Q86UR1 (NOXA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	NOXA1
Synonyms:	P51NOX

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	476 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1 Ref.2 Ref.3 Ref.7 Ref.8 Ref.9 Ref.10 Ref.13 Ref.16
Subunit structure	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. Ref.2 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17
Subcellular location	Cytoplasm. Cell membrane. Note: Translocation to membranes depends on NOXO1 or NCF1 and maybe RAC1. Ref.12 Ref.13
Tissue specificity	Widely expressed. Detected in pancreas, liver, kidney, spleen, prostate, small intestine and colon. Ref.2
Developmental stage	Expressed in fetal kidney. Ref.10
Domain	The SH3 domain mediates interaction with NOXO1 and NCF1 and has autoregulatory function. The TPR repeats mediate interaction with RAC1.
Post-translational modification	Interaction with YWHAZ depends on phosphorylation by PKA.
Sequence similarities	Belongs to the NCF2/NOXA1 family. Contains 1 OPR domain. Contains 1 SH3 domain. Contains 4 TPR repeats.
Sequence caution	The sequence AAY16126.1 differs from that shown. Reason: Frameshift at position 305.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat SH3 domain TPR repeat
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	regulation of hydrogen peroxide metabolic process Inferred from mutant phenotype Ref.11. Source: BHF-UCL regulation of respiratory burst Inferred from mutant phenotype Ref.11. Source: BHF-UCL superoxide metabolic process Inferred from mutant phenotype Ref.17. Source: UniProtKB
Cellular_component	NADPH oxidase complex Inferred from direct assay Ref.11. Source: BHF-UCL cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	superoxide-generating NADPH oxidase activator activity Inferred from direct assay Ref.17. Source: UniProtKB
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q86UR1-1)

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 2 (identifier: Q86UR1-2)

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.

Isoform 3 (identifier: Q86UR1-3)

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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 476	476	NADPH oxidase activator 1		PRO_0000314609
Regions
	Repeat	7 – 38	32	TPR 1
	Repeat	39 – 71	33	TPR 2
	Repeat	73 – 105	33	TPR 3
	Repeat	122 – 155	34	TPR 4
	Domain	315 – 395	81	OPR
	Domain	399 – 458	60	SH3
	Region	1 – 224	224	Mediates interaction with RAC1
Amino acid modifications
	Modified residue	172	1	Phosphoserine; by PKA Ref.15
	Modified residue	461	1	Phosphoserine; by PKA Ref.15
Natural variations
	Alternative sequence	168 – 223	56	Missing in isoform 3.		VSP_030335
	Alternative sequence	431	1	E → EEPDVPLA in isoform 2 and isoform 3.		VSP_030336
	Natural variant	274 – 476	203	Missing in NOXA1truncated, a cDNA isolated from Caco-2 cells treated with butyrate.		VAR_037985
	Natural variant	286	1	P → L. Ref.3 Corresponds to variant rs34155071 [ dbSNP | Ensembl ].		VAR_037986
Experimental info
	Mutagenesis	34	1	P → A: Partial loss of function. Ref.3
	Mutagenesis	37	1	P → A: Partial loss of function. Ref.3
	Mutagenesis	68	1	D → A: Loss of function and loss of interaction with RAC1. Ref.11
	Mutagenesis	103	1	R → E: Loss of function and loss of interaction with RAC1. Loss of localization to membranes. Ref.2 Ref.11 Ref.12
	Mutagenesis	172	1	S → A: Loss of phosphorylation. Loss of interaction with YHAWZ; when associated with A-461. Ref.15
	Mutagenesis	172	1	S → E: Constitutively interacts with YWHAZ; when associated with E-461. Ref.15
	Mutagenesis	205	1	V → A: Unable to activate NOX2. Ref.8
	Mutagenesis	436	1	W → R: Loss of interaction with NOXO1 and NCF1. Loss of localization to membranes. Partial loss of function. Ref.2 Ref.3 Ref.12
	Mutagenesis	461	1	S → A: Loss of phosphorylation. Loss of interaction with YHAWZ; when associated with A-172. Ref.15
	Mutagenesis	461	1	S → E: Constitutively interacts with YWHAZ; when associated with E-172. Ref.15
	Sequence conflict	51	1	A → T in AAY16126. Ref.3
	Sequence conflict	56	1	A → T in AAY16127. Ref.3
	Sequence conflict	73	1	V → L in AAY16127. Ref.3
	Sequence conflict	142	1	A → T in AAY16127. Ref.3
	Sequence conflict	261	1	T → A in AAY16126. Ref.3
	Sequence conflict	277	1	K → E in AAY16126. Ref.3
	Sequence conflict	278	1	Q → V in AAC18046. Ref.6
	Sequence conflict	320	1	C → R in AAY16127. Ref.3
	Sequence conflict	329	1	R → G in AAC18046. Ref.6
	Sequence conflict	345 – 346	2	LP → FL in AAC18046. Ref.6
	Sequence conflict	354	1	L → F in AAC18046. Ref.6
	Sequence conflict	409	1	S → R in AAC18046. Ref.6
	Sequence conflict	441	1	C → R in AAI10841. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 64DFBF64C59722AD	FASTA	476	50,933
	10 20 30 40 50 60 MASLGDLVRA WHLGAQAVDR GDWARALHLF SGVPAPPARL CFNAGCVHLL AGDPEAALRA 70 80 90 100 110 120 FDQAVTKDTC MAVGFFQRGV ANFQLARFQE ALSDFWLALE QLRGHAAIDY TQLGLRFKLQ 130 140 150 160 170 180 AWEVLHNVAS AQCQLGLWTE AASSLREAMS KWPEGSLNGL DSALDQVQRR GSLPPRQVPR 190 200 210 220 230 240 GEVFRPHRWH LKHLEPVDFL GKAKVVASAI PDDQGWGVRP QQPQGPGANH DARSLIMDSP 250 260 270 280 290 300 RAGTHQGPLD AETEVGADRC TSTAYQEQRP QVEQVGKQAP LSPGLPAMGG PGPGPCEDPA 310 320 330 340 350 360 GAGGAGAGGS EPLVTVTVQC AFTVALRARR GADLSSLRAL LGQALPHQAQ LGQLSYLAPG 370 380 390 400 410 420 EDGHWVPIPE EESLQRAWQD AAACPRGLQL QCRGAGGRPV LYQVVAQHSY SAQGPEDLGF 430 440 450 460 470 RQGDTVDVLC EVDQAWLEGH CDGRIGIFPK CFVVPAGPRM SGAPGRLPRS QQGDQP
	Isoform 2 [UniParc]. Checksum: 3C3B2AC24286D2D2	FASTA	483	51,655
	10 20 30 40 50 60 MASLGDLVRA WHLGAQAVDR GDWARALHLF SGVPAPPARL CFNAGCVHLL AGDPEAALRA 70 80 90 100 110 120 FDQAVTKDTC MAVGFFQRGV ANFQLARFQE ALSDFWLALE QLRGHAAIDY TQLGLRFKLQ 130 140 150 160 170 180 AWEVLHNVAS AQCQLGLWTE AASSLREAMS KWPEGSLNGL DSALDQVQRR GSLPPRQVPR 190 200 210 220 230 240 GEVFRPHRWH LKHLEPVDFL GKAKVVASAI PDDQGWGVRP QQPQGPGANH DARSLIMDSP 250 260 270 280 290 300 RAGTHQGPLD AETEVGADRC TSTAYQEQRP QVEQVGKQAP LSPGLPAMGG PGPGPCEDPA 310 320 330 340 350 360 GAGGAGAGGS EPLVTVTVQC AFTVALRARR GADLSSLRAL LGQALPHQAQ LGQLSYLAPG 370 380 390 400 410 420 EDGHWVPIPE EESLQRAWQD AAACPRGLQL QCRGAGGRPV LYQVVAQHSY SAQGPEDLGF 430 440 450 460 470 480 RQGDTVDVLC EEPDVPLAVD QAWLEGHCDG RIGIFPKCFV VPAGPRMSGA PGRLPRSQQG DQP
	Isoform 3 (NOXA1inhib) [UniParc]. Checksum: 122CD814C315AA08	FASTA	427	45,245
	10 20 30 40 50 60 MASLGDLVRA WHLGAQAVDR GDWARALHLF SGVPAPPARL CFNAGCVHLL AGDPEAALRA 70 80 90 100 110 120 FDQAVTKDTC MAVGFFQRGV ANFQLARFQE ALSDFWLALE QLRGHAAIDY TQLGLRFKLQ 130 140 150 160 170 180 AWEVLHNVAS AQCQLGLWTE AASSLREAMS KWPEGSLNGL DSALDQVQGP GANHDARSLI 190 200 210 220 230 240 MDSPRAGTHQ GPLDAETEVG ADRCTSTAYQ EQRPQVEQVG KQAPLSPGLP AMGGPGPGPC 250 260 270 280 290 300 EDPAGAGGAG AGGSEPLVTV TVQCAFTVAL RARRGADLSS LRALLGQALP HQAQLGQLSY 310 320 330 340 350 360 LAPGEDGHWV PIPEEESLQR AWQDAAACPR GLQLQCRGAG GRPVLYQVVA QHSYSAQGPE 370 380 390 400 410 420 DLGFRQGDTV DVLCEEPDVP LAVDQAWLEG HCDGRIGIFP KCFVVPAGPR MSGAPGRLPR SQQGDQP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"NOX1 NADPH oxidase regulation by the NOXA1 SH3 domain." Valente A.J., Jamali A.E., Epperson T.K., Gamez M.J., Pearson D.W., Clark R.A. Free Radic. Biol. Med. 43:384-396(2007) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00216835. IPI00654838. IPI00879507.
RefSeq	NP_001242996.1. NM_001256067.1. NP_001242997.1. NM_001256068.1. NP_006638.1. NM_006647.1.
UniGene	Hs.495554.
3D structure databases
HSSP	HSSP built from PDB template 1K4U based on UniProtKB P19878.
ProteinModelPortal	Q86UR1.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q86UR1. 4 interactions.
MINT	MINT-1211202.
STRING	9606.ENSP00000342848.
PTM databases
PhosphoSite	Q86UR1.
Polymorphism databases
DMDM	74759404.
Proteomic databases
PaxDb	Q86UR1.
PRIDE	Q86UR1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000341349; ENSP00000342848; ENSG00000188747. ENST00000392815; ENSP00000376562; ENSG00000188747.
GeneID	10811.
KEGG	hsa:10811.
UCSC	uc004cmu.3. human. uc004cmv.3. human. uc010nch.3. human.
Organism-specific databases
CTD	10811.
GeneCards	GC09P140317.
H-InvDB	HIX0018704.
HGNC	HGNC:10668. NOXA1.
HPA	HPA044781.
MIM	611255. gene.
neXtProt	NX_Q86UR1.
PharmGKB	PA35598.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG272945.
HOGENOM	HOG000237312.
HOVERGEN	HBG098043.
InParanoid	Q86UR1.
OMA	FPKCFVV.
OrthoDB	EOG4ZW5BJ.
Gene expression databases
Bgee	Q86UR1.
CleanEx	HS_NOXA1.
Genevestigator	Q86UR1.
Family and domain databases
Gene3D	1.25.40.10. 1 hit.
InterPro	IPR000270. OPR_PB1. IPR000108. p67phox. IPR001452. SH3_domain. IPR013026. TPR-contain_dom. IPR011990. TPR-like_helical. IPR013105. TPR_2. IPR019734. TPR_repeat. [Graphical view]
Pfam	PF00564. PB1. 1 hit. PF00018. SH3_1. 1 hit. PF07719. TPR_2. 1 hit. [Graphical view]
PRINTS	PR00499. P67PHOX.
SMART	SM00666. PB1. 1 hit. SM00326. SH3. 1 hit. SM00028. TPR. 3 hits. [Graphical view]
SUPFAM	SSF50044. SH3. 1 hit.
PROSITE	PS50002. SH3. 1 hit. PS50005. TPR. False negative. PS50293. TPR_REGION. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	10811.
NextBio	41071.
SOURCE	Search...

Entry information

Entry name

NOXA1_HUMAN

Accession

Primary (citable) accession number: Q86UR1
Secondary accession number(s): O60533 , Q29VU9, Q29VV0, Q2TAM1, Q8IUS3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 87 of the entry and version 1 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.