dbPTM

NAAA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NAAA_HUMAN
UniProt AC	Q02083
Protein Name	N-acylethanolamine-hydrolyzing acid amidase
Gene Name	NAAA
Organism	Homo sapiens (Human).
Sequence Length	359
Subcellular Localization	Lysosome .
Protein Description	Degrades bioactive fatty acid amides to their corresponding acids, with the following preference: N-palmitoylethanolamine > N-myristoylethanolamine > N-lauroylethanolamine = N-stearoylethanolamine > N-arachidonoylethanolamine > N-oleoylethanolamine. Also exhibits weak hydrolytic activity against the ceramides N-lauroylsphingosine and N-palmitoylsphingosine..
Protein Sequence	MRTADREARPGLPSLLLLLLAGAGLSAASPPAAPRFNVSLDSVPELRWLPVLRHYDLDLVRAAMAQVIGDRVPKWVHVLIGKVVLELERFLPQPFTGEIRGMCDFMNLSLADCLLVNLAYESSVFCTSIVAQDSRGHIYHGRNLDYPFGNVLRKLTVDVQFLKNGQIAFTGTTFIGYVGLWTGQSPHKFTVSGDERDKGWWWENAIAALFRRHIPVSWLIRATLSESENFEAAVGKLAKTPLIADVYYIVGGTSPREGVVITRNRDGPADIWPLDPLNGAWFRVETNYDHWKPAPKEDDRRTSAIKALNATGQANLSLEALFQILSVVPVYNNFTIYTTVMSAGSPDKYMTRIRNPSRK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
37	N-linked_Glycosylation	PPAAPRFNVSLDSVP CCCCCCCCCCCCCCC	24.61	30301806
39	O-linked_Glycosylation	AAPRFNVSLDSVPEL CCCCCCCCCCCCCHH	27.80	28657654
107	N-linked_Glycosylation	RGMCDFMNLSLADCL HHHHHHCCCCHHHHH	26.86	22040171
239	Ubiquitination	AAVGKLAKTPLIADV HHHHHHHCCCEEEEE	62.20	-
292	Ubiquitination	ETNYDHWKPAPKEDD EECCCCCCCCCCCCC	28.07	-
309	N-linked_Glycosylation	TSAIKALNATGQANL HHHHHHHHHHCCCCC	40.07	17980170
333	N-linked_Glycosylation	SVVPVYNNFTIYTTV HCEEEECCEEEEEEE	20.11	17980170

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 NAAA_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NAAA_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 NAAA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
TMEM2_HUMAN	TMEM2	physical	26186194
TECT2_HUMAN	TCTN2	physical	26186194
T132A_HUMAN	TMEM132A	physical	26186194
ENTP6_HUMAN	ENTPD6	physical	26186194
PGLT1_HUMAN	POGLUT1	physical	26186194
MANEL_HUMAN	MANEAL	physical	26186194
S38AA_HUMAN	SLC38A10	physical	26186194
ARSK_HUMAN	ARSK	physical	26186194
GALNS_HUMAN	GALNS	physical	26186194
OAF_HUMAN	OAF	physical	26186194
EXT1_HUMAN	EXT1	physical	26186194
SYVN1_HUMAN	SYVN1	physical	26186194
OS9_HUMAN	OS9	physical	26186194
TTC17_HUMAN	TTC17	physical	26186194
SCRB1_HUMAN	SCARB1	physical	26186194
SC65_HUMAN	P3H4	physical	26186194
TBA1A_HUMAN	TUBA1A	physical	26186194
UGDH_HUMAN	UGDH	physical	26186194
EDEM1_HUMAN	EDEM1	physical	26186194
ANAG_HUMAN	NAGLU	physical	26186194
TBB8_HUMAN	TUBB8	physical	26186194
SULF2_HUMAN	SULF2	physical	26186194
NDST1_HUMAN	NDST1	physical	26186194
MA2A1_HUMAN	MAN2A1	physical	26186194
SPHM_HUMAN	SGSH	physical	26186194
NHLC3_HUMAN	NHLRC3	physical	26186194
NXPH4_HUMAN	NXPH4	physical	26186194
NB5R1_HUMAN	CYB5R1	physical	26186194
GLBL2_HUMAN	GLB1L2	physical	26186194
ZN507_HUMAN	ZNF507	physical	26186194
SC24D_HUMAN	SEC24D	physical	26186194
CLN5_HUMAN	CLN5	physical	26186194
BMP7_HUMAN	BMP7	physical	26186194
NRP2_HUMAN	NRP2	physical	26186194
ARSB_HUMAN	ARSB	physical	26186194
CNTP3_HUMAN	CNTNAP3	physical	26186194
SMG8_HUMAN	SMG8	physical	26186194
PCSK5_HUMAN	PCSK5	physical	26186194
FUT11_HUMAN	FUT11	physical	26186194
DCBD2_HUMAN	DCBLD2	physical	26186194
ERF_HUMAN	ERF	physical	26186194
ITA4_HUMAN	ITGA4	physical	26186194
CHSTC_HUMAN	CHST12	physical	26186194
PLTP_HUMAN	PLTP	physical	26186194
MA2B2_HUMAN	MAN2B2	physical	26186194
EDEM2_HUMAN	EDEM2	physical	26186194
WDR73_HUMAN	WDR73	physical	26186194
MA2B2_HUMAN	MAN2B2	physical	28514442
EDEM1_HUMAN	EDEM1	physical	28514442
ARSB_HUMAN	ARSB	physical	28514442
NDST1_HUMAN	NDST1	physical	28514442
ARSK_HUMAN	ARSK	physical	28514442
OAF_HUMAN	OAF	physical	28514442
TMEM2_HUMAN	TMEM2	physical	28514442
FUT11_HUMAN	FUT11	physical	28514442
CNTP3_HUMAN	CNTNAP3	physical	28514442
PCSK5_HUMAN	PCSK5	physical	28514442
SULF2_HUMAN	SULF2	physical	28514442
ANAG_HUMAN	NAGLU	physical	28514442
PLTP_HUMAN	PLTP	physical	28514442
DCBD2_HUMAN	DCBLD2	physical	28514442
ITA4_HUMAN	ITGA4	physical	28514442
PGLT1_HUMAN	POGLUT1	physical	28514442
GALNS_HUMAN	GALNS	physical	28514442
NB5R1_HUMAN	CYB5R1	physical	28514442
ITAV_HUMAN	ITGAV	physical	28514442
SYVN1_HUMAN	SYVN1	physical	28514442
UGDH_HUMAN	UGDH	physical	28514442
NRP2_HUMAN	NRP2	physical	28514442
TECT1_HUMAN	TCTN1	physical	28514442
EDEM2_HUMAN	EDEM2	physical	28514442
T132A_HUMAN	TMEM132A	physical	28514442
TBB8_HUMAN	TUBB8	physical	28514442
S23IP_HUMAN	SEC23IP	physical	28514442
EXT1_HUMAN	EXT1	physical	28514442
BMP7_HUMAN	BMP7	physical	28514442
ERF_HUMAN	ERF	physical	28514442
OS9_HUMAN	OS9	physical	28514442
TTC17_HUMAN	TTC17	physical	28514442
MANEL_HUMAN	MANEAL	physical	28514442
TBA4A_HUMAN	TUBA4A	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.

Regulatory Network of NAAA_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"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-37, AND MASS SPECTROMETRY.	19159218 [Abstract]