LMPD Database

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LMP006488

UniProt Annotations

Entry Information
Gene Nameneutrophil cytosolic factor 1
Protein EntryNCF1_HUMAN
UniProt IDP14598
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=1; IsoId=P14598-1; Sequence=Displayed; Name=2; IsoId=P14598-2; Sequence=VSP_035032, VSP_035033; Note=Due to intron retention.;
DiseaseGranulomatous disease, chronic, cytochrome-b-positive 1, autosomal recessive (CGD1) [MIM
DomainThe PX domain mediates interaction with phosphatidylinositol 3,4-bisphosphate and other anionic phospholipids. In the autoinhibited, unphosphorylated state an intramolecular interaction with the C-terminal SH3 domain precludes phospholipid binding and interaction with CYBA. Phosphorylation disrupts the autoinhibited state.
FunctionNCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production). {ECO
InteractionQ8IZP0:ABI1; NbExp=5; IntAct=EBI-395044, EBI-375446; P60709:ACTB; NbExp=3; IntAct=EBI-395044, EBI-353944; P13498:CYBA; NbExp=7; IntAct=EBI-395044, EBI-986058; P04899:GNAI2; NbExp=2; IntAct=EBI-395044, EBI-353997; P19878:NCF2; NbExp=11; IntAct=EBI-395044, EBI-489611; Q15080:NCF4; NbExp=2; IntAct=EBI-395044, EBI-1036870;
PtmPhosphorylated by PRKCD; phosphorylation induces activation of NCF1 and NADPH oxidase activity. {ECO
Sequence CautionSequence=BAF84783.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence= ; Sequence=BAG54596.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence= ;
SimilarityContains 1 PX (phox homology) domain.
SimilarityContains 2 SH3 domains. {ECO
Subcellular LocationCytoplasm, cytosol. Membrane; Peripheral membrane protein; Cytoplasmic side.
SubunitComponent of an NADPH oxidase complex composed of a heterodimer formed by the membrane proteins CYBA and CYBB and the cytosolic subunits NCF1, NCF2 and NCF4. Interacts (via C-terminus) with NCF2 (via the C-terminal SH3 domain). Interacts with NCF4. Interacts with CYBB. Interacts (via the second SH3 domain) with CYBA. Interacts with NOXA1. Interacts with ADAM15. Interacts with TRAF4. Interacts with FASLG. {ECO
Tissue SpecificityDetected in peripheral blood monocytes and neutrophils (at protein level). {ECO
Web ResourceName=NCF1base; Note=NCF1 deficiency database; URL="http://bioinf.uta.fi/NCF1base/";