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Protein

NADPH oxidase activator 1

Gene

NOXA1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 NOX3.8 Publications

GO - Molecular functioni

  • enzyme binding Source: BHF-UCL
  • Rac GTPase binding Source: BHF-UCL
  • SH3 domain binding Source: UniProtKB
  • superoxide-generating NADPH oxidase activator activity Source: UniProtKB

GO - Biological processi

  • positive regulation of catalytic activity Source: GOC
  • regulation of hydrogen peroxide metabolic process Source: BHF-UCL
  • regulation of respiratory burst Source: BHF-UCL
  • superoxide metabolic process Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-HSA-5668599. RHO GTPases Activate NADPH Oxidases.
SIGNORiQ86UR1.

Names & Taxonomyi

Protein namesi
Recommended name:
NADPH oxidase activator 1
Short name:
NOX activator 1
Alternative name(s):
Antigen NY-CO-31
NCF2-like protein
P67phox-like factor
p51-nox
Gene namesi
Name:NOXA1
Synonyms:P51NOX
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:10668. NOXA1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • NADPH oxidase complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi34 – 341P → A: Partial loss of function. 1 Publication
Mutagenesisi37 – 371P → A: Partial loss of function. 1 Publication
Mutagenesisi68 – 681D → A: Loss of function and loss of interaction with RAC1. 1 Publication
Mutagenesisi103 – 1031R → E: Loss of function and loss of interaction with RAC1. Loss of localization to membranes. 3 Publications
Mutagenesisi172 – 1721S → A: Loss of phosphorylation. Loss of interaction with YHAWZ; when associated with A-461. 1 Publication
Mutagenesisi172 – 1721S → E: Constitutively interacts with YWHAZ; when associated with E-461. 1 Publication
Mutagenesisi205 – 2051V → A: Unable to activate NOX2. 1 Publication
Mutagenesisi436 – 4361W → R: Loss of interaction with NOXO1 and NCF1. Loss of localization to membranes. Partial loss of function. 3 Publications
Mutagenesisi461 – 4611S → A: Loss of phosphorylation. Loss of interaction with YHAWZ; when associated with A-172. 1 Publication
Mutagenesisi461 – 4611S → E: Constitutively interacts with YWHAZ; when associated with E-172. 1 Publication

Organism-specific databases

PharmGKBiPA35598.

Polymorphism and mutation databases

BioMutaiNOXA1.
DMDMi74759404.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 476476NADPH oxidase activator 1PRO_0000314609Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei172 – 1721Phosphoserine; by PKA1 Publication
Modified residuei461 – 4611Phosphoserine; by PKA1 Publication

Post-translational modificationi

Interaction with YWHAZ depends on phosphorylation by PKA.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ86UR1.
PRIDEiQ86UR1.

PTM databases

iPTMnetiQ86UR1.
PhosphoSiteiQ86UR1.

Expressioni

Tissue specificityi

Widely expressed. Detected in pancreas, liver, kidney, spleen, prostate, small intestine and colon.1 Publication

Developmental stagei

Expressed in fetal kidney.1 Publication

Gene expression databases

BgeeiQ86UR1.
CleanExiHS_NOXA1.
GenevisibleiQ86UR1. HS.

Organism-specific databases

HPAiHPA044781.

Interactioni

Subunit structurei

NOX1, NOXA1, NOXO1, RAC1 and CYBA forms a functional multimeric complex supporting ROS production. Interaction with YWHAZ prevents the interaction of NOXA1 with NOXO1 and RAC1 and its targeting to membranes, hence reducing its ability to activate NOX1. Interacts (via N-terminus) with SH3PXD2A and SH3PXD2B; the interaction is direct.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NOXO1Q8NFA26EBI-949814,EBI-7130806
RIMBP3Q9UFD93EBI-949814,EBI-10182375

GO - Molecular functioni

  • enzyme binding Source: BHF-UCL
  • Rac GTPase binding Source: BHF-UCL
  • SH3 domain binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116025. 13 interactions.
IntActiQ86UR1. 8 interactions.
MINTiMINT-1211202.
STRINGi9606.ENSP00000342848.

Structurei

3D structure databases

ProteinModelPortaliQ86UR1.
SMRiQ86UR1. Positions 3-186, 403-453.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati7 – 3832TPR 1Add
BLAST
Repeati39 – 7133TPR 2Add
BLAST
Repeati73 – 10533TPR 3Add
BLAST
Repeati122 – 15534TPR 4Add
BLAST
Domaini315 – 39581PB1PROSITE-ProRule annotationAdd
BLAST
Domaini399 – 45860SH3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 224224Mediates interaction with RAC1Add
BLAST

Domaini

The SH3 domain mediates interaction with NOXO1 and NCF1 and has autoregulatory function.
The TPR repeats mediate interaction with RAC1.

Sequence similaritiesi

Belongs to the NCF2/NOXA1 family.Curated
Contains 1 PB1 domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation
Contains 4 TPR repeats.Curated

Keywords - Domaini

Repeat, SH3 domain, TPR repeat

Phylogenomic databases

eggNOGiKOG4225. Eukaryota.
ENOG41110AD. LUCA.
GeneTreeiENSGT00530000063843.
HOGENOMiHOG000237312.
HOVERGENiHBG098043.
InParanoidiQ86UR1.
OMAiFQLERFQ.
OrthoDBiEOG7S7SF5.
PhylomeDBiQ86UR1.
TreeFamiTF329087.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR000270. PB1_dom.
IPR001452. SH3_domain.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF00564. PB1. 1 hit.
PF00018. SH3_1. 1 hit.
PF13176. TPR_7. 1 hit.
[Graphical view]
SMARTiSM00666. PB1. 1 hit.
SM00326. SH3. 1 hit.
SM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
SSF50044. SSF50044. 1 hit.
PROSITEiPS51745. PB1. 1 hit.
PS50002. SH3. 1 hit.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q86UR1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASLGDLVRA WHLGAQAVDR GDWARALHLF SGVPAPPARL CFNAGCVHLL
60 70 80 90 100
AGDPEAALRA FDQAVTKDTC MAVGFFQRGV ANFQLARFQE ALSDFWLALE
110 120 130 140 150
QLRGHAAIDY TQLGLRFKLQ AWEVLHNVAS AQCQLGLWTE AASSLREAMS
160 170 180 190 200
KWPEGSLNGL DSALDQVQRR GSLPPRQVPR GEVFRPHRWH LKHLEPVDFL
210 220 230 240 250
GKAKVVASAI PDDQGWGVRP QQPQGPGANH DARSLIMDSP RAGTHQGPLD
260 270 280 290 300
AETEVGADRC TSTAYQEQRP QVEQVGKQAP LSPGLPAMGG PGPGPCEDPA
310 320 330 340 350
GAGGAGAGGS EPLVTVTVQC AFTVALRARR GADLSSLRAL LGQALPHQAQ
360 370 380 390 400
LGQLSYLAPG EDGHWVPIPE EESLQRAWQD AAACPRGLQL QCRGAGGRPV
410 420 430 440 450
LYQVVAQHSY SAQGPEDLGF RQGDTVDVLC EVDQAWLEGH CDGRIGIFPK
460 470
CFVVPAGPRM SGAPGRLPRS QQGDQP
Length:476
Mass (Da):50,933
Last modified:June 1, 2003 - v1
Checksum:i64DFBF64C59722AD
GO
Isoform 2 (identifier: Q86UR1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     431-431: E → EEPDVPLA

Note: Mostly inactive for NOX1 activation. Does not interact with NOXO1.
Show »
Length:483
Mass (Da):51,655
Checksum:i3C3B2AC24286D2D2
GO
Isoform 3 (identifier: Q86UR1-3) [UniParc]FASTAAdd to basket

Also known as: NOXA1inhib

The sequence of this isoform differs from the canonical sequence as follows:
     168-223: Missing.
     431-431: E → EEPDVPLA

Note: Inactive for NOX1 activation. No experimental confirmation available.
Show »
Length:427
Mass (Da):45,245
Checksum:i122CD814C315AA08
GO

Sequence cautioni

The sequence AAY16126.1 differs from that shown. Reason: Frameshift at position 305. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti51 – 511A → T in AAY16126 (PubMed:17602954).Curated
Sequence conflicti56 – 561A → T in AAY16127 (PubMed:17602954).Curated
Sequence conflicti73 – 731V → L in AAY16127 (PubMed:17602954).Curated
Sequence conflicti142 – 1421A → T in AAY16127 (PubMed:17602954).Curated
Sequence conflicti261 – 2611T → A in AAY16126 (PubMed:17602954).Curated
Sequence conflicti277 – 2771K → E in AAY16126 (PubMed:17602954).Curated
Sequence conflicti278 – 2781Q → V in AAC18046 (PubMed:9610721).Curated
Sequence conflicti320 – 3201C → R in AAY16127 (PubMed:17602954).Curated
Sequence conflicti329 – 3291R → G in AAC18046 (PubMed:9610721).Curated
Sequence conflicti345 – 3462LP → FL in AAC18046 (PubMed:9610721).Curated
Sequence conflicti354 – 3541L → F in AAC18046 (PubMed:9610721).Curated
Sequence conflicti409 – 4091S → R in AAC18046 (PubMed:9610721).Curated
Sequence conflicti441 – 4411C → R in AAI10841 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti274 – 476203Missing Found in a truncated form isolated from Caco-2 cells treated with butyrate.
VAR_037985Add
BLAST
Natural varianti286 – 2861P → L.1 Publication
Corresponds to variant rs34155071 [ dbSNP | Ensembl ].
VAR_037986

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei168 – 22356Missing in isoform 3. 1 PublicationVSP_030335Add
BLAST
Alternative sequencei431 – 4311E → EEPDVPLA in isoform 2 and isoform 3. 2 PublicationsVSP_030336

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY255769 mRNA. Translation: AAP13480.1.
AB095031 mRNA. Translation: BAC76710.1.
AY927790 mRNA. Translation: AAY16126.1. Frameshift.
AY927791 mRNA. Translation: AAY16127.1.
BX322799 Genomic DNA. Translation: CAM24776.1.
BC041594 mRNA. Translation: AAH41594.1.
BC110840 mRNA. Translation: AAI10841.1.
AF039697 mRNA. Translation: AAC18046.1.
CCDSiCCDS59157.1. [Q86UR1-3]
CCDS7042.1. [Q86UR1-2]
RefSeqiNP_001242996.1. NM_001256067.1. [Q86UR1-1]
NP_001242997.1. NM_001256068.1. [Q86UR1-3]
NP_006638.1. NM_006647.1. [Q86UR1-2]
UniGeneiHs.495554.

Genome annotation databases

EnsembliENST00000341349; ENSP00000342848; ENSG00000188747. [Q86UR1-2]
ENST00000392815; ENSP00000376562; ENSG00000188747. [Q86UR1-3]
GeneIDi10811.
KEGGihsa:10811.
UCSCiuc004cmu.4. human. [Q86UR1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY255769 mRNA. Translation: AAP13480.1.
AB095031 mRNA. Translation: BAC76710.1.
AY927790 mRNA. Translation: AAY16126.1. Frameshift.
AY927791 mRNA. Translation: AAY16127.1.
BX322799 Genomic DNA. Translation: CAM24776.1.
BC041594 mRNA. Translation: AAH41594.1.
BC110840 mRNA. Translation: AAI10841.1.
AF039697 mRNA. Translation: AAC18046.1.
CCDSiCCDS59157.1. [Q86UR1-3]
CCDS7042.1. [Q86UR1-2]
RefSeqiNP_001242996.1. NM_001256067.1. [Q86UR1-1]
NP_001242997.1. NM_001256068.1. [Q86UR1-3]
NP_006638.1. NM_006647.1. [Q86UR1-2]
UniGeneiHs.495554.

3D structure databases

ProteinModelPortaliQ86UR1.
SMRiQ86UR1. Positions 3-186, 403-453.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116025. 13 interactions.
IntActiQ86UR1. 8 interactions.
MINTiMINT-1211202.
STRINGi9606.ENSP00000342848.

PTM databases

iPTMnetiQ86UR1.
PhosphoSiteiQ86UR1.

Polymorphism and mutation databases

BioMutaiNOXA1.
DMDMi74759404.

Proteomic databases

PaxDbiQ86UR1.
PRIDEiQ86UR1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000341349; ENSP00000342848; ENSG00000188747. [Q86UR1-2]
ENST00000392815; ENSP00000376562; ENSG00000188747. [Q86UR1-3]
GeneIDi10811.
KEGGihsa:10811.
UCSCiuc004cmu.4. human. [Q86UR1-1]

Organism-specific databases

CTDi10811.
GeneCardsiNOXA1.
H-InvDBHIX0018704.
HGNCiHGNC:10668. NOXA1.
HPAiHPA044781.
MIMi611255. gene.
neXtProtiNX_Q86UR1.
PharmGKBiPA35598.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4225. Eukaryota.
ENOG41110AD. LUCA.
GeneTreeiENSGT00530000063843.
HOGENOMiHOG000237312.
HOVERGENiHBG098043.
InParanoidiQ86UR1.
OMAiFQLERFQ.
OrthoDBiEOG7S7SF5.
PhylomeDBiQ86UR1.
TreeFamiTF329087.

Enzyme and pathway databases

ReactomeiR-HSA-5668599. RHO GTPases Activate NADPH Oxidases.
SIGNORiQ86UR1.

Miscellaneous databases

GeneWikiiNOXA1.
GenomeRNAii10811.
PROiQ86UR1.
SOURCEiSearch...

Gene expression databases

BgeeiQ86UR1.
CleanExiHS_NOXA1.
GenevisibleiQ86UR1. HS.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR000270. PB1_dom.
IPR001452. SH3_domain.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF00564. PB1. 1 hit.
PF00018. SH3_1. 1 hit.
PF13176. TPR_7. 1 hit.
[Graphical view]
SMARTiSM00666. PB1. 1 hit.
SM00326. SH3. 1 hit.
SM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
SSF50044. SSF50044. 1 hit.
PROSITEiPS51745. PB1. 1 hit.
PS50002. SH3. 1 hit.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Proteins homologous to p47phox and p67phox support superoxide production by NAD(P)H oxidase 1 in colon epithelial cells."
    Geiszt M., Lekstrom K., Witta J., Leto T.L.
    J. Biol. Chem. 278:20006-20012(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION AS NOX1 ACTIVATOR.
    Tissue: Kidney.
  2. "Novel human homologues of p47phox and p67phox participate in activation of superoxide-producing NADPH oxidases."
    Takeya R., Ueno N., Kami K., Taura M., Kohjima M., Izaki T., Nunoi H., Sumimoto H.
    J. Biol. Chem. 278:25234-25246(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION AS NOX1 ACTIVATOR, INTERACTION WITH NCF1; NOXO1 AND RAC1, MUTAGENESIS OF ARG-103 AND TRP-436, TISSUE SPECIFICITY.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION AS NOX1 ACTIVATOR, MUTAGENESIS OF PRO-34; PRO-37 AND TRP-436, VARIANTS LEU-286 AND NOXA1TRUNCATED.
    Tissue: Colon adenocarcinoma.
  4. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Brain and Colon.
  6. "Characterization of human colon cancer antigens recognized by autologous antibodies."
    Scanlan M.J., Chen Y.-T., Williamson B., Gure A.O., Stockert E., Gordan J.D., Tuereci O., Sahin U., Pfreundschuh M., Old L.J.
    Int. J. Cancer 76:652-658(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 245-476 (ISOFORM 1).
    Tissue: Colon cancer.
  7. "NOXO1, regulation of lipid binding, localization, and activation of Nox1 by the Phox homology (PX) domain."
    Cheng G., Lambeth J.D.
    J. Biol. Chem. 279:4737-4742(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS NOX1 ACTIVATOR.
  8. "Nox3 regulation by NOXO1, p47phox, and p67phox."
    Cheng G., Ritsick D., Lambeth J.D.
    J. Biol. Chem. 279:34250-34255(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS CYBB AND NOX3 ACTIVATOR, MUTAGENESIS OF VAL-205.
  9. "Role of nicotinamide adenine dinucleotide phosphate oxidase 1 in oxidative burst response to Toll-like receptor 5 signaling in large intestinal epithelial cells."
    Kawahara T., Kuwano Y., Teshima-Kondo S., Takeya R., Sumimoto H., Kishi K., Tsunawaki S., Hirayama T., Rokutan K.
    J. Immunol. 172:3051-3058(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "The NADPH oxidase Nox3 constitutively produces superoxide in a p22phox-dependent manner: its regulation by oxidase organizers and activators."
    Ueno N., Takeya R., Miyano K., Kikuchi H., Sumimoto H.
    J. Biol. Chem. 280:23328-23339(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE.
  11. "Nox1-dependent reactive oxygen generation is regulated by Rac1."
    Cheng G., Diebold B.A., Hughes Y., Lambeth J.D.
    J. Biol. Chem. 281:17718-17726(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX CONTAINING NOX1; NOXO1; NOXA1 AND RAC1, MUTAGENESIS OF ASP-68 AND ARG-103.
  12. "Direct involvement of the small GTPase Rac in activation of the superoxide-producing NADPH oxidase Nox1."
    Miyano K., Ueno N., Takeya R., Sumimoto H.
    J. Biol. Chem. 281:21857-21868(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH RAC1, MUTAGENESIS OF ARG-103 AND TRP-436.
  13. "Involvement of Rac1 in activation of multicomponent Nox1- and Nox3-based NADPH oxidases."
    Ueyama T., Geiszt M., Leto T.L.
    Mol. Cell. Biol. 26:2160-2174(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF THE FUNCTIONAL NOX1 OXIDASE COMPLEX, SUBCELLULAR LOCATION.
  14. "Interaction between the SH3 domains and C-terminal proline-rich region in NADPH oxidase organizer 1 (Noxo1)."
    Yamamoto A., Kami K., Takeya R., Sumimoto H.
    Biochem. Biophys. Res. Commun. 352:560-565(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NOXO1.
  15. "Regulation of Nox1 activity via PKA-mediated phosphorylation of NoxA1 and 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH YWHAZ, MUTAGENESIS OF SER-172 AND SER-461, PHOSPHORYLATION AT SER-172 AND SER-461.
  16. "Novel p47(phox)-related organizers regulate localized NADPH oxidase 1 (Nox1) activity."
    Gianni D., Diaz B., Taulet N., Fowler B., Courtneidge S.A., Bokoch G.M.
    Sci. Signal. 2:RA54-RA54(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SH3PXD2A AND SH3PXD2B.
  17. "Direct interaction between Tks proteins and the N-terminal proline-rich region (PRR) of NoxA1 mediates Nox1-dependent ROS generation."
    Gianni D., Dermardirossian C., Bokoch G.M.
    Eur. J. Cell Biol. 90:164-171(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SH3PXD2A AND SH3PXD2B.

Entry informationi

Entry nameiNOXA1_HUMAN
AccessioniPrimary (citable) accession number: Q86UR1
Secondary accession number(s): O60533
, Q29VU9, Q29VV0, Q2TAM1, Q8IUS3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 1, 2003
Last modified: June 8, 2016
This is version 118 of the entry and version 1 of the sequence. [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 9
    Human chromosome 9: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.