ASM_HUMAN - dbPTM
ASM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ASM_HUMAN
UniProt AC P17405
Protein Name Sphingomyelin phosphodiesterase
Gene Name SMPD1
Organism Homo sapiens (Human).
Sequence Length 629
Subcellular Localization Lysosome . Secreted .
Protein Description Converts sphingomyelin to ceramide. [PubMed: 1840600]
Protein Sequence MPRYGASLRQSCPRSGREQGQDGTAGAPGLLWMGLVLALALALALALSDSRVLWAPAEAHPLSPQGHPARLHRIVPRLRDVFGWGNLTCPICKGLFTAINLGLKKEPNVARVGSVAIKLCNLLKIAPPAVCQSIVHLFEDDMVEVWRRSVLSPSEACGLLLGSTCGHWDIFSSWNISLPTVPKPPPKPPSPPAPGAPVSRILFLTDLHWDHDYLEGTDPDCADPLCCRRGSGLPPASRPGAGYWGEYSKCDLPLRTLESLLSGLGPAGPFDMVYWTGDIPAHDVWHQTRQDQLRALTTVTALVRKFLGPVPVYPAVGNHESTPVNSFPPPFIEGNHSSRWLYEAMAKAWEPWLPAEALRTLRIGGFYALSPYPGLRLISLNMNFCSRENFWLLINSTDPAGQLQWLVGELQAAEDRGDKVHIIGHIPPGHCLKSWSWNYYRIVARYENTLAAQFFGHTHVDEFEVFYDEETLSRPLAVAFLAPSATTYIGLNPGYRVYQIDGNYSGSSHVVLDHETYILNLTQANIPGAIPHWQLLYRARETYGLPNTLPTAWHNLVYRMRGDMQLFQTFWFLYHKGHPPSEPCGTPCRLATLCAQLSARADSPALCRHLMPDGSLPEAQSLWPRPLFC
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 Orthologous
Protein Cluster
7Phosphorylation-MPRYGASLRQSCPR
-CCCCCCCHHHHCCC
21.5230631047
86N-linked_GlycosylationRDVFGWGNLTCPICK
HHHHCCCCCCCHHHH
26.1827349982
88N-linked_GlycosylationVFGWGNLTCPICKGL
HHCCCCCCCHHHHHH
21.8927349982
88N-linked_GlycosylationVFGWGNLTCPICKGL
HHCCCCCCCHHHHHH
21.8927349982
114PhosphorylationPNVARVGSVAIKLCN
CCCHHHHHHHHHHHH
12.9117322306
116PhosphorylationVARVGSVAIKLCNLL
CHHHHHHHHHHHHHH
8.5617322306
120S-nitrosylationGSVAIKLCNLLKIAP
HHHHHHHHHHHHHCC
2.6119483679
120S-nitrosocysteineGSVAIKLCNLLKIAP
HHHHHHHHHHHHHCC
2.61-
175N-linked_GlycosylationWDIFSSWNISLPTVP
HHHHHCCEECCCCCC
18.8727349982
177N-linked_GlycosylationIFSSWNISLPTVPKP
HHHCCEECCCCCCCC
25.6927349982
231PhosphorylationPLCCRRGSGLPPASR
CCHHCCCCCCCCCCC
35.0327251275
237PhosphorylationGSGLPPASRPGAGYW
CCCCCCCCCCCCCCC
44.7927251275
239PhosphorylationGLPPASRPGAGYWGE
CCCCCCCCCCCCCCC
34.1927251275
335N-linked_GlycosylationPPPFIEGNHSSRWLY
CCCCCCCCCCHHHHH
21.0527349982
337N-linked_GlycosylationPFIEGNHSSRWLYEA
CCCCCCCCHHHHHHH
26.1227349982
337N-linked_GlycosylationPFIEGNHSSRWLYEA
CCCCCCCCHHHHHHH
26.1227349982
395N-linked_GlycosylationENFWLLINSTDPAGQ
CCEEEEEECCCCHHH
38.5327349982
397N-linked_GlycosylationFWLLINSTDPAGQLQ
EEEEEECCCCHHHHH
41.3227349982
503N-linked_GlycosylationRVYQIDGNYSGSSHV
EEEEECCCCCCCEEE
24.8527349982
505N-linked_GlycosylationYQIDGNYSGSSHVVL
EEECCCCCCCEEEEE
35.8827349982
508PhosphorylationDGNYSGSSHVVLDHE
CCCCCCCEEEEECCC
24.6717698617
510PhosphorylationNYSGSSHVVLDHETY
CCCCCEEEEECCCEE
5.0317303575
520N-linked_GlycosylationDHETYILNLTQANIP
CCCEEEEEHHHCCCC
31.3327349982
522N-linked_GlycosylationETYILNLTQANIPGA
CEEEEEHHHCCCCCC
25.2727349982

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
510SPhosphorylationKinasePRKCDQ05655
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
510SPhosphorylation

20807762

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 ASM_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
OS9_HUMANOS9physical
26186194
AL3A2_HUMANALDH3A2physical
26186194
ALG11_HUMANALG11physical
26186194
S27A2_HUMANSLC27A2physical
26186194
CALX_HUMANCANXphysical
28514442
SE1L1_HUMANSEL1Lphysical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
257200Niemann-Pick disease A (NPDA)
607616Niemann-Pick disease B (NPDB)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ASM_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Functional characterization of the N-glycosylation sites of humanacid sphingomyelinase by site-directed mutagenesis.";
Ferlinz K., Hurwitz R., Moczall H., Lansmann S., Schuchman E.H.,Sandhoff K.;
Eur. J. Biochem. 243:511-517(1997).
Cited for: GLYCOSYLATION AT ASN-86; ASN-175; ASN-335; ASN-395 AND ASN-520.

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