Q9Y5S8 (NOX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
NADPH oxidase 1
Short name=NOX-1
EC=1.-.-.-

Alternative name(s):
Mitogenic oxidase 1
Short name=MOX-1
NADH/NADPH mitogenic oxidase subunit P65-MOX
NOH-1

Gene names

Name:	NOX1
Synonyms:	MOX1, NOH1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	564 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	NOH-1S is a voltage-gated proton channel that mediates the H+ currents of resting phagocytes and other tissues. It participates in the regulation of cellular pH and is blocked by zinc. NOH-1L is a pyridine nucleotide-dependent oxidoreductase that generates superoxide and might conduct H+ ions as part of its electron transport mechanism, whereas NOH-1S does not contain an electron transport chain.
Cofactor	NADP Potential. FAD Potential.
Enzyme regulation	The oxidase activity is potentiated by NOXA1 and NOXO1. Ref.8 Ref.9
Subunit structure	NOX1, NOXA1, NOXO1, RAC1 and CYBA forms a functional multimeric complex supporting ROS production. Interacts with NOXA1 and NOXO1. Ref.9 Ref.10
Subcellular location	Cell projection › invadopodium membrane; Multi-pass membrane protein Ref.11.
Tissue specificity	NOH-1L is detected in colon, uterus, prostate, and colon carcinoma, but not in peripheral blood leukocytes. NOH-1S is detected only in colon and colon carcinoma cells.
Sequence similarities	Contains 1 FAD-binding FR-type domain. Contains 1 ferric oxidoreductase domain.

Ontologies

Keywords
Biological process	Electron transport Ion transport Transport
Cellular component	Cell junction Cell membrane Cell projection Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transmembrane Transmembrane helix
Ligand	FAD Heme Iron Metal-binding NADP
Molecular function	Ion channel Oxidoreductase Voltage-gated channel
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	FADH2 metabolic process Non-traceable author statement. Source: UniProtKB NADP metabolic process Inferred by curator Ref.1. Source: BHF-UCL angiogenesis Inferred from mutant phenotype PubMed 11805326. Source: BHF-UCL cell migration Inferred from mutant phenotype PubMed 18023288. Source: BHF-UCL electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW extracellular matrix organization Inferred from electronic annotation. Source: Compara hydrogen peroxide metabolic process Inferred from direct assay PubMed 11331784. Source: BHF-UCL inflammatory response Traceable author statement PubMed 18347018. Source: BHF-UCL intracellular pH elevation Inferred from direct assay Ref.2. Source: BHF-UCL oxygen metabolic process Inferred from electronic annotation. Source: Compara positive regulation of integrin biosynthetic process Inferred from mutant phenotype PubMed 18023288. Source: BHF-UCL positive regulation of smooth muscle cell proliferation Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL positive regulation vascular endothelial growth factor production Inferred from expression pattern PubMed 11805326. Source: BHF-UCL regulation of blood pressure Traceable author statement PubMed 18347018. Source: BHF-UCL regulation of systemic arterial blood pressure by renin-angiotensin Inferred from electronic annotation. Source: Compara respiratory burst Traceable author statement Ref.10. Source: BHF-UCL response to pH Inferred from direct assay Ref.2. Source: BHF-UCL signal transduction Traceable author statement PubMed 17673675. Source: BHF-UCL superoxide anion generation Inferred from direct assay Ref.1. Source: BHF-UCL
Cellular_component	NADPH oxidase complex Inferred from direct assay Ref.10. Source: BHF-UCL cell junction Inferred from electronic annotation. Source: UniProtKB-KW early endosome Inferred from direct assay PubMed 17673675. Source: BHF-UCL invadopodium membrane Inferred from direct assay Ref.11. Source: UniProtKB
Molecular_function	NADP binding Inferred by curator Ref.1. Source: BHF-UCL metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW superoxide-generating NADPH oxidase activity Traceable author statement Ref.1. Source: UniProtKB voltage-gated proton channel activity Inferred from direct assay Ref.2. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform NOH-1L (identifier: Q9Y5S8-1)

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.

Isoform NOH-1S (identifier: Q9Y5S8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     159-190: QSRNTTVEYVTFTSIAGLTGVIMTIALILMVT → HPHITPTVYMFTVTFDMVLSSVNSNLLFLLIK
     191-564: Missing.

Isoform NOH-1LV (identifier: Q9Y5S8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     433-481: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 564	564	NADPH oxidase 1		PRO_0000210148
Regions
	Topological domain	1 – 9	9	Cytoplasmic Potential
	Transmembrane	10 – 30	21	Helical; Potential
	Topological domain	31 – 44	14	Extracellular Potential
	Transmembrane	45 – 72	28	Helical; Potential
	Topological domain	73 – 102	30	Cytoplasmic Potential
	Transmembrane	103 – 123	21	Helical; Potential
	Topological domain	124 – 168	45	Extracellular Potential
	Transmembrane	169 – 189	21	Helical; Potential
	Topological domain	190 – 206	17	Cytoplasmic Potential
	Transmembrane	207 – 227	21	Helical; Potential
	Topological domain	228 – 396	169	Extracellular Potential
	Transmembrane	397 – 417	21	Helical; Potential
	Topological domain	418 – 564	147	Cytoplasmic Potential
	Domain	54 – 283	230	Ferric oxidoreductase
	Domain	284 – 391	108	FAD-binding FR-type
	Nucleotide binding	338 – 344	7	FAD Potential
	Region	397 – 536	140	Interaction with NOXO1
Sites
	Metal binding	101	1	Iron (heme axial ligand) Probable
	Metal binding	115	1	Iron (heme axial ligand) Probable
	Metal binding	209	1	Iron (heme axial ligand) Probable
	Metal binding	221	1	Iron (heme axial ligand) Probable
Amino acid modifications
	Glycosylation	162	1	N-linked (GlcNAc...) Potential
	Glycosylation	236	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	159 – 190	32	QSRNT…ILMVT → HPHITPTVYMFTVTFDMVLS SVNSNLLFLLIK in isoform NOH-1S.		VSP_001577
	Alternative sequence	191 – 564	374	Missing in isoform NOH-1S.		VSP_001578
	Alternative sequence	433 – 481	49	Missing in isoform NOH-1LV.		VSP_001579
	Natural variant	315	1	R → H. Corresponds to variant rs2071756 [ dbSNP | Ensembl ].		VAR_049101
	Natural variant	360	1	D → N. Corresponds to variant rs34688635 [ dbSNP | Ensembl ].		VAR_061176
	Natural variant	378	1	R → K. Corresponds to variant rs35404864 [ dbSNP | Ensembl ].		VAR_049102
Experimental info
	Sequence conflict	173	1	I → V in AAD38133. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform NOH-1L [UniParc]. Last modified May 1, 2000. Version 2. Checksum: C3BE290F4E6DBC9A	FASTA	564	64,871
	10 20 30 40 50 60 MGNWVVNHWF SVLFLVVWLG LNVFLFVDAF LKYEKADKYY YTRKILGSTL ACARASALCL 70 80 90 100 110 120 NFNSTLILLP VCRNLLSFLR GTCSFCSRTL RKQLDHNLTF HKLVAYMICL HTAIHIIAHL 130 140 150 160 170 180 FNFDCYSRSR QATDGSLASI LSSLSHDEKK GGSWLNPIQS RNTTVEYVTF TSIAGLTGVI 190 200 210 220 230 240 MTIALILMVT SATEFIRRSY FEVFWYTHHL FIFYILGLGI HGIGGIVRGQ TEESMNESHP 250 260 270 280 290 300 RKCAESFEMW DDRDSHCRRP KFEGHPPESW KWILAPVILY ICERILRFYR SQQKVVITKV 310 320 330 340 350 360 VMHPSKVLEL QMNKRGFSME VGQYIFVNCP SISLLEWHPF TLTSAPEEDF FSIHIRAAGD 370 380 390 400 410 420 WTENLIRAFE QQYSPIPRIE VDGPFGTASE DVFQYEVAVL VGAGIGVTPF ASILKSIWYK 430 440 450 460 470 480 FQCADHNLKT KKIYFYWICR ETGAFSWFNN LLTSLEQEME ELGKVGFLNY RLFLTGWDSN 490 500 510 520 530 540 IVGHAALNFD KATDIVTGLK QKTSFGRPMW DNEFSTIATS HPKSVVGVFL CGPRTLAKSL 550 560 RKCCHRYSSL DPRKVQFYFN KENF
	Isoform NOH-1S [UniParc]. Checksum: 75C0B809E9AE8E3D	FASTA	190	21,704
	10 20 30 40 50 60 MGNWVVNHWF SVLFLVVWLG LNVFLFVDAF LKYEKADKYY YTRKILGSTL ACARASALCL 70 80 90 100 110 120 NFNSTLILLP VCRNLLSFLR GTCSFCSRTL RKQLDHNLTF HKLVAYMICL HTAIHIIAHL 130 140 150 160 170 180 FNFDCYSRSR QATDGSLASI LSSLSHDEKK GGSWLNPIHP HITPTVYMFT VTFDMVLSSV 190 NSNLLFLLIK
	Isoform NOH-1LV [UniParc]. Checksum: 1D79577159D69688	FASTA	515	58,972
	10 20 30 40 50 60 MGNWVVNHWF SVLFLVVWLG LNVFLFVDAF LKYEKADKYY YTRKILGSTL ACARASALCL 70 80 90 100 110 120 NFNSTLILLP VCRNLLSFLR GTCSFCSRTL RKQLDHNLTF HKLVAYMICL HTAIHIIAHL 130 140 150 160 170 180 FNFDCYSRSR QATDGSLASI LSSLSHDEKK GGSWLNPIQS RNTTVEYVTF TSIAGLTGVI 190 200 210 220 230 240 MTIALILMVT SATEFIRRSY FEVFWYTHHL FIFYILGLGI HGIGGIVRGQ TEESMNESHP 250 260 270 280 290 300 RKCAESFEMW DDRDSHCRRP KFEGHPPESW KWILAPVILY ICERILRFYR SQQKVVITKV 310 320 330 340 350 360 VMHPSKVLEL QMNKRGFSME VGQYIFVNCP SISLLEWHPF TLTSAPEEDF FSIHIRAAGD 370 380 390 400 410 420 WTENLIRAFE QQYSPIPRIE VDGPFGTASE DVFQYEVAVL VGAGIGVTPF ASILKSIWYK 430 440 450 460 470 480 FQCADHNLKT KKVGHAALNF DKATDIVTGL KQKTSFGRPM WDNEFSTIAT SHPKSVVGVF 490 500 510 LCGPRTLAKS LRKCCHRYSS LDPRKVQFYF NKENF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cell transformation by the superoxide-generating oxidase Mox1." Suh Y.-A., Arnold R.S., Lassegue B., Shi J., Xu X., Sorescu D., Chung A.B., Griendling K.K., Lambeth J.D. Nature 401:79-82(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM NOH-1L). Tissue: Colon epithelium.
[2]	"A mammalian H+ channel, generated through alternative splicing of the NADPH oxidase homolog NOH-1." Banfi B., Maturana A., Jaconi S., Arnaudeau S., Laforge T., Sinha B., Ligeti E., Demaurex N., Krause K.-H. Science 287:138-142(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS NOH-1L; NOH-1LV AND NOH-1S).
[3]	NHLBI resequencing and genotyping service (RS&G) Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM NOH-1L). Tissue: Colon.
[5]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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] (ISOFORM NOH-1L).
[8]	"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: ENZYME REGULATION.
[9]	"Molecular interaction of NADPH oxidase 1 with betaPix and Nox Organizer 1." Park H.S., Park D., Bae Y.S. Biochem. Biophys. Res. Commun. 339:985-990(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NOXO1, ENZYME REGULATION.
[10]	"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.
[11]	"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: SUBCELLULAR LOCATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF127763 mRNA. Translation: AAD38133.1. AF166326 mRNA. Translation: AAF23232.1. AF166327 mRNA. Translation: AAF23233.1. AF166328 mRNA. Translation: AAF23234.1. DQ314883 Genomic DNA. Translation: ABC40742.1. AK292201 mRNA. Translation: BAF84890.1. Z83819 Genomic DNA. Translation: CAI42336.1. Z83819 Genomic DNA. Translation: CAI42337.1. CH471115 Genomic DNA. Translation: EAX02820.1. BC075014 mRNA. Translation: AAH75014.1. BC075015 mRNA. Translation: AAH75015.1.
IPI	IPI00216593. IPI00292186. IPI00336126.
RefSeq	NP_001258744.1. NM_001271815.1. NP_008983.2. NM_007052.4. NP_039249.1. NM_013955.2.
UniGene	Hs.592227.
3D structure databases
ProteinModelPortal	Q9Y5S8.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000362057.
Protein family/group databases
PeroxiBase	5410. HsNOx01.
TCDB	5.B.1.1.3. phagocyte (gp91phox) NADPH oxidase family.
PTM databases
PhosphoSite	Q9Y5S8.
Polymorphism databases
DMDM	8134597.
Proteomic databases
PaxDb	Q9Y5S8.
PRIDE	Q9Y5S8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000217885; ENSP00000217885; ENSG00000007952. ENST00000372966; ENSP00000362057; ENSG00000007952.
GeneID	27035.
KEGG	hsa:27035.
UCSC	uc004egj.3. human. uc004egl.4. human.
Organism-specific databases
CTD	27035.
GeneCards	GC0XM100098.
HGNC	HGNC:7889. NOX1.
HPA	HPA035299. HPA035300.
MIM	300225. gene.
neXtProt	NX_Q9Y5S8.
PharmGKB	PA31690.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG287712.
HOGENOM	HOG000216669.
HOVERGEN	HBG003760.
InParanoid	Q9Y5S8.
KO	K08008.
OMA	KEFWEQI.
OrthoDB	EOG4Z8XW4.
PhylomeDB	Q9Y5S8.
Gene expression databases
ArrayExpress	Q9Y5S8.
Bgee	Q9Y5S8.
CleanEx	HS_NOX1.
Genevestigator	Q9Y5S8.
GermOnline	ENSG00000007952. Homo sapiens.
Family and domain databases
InterPro	IPR000778. Cyt_b245_heavy_chain. IPR013112. FAD-bd_8. IPR017927. Fd_Rdtase_FAD-bd. IPR013130. Fe3_Rdtase_TM_dom. IPR013121. Fe_red_NAD-bd_6. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view]
Pfam	PF08022. FAD_binding_8. 1 hit. PF01794. Ferric_reduct. 1 hit. PF08030. NAD_binding_6. 1 hit. [Graphical view]
PRINTS	PR00466. GP91PHOX.
SUPFAM	SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITE	PS51384. FAD_FR. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q9Y5S8.
ChEMBL	CHEMBL1287628.
GenomeRNAi	27035.
NextBio	49586.
SOURCE	Search...

Entry information

Entry name

NOX1_HUMAN

Accession

Primary (citable) accession number: Q9Y5S8
Secondary accession number(s): A8K836, O95691, Q2PP02

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 119 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.