dbPTM

NAGAB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NAGAB_HUMAN
UniProt AC	P17050
Protein Name	Alpha-N-acetylgalactosaminidase
Gene Name	NAGA
Organism	Homo sapiens (Human).
Sequence Length	411
Subcellular Localization	Lysosome.
Protein Description	Removes terminal alpha-N-acetylgalactosamine residues from glycolipids and glycopeptides. Required for the breakdown of glycolipids..
Protein Sequence	MLLKTVLLLGHVAQVLMLDNGLLQTPPMGWLAWERFRCNINCDEDPKNCISEQLFMEMADRMAQDGWRDMGYTYLNIDDCWIGGRDASGRLMPDPKRFPHGIPFLADYVHSLGLKLGIYADMGNFTCMGYPGTTLDKVVQDAQTFAEWKVDMLKLDGCFSTPEERAQGYPKMAAALNATGRPIAFSCSWPAYEGGLPPRVNYSLLADICNLWRNYDDIQDSWWSVLSILNWFVEHQDILQPVAGPGHWNDPDMLLIGNFGLSLEQSRAQMALWTVLAAPLLMSTDLRTISAQNMDILQNPLMIKINQDPLGIQGRRIHKEKSLIEVYMRPLSNKASALVFFSCRTDMPYRYHSSLGQLNFTGSVIYEAQDVYSGDIISGLRDETNFTVIINPSGVVMWYLYPIKNLEMSQQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
72	Phosphorylation	DGWRDMGYTYLNIDD CCCHHHCCEEEEECC	5.88	24114839
73	Phosphorylation	GWRDMGYTYLNIDDC CCHHHCCEEEEECCC	18.79	24114839
74	Phosphorylation	WRDMGYTYLNIDDCW CHHHCCEEEEECCCE	6.83	24114839
124	N-linked_Glycosylation	GIYADMGNFTCMGYP EEEEECCCEEECCCC	23.55	19683538
160	Phosphorylation	LKLDGCFSTPEERAQ EECCCCCCCHHHHHC	47.32	27251275
161	Phosphorylation	KLDGCFSTPEERAQG ECCCCCCCHHHHHCC	17.92	27251275
177	N-linked_Glycosylation	PKMAAALNATGRPIA HHHHHHHHCCCCCEE	30.63	19683538
201	N-linked_Glycosylation	GGLPPRVNYSLLADI CCCCCCCCHHHHHHH	23.19	16399764
201	N-linked_Glycosylation	GGLPPRVNYSLLADI CCCCCCCCHHHHHHH	23.19	16399764
288	Phosphorylation	LMSTDLRTISAQNMD HHCCCCCHHCCCCCH	26.95	21406692
290	Phosphorylation	STDLRTISAQNMDIL CCCCCHHCCCCCHHH	24.16	21406692
304	Ubiquitination	LQNPLMIKINQDPLG HCCCEEEEECCCCCC	22.95	21906983
322	Phosphorylation	RRIHKEKSLIEVYMR CCCCCCCCCEEEECH	35.35	26074081
327	Phosphorylation	EKSLIEVYMRPLSNK CCCCEEEECHHCCCC	3.74	26074081
332	Phosphorylation	EVYMRPLSNKASALV EEECHHCCCCCCEEE	38.68	11251574
336	Phosphorylation	RPLSNKASALVFFSC HHCCCCCCEEEEEEE	24.60	26074081
342	Phosphorylation	ASALVFFSCRTDMPY CCEEEEEEECCCCCC	7.39	26074081
345	Phosphorylation	LVFFSCRTDMPYRYH EEEEEECCCCCCCCC	40.76	26074081
349	Phosphorylation	SCRTDMPYRYHSSLG EECCCCCCCCCCCCC	19.71	26074081
359	N-linked_Glycosylation	HSSLGQLNFTGSVIY CCCCCCCCCCCEEEE	25.25	UniProtKB CARBOHYD
366	Phosphorylation	NFTGSVIYEAQDVYS CCCCEEEEEEEEECC	11.76	-
372	Phosphorylation	IYEAQDVYSGDIISG EEEEEEECCCCCCEE	18.41	-
378	Phosphorylation	VYSGDIISGLRDETN ECCCCCCEECCCCCC	31.91	24719451
385	N-linked_Glycosylation	SGLRDETNFTVIINP EECCCCCCEEEEECC	28.66	19683538

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

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NAGAB_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
Oops, there are no SNP-PTM records of NAGAB_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
A4_HUMAN	APP	physical	21832049

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
609241	Schindler disease (SCHIND)
609242	Kanzaki disease (KANZD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of NAGAB_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"The 1.9 A structure of human alpha-N-acetylgalactosaminidase: themolecular basis of Schindler and Kanzaki diseases."; Clark N.E., Garman S.C.; J. Mol. Biol. 393:435-447(2009). Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 18-411 IN COMPLEXES WITHN-ACETYLGALACTOSAMINE AND GALACTOSE, DISULFIDE BONDS, GLYCOSYLATION ATASN-124; ASN-177 AND ASN-385, SUBUNIT, CATALYTIC ACTIVITY, ANDMUTAGENESIS OF ASN-201.	19683538 [Abstract]
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-177 AND ASN-201, AND MASSSPECTROMETRY.	19159218 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction."; Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.; Mol. Cell. Proteomics 6:1952-1967(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322 AND SER-332, ANDMASS SPECTROMETRY.	17693683 [Abstract]