NCF4_HUMAN - dbPTM
NCF4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NCF4_HUMAN
UniProt AC Q15080
Protein Name Neutrophil cytosol factor 4
Gene Name NCF4
Organism Homo sapiens (Human).
Sequence Length 339
Subcellular Localization Cytoplasm, cytosol . Endosome membrane
Peripheral membrane protein
Cytoplasmic side . Membrane
Peripheral membrane protein .
Protein Description Component of the NADPH-oxidase, a multicomponent enzyme system responsible for the oxidative burst in which electrons are transported from NADPH to molecular oxygen, generating reactive oxidant intermediates. It may be important for the assembly and/or activation of the NADPH-oxidase complex..
Protein Sequence MAVAQQLRAESDFEQLPDDVAISANIADIEEKRGFTSHFVFVIEVKTKGGSKYLIYRRYRQFHALQSKLEERFGPDSKSSALACTLPTLPAKVYVGVKQEIAEMRIPALNAYMKSLLSLPVWVLMDEDVRIFFYQSPYDSEQVPQALRRLRPRTRKVKSVSPQGNSVDRMAAPRAEALFDFTGNSKLELNFKAGDVIFLLSRINKDWLEGTVRGATGIFPLSFVKILKDFPEEDDPTNWLRCYYYEDTISTIKDIAVEEDLSSTPLLKDLLELTRREFQREDIALNYRDAEGDLVRLLSDEDVALMVRQARGLPSQKRLFPWKLHITQKDNYRVYNTMP
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
11PhosphorylationAQQLRAESDFEQLPD
HHHHHHHCCHHHCCC
46.76-
23PhosphorylationLPDDVAISANIADIE
CCCCEEEECCCCCHH
12.91-
47PhosphorylationVFVIEVKTKGGSKYL
EEEEEEEECCCCEEE
39.85-
51PhosphorylationEVKTKGGSKYLIYRR
EEEECCCCEEEEEEE
27.13-
53PhosphorylationKTKGGSKYLIYRRYR
EECCCCEEEEEEEHH
10.46-
154PhosphorylationLRRLRPRTRKVKSVS
HHHHCCCCCCCCCCC
37.2115035643
159PhosphorylationPRTRKVKSVSPQGNS
CCCCCCCCCCCCCCC
30.7128450419
161PhosphorylationTRKVKSVSPQGNSVD
CCCCCCCCCCCCCCH
20.7123401153
161 (in isoform 3)Phosphorylation-20.7127251275
166PhosphorylationSVSPQGNSVDRMAAP
CCCCCCCCCHHCCCC
32.0228450419
166 (in isoform 3)Phosphorylation-32.0227251275
201PhosphorylationGDVIFLLSRINKDWL
CCEEEEEEECCHHHH
33.0124114839
225 (in isoform 1)Ubiquitination-40.0721890473
225UbiquitinationIFPLSFVKILKDFPE
EEEHHHHHHHHCCCC
40.0721890473
225UbiquitinationIFPLSFVKILKDFPE
EEEHHHHHHHHCCCC
40.0721890473
228UbiquitinationLSFVKILKDFPEEDD
HHHHHHHHCCCCCCC
61.88-
243PhosphorylationPTNWLRCYYYEDTIS
CCCCEEEEEECCHHH
11.57-
245PhosphorylationNWLRCYYYEDTISTI
CCEEEEEECCHHHHH
4.85-
264PhosphorylationVEEDLSSTPLLKDLL
HHCCCCCCHHHHHHH
17.9924719451
274PhosphorylationLKDLLELTRREFQRE
HHHHHHHHHHHHHHH
20.5027542207
275 (in isoform 3)Phosphorylation-49.0825690035
276 (in isoform 3)Phosphorylation-43.7925690035
299PhosphorylationGDLVRLLSDEDVALM
CCEEEECCHHHHHHH
43.4727251275
315PhosphorylationRQARGLPSQKRLFPW
HHHCCCCCCCCCCCE
54.078280052
3172-HydroxyisobutyrylationARGLPSQKRLFPWKL
HCCCCCCCCCCCEEE
56.24-

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
154TPhosphorylationKinasePRKCAP17252
GPS
154TPhosphorylationKinasePKCAP05696
PSP
154TPhosphorylationKinasePKC-FAMILY-GPS
154TPhosphorylationKinasePKC_GROUP-PhosphoELM
315SPhosphorylationKinasePRKCAP17252
GPS
315SPhosphorylationKinasePKC-FAMILY-GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NCF4_HUMAN !!

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 NCF4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XRCC6_HUMANXRCC6physical
9914162
NCF2_HUMANNCF2physical
9083043
NCF1_HUMANNCF1physical
9083043
NCF2_HUMANNCF2physical
12887891
NCF2_HUMANNCF2physical
12813044

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613960Granulomatous disease, chronic, cytochrome-b-positive 3, autosomal recessive (CGD3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00514Dextromethorphan
Regulatory Network of NCF4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"p40(phox) is phosphorylated on threonine 154 and serine 315 duringactivation of the phagocyte NADPH oxidase. Implication of a proteinkinase c-type kinase in the phosphorylation process.";
Bouin A.-P., Grandvaux N., Vignais P.V., Fuchs A.;
J. Biol. Chem. 273:30097-30103(1998).
Cited for: PHOSPHORYLATION AT THR-154 AND SER-315, AND MUTAGENESIS OF THR-154;THR-211; THR-251; THR-274; SER-315 AND THR-327.

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