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  • 11.0 [archived version]
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TM2D2 TM2D2 PPAPDC1B PPAPDC1B LSM1 LSM1 PROSC PROSC FAM222A FAM222A DDHD2 DDHD2 WHSC1L1 WHSC1L1 DDHD1 DDHD1 ERLIN2 ERLIN2 AP4S1 AP4S1 PNPLA6 PNPLA6
"DDHD2" - Phospholipase DDHD2 in Homo sapiens
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Predicted Interactions
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textmining
co-expression
protein homology
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DDHD2Phospholipase DDHD2; Phospholipase that hydrolyzes preferentially phosphatidic acid, including 1,2-dioleoyl-sn-phosphatidic acid, and phosphatidylethanolamine. Specifically binds to phosphatidylinositol 3-phosphate (PI(3)P), phosphatidylinositol 4- phosphate (PI(4)P), phosphatidylinositol 5-phosphate (PI(5)P) and possibly phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2). May be involved in the maintenance of the endoplasmic reticulum and/or Golgi structures. May regulate the transport between Golgi apparatus and plasma membrane; Sterile alpha motif domain containing (711 aa)    
Predicted Functional Partners:
DDHD1
Phospholipase DDHD1; Phospholipase that hydrolyzes phosphatidic acid, including 1,2-dioleoyl-sn-phosphatidic acid. The different isoforms may change the substrate specificity; Belongs to the PA-PLA1 family (900 aa)
     
 
0.932
ERLIN2
Erlin-2; Component of the ERLIN1/ERLIN2 complex which mediates the endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs) such as ITPR1. Promotes sterol-accelerated ERAD of HMGCR probably implicating an AMFR/gp78-containing ubiquitin ligase complex. Involved in regulation of cellular cholesterol homeostasis by regulation the SREBP signaling pathway. May promote ER retention of the SCAP-SREBF complex (339 aa)
     
   
  0.708
PPAPDC1B
Phospholipid phosphatase 5; Displays magnesium-independent phosphatidate phosphatase activity in vitro. Catalyzes the conversion of phosphatidic acid to diacylglycerol. May be a metastatic suppressor for hepatocellular carcinoma (264 aa)
     
   
  0.700
PROSC
Pyridoxal phosphate homeostasis protein; Pyridoxal 5’-phosphate (PLP)-binding protein, which may be involved in intracellular homeostatic regulation of pyridoxal 5’-phosphate (PLP), the active form of vitamin B6 (275 aa)
           
  0.669
PNPLA6
Neuropathy target esterase; Phospholipase B that deacylates intracellular phosphatidylcholine (PtdCho), generating glycerophosphocholine (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 positions of PtdCho. Its specific chemical modification by certain organophosphorus (OP) compounds leads to distal axonopathy; Patatin like phospholipase domain containing (1375 aa)
     
   
  0.647
LSM1
U6 snRNA-associated Sm-like protein LSm1; Plays a role in the degradation of histone mRNAs, the only eukaryotic mRNAs that are not polyadenylated. Probably also part of an LSm subunits- containing complex involved in the general process of mRNA degradation (By similarity); Belongs to the snRNP Sm proteins family (133 aa)
     
   
  0.630
FAM222A
Protein FAM222A; Family with sequence similarity 222 member A; Belongs to the FAM222 family (452 aa)
           
  0.617
TM2D2
TM2 domain containing 2 (214 aa)
           
  0.617
WHSC1L1
Histone-lysine N-methyltransferase NSD3; Histone methyltransferase. Preferentially methylates ’Lys-4’ and ’Lys-27’ of histone H3. H3 ’Lys-4’ methylation represents a specific tag for epigenetic transcriptional activation, while ’Lys-27’ is a mark for transcriptional repression (1437 aa)
     
   
  0.614
AP4S1
AP-4 complex subunit sigma-1; Component of the adaptor protein complex 4 (AP-4). Adaptor protein complexes are vesicle coat components involved both in vesicle formation and cargo selection. They control the vesicular transport of proteins in different trafficking pathways. AP-4 forms a non clathrin- associated coat on vesicles departing the trans-Golgi network (TGN) and may be involved in the targeting of proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system. It is also involved in protein sorting to the basolateral membrane in epithelial cells and the proper a [...] (159 aa)
     
   
  0.611
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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