dbPTM

ASAH1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ASAH1_HUMAN
UniProt AC	Q13510
Protein Name	Acid ceramidase
Gene Name	ASAH1
Organism	Homo sapiens (Human).
Sequence Length	395
Subcellular Localization	Lysosome.
Protein Description	Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid..
Protein Sequence	MPGRSCVALVLLAAAVSCAVAQHAPPWTEDCRKSTYPPSGPTYRGAVPWYTINLDLPPYKRWHELMLDKAPVLKVIVNSLKNMINTFVPSGKIMQVVDEKLPGLLGNFPGPFEEEMKGIAAVTDIPLGEIISFNIFYELFTICTSIVAEDKKGHLIHGRNMDFGVFLGWNINNDTWVITEQLKPLTVNLDFQRNNKTVFKASSFAGYVGMLTGFKPGLFSLTLNERFSINGGYLGILEWILGKKDVMWIGFLTRTVLENSTSYEEAKNLLTKTKILAPAYFILGGNQSGEGCVITRDRKESLDVYELDAKQGRWYVVQTNYDRWKHPFFLDDRRTPAKMCLNRTSQENISFETMYDVLSTKPVLNKLTVYTTLIDVTKGQFETYLRDCPDPCIGW

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
39	Phosphorylation	RKSTYPPSGPTYRGA HHCCCCCCCCCCCCC	53.55	-
42	Phosphorylation	TYPPSGPTYRGAVPW CCCCCCCCCCCCCCE	29.40	-
43	Phosphorylation	YPPSGPTYRGAVPWY CCCCCCCCCCCCCEE	15.35	-
86	Phosphorylation	SLKNMINTFVPSGKI HHHHHHHHHCCCCCH	18.32	21406692
90	Phosphorylation	MINTFVPSGKIMQVV HHHHHCCCCCHHHHH	47.63	21406692
92 (in isoform 1)	Ubiquitination	-	39.07	21890473
92	Ubiquitination	NTFVPSGKIMQVVDE HHHCCCCCHHHHHCC	39.07	2189047
100	Ubiquitination	IMQVVDEKLPGLLGN HHHHHCCCCCCHHCC	56.36	-
108 (in isoform 2)	Ubiquitination	-	7.60	21890473
123	Phosphorylation	MKGIAAVTDIPLGEI HCCEEEEECCCHHHH	24.39	22210691
132	Phosphorylation	IPLGEIISFNIFYEL CCHHHHHHHHHHHHH	20.22	22210691
137	Phosphorylation	IISFNIFYELFTICT HHHHHHHHHHHHHHH	14.13	22210691
173	N-linked_Glycosylation	FLGWNINNDTWVITE EEEEEECCCEEEEEE	44.27	29692406
195	N-linked_Glycosylation	NLDFQRNNKTVFKAS EEECCCCCCEEEEEH	43.49	UniProtKB CARBOHYD
197	Phosphorylation	DFQRNNKTVFKASSF ECCCCCCEEEEEHHH	33.04	-
202	Phosphorylation	NKTVFKASSFAGYVG CCEEEEEHHHHHHHH	26.95	-
253	Phosphorylation	VMWIGFLTRTVLENS EEEHHHHHHHHHHCC	23.25	-
255	Phosphorylation	WIGFLTRTVLENSTS EHHHHHHHHHHCCCC	24.98	-
259	N-linked_Glycosylation	LTRTVLENSTSYEEA HHHHHHHCCCCHHHH	46.56	16263699
272	Ubiquitination	EAKNLLTKTKILAPA HHHHHHHHHHEEECE	48.03	-
273	Phosphorylation	AKNLLTKTKILAPAY HHHHHHHHHEEECEE	20.34	30576142
280	Phosphorylation	TKILAPAYFILGGNQ HHEEECEEEECCCCC	7.06	30576142
286	N-linked_Glycosylation	AYFILGGNQSGEGCV EEEECCCCCCCCCEE	30.92	12754519
295	Phosphorylation	SGEGCVITRDRKESL CCCCEEEECCCCCCE	13.20	30576142
299	Ubiquitination	CVITRDRKESLDVYE EEEECCCCCCEEEEE	56.81	-
301	Phosphorylation	ITRDRKESLDVYELD EECCCCCCEEEEEEE	32.67	23312004
305	Phosphorylation	RKESLDVYELDAKQG CCCCEEEEEEECCCC	15.50	-
310	Ubiquitination	DVYELDAKQGRWYVV EEEEEECCCCCEEEE	53.61	-
342	N-linked_Glycosylation	TPAKMCLNRTSQENI CCHHHHCCCCCCCCC	40.01	29692406
348	N-linked_Glycosylation	LNRTSQENISFETMY CCCCCCCCCCHHHHH	27.80	UniProtKB CARBOHYD
359	Phosphorylation	ETMYDVLSTKPVLNK HHHHHHHCCCHHHCC	33.94	-
360	Phosphorylation	TMYDVLSTKPVLNKL HHHHHHCCCHHHCCE	34.90	-

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 ASAH1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ASAH1_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 ASAH1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SETB1_HUMAN	SETDB1	physical	16169070
T22D1_HUMAN	TSC22D1	physical	16169070
KCC1D_HUMAN	CAMK1D	physical	21988832
NFH_HUMAN	NEFH	physical	26186194
KCC2B_HUMAN	CAMK2B	physical	26186194
NONO_HUMAN	NONO	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
228000	Farber lipogranulomatosis (FL)
159950	Spinal muscular atrophy with progressive myoclonic epilepsy (SMAPME)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ASAH1_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-259 AND ASN-286, AND MASSSPECTROMETRY.	19159218 [Abstract]
"Elucidation of N-glycosylation sites on human platelet proteins: aglycoproteomic approach."; Lewandrowski U., Moebius J., Walter U., Sickmann A.; Mol. Cell. Proteomics 5:226-233(2006). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-259, AND MASSSPECTROMETRY.	16263699 [Abstract]
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-259, AND MASSSPECTROMETRY.	16335952 [Abstract]
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry."; Zhang H., Li X.-J., Martin D.B., Aebersold R.; Nat. Biotechnol. 21:660-666(2003). Cited for: GLYCOSYLATION AT ASN-259 AND ASN-286.	12754519 [Abstract]