SGMS2
entrez
166929
canonical
uniprot
Q8NHU3
canonical
ensembl
ENSG00000164023
resolver
ensp
ENSP00000351981
resolver
ensp
ENSP00000378176
resolver
ensp
ENSP00000378178
resolver
ensp
ENSP00000508566
resolver
ensp
ENSP00000526708
resolver
ensp
ENSP00000526709
resolver
ensp
ENSP00000526710
resolver
ensp
ENSP00000526711
resolver
ensp
ENSP00000526712
resolver
ensp
ENSP00000526713
resolver
ensp
ENSP00000526714
resolver
ensp
ENSP00000526715
resolver
ensp
ENSP00000614847
resolver
ensp
ENSP00000614848
resolver
ensp
ENSP00000614849
resolver
ensp
ENSP00000614850
resolver
ensp
ENSP00000788854
resolver
ensp
ENSP00000795373
resolver
enst
ENST00000359079
resolver
enst
ENST00000394684
resolver
enst
ENST00000394686
resolver
enst
ENST00000690982
resolver
enst
ENST00000856649
resolver
enst
ENST00000856650
resolver
enst
ENST00000856651
resolver
enst
ENST00000856652
resolver
enst
ENST00000856653
resolver
enst
ENST00000856654
resolver
enst
ENST00000856655
resolver
enst
ENST00000856656
resolver
enst
ENST00000944788
resolver
enst
ENST00000944789
resolver
enst
ENST00000944790
resolver
enst
ENST00000944791
resolver
genesymbol
SGMS2
resolver
genesymbol_syn
SMS2
resolver
hgnc
HGNC:28395
resolver
uniprot
A8K2S9
resolver
uniprot
B2RA61
resolver
uniprot_entry
SMS2_HUMAN
resolver
uniprot_sec
A8K2S9
resolver
uniprot_sec
B2RA61
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by bacterial PC-phospholipase C inhibitor D609. {ECO:0000269|PubMed:14685263}.
uniprot
proteins
amino_acid_sequence
MDIIETAKLEEHLENQPSDPTNTYARPAEPVEEENKNGNGKPKSLSSGLRKGTKKYPDYIQIAMPTESRNKFPLEWWKTGIAFIYAVFNLVLTTVMITVVHERVPPKELSPPLPDKFFDYIDRVKWAFSVSEINGIILVGLWITQWLFLRYKSIVGRRFCFIIGTLYLYRCITMYVTTLPVPGMHFQCAPKLNGDSQAKVQRILRLISGGGLSITGSHILCGDFLFSGHTVTLTLTYLFIKEYSPRHFWWYHLICWLLSAAGIICILVAHEHYTIDVIIAYYITTRLFWWYHSMANEKNLKVSSQTNFLSRAWWFPIFYFFEKNVQGSIPCCFSWPLSWPPGCFKSSCKKYSRVQKIGEDNEKST
uniprot
proteins
disease_involvement
DISEASE: Calvarial doughnut lesions with bone fragility (CDL) [MIM:126550]: A rare autosomal dominant bone disease characterized by low bone density, distinctive X-ray translucencies of the skull, multiple fractures, elevated serum alkaline phosphatase, and dental caries. Patients present with childhood onset of primary osteoporosis and typical sclerotic doughnut-shaped lesions in the cranial bones. {ECO:0000269|PubMed:30779713}. Note=The disease may be caused by variants affecting the gene represented in this entry.; DISEASE: Calvarial doughnut lesions with bone fragility and spondylometaphyseal dysplasia (CDLSMD) [MIM:126550]: A severe form of calvarial doughnut lesions with bone fragility, a rare autosomal dominant disease characterized by low bone density, distinctive X-ray translucencies of the skull, multiple fractures, elevated serum alkaline phosphatase, and dental caries. CDLSMD patients show neonatal onset of fractures, severe short stature, marked cranial sclerosis, and spondylometaphyseal dysplasia. {ECO:0000269|PubMed:30779713}. Note=The disease may be caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.8.27
uniprot
proteins
function
FUNCTION: Sphingomyelin synthase that primarily contributes to sphingomyelin synthesis and homeostasis at the plasma membrane. Catalyzes the reversible transfer of phosphocholine moiety in sphingomyelin biosynthesis: in the forward reaction transfers phosphocholine head group of phosphatidylcholine (PC) on to ceramide (CER) to form ceramide phosphocholine (sphingomyelin, SM) and diacylglycerol (DAG) as by-product, and in the reverse reaction transfers phosphocholine from SM to DAG to form PC and CER (PubMed:14685263, PubMed:17449912, PubMed:17982138, PubMed:18370930, PubMed:38388831). The direction of the reaction appears to depend on the levels of CER and DAG in the plasma membrane (PubMed:14685263, PubMed:17449912, PubMed:17982138, PubMed:18370930). Does not use free phosphorylcholine or CDP-choline as donors (PubMed:14685263). Can also transfer phosphoethanolamine head group of phosphatidylethanolamine (PE) on to ceramide (CER) to form ceramide phosphoethanolamine (CPE) (PubMed:19454763). Regulates receptor-mediated signal transduction via mitogenic DAG and proapoptotic CER, as well as via SM, a structural component of membrane rafts that serve as platforms for signal transduction and protein sorting (PubMed:17449912, PubMed:17982138). To a lesser extent, plays a role in secretory transport via regulation of DAG pool at the Golgi apparatus and its downstream effects on PRKD1 (PubMed:18370930, PubMed:21980337). Required for normal bone matrix mineralization (PubMed:30779713). {ECO:0000269|PubMed:14685263, ECO:0000269|PubMed:17449912, ECO:0000269|PubMed:17982138, ECO:0000269|PubMed:18370930, ECO:0000269|PubMed:19454763, ECO:0000269|PubMed:21980337, ECO:0000269|PubMed:30779713, ECO:0000269|PubMed:38388831}.
uniprot
proteins
mass_dalton
42280
uniprot
proteins
mutagenesis
MUTAGEN 227; /note="S->A: Abolishes enzyme activity by about 70%. No change in subcellular location."; /evidence="ECO:0000269|PubMed:18694848"; MUTAGEN 229; /note="H->A: Completely abolishes enzyme activity. No change in subcellular location."; /evidence="ECO:0000269|PubMed:18694848"; MUTAGEN 272; /note="H->A: Completely abolishes enzyme activity. No change in subcellular location."; /evidence="ECO:0000269|PubMed:18694848"; MUTAGEN 276; /note="D->E,A: Completely abolishes enzyme activity. No change in subcellular location."; /evidence="ECO:0000269|PubMed:18694848, ECO:0000269|PubMed:30779713"; MUTAGEN 331..332; /note="CC->AA: Little effect on palmitoylation; when associated with A-343 or A-348. Abolishes palmitoylation and dramatically reduces plasma membrane localization; when associated with A-343 and A-348."; /evidence="ECO:0000269|PubMed:19233134"; MUTAGEN 343; /note="C->A: Strongly decreases palmitoylation; when associated with A-348. Abolishes palmitoylation and dramatically reduces plasma membrane localization; when associated with 331-A-A-332 and A-348."; /evidence="ECO:0000269|PubMed:19233134"; MUTAGEN 348; /note="C->A: Strongly decreases palmitoylation; when associated with A-343. Abolishes palmitoylation and dramatically reduces plasma membrane localization; when associated with 331-A-A-332 and A-343."; /evidence="ECO:0000269|PubMed:19233134
uniprot
proteins
pathway_participation
PATHWAY: Sphingolipid metabolism. {ECO:0000269|PubMed:17982138}.
uniprot
proteins
post_translational_modification
PTM: Palmitoylated on Cys-331, Cys-332, Cys-343 and Cys-348; which plays an important role in plasma membrane localization. {ECO:0000269|PubMed:19233134}.
uniprot
proteins
protein_family
Sphingomyelin synthase family
uniprot
proteins
pubmed
14685263
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16508036
uniprot
proteins
pubmed
17449912
uniprot
proteins
pubmed
17982138
uniprot
proteins
pubmed
18370930
uniprot
proteins
pubmed
18694848
uniprot
proteins
pubmed
19233134
uniprot
proteins
pubmed
19454763
uniprot
proteins
pubmed
21980337
uniprot
proteins
pubmed
30779713
uniprot
proteins
pubmed
38388831
uniprot
proteins
sequence_length
365
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14685263, ECO:0000269|PubMed:30779713}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:14685263, ECO:0000269|PubMed:18370930}; Multi-pass membrane protein {ECO:0000255}. Note=Primarily localized at the plasma membrane with a small fraction at the Golgi apparatus. {ECO:0000269|PubMed:14685263}.
uniprot
proteins
transmembrane_region
TRANSMEM 80..100; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 128..148; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 159..179; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 206..226; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 248..268; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 275..295; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins