECHH	16.46	24719451
507	Phosphorylation	PRINKLGSGSDFEAY CCHHCCCCCCHHHHH	45.63	29759185
522	Phosphorylation	FQRLGIASGRARYTK HHHHCCCCCCCEECC	27.22	-
527	Phosphorylation	IASGRARYTKNKKTD CCCCCCEECCCCCCC	22.53	30576142
528	Phosphorylation	ASGRARYTKNKKTDK CCCCCEECCCCCCCC	23.69	30576142
603	N-linked_Glycosylation	NYAASIYNLSKKHDQ HHHHHHHCCCHHHCH	35.85	UniProtKB CARBOHYD
628	N-linked_Glycosylation	SLFSAVKNFSEAASD HHHHHHHCHHHHHHH	38.79	19678840

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

Oops, there are no upstream regulatory protein records of NALD2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NALD2_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 NALD2_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of NALD2_HUMAN !!

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

N-linked Glycosylation

"Structural insight into the evolutionary and pharmacologic homologyof glutamate carboxypeptidases II and III.";
Hlouchova K., Barinka C., Konvalinka J., Lubkowski J.;
FEBS J. 276:4448-4462(2009).
Cited for: X-RAY CRYSTALLOGRAPHY (1.29 ANGSTROMS) OF 36-740 ALONE AND IN COMPLEXWITH GLUTAMATE AND INHIBITORS, SUBUNIT, ZINC-BINDING SITES, ANDGLYCOSYLATION AT ASN-111; ASN-185; ASN-449 AND ASN-628.
PubMed: 19678840