SMS2_HUMAN - dbPTM
SMS2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMS2_HUMAN
UniProt AC Q8NHU3
Protein Name Phosphatidylcholine:ceramide cholinephosphotransferase 2
Gene Name SGMS2
Organism Homo sapiens (Human).
Sequence Length 365
Subcellular Localization Cell membrane
Multi-pass membrane protein. Golgi apparatus membrane
Multi-pass membrane protein. Predominantly plasma membrane, some in Golgi apparatus. Some localization in the perinuclear region where it colocalizes with a sialyltransferase.
Protein Description Sphingomyelin synthases synthesize the sphingolipid, sphingomyelin, through transfer of the phosphatidyl head group, phosphatidylcholine, on to the primary hydroxyl of ceramide. The reaction is bidirectional depending on the respective levels of the sphingolipid and ceramide. Plasma membrane SMS2 can also convert phosphatidylethanolamine (PE) to ceramide phosphatidylethanolamine (CPE). Major form in liver. Required for cell growth in certain cell types. Regulator of cell surface levels of ceramide, an important mediator of signal transduction and apoptosis. Regulation of sphingomyelin (SM) levels at the cell surface affects insulin sensitivity..
Protein Sequence MDIIETAKLEEHLENQPSDPTNTYARPAEPVEEENKNGNGKPKSLSSGLRKGTKKYPDYIQIAMPTESRNKFPLEWWKTGIAFIYAVFNLVLTTVMITVVHERVPPKELSPPLPDKFFDYIDRVKWAFSVSEINGIILVGLWITQWLFLRYKSIVGRRFCFIIGTLYLYRCITMYVTTLPVPGMHFQCAPKLNGDSQAKVQRILRLISGGGLSITGSHILCGDFLFSGHTVTLTLTYLFIKEYSPRHFWWYHLICWLLSAAGIICILVAHEHYTIDVIIAYYITTRLFWWYHSMANEKNLKVSSQTNFLSRAWWFPIFYFFEKNVQGSIPCCFSWPLSWPPGCFKSSCKKYSRVQKIGEDNEKST
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
18PhosphorylationEHLENQPSDPTNTYA
HHHHCCCCCCCCCCC
46.5921945579
21PhosphorylationENQPSDPTNTYARPA
HCCCCCCCCCCCCCC
45.2221945579
23PhosphorylationQPSDPTNTYARPAEP
CCCCCCCCCCCCCCC
22.4921945579
24PhosphorylationPSDPTNTYARPAEPV
CCCCCCCCCCCCCCC
11.5921945579
44PhosphorylationNGNGKPKSLSSGLRK
CCCCCCCCHHHHHCC
41.8523927012
46PhosphorylationNGKPKSLSSGLRKGT
CCCCCCHHHHHCCCC
29.4723403867
47PhosphorylationGKPKSLSSGLRKGTK
CCCCCHHHHHCCCCC
47.3323403867
55UbiquitinationGLRKGTKKYPDYIQI
HHCCCCCCCCCCEEE
62.95-
56PhosphorylationLRKGTKKYPDYIQIA
HCCCCCCCCCCEEEE
11.6821945579
59PhosphorylationGTKKYPDYIQIAMPT
CCCCCCCCEEEECCC
7.1021945579
66PhosphorylationYIQIAMPTESRNKFP
CEEEECCCCCCCCCC
33.2421945579
68PhosphorylationQIAMPTESRNKFPLE
EEECCCCCCCCCCHH
43.5621945579
71UbiquitinationMPTESRNKFPLEWWK
CCCCCCCCCCHHHHH
47.45-
116UbiquitinationLSPPLPDKFFDYIDR
CCCCCCHHHHHHHHH
46.0921906983
191UbiquitinationMHFQCAPKLNGDSQA
CCEEECCCCCCCHHH
35.74-
331S-palmitoylationNVQGSIPCCFSWPLS
CCCCCCCEEEECCCC
3.3119233134
332S-palmitoylationVQGSIPCCFSWPLSW
CCCCCCEEEECCCCC
2.2519233134
343S-palmitoylationPLSWPPGCFKSSCKK
CCCCCCCHHHHHHHH
4.8419233134
348S-palmitoylationPGCFKSSCKKYSRVQ
CCHHHHHHHHHHCCC
5.9419233134
363UbiquitinationKIGEDNEKST-----
CCCCCCCCCC-----
66.7021906983
365PhosphorylationGEDNEKST-------
CCCCCCCC-------
54.4124719451

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 SMS2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
331CPalmitoylation

19233134
332CPalmitoylation

19233134
343CPalmitoylation

19233134
348CPalmitoylation

19233134

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 SMS2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SMS2_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.
Regulatory Network of SMS2_HUMAN

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Related Literatures of Post-Translational Modification
Palmitoylation
ReferencePubMed
"Sphingomyelin synthase 2 is palmitoylated at the COOH-terminal tail,which is involved in its localization in plasma membranes.";
Tani M., Kuge O.;
Biochem. Biophys. Res. Commun. 381:328-332(2009).
Cited for: SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-331; CYS-332; CYS-343 ANDCYS-348, AND MUTAGENESIS OF 331-CYS-CYS-332; CYS-343 AND CYS-348.

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