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Protein

Phosphatidylcholine:ceramide cholinephosphotransferase 2

Gene

SGMS2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.2 Publications

Miscellaneous

Overexpression of the human protein in mouse causes increased non-HDL-sphingomyelin and non-HDL cholesterol levels, decreased HDL-sphingomyelin and HDL-cholesterol levels and increases lipoprotein atherogenic potential.

Catalytic activityi

A ceramide + a phosphatidylcholine = a sphingomyelin + a 1,2-diacyl-sn-glycerol.

Enzyme regulationi

Inhibited by bacterial PC-phospholipase C inhibitor D609.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei2291 Publication1
Active sitei2721 Publication1
Active sitei2761 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionKinase, Transferase
Biological processLipid metabolism, Sphingolipid metabolism

Enzyme and pathway databases

BRENDAi2.7.8.27 2681
ReactomeiR-HSA-1660661 Sphingolipid de novo biosynthesis

Chemistry databases

SwissLipidsiSLP:000000172

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylcholine:ceramide cholinephosphotransferase 2 (EC:2.7.8.27)
Alternative name(s):
Sphingomyelin synthase 2
Gene namesi
Name:SGMS2
Synonyms:SMS2
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

EuPathDBiHostDB:ENSG00000164023.14
HGNCiHGNC:28395 SGMS2
MIMi611574 gene
neXtProtiNX_Q8NHU3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei80 – 100HelicalSequence analysisAdd BLAST21
Transmembranei128 – 148HelicalSequence analysisAdd BLAST21
Transmembranei159 – 179HelicalSequence analysisAdd BLAST21
Transmembranei206 – 226HelicalSequence analysisAdd BLAST21
Transmembranei248 – 268HelicalSequence analysisAdd BLAST21
Transmembranei275 – 295HelicalSequence analysisAdd BLAST21
Topological domaini296 – 365CytoplasmicSequence analysisAdd BLAST70

Keywords - Cellular componenti

Cell membrane, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi227S → A: Abolishes enzyme activity by about 70%. No change in subcellular location. 1 Publication1
Mutagenesisi229H → A: Completely abolishes enzyme activity. No change in subcellular location. 1 Publication1
Mutagenesisi272H → A: Completely abolishes enzyme activity. No change in subcellular location. 1 Publication1
Mutagenesisi276D → A: Completely abolishes enzyme activity. No change in subcellular location. 1 Publication1
Mutagenesisi331 – 332CC → 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. 1 Publication2
Mutagenesisi343C → 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. 1 Publication1
Mutagenesisi348C → 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. 1 Publication1

Organism-specific databases

DisGeNETi166929
OpenTargetsiENSG00000164023
PharmGKBiPA162403069

Chemistry databases

ChEMBLiCHEMBL3112379
GuidetoPHARMACOLOGYi2521

Polymorphism and mutation databases

BioMutaiSGMS2
DMDMi44888519

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002210721 – 365Phosphatidylcholine:ceramide cholinephosphotransferase 2Add BLAST365

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi331S-palmitoyl cysteine1 Publication1
Lipidationi332S-palmitoyl cysteine1 Publication1
Lipidationi343S-palmitoyl cysteine1 Publication1
Lipidationi348S-palmitoyl cysteine1 Publication1

Post-translational modificationi

Palmitoylated on Cys-331, Cys-332, Cys-343 and Cys-348; which plays an important role in plasma membrane localization.1 Publication

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

MaxQBiQ8NHU3
PaxDbiQ8NHU3
PeptideAtlasiQ8NHU3
PRIDEiQ8NHU3

PTM databases

iPTMnetiQ8NHU3
PhosphoSitePlusiQ8NHU3

Expressioni

Tissue specificityi

Brain, heart, kidney, liver, muscle and stomach. Also expressed in a number of cell lines such as carcinoma HeLa cells, hepatoma Hep-G2 cells, and colon carcinoma Caco-2 cells.1 Publication

Gene expression databases

BgeeiENSG00000164023
CleanExiHS_SGMS2
ExpressionAtlasiQ8NHU3 baseline and differential
GenevisibleiQ8NHU3 HS

Organism-specific databases

HPAiHPA015076

Interactioni

Protein-protein interaction databases

BioGridi127938, 9 interactors
IntActiQ8NHU3, 11 interactors
STRINGi9606.ENSP00000351981

Chemistry databases

BindingDBiQ8NHU3

Structurei

3D structure databases

ProteinModelPortaliQ8NHU3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the sphingomyelin synthase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3058 Eukaryota
ENOG410XNSC LUCA
GeneTreeiENSGT00390000001630
HOGENOMiHOG000233822
HOVERGENiHBG048216
InParanoidiQ8NHU3
KOiK04714
OMAiVIVAYYI
OrthoDBiEOG091G0J6C
PhylomeDBiQ8NHU3
TreeFamiTF314547

Family and domain databases

InterProiView protein in InterPro
IPR025749 Sphingomyelin_synth-like_dom
PfamiView protein in Pfam
PF14360 PAP2_C, 1 hit

Sequencei

Sequence statusi: Complete.

Q8NHU3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDIIETAKLE EHLENQPSDP TNTYARPAEP VEEENKNGNG KPKSLSSGLR
60 70 80 90 100
KGTKKYPDYI QIAMPTESRN KFPLEWWKTG IAFIYAVFNL VLTTVMITVV
110 120 130 140 150
HERVPPKELS PPLPDKFFDY IDRVKWAFSV SEINGIILVG LWITQWLFLR
160 170 180 190 200
YKSIVGRRFC FIIGTLYLYR CITMYVTTLP VPGMHFQCAP KLNGDSQAKV
210 220 230 240 250
QRILRLISGG GLSITGSHIL CGDFLFSGHT VTLTLTYLFI KEYSPRHFWW
260 270 280 290 300
YHLICWLLSA AGIICILVAH EHYTIDVIIA YYITTRLFWW YHSMANEKNL
310 320 330 340 350
KVSSQTNFLS RAWWFPIFYF FEKNVQGSIP CCFSWPLSWP PGCFKSSCKK
360
YSRVQKIGED NEKST
Length:365
Mass (Da):42,280
Last modified:October 1, 2002 - v1
Checksum:i49B3560AFB87CF40
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti313W → R in BAF83033 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05202521T → M. Corresponds to variant dbSNP:rs17038204Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF452717 mRNA Translation: AAP13352.1
AK290344 mRNA Translation: BAF83033.1
AK314049 mRNA Translation: BAG36758.1
CH471057 Genomic DNA Translation: EAX06211.1
BC028705 mRNA Translation: AAH28705.1
BC041369 mRNA Translation: AAH41369.1
AC096564 Genomic DNA No translation available.
CCDSiCCDS3677.1
RefSeqiNP_001129729.1, NM_001136257.1
NP_001129730.1, NM_001136258.1
NP_689834.1, NM_152621.5
XP_011530000.1, XM_011531698.2
XP_011530001.1, XM_011531699.2
XP_011530002.1, XM_011531700.2
XP_011530003.1, XM_011531701.2
XP_011530004.1, XM_011531702.2
XP_016863328.1, XM_017007839.1
XP_016863329.1, XM_017007840.1
UniGeneiHs.595423

Genome annotation databases

EnsembliENST00000359079; ENSP00000351981; ENSG00000164023
ENST00000394684; ENSP00000378176; ENSG00000164023
ENST00000394686; ENSP00000378178; ENSG00000164023
GeneIDi166929
KEGGihsa:166929
UCSCiuc003hyl.6 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiSMS2_HUMAN
AccessioniPrimary (citable) accession number: Q8NHU3
Secondary accession number(s): A8K2S9, B2RA61
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: October 1, 2002
Last modified: April 25, 2018
This is version 122 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

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