AOXA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AOXA_HUMAN
• UniProt AC: Q06278
• Protein Name: Aldehyde oxidase {ECO:0000312|HGNC:HGNC:553}
• Gene Name: AOX1 {ECO:0000312|HGNC:HGNC:553}
• Organism: Homo sapiens (Human).
• Sequence Length: 1338
• Subcellular Localization: Cytoplasm .
• Protein Description: 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..
• Protein Sequence: MDRASELLFYVNGRKVIEKNVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACTVMISRYNPITKRIRHHPANACLIPICSLYGAAVTTVEGIGSTHTRIHPVQERIAKCHGTQCGFCTPGMVMSIYTLLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACKTFCKTSGCCQSKENGVCCLDQGINGLPEFEEGSKTSPKLFAEEEFLPLDPTQELIFPPELMIMAEKQSQRTRVFGSERMMWFSPVTLKELLEFKFKYPQAPVIMGNTSVGPEVKFKGVFHPVIISPDRIEELSVVNHAYNGLTLGAGLSLAQVKDILADVVQKLPEEKTQMYHALLKHLGTLAGSQIRNMASLGGHIISRHPDSDLNPILAVGNCTLNLLSKEGKRQIPLNEQFLSKCPNADLKPQEILVSVNIPYSRKWEFVSAFRQAQRQENALAIVNSGMRVFFGEGDGIIRELCISYGGVGPATICAKNSCQKLIGRHWNEQMLDIACRLILNEVSLLGSAPGGKVEFKRTLIISFLFKFYLEVSQILKKMDPVHYPSLADKYESALEDLHSKHHCSTLKYQNIGPKQHPEDPIGHPIMHLSGVKHATGEAIYCDDMPLVDQELFLTFVTSSRAHAKIVSIDLSEALSMPGVVDIMTAEHLSDVNSFCFFTEAEKFLATDKVFCVGQLVCAVLADSEVQAKRAAKRVKIVYQDLEPLILTIEESIQHNSSFKPERKLEYGNVDEAFKVVDQILEGEIHMGGQEHFYMETQSMLVVPKGEDQEMDVYVSTQFPKYIQDIVASTLKLPANKVMCHVRRVGGAFGGKVLKTGIIAAVTAFAANKHGRAVRCVLERGEDMLITGGRHPYLGKYKAGFMNDGRILALDMEHYSNAGASLDESLFVIEMGLLKMDNAYKFPNLRCRGWACRTNLPSNTAFRGFGFPQAALITESCITEVAAKCGLSPEKVRIINMYKEIDQTPYKQEINAKNLIQCWRECMAMSSYSLRKVAVEKFNAENYWKKKGLAMVPLKFPVGLGSRAAGQAAALVHIYLDGSVLVTHGGIEMGQGVHTKMIQVVSRELRMPMSNVHLRGTSTETVPNANISGGSVVADLNGLAVKDACQTLLKRLEPIISKNPKGTWKDWAQTAFDESINLSAVGYFRGYESDMNWEKGEGQPFEYFVYGAACSEVEIDCLTGDHKNIRTDIVMDVGCSINPAIDIGQIEGAFIQGMGLYTIEELNYSPQGILHTRGPDQYKIPAICDMPTELHIALLPPSQNSNTLYSSKGLGESGVFLGCSVFFAIHDAVSAARQERGLHGPLTLNSPLTPEKIRMACEDKFTKMIPRDEPGSYVPWNVPI

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
59	Phosphorylation	CTVMISRYNPITKRI HHHEEECCCCCCHHH		50565719
195	Phosphorylation	LPEFEEGSKTSPKLF CCCCCCCCCCCCCCC		28857561
197	Phosphorylation	EFEEGSKTSPKLFAE CCCCCCCCCCCCCCC		28857561
198	Phosphorylation	FEEGSKTSPKLFAEE CCCCCCCCCCCCCCC		69010879
256	Acetylation	LKELLEFKFKYPQAP HHHHHHHCCCCCCCC		27178108
269	Phosphorylation	APVIMGNTSVGPEVK CCEEECCCCCCCCCE		46164825
270	Phosphorylation	PVIMGNTSVGPEVKF CEEECCCCCCCCCEE		30336225
287	Phosphorylation	VFHPVIISPDRIEEL EEECEEECHHHCCCC		24260401
347	Phosphorylation	HLGTLAGSQIRNMAS HHHHHHHHHHHHHHH		46164813
527	Phosphorylation	ISFLFKFYLEVSQIL HHHHHHHHHHHHHHH		46164831
531	Phosphorylation	FKFYLEVSQILKKMD HHHHHHHHHHHHHCC		46164819
542	Phosphorylation	KKMDPVHYPSLADKY HHCCCCCCHHHHHHH		22817900
549	Phosphorylation	YPSLADKYESALEDL CHHHHHHHHHHHHHH		68698769
551	Phosphorylation	SLADKYESALEDLHS HHHHHHHHHHHHHHH		68698775
558	Phosphorylation	SALEDLHSKHHCSTL HHHHHHHHHHCCCCC		68698781
697	Phosphorylation	AKRVKIVYQDLEPLI HHHEEEEECCCHHHE		50565711
722	Ubiquitination	SSFKPERKLEYGNVD CCCCCCHHCCCCCHH		29967540
788	Phosphorylation	IQDIVASTLKLPANK HHHHHHHHCCCCCCE		22210691
814	Phosphorylation	FGGKVLKTGIIAAVT CCCCHHHHHHHHHHH		68720047
821	Phosphorylation	TGIIAAVTAFAANKH HHHHHHHHHHHHCCC		68720053
851	Phosphorylation	ITGGRHPYLGKYKAG ECCCCCCCCCCCCCC		50565735
898	Phosphorylation	LLKMDNAYKFPNLRC EEECCCCCCCCCCEE		30576142
965	Ubiquitination	EIDQTPYKQEINAKN HCCCCCCCCCCCHHH		29967540
984	Phosphorylation	WRECMAMSSYSLRKV HHHHHHHCCCHHHHH		50565727
987	Phosphorylation	CMAMSSYSLRKVAVE HHHHCCCHHHHHHHH		24719451
1068	Phosphorylation	RELRMPMSNVHLRGT HHHCCCCCCEEECCC		26842593
1105	Phosphorylation	AVKDACQTLLKRLEP CHHHHHHHHHHHHHH		22210691
1108	Ubiquitination	DACQTLLKRLEPIIS HHHHHHHHHHHHHHC		-
1121	Phosphorylation	ISKNPKGTWKDWAQT HCCCCCCCHHHHHHH		30619164
1128	Phosphorylation	TWKDWAQTAFDESIN CHHHHHHHHHHCCCC		69008133
1304	Phosphorylation	HGPLTLNSPLTPEKI CCCCCCCCCCCHHHH		27794612
1307	Phosphorylation	LTLNSPLTPEKIRMA CCCCCCCCHHHHHHH		21815630
1318	Acetylation	IRMACEDKFTKMIPR HHHHHHHCCCCCCCC		30586949
1318	Ubiquitination	IRMACEDKFTKMIPR HHHHHHHCCCCCCCC		-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of AOXA_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of AOXA_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of AOXA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RBL1_HUMAN	RBL1	physical	21988832
CRKL_HUMAN	CRKL	physical	21988832
GLPK_HUMAN	GK	physical	21988832
ZN363_HUMAN	RCHY1	physical	21988832

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
• DB00437: Allopurinol
• DB00513: Aminocaproic Acid
• DB00484: Brimonidine
• DB00426: Famciclovir
• DB00170: Menadione
• DB01033: Mercaptopurine
• DB00563: Methotrexate
• DB00339: Pyrazinamide
• DB00481: Raloxifene
• DB00962: Zaleplon
• DB00909: Zonisamide