NSMA2_HUMAN - dbPTM
NSMA2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NSMA2_HUMAN
UniProt AC Q9NY59
Protein Name Sphingomyelin phosphodiesterase 3
Gene Name SMPD3
Organism Homo sapiens (Human).
Sequence Length 655
Subcellular Localization Golgi apparatus membrane
Lipid-anchor . Cell membrane
Lipid-anchor . May localize to detergent-resistant subdomains of Golgi membranes of hypothalamic neurosecretory neurons (PubMed:10823942). Localizes to plasma membrane in confluent contact-inh
Protein Description Catalyzes the hydrolysis of sphingomyelin to form ceramide and phosphocholine. Ceramide mediates numerous cellular functions, such as apoptosis and growth arrest, and is capable of regulating these 2 cellular events independently. Also hydrolyzes sphingosylphosphocholine. Regulates the cell cycle by acting as a growth suppressor in confluent cells. Probably acts as a regulator of postnatal development and participates in bone and dentin mineralization..
Protein Sequence MVLYTTPFPNSCLSALHCVSWALIFPCYWLVDRLAASFIPTTYEKRQRADDPCCLQLLCTALFTPIYLALLVASLPFAFLGFLFWSPLQSARRPYIYSRLEDKGLAGGAALLSEWKGTGPGKSFCFATANVCLLPDSLARVNNLFNTQARAKEIGQRIRNGAARPQIKIYIDSPTNTSISAASFSSLVSPQGGDGVARAVPGSIKRTASVEYKGDGGRHPGDEAANGPASGDPVDSSSPEDACIVRIGGEEGGRPPEADDPVPGGQARNGAGGGPRGQTPNHNQQDGDSGSLGSPSASRESLVKGRAGPDTSASGEPGANSKLLYKASVVKKAAARRRRHPDEAFDHEVSAFFPANLDFLCLQEVFDKRAATKLKEQLHGYFEYILYDVGVYGCQGCCSFKCLNSGLLFASRYPIMDVAYHCYPNKCNDDALASKGALFLKVQVGSTPQDQRIVGYIACTHLHAPQEDSAIRCGQLDLLQDWLADFRKSTSSSSAANPEELVAFDVVCGDFNFDNCSSDDKLEQQHSLFTHYRDPCRLGPGEEKPWAIGTLLDTNGLYDEDVCTPDNLQKVLESEEGRREYLAFPTSKSSGQKGRKELLKGNGRRIDYMLHAEEGLCPDWKAEVEEFSFITQLSGLTDHLPVAMRLMVSSGEEEA
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
53S-palmitoylationRQRADDPCCLQLLCT
HHCCCCHHHHHHHHH		4.68-
54S-palmitoylationQRADDPCCLQLLCTA
HCCCCHHHHHHHHHH		3.10-
59S-palmitoylationPCCLQLLCTALFTPI
HHHHHHHHHHHHHHH		2.58-
98PhosphorylationARRPYIYSRLEDKGL
CCCCHHHHHHHHCCC		22.3424719451
152AcetylationFNTQARAKEIGQRIR
HCHHHHHHHHHHHHH		44.2925953088
173PhosphorylationQIKIYIDSPTNTSIS
CEEEEEECCCCCEEE		24.8626657352
175PhosphorylationKIYIDSPTNTSISAA
EEEEECCCCCEEEHH		55.8926657352
177PhosphorylationYIDSPTNTSISAASF
EEECCCCCEEEHHHH		29.8926657352
178PhosphorylationIDSPTNTSISAASFS
EECCCCCEEEHHHHH		19.3326657352
180PhosphorylationSPTNTSISAASFSSL
CCCCCEEEHHHHHHC		19.9726657352
183PhosphorylationNTSISAASFSSLVSP
CCEEEHHHHHHCCCC		25.9426657352
186PhosphorylationISAASFSSLVSPQGG
EEHHHHHHCCCCCCC		30.6825921289
203PhosphorylationVARAVPGSIKRTASV
HHHCCCCCEEEEEEE		20.9023312004
207PhosphorylationVPGSIKRTASVEYKG
CCCCEEEEEEEEEEC		20.4826657352
209PhosphorylationGSIKRTASVEYKGDG
CCEEEEEEEEEECCC		18.1826657352
212PhosphorylationKRTASVEYKGDGGRH
EEEEEEEEECCCCCC		20.3723312004
236PhosphorylationASGDPVDSSSPEDAC
CCCCCCCCCCCCCCE		32.7126657352
237PhosphorylationSGDPVDSSSPEDACI
CCCCCCCCCCCCCEE		45.5123312004
238PhosphorylationGDPVDSSSPEDACIV
CCCCCCCCCCCCEEE		35.9423312004
279PhosphorylationGGGPRGQTPNHNQQD
CCCCCCCCCCCCCCC		28.9623684312
289PhosphorylationHNQQDGDSGSLGSPS
CCCCCCCCCCCCCCC		35.4926657352
291PhosphorylationQQDGDSGSLGSPSAS
CCCCCCCCCCCCCCC		33.2426657352
294PhosphorylationGDSGSLGSPSASRES
CCCCCCCCCCCCHHH		22.4529116813
296PhosphorylationSGSLGSPSASRESLV
CCCCCCCCCCHHHHH		40.3423684312
298PhosphorylationSLGSPSASRESLVKG
CCCCCCCCHHHHHCC		40.7023684312
301PhosphorylationSPSASRESLVKGRAG
CCCCCHHHHHCCCCC		37.0324505115
312PhosphorylationGRAGPDTSASGEPGA
CCCCCCCCCCCCCCC		28.0229116813
314PhosphorylationAGPDTSASGEPGANS
CCCCCCCCCCCCCCC		43.3829116813
321PhosphorylationSGEPGANSKLLYKAS
CCCCCCCCHHHHHHH		24.9329116813
325PhosphorylationGANSKLLYKASVVKK
CCCCHHHHHHHHHHH		18.2323312004
328PhosphorylationSKLLYKASVVKKAAA
CHHHHHHHHHHHHHH		24.2427966365
397S-palmitoylationGVYGCQGCCSFKCLN
CCCCCCCCHHHEECC		0.48-
398S-palmitoylationVYGCQGCCSFKCLNS
CCCCCCCHHHEECCC		7.38-
435UbiquitinationNDDALASKGALFLKV
CHHHHHHCCCEEEEE		42.47-
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 NSMA2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NSMA2_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 NSMA2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CAV1_HUMANCAV1physical
28514442
ENDD1_HUMANENDOD1physical
28514442
STOM_HUMANSTOMphysical
28514442
TM135_HUMANTMEM135physical
28514442
CANB1_HUMANPPP3R1physical
28514442
VPP1_HUMANATP6V0A1physical
28514442
SOAT1_HUMANSOAT1physical
28514442
PP2BA_HUMANPPP3CAphysical
28514442
APOB_HUMANAPOBphysical
28514442
EED_HUMANEEDphysical
20080539
RACK1_HUMANGNB2L1physical
20080539
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NSMA2_HUMAN

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Related Literatures of Post-Translational Modification

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