AOX1

Functionⁱ

Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. Also may catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. May play a role in adipogenesis (By similarity).By similarity

Miscellaneous

AOX genes evolved from a xanthine oxidoreductase ancestral precursor via a series of gene duplication and suppression/deletion events. Different animal species contain a different complement of AOX genes encoding an equivalent number of AOX isoenzymes. In mammals, the two extremes are represented by certain rodents such as mice and rats, which are endowed with 4 AOX genes, and by humans, whose genome is characterized by a single active gene (PubMed:23263164).1 Publication

Catalytic activityⁱ

An aldehyde + H₂O + O₂ = a carboxylate + H₂O₂.By similarity

Retinal + O₂ + H₂O = retinoate + H₂O₂.By similarity

Cofactorⁱ

Protein has several cofactor binding sites:

[2Fe-2S] cluster
By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:O54754 (AOXA_MOUSE)
Note: Binds 2 [2Fe-2S] clusters per subunit.
By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:O54754 (AOXA_MOUSE)
FADBy similarity
Note: Binds 1 FAD per subunit.
By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:O54754 (AOXA_MOUSE)
Mo-molybdopterin
By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:O54754 (AOXA_MOUSE)
Note: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:O54754 (AOXA_MOUSE)

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	113	MolybdopterinBy similarity	1
Binding siteⁱ	151	MolybdopterinBy similarity	1
Binding siteⁱ	345	FAD; via amide nitrogenBy similarity	1
Binding siteⁱ	354	FADBy similarity	1
Binding siteⁱ	358	FADBy similarity	1
Binding siteⁱ	367	FADBy similarity	1
Binding siteⁱ	411	FAD; via amide nitrogen and carbonyl oxygenBy similarity	1
Binding siteⁱ	1047	Molybdopterin; via carbonyl oxygenBy similarity	1
Binding siteⁱ	1203	MolybdopterinBy similarity	1
Binding siteⁱ	1268	Molybdopterin; via carbonyl oxygenBy similarity	1
Active siteⁱ	1270	Proton acceptor; for azaheterocycle hydroxylase activityBy similarity	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	264 – 271	FADBy similarity		8

GO - Molecular functionⁱ

2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
aldehyde oxidase activity Source: UniProtKB-EC
electron transfer activity Source: InterPro
flavin adenine dinucleotide binding Source: InterPro
geranial:oxygen oxidoreductase activity Source: UniProtKB-EC
heptaldehyde:oxygen oxidoreductase activity Source: UniProtKB-EC
iron ion binding Source: InterPro
molybdopterin cofactor binding Source: InterPro
NAD binding Source: InterPro
oxidoreductase activity, acting on CH-OH group of donors Source: InterPro

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase
Ligand	2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum

Enzyme and pathway databases

BRENDAⁱ	1.2.3.1. 1793.
SABIO-RKⁱ	Q5FB27.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Aldehyde oxidase 1 (EC:1.2.3.1By similarity) Alternative name(s): Azaheterocycle hydroxylase 1 (EC:1.17.3.-)
Gene namesⁱ	Name:AOX1
Organismⁱ	Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Taxonomic identifierⁱ	9541 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Cercopithecoidea › Cercopithecidae › Cercopithecinae › Macaca

Keywords - Cellular componentⁱ

Cytoplasm

Pathology & Biotechⁱ

Chemistry databases

ChEMBLⁱ	CHEMBL1641357.

ChEMBLⁱ

CHEMBL1641357.

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000166105	1 – 1338	Aldehyde oxidase 1Add BLAST		1338

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	1068	PhosphoserineBy similarity		1

Keywords - PTMⁱ

Phosphoprotein

Expressionⁱ

Tissue specificityⁱ

Detected at high levels in liver, also detected in lung, kidney, lacrimal gland and olfactory mucosa.1 Publication

Interactionⁱ

Subunit structureⁱ

Homodimer.By similarity

Chemistry databases

BindingDBⁱ

Q5FB27.

Structureⁱ

3D structure databases

SMRⁱ	Q5FB27.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	5 – 92	2Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST		88
Domainⁱ	236 – 421	FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST		186

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	806 – 807	Molybdopterin bindingBy similarity		2
Regionⁱ	1088 – 1091	Molybdopterin bindingBy similarity		4

Sequence similaritiesⁱ

Belongs to the xanthine dehydrogenase family.Curated

Phylogenomic databases

HOVERGENⁱ	HBG004182.
KEGG Orthology (KO) More...KOⁱ	K00157.

Family and domain databases

InterProⁱ	View protein in InterPro IPR002888. 2Fe-2S-bd. IPR036884. 2Fe-2S-bd_dom_sf. IPR036010. 2Fe-2S_ferredoxin-like_sf. IPR001041. 2Fe-2S_ferredoxin-type. IPR006058. 2Fe2S_fd_BS. IPR000674. Ald_Oxase/Xan_DH_a/b. IPR036856. Ald_Oxase/Xan_DH_a/b_sf. IPR016208. Ald_Oxase/xanthine_DH. IPR014313. Aldehyde_oxidase. IPR008274. AldOxase/xan_DH_Mopterin-bd. IPR037165. AldOxase/xan_DH_Mopterin-bd_sf. IPR005107. CO_DH_flav_C. IPR036683. CO_DH_flav_C_dom_sf. IPR016166. FAD-bd_2. IPR036318. FAD-bd_2-like_sf. IPR002346. Mopterin_DH_FAD-bd. IPR022407. OxRdtase_Mopterin_BS.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01315. Ald_Xan_dh_C. 1 hit. PF02738. Ald_Xan_dh_C2. 1 hit. PF03450. CO_deh_flav_C. 1 hit. PF00941. FAD_binding_5. 1 hit. PF00111. Fer2. 1 hit. PF01799. Fer2_2. 1 hit.
PIRSFⁱ	PIRSF000127. Xanthine_DH. 1 hit.
SMARTⁱ	View protein in SMART SM01008. Ald_Xan_dh_C. 1 hit. SM01092. CO_deh_flav_C. 1 hit.
SUPFAMⁱ	SSF47741. SSF47741. 1 hit. SSF54292. SSF54292. 1 hit. SSF54665. SSF54665. 1 hit. SSF55447. SSF55447. 1 hit. SSF56003. SSF56003. 1 hit. SSF56176. SSF56176. 1 hit.
TIGRFAMsⁱ	TIGR02969. mam_aldehyde_ox. 1 hit.
PROSITEⁱ	View protein in PROSITE PS00197. 2FE2S_FER_1. 1 hit. PS51085. 2FE2S_FER_2. 1 hit. PS51387. FAD_PCMH. 1 hit. PS00559. MOLYBDOPTERIN_EUK. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

Q5FB27-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MDRASELLFY VNGRKVIEKN VDPETMLLPY LRKKLRLTGT KYGCGGGGCG 
        60         70         80         90        100
ACTVMISRYN PITNRIRHHP ANACLIPICS LYGTAVTTVE GIGSTHTRIH 
       110        120        130        140        150
PVQERIAKCH GTQCGFCTPG MVMSIYTLLR NHPEPTLDQL TDALGGNLCR 
       160        170        180        190        200
CTGYRPIIDA CKTFCETSGC CQSKENGVCC LDQRINGLPE FEEGSKTSPK 
       210        220        230        240        250
LFAEEEFLPL DPTQELIFPP ELMIMAEKQP QRTRVFGSER MMWFSPVTLK 
       260        270        280        290        300
ELLEFKFKYP QAPVIMGNTS VGPQMKFKGV FHPVIISPDR IEELSVVNHT 
       310        320        330        340        350
HNGLTLGAGL SLAQVKDILA DVVQKLPGEK TQTYHALLKH LGTLAGSQIR 
       360        370        380        390        400
NMASLGGHII SRHPDSDLNP ILAVGNCTLN LLSKEGKRQI PLNEQFLSKC 
       410        420        430        440        450
PNADLKPQEI LVSVNIPYSR KLEFVSAFRQ AQRQENALAI VNSGMRVFFG 
       460        470        480        490        500
EGHGIIRELS ISYGGVGPAT ICAKNSCQKL IGRHWNEEML DTACRLVLEE 
       510        520        530        540        550
VSLSGSAPGG RVEFKRTLII SFLFKFYLEV SQILKKMDPI RYPSLADKHE 
       560        570        580        590        600
SALEDLHSKH HCSTLKYQHM GPKQHPEDPI GHPIMHLSGV KHATGEAIYC 
       610        620        630        640        650
DDMPLVDQEL FLTFVTSSRA HAKIVSIDLS EALSMPGVVD VITAEHLSDV 
       660        670        680        690        700
NSFCFFTEAE EFLATDKVFC VGQLVCAVLA DSEVQAKRAA KQVKIVYQDL 
       710        720        730        740        750
EPLILTIKEA IQHNSFFEPE RKLEYGNVDE AFKVVDQILE GEIHMGGQEH 
       760        770        780        790        800
FYMETQSMLV VPKGEDQEMD VYVSTQFPKY IQDIVASTLK LPANKVMCHV 
       810        820        830        840        850
KRVGGAFGGK AFKTGVIAAV TAFAANKHGR AVRCVLERGE DMLITGGRHP 
       860        870        880        890        900
YLGKYKAGFM NDGRILALDM EHYSNAGNSL DESLLVIEMG LLKMDNAYKF 
       910        920        930        940        950
PNLRCRGWAC RTNLPSNTAF RGFGFPQAGL ITESCIMEVA AKCGLSPEKV 
       960        970        980        990       1000
RMINMYKEID QTPYKQEINA KNLIQCWREC MAVSSYSLRK AAVEKFNAEN 
      1010       1020       1030       1040       1050
YWKKKGLAMV PLKYPVGLGS RAAGQAAALV HIYLDGSVLV THGGIEMGQG 
      1060       1070       1080       1090       1100
VHTKMIQVVS RELGMPISNV HLRGTSTETV PNANVSGGSV VADLNGLAVK 
      1110       1120       1130       1140       1150
DACQTLLKRL EPIISKNPKG TWKDWAQTAF DESISLSAVG YFRGYESDIN 
      1160       1170       1180       1190       1200
WEKGEGHPFE YFVYGAACSE VEIDCLTGDH KNIRTDIVMD VGCSINPAID 
      1210       1220       1230       1240       1250
IGQIEGAFIQ GMGLYTIEEL NYSPQGVLHT RGPDQYKIPA ICDTPTEFHI 
      1260       1270       1280       1290       1300
SLLPPSENSN TLYSSKGLGE SGVFLGCSVF FAIHDAVSAA RRERGLHGPL 
      1310       1320       1330 
SLNSPLTPEK IRMACEDKFT KMIPRDEPGS CVPWNVPI

Length:1,338

Mass (Da):147,691

Last modified:February 19, 2014 - v2

Checksum:ⁱC82ACFAB5FA7019C

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	184	R → G in BAD89382 (Ref. 1) Curated	1
Sequence conflictⁱ	275	M → V in BAD89382 (Ref. 1) Curated	1
Sequence conflictⁱ	284 – 286	VII → GYN in BAD89382 (Ref. 1) Curated	3
Sequence conflictⁱ	294 – 302	LSVVNHTHN → PECCKPYTY in BAD89382 (Ref. 1) Curated	9
Sequence conflictⁱ	328	G → E in BAD89382 (Ref. 1) Curated	1
Sequence conflictⁱ	511	R → K in BAD89382 (Ref. 1) Curated	1
Sequence conflictⁱ	541	R → H in BAD89382 (Ref. 1) Curated	1
Sequence conflictⁱ	549	H → Y in BAD89382 (Ref. 1) Curated	1
Sequence conflictⁱ	605	L → P in BAD89382 (Ref. 1) Curated	1
Sequence conflictⁱ	1105	T → I in BAD89382 (Ref. 1) Curated	1
Sequence conflictⁱ	1139	V → I in BAD89382 (Ref. 1) Curated	1
Sequence conflictⁱ	1301	S → T in BAD89382 (Ref. 1) Curated	1
Sequence conflictⁱ	1338	I → V in BAD89382 (Ref. 1) Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AB201545 mRNA. Translation: BAD89382.1. FJ751935 mRNA. Translation: ACQ73553.1.
NCBI Reference Sequences More...RefSeqⁱ	NP_001271673.1. NM_001284744.1.
UniGeneⁱ	Mfa.7431.

Genome annotation databases

GeneIDⁱ	102131116.
KEGGⁱ	mcf:102131116.

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
Q5FB27	Q06278 B4DNI5 UPI00083C8473 A0A286LWX1 U3BBZ3 K7D3F1 A0A2K6RFN7 A0A2I3GID8 I0FRB2 F6T457 +53	Homo sapiens (Human) Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti) Callithrix jacchus (White-tufted-ear marmoset) Pan troglodytes (Chimpanzee) Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana) Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys) Macaca mulatta (Rhesus macaque) Gorilla gorilla gorilla (Western lowland gorilla) Gorilla gorilla (western gorilla) Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) And more	1,338	UniRef90_Q06278	Cluster: Aldehyde oxidase	64

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
Q5FB27	Q06278 B4DNI5 UPI00083C8473 A0A2I3GID8 A0A2K5D076 A0A1W7AET4 A0A2K6UKR4 K7D3F1 I0FRB2 Q5RAF7 +130	Homo sapiens (Human) Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti) Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys) Aotus nancymaae (Ma's night monkey) Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) Saimiri boliviensis boliviensis (Bolivian squirrel monkey) Pan troglodytes (Chimpanzee) Macaca mulatta (Rhesus macaque) Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys) And more	1,338	UniRef50_Q06278	Cluster: Aldehyde oxidase	141

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AB201545 mRNA. Translation: BAD89382.1. FJ751935 mRNA. Translation: ACQ73553.1.
NCBI Reference Sequences More...RefSeqⁱ	NP_001271673.1. NM_001284744.1.
UniGeneⁱ	Mfa.7431.

3D structure databases

SMRⁱ	Q5FB27.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Chemistry databases

BindingDBⁱ	Q5FB27.
ChEMBLⁱ	CHEMBL1641357.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

GeneIDⁱ	102131116.
KEGGⁱ	mcf:102131116.

Organism-specific databases

CTDⁱ	316.

CTDⁱ

316.

Phylogenomic databases

HOVERGENⁱ	HBG004182.
KEGG Orthology (KO) More...KOⁱ	K00157.

Enzyme and pathway databases

BRENDAⁱ	1.2.3.1. 1793.
SABIO-RKⁱ	Q5FB27.

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:Q5FB27.

PROⁱ

PR:Q5FB27.

Family and domain databases

InterProⁱ	View protein in InterPro IPR002888. 2Fe-2S-bd. IPR036884. 2Fe-2S-bd_dom_sf. IPR036010. 2Fe-2S_ferredoxin-like_sf. IPR001041. 2Fe-2S_ferredoxin-type. IPR006058. 2Fe2S_fd_BS. IPR000674. Ald_Oxase/Xan_DH_a/b. IPR036856. Ald_Oxase/Xan_DH_a/b_sf. IPR016208. Ald_Oxase/xanthine_DH. IPR014313. Aldehyde_oxidase. IPR008274. AldOxase/xan_DH_Mopterin-bd. IPR037165. AldOxase/xan_DH_Mopterin-bd_sf. IPR005107. CO_DH_flav_C. IPR036683. CO_DH_flav_C_dom_sf. IPR016166. FAD-bd_2. IPR036318. FAD-bd_2-like_sf. IPR002346. Mopterin_DH_FAD-bd. IPR022407. OxRdtase_Mopterin_BS.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01315. Ald_Xan_dh_C. 1 hit. PF02738. Ald_Xan_dh_C2. 1 hit. PF03450. CO_deh_flav_C. 1 hit. PF00941. FAD_binding_5. 1 hit. PF00111. Fer2. 1 hit. PF01799. Fer2_2. 1 hit.
PIRSFⁱ	PIRSF000127. Xanthine_DH. 1 hit.
SMARTⁱ	View protein in SMART SM01008. Ald_Xan_dh_C. 1 hit. SM01092. CO_deh_flav_C. 1 hit.
SUPFAMⁱ	SSF47741. SSF47741. 1 hit. SSF54292. SSF54292. 1 hit. SSF54665. SSF54665. 1 hit. SSF55447. SSF55447. 1 hit. SSF56003. SSF56003. 1 hit. SSF56176. SSF56176. 1 hit.
TIGRFAMsⁱ	TIGR02969. mam_aldehyde_ox. 1 hit.
PROSITEⁱ	View protein in PROSITE PS00197. 2FE2S_FER_1. 1 hit. PS51085. 2FE2S_FER_2. 1 hit. PS51387. FAD_PCMH. 1 hit. PS00559. MOLYBDOPTERIN_EUK. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	AOXA_MACFA
Accessionⁱ	Q5FB27Primary (citable) accession number: Q5FB27 Secondary accession number(s): D6BND8
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	April 12, 2005
	Last sequence update:	February 19, 2014
	Last modified:	March 28, 2018
	This is version 85 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

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UniProtKB - Q5FB27 (AOXA_MACFA)

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Aldehyde oxidase 1

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

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Other locations

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

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<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

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Protocols and materials databases

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Functionⁱ

GO - Molecular functionⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ