AOFA_HUMAN - dbPTM
AOFA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AOFA_HUMAN
UniProt AC P21397
Protein Name Amine oxidase [flavin-containing] A
Gene Name MAOA
Organism Homo sapiens (Human).
Sequence Length 527
Subcellular Localization Mitochondrion outer membrane
Single-pass type IV membrane protein
Cytoplasmic side.
Protein Description Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOA preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT), norepinephrine and epinephrine..
Protein Sequence MENQEKASIAGHMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVDYVDVGGAYVGPTQNRILRLSKELGIETYKVNVSERLVQYVKGKTYPFRGAFPPVWNPIAYLDYNNLWRTIDNMGKEIPTDAPWEAQHADKWDKMTMKELIDKICWTKTARRFAYLFVNINVTSEPHEVSALWFLWYVKQCGGTTRIFSVTNGGQERKFVGGSGQVSERIMDLLGDQVKLNHPVTHVDQSSDNIIIETLNHEHYECKYVINAIPPTLTAKIHFRPELPAERNQLIQRLPMGAVIKCMMYYKEAFWKKKDYCGCMIIEDEDAPISITLDDTKPDGSLPAIMGFILARKADRLAKLHKEIRKKKICELYAKVLGSQEALHPVHYEEKNWCEEQYSGGCYTAYFPPGIMTQYGRVIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAAREVLNGLGKVTEKDIWVQEPESKDVPAVEITHTFWERNLPSVSGLLKIIGFSTSVTALGFVLYKYKLLPRS
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 Orthologous
Protein Cluster
1Acetylation-------MENQEKAS
-------CCHHHHHH
11.1511812236
52PhosphorylationRDRVGGRTYTIRNEH
CCCCCCEEEEEECCC
28.43-
53PhosphorylationDRVGGRTYTIRNEHV
CCCCCEEEEEECCCC
9.9820833797
54PhosphorylationRVGGRTYTIRNEHVD
CCCCEEEEEECCCCC
16.9124719451
136AcetylationRTIDNMGKEIPTDAP
HHHHCCCCCCCCCCC
41.5220167786
209PhosphorylationGGTTRIFSVTNGGQE
CCCEEEEEEECCCEE
26.1722817900
218UbiquitinationTNGGQERKFVGGSGQ
ECCCEEEEEECCCCH
43.5821890473
268PhosphorylationHEHYECKYVINAIPP
CCCEECEEEEECCCC
20.44-
345PhosphorylationDDTKPDGSLPAIMGF
CCCCCCCCHHHHHHH
38.26-
383PhosphorylationLYAKVLGSQEALHPV
HHHHHHCCCCHHCCC
22.2328857561
383O-linked_GlycosylationLYAKVLGSQEALHPV
HHHHHHCCCCHHCCC
22.2330379171
392PhosphorylationEALHPVHYEEKNWCE
CHHCCCCCCCCCCCC
26.4727251275
406S-8alpha-FAD cysteineEEQYSGGCYTAYFPP
CHHCCCCCEEEECCC
2.88-
406OtherEEQYSGGCYTAYFPP
CHHCCCCCEEEECCC
2.8818391214
469UbiquitinationGLGKVTEKDIWVQEP
CCCCCCHHHCEECCC
45.1821890473
469UbiquitinationGLGKVTEKDIWVQEP
CCCCCCHHHCEECCC
45.1821890473

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
209SPhosphorylationKinaseMAPK14Q16539
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

Disease-associated PTM Sites based on SAP

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

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

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

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AOFB_HUMANMAOBphysical
28514442
MID51_HUMANMIEF1physical
28514442

Drug and Disease Associations
Kegg Disease
H00548 Brunner syndrome; MAOA deficiency
OMIM Disease
300615Brunner syndrome (BRUNS)
Kegg Drug
D00076 Noradrenaline (JP16); Norepinephrine (INN); Nor adrenalin (TN)
D00095 Adrenaline (JP16); Epinephrine (USP/INN); Adrenalin (TN); Auvi-q (TN); Epipen (TN)
D00346 Isoniazid (JP16/USP/INN); Laniazid (TN)
D00415 Zolmitriptan (JAN/USAN/INN); Zomig (TN)
D00451 Sumatriptan (JAN/USP/INN); Imigran (TN); Imitrex (TN)
D00505 Phenelzine sulfate (USP); Nardil (TN)
D00675 Rizatriptan benzoate (JAN/USAN); Maxalt (TN)
D00676 Sumatriptan succinate (JAN/USAN); Alsuma (TN); Imitrex (TN); Sumave dosepro (TN); Zecutity (TN)
D00826 Tranylcypromine sulfate (USP XXI); Parnate (TN)
D01304 Amezinium metilsulfate (JAN); Risumic (TN)
D01501 Isoniazid calcium pyruvinate (JAN); Pyruvic acid calcium isoniazid
D01888 Safrazine hydrochloride (JAN)
D02002 Isoniazid sodium methanesulfonate hydrate (JAN); Isoniazid sodium methanesulfonate monohydrate; Ison
D02559 Toloxatone (INN); Humoryl (TN)
D02560 Brofaromine (INN); Consonar (TN)
D02561 Moclobemide (USAN/INN); Aurorix (TN)
D02563 Befloxatone (INN)
D02564 Pargyline hydrochloride (USAN); Eutonyl (TN)
D02579 Iproniazid (INN)
D02580 Isocarboxazid (INN); Marplan (TN)
D02581 Cimoxatone (INN)
D03239 Ladostigil tartrate (USAN)
D03248 Clorgiline (INN); Clorgyline
D03409 Caroxazone (USAN/INN)
D04092 Etryptamine acetate (USAN)
D05039 Minaprine (USAN/INN); Cantor (TN)
D05040 Minaprine hydrochloride (USAN)
D07337 Nialamide (INN); Niamid (TN)
D07338 Iproclozide (INN); Iproclozide (TN)
D08085 Iproniazid phosphate; Marsilid (TN)
D08284 Norepinephrine hydrochoride; (-)-Noradrenaline hydrochloride; Arterenol (TN)
D08349 Phenelzine (BAN)
D08392 Pirlindole (INN); Pyrazidol (TN)
D08393 Pirlindole hydrochloride; Implementor (TN)
D08453 Pargyline (INN)
D08625 Tranylcypromine (INN); Parnate (TN)
D09773 Isoniazid glucuronate sodium (JAN)
D09794 Norepinephrine hydrochloride (JAN); (+/-)-Noradrenaline hydrochloride
DrugBank
DB00918Almotriptan
DB00988Dopamine
DB01363Ephedra
DB03147Flavin adenine dinucleotide
DB00614Furazolidone
DB01247Isocarboxazid
DB00601Linezolid
DB01577Methamphetamine
DB00805Minaprine
DB01171Moclobemide
DB08804Nandrolone decanoate
DB00952Naratriptan
DB00184Nicotine
DB01626Pargyline
DB00780Phenelzine
DB00191Phentermine
DB00388Phenylephrine
DB00397Phenylpropanolamine
DB00721Procaine
DB00852Pseudoephedrine
DB00140Riboflavin
DB00953Rizatriptan
DB01037Selegiline
DB01104Sertraline
DB00669Sumatriptan
DB00624Testosterone
DB00752Tranylcypromine
DB00315Zolmitriptan
DB00909Zonisamide
Regulatory Network of AOFA_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"High-level expression of human liver monoamine oxidase A in Pichiapastoris: comparison with the enzyme expressed in Saccharomycescerevisiae.";
Li M., Hubalek F., Newton-Vinson P., Edmondson D.E.;
Protein Expr. Purif. 24:152-162(2002).
Cited for: PARTIAL PROTEIN SEQUENCE, ACETYLATION AT MET-1, AND MASS SPECTROMETRY.

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