ANAG_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ANAG_HUMAN
• UniProt AC: P54802
• Protein Name: Alpha-N-acetylglucosaminidase
• Gene Name: NAGLU
• Organism: Homo sapiens (Human).
• Sequence Length: 743
• Subcellular Localization: Lysosome.
• Protein Description: Involved in the degradation of heparan sulfate..
• Protein Sequence: MEAVAVAAAVGVLLLAGAGGAAGDEAREAAAVRALVARLLGPGPAADFSVSVERALAAKPGLDTYSLGGGGAARVRVRGSTGVAAAAGLHRYLRDFCGCHVAWSGSQLRLPRPLPAVPGELTEATPNRYRYYQNVCTQSYSFVWWDWARWEREIDWMALNGINLALAWSGQEAIWQRVYLALGLTQAEINEFFTGPAFLAWGRMGNLHTWDGPLPPSWHIKQLYLQHRVLDQMRSFGMTPVLPAFAGHVPEAVTRVFPQVNVTKMGSWGHFNCSYSCSFLLAPEDPIFPIIGSLFLRELIKEFGTDHIYGADTFNEMQPPSSEPSYLAAATTAVYEAMTAVDTEAVWLLQGWLFQHQPQFWGPAQIRAVLGAVPRGRLLVLDLFAESQPVYTRTASFQGQPFIWCMLHNFGGNHGLFGALEAVNGGPEAARLFPNSTMVGTGMAPEGISQNEVVYSLMAELGWRKDPVPDLAAWVTSFAARRYGVSHPDAGAAWRLLLRSVYNCSGEACRGHNRSPLVRRPSLQMNTSIWYNRSDVFEAWRLLLTSAPSLATSPAFRYDLLDLTRQAVQELVSLYYEEARSAYLSKELASLLRAGGVLAYELLPALDEVLASDSRFLLGSWLEQARAAAVSEAEADFYEQNSRYQLTLWGPEGNILDYANKQLAGLVANYYTPRWRLFLEALVDSVAQGIPFQQHQFDKNVFQLEQAFVLSKQRYPSQPRGDTVDLAKKIFLKYYPRWVAGSW

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
59	Ubiquitination	VERALAAKPGLDTYS HHHHHHCCCCCCEEE	33.73	21890473
261	N-linked_Glycosylation	TRVFPQVNVTKMGSW HHHCCCEEEEECCCC	30.41	UniProtKB CARBOHYD
267	Phosphorylation	VNVTKMGSWGHFNCS EEEEECCCCCCCCCC	26.79	22210691
272	N-linked_Glycosylation	MGSWGHFNCSYSCSF CCCCCCCCCCCEECE	14.25	UniProtKB CARBOHYD
276	Phosphorylation	GHFNCSYSCSFLLAP CCCCCCCEECEEECC	6.23	22210691
435	N-linked_Glycosylation	EAARLFPNSTMVGTG HHHHHCCCCCEECCC	42.66	UniProtKB CARBOHYD
465	Ubiquitination	MAELGWRKDPVPDLA HHHHCCCCCCCCCHH	60.93	-
500	Phosphorylation	AWRLLLRSVYNCSGE HHHHHHHHHHCCCCC	28.99	-
503	N-linked_Glycosylation	LLLRSVYNCSGEACR HHHHHHHCCCCCCCC	16.01	UniProtKB CARBOHYD
526	N-linked_Glycosylation	RRPSLQMNTSIWYNR CCCCCCCCCEEEECH	20.08	UniProtKB CARBOHYD
532	N-linked_Glycosylation	MNTSIWYNRSDVFEA CCCEEEECHHHHHHH	23.22	19159218
553	Phosphorylation	SAPSLATSPAFRYDL CCHHHCCCCCHHHHH	14.50	24719451
558	Phosphorylation	ATSPAFRYDLLDLTR CCCCCHHHHHHHHHH	12.42	24114839
583	Phosphorylation	YEEARSAYLSKELAS HHHHHHHHHHHHHHH	16.86	19664995
586	Ubiquitination	ARSAYLSKELASLLR HHHHHHHHHHHHHHH	54.90	21890473
590	Phosphorylation	YLSKELASLLRAGGV HHHHHHHHHHHHCCH	40.33	24719451
631	Phosphorylation	QARAAAVSEAEADFY HHHHHHHHHHHHHHH	26.77	-
715	Phosphorylation	FVLSKQRYPSQPRGD HHHHCCCCCCCCCCC	12.54	-
717	Phosphorylation	LSKQRYPSQPRGDTV HHCCCCCCCCCCCHH	43.83	-

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ANAG_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 ANAG_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TMEDA_HUMAN	TMED10	physical	26344197
TMED4_HUMAN	TMED4	physical	26344197
TMED9_HUMAN	TMED9	physical	26344197

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 252920: Mucopolysaccharidosis 3B (MPS3B)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• DB00141: N-Acetyl-D-glucosamine

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"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-532, AND MASSSPECTROMETRY.
PubMed: 19159218