ASM3A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ASM3A_HUMAN
• UniProt AC: Q92484
• Protein Name: Acid sphingomyelinase-like phosphodiesterase 3a
• Gene Name: SMPDL3A
• Organism: Homo sapiens (Human).
• Sequence Length: 453
• Subcellular Localization: Secreted .
• Protein Description: Has in vitro nucleotide phosphodiesterase activity with nucleoside triphosphates, such as ATP. [PubMed: 25288789]
• Protein Sequence: MALVRALVCCLLTAWHCRSGLGLPVAPAGGRNPPPAIGQFWHVTDLHLDPTYHITDDHTKVCASSKGANASNPGPFGDVLCDSPYQLILSAFDFIKNSGQEASFMIWTGDSPPHVPVPELSTDTVINVITNMTTTIQSLFPNLQVFPALGNHDYWPQDQLPVVTSKVYNAVANLWKPWLDEEAISTLRKGGFYSQKVTTNPNLRIISLNTNLYYGPNIMTLNKTDPANQFEWLESTLNNSQQNKEKVYIIAHVPVGYLPSSQNITAMREYYNEKLIDIFQKYSDVIAGQFYGHTHRDSIMVLSDKKGSPVNSLFVAPAVTPVKSVLEKQTNNPGIRLFQYDPRDYKLLDMLQYYLNLTEANLKGESIWKLEYILTQTYDIEDLQPESLYGLAKQFTILDSKQFIKYYNYFFVSYDSSVTCDKTCKAFQICAIMNLDNISYADCLKQLYIKHNY

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
69	N-linked_Glycosylation	CASSKGANASNPGPF ECCCCCCCCCCCCCC	53.20	26783088
131	N-linked_Glycosylation	TVINVITNMTTTIQS HHHHHHHCCCHHHHH	18.06	26783088
198	Phosphorylation	GFYSQKVTTNPNLRI CCCCCEECCCCCCEE	28.08	24043423
199	Phosphorylation	FYSQKVTTNPNLRII CCCCEECCCCCCEEE	52.22	24043423
207	Phosphorylation	NPNLRIISLNTNLYY CCCCEEEECCCCEEE	17.13	24043423
210	Phosphorylation	LRIISLNTNLYYGPN CEEEECCCCEEECCC	31.71	24043423
213	Phosphorylation	ISLNTNLYYGPNIMT EECCCCEEECCCEEC	14.40	24043423
214	Phosphorylation	SLNTNLYYGPNIMTL ECCCCEEECCCEECC	29.31	24043423
220	Phosphorylation	YYGPNIMTLNKTDPA EECCCEECCCCCCCC	24.31	24043423
222	N-linked_Glycosylation	GPNIMTLNKTDPANQ CCCEECCCCCCCCHH	35.69	19159218
224	Phosphorylation	NIMTLNKTDPANQFE CEECCCCCCCCHHHH	46.25	29978859
235	Phosphorylation	NQFEWLESTLNNSQQ HHHHHHHHHCCCCCC	35.70	29978859
236	Phosphorylation	QFEWLESTLNNSQQN HHHHHHHHCCCCCCC	24.91	29978859
238	N-linked_Glycosylation	EWLESTLNNSQQNKE HHHHHHCCCCCCCCC	46.31	UniProtKB CARBOHYD
240	Phosphorylation	LESTLNNSQQNKEKV HHHHCCCCCCCCCCE	31.88	29978859
263	N-linked_Glycosylation	GYLPSSQNITAMREY CCCCCCCCHHHHHHH	35.21	19159218
291	Phosphorylation	DVIAGQFYGHTHRDS HHHHHHCCCCCCCCE	10.50	-
303	Phosphorylation	RDSIMVLSDKKGSPV CCEEEEEECCCCCCC	35.65	23532336
356	N-linked_Glycosylation	DMLQYYLNLTEANLK HHHHHHHHHHHHCCC	28.88	26783088
372	Phosphorylation	ESIWKLEYILTQTYD CHHEEEEEEEEECCC	16.21	-
377	Phosphorylation	LEYILTQTYDIEDLQ EEEEEEECCCHHHCC	20.23	-
378	Phosphorylation	EYILTQTYDIEDLQP EEEEEECCCHHHCCH	12.71	-
437	N-linked_Glycosylation	CAIMNLDNISYADCL HHEEECCCCCHHHHH	28.42	UniProtKB CARBOHYD

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

Oops, there are no upstream regulatory protein records of ASM3A_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ASM3A_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 ASM3A_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of ASM3A_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

"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-222; ASN-263 AND ASN-356,AND MASS SPECTROMETRY.
PubMed: 19159218