NOXA1_HUMAN - dbPTM
NOXA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NOXA1_HUMAN
UniProt AC Q86UR1
Protein Name NADPH oxidase activator 1
Gene Name NOXA1
Organism Homo sapiens (Human).
Sequence Length 476
Subcellular Localization Cytoplasm. Cell membrane. Translocation to membranes depends on NOXO1 or NCF1 and maybe RAC1.
Protein Description Functions as an activator of NOX1, a superoxide-producing NADPH oxidase. Functions in the production of reactive oxygen species (ROS) which participate in a variety of biological processes including host defense, hormone biosynthesis, oxygen sensing and signal transduction. May also activate CYBB/gp91phox and NOX3..
Protein Sequence MASLGDLVRAWHLGAQAVDRGDWARALHLFSGVPAPPARLCFNAGCVHLLAGDPEAALRAFDQAVTKDTCMAVGFFQRGVANFQLARFQEALSDFWLALEQLRGHAAIDYTQLGLRFKLQAWEVLHNVASAQCQLGLWTEAASSLREAMSKWPEGSLNGLDSALDQVQRRGSLPPRQVPRGEVFRPHRWHLKHLEPVDFLGKAKVVASAIPDDQGWGVRPQQPQGPGANHDARSLIMDSPRAGTHQGPLDAETEVGADRCTSTAYQEQRPQVEQVGKQAPLSPGLPAMGGPGPGPCEDPAGAGGAGAGGSEPLVTVTVQCAFTVALRARRGADLSSLRALLGQALPHQAQLGQLSYLAPGEDGHWVPIPEEESLQRAWQDAAACPRGLQLQCRGAGGRPVLYQVVAQHSYSAQGPEDLGFRQGDTVDVLCEVDQAWLEGHCDGRIGIFPKCFVVPAGPRMSGAPGRLPRSQQGDQP
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
3Phosphorylation-----MASLGDLVRA
-----CCCHHHHHHH
31.4225072903
110PhosphorylationRGHAAIDYTQLGLRF
CCCCCCCHHHHCHHH
7.1220943948
172PhosphorylationDQVQRRGSLPPRQVP
HHHHHHCCCCCCCCC
35.5717913709
202UbiquitinationEPVDFLGKAKVVASA
CCCCHHCEEEEEEEE
47.3729967540
234PhosphorylationGANHDARSLIMDSPR
CCCCCHHHHHHCCCC
24.7823312004
239PhosphorylationARSLIMDSPRAGTHQ
HHHHHHCCCCCCCCC
10.0221815630
282PhosphorylationVGKQAPLSPGLPAMG
HHCCCCCCCCCCCCC
18.8320110267
335PhosphorylationARRGADLSSLRALLG
HHCCCCHHHHHHHHH
28.0730301811
336PhosphorylationRRGADLSSLRALLGQ
HCCCCHHHHHHHHHH
29.2225954137
409PhosphorylationYQVVAQHSYSAQGPE
EEEEECCCCCCCCCH
14.5424719451
461PhosphorylationVPAGPRMSGAPGRLP
EECCCCCCCCCCCCC
32.8417913709
470PhosphorylationAPGRLPRSQQGDQP-
CCCCCCHHHCCCCC-
25.5624719451
477PhosphorylationSQQGDQP--------
HHCCCCC--------
24719451

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
110YPhosphorylationKinaseSRCP12931
PSP
172SPhosphorylationKinasePRKACAP17612
GPS
172SPhosphorylationKinasePRKCAP17252
GPS
172SPhosphorylationKinasePKA-FAMILY-GPS
172SPhosphorylationKinasePKC-FAMILY-GPS
172SPhosphorylationKinasePKA-Uniprot
239SPhosphorylationKinaseMAPK14Q16539
GPS
282SPhosphorylationKinaseMAPK1P28482
GPS
282SPhosphorylationKinaseMAPK3P27361
GPS
282SPhosphorylationKinaseMAPK14Q16539
GPS
282SPhosphorylationKinaseERK-SUBFAMILY-GPS
282SPhosphorylationKinaseMAPK-FAMILY-GPS
461SPhosphorylationKinasePRKACAP17612
GPS
461SPhosphorylationKinasePKA-FAMILY-GPS
461SPhosphorylationKinasePKA-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NOXA1_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 NOXA1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NOX1_HUMANNOX1physical
20110267
RAC1_HUMANRAC1physical
20110267
RIM3A_HUMANRIMBP3physical
25416956

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NOXA1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Regulation of Nox1 activity via PKA-mediated phosphorylation of NoxA1and 14-3-3 binding.";
Kim J.-S., Diebold B.A., Babior B.M., Knaus U.G., Bokoch G.M.;
J. Biol. Chem. 282:34787-34800(2007).
Cited for: INTERACTION WITH YWHAZ, MUTAGENESIS OF SER-172 AND SER-461, ANDPHOSPHORYLATION AT SER-172 AND SER-461.

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