AOFB_HUMAN - dbPTM
AOFB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AOFB_HUMAN
UniProt AC P27338
Protein Name Amine oxidase [flavin-containing] B
Gene Name MAOB
Organism Homo sapiens (Human).
Sequence Length 520
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. MAOB preferentially degrades benzylamine and phenylethylamine..
Protein Sequence MSNKCDVVVVGGGISGMAAAKLLHDSGLNVVVLEARDRVGGRTYTLRNQKVKYVDLGGSYVGPTQNRILRLAKELGLETYKVNEVERLIHHVKGKSYPFRGPFPPVWNPITYLDHNNFWRTMDDMGREIPSDAPWKAPLAEEWDNMTMKELLDKLCWTESAKQLATLFVNLCVTAETHEVSALWFLWYVKQCGGTTRIISTTNGGQERKFVGGSGQVSERIMDLLGDRVKLERPVIYIDQTRENVLVETLNHEMYEAKYVISAIPPTLGMKIHFNPPLPMMRNQMITRVPLGSVIKCIVYYKEPFWRKKDYCGTMIIDGEEAPVAYTLDDTKPEGNYAAIMGFILAHKARKLARLTKEERLKKLCELYAKVLGSLEALEPVHYEEKNWCEEQYSGGCYTTYFPPGILTQYGRVLRQPVDRIYFAGTETATHWSGYMEGAVEAGERAAREILHAMGKIPEDEIWQSEPESVDVPAQPITTTFLERHLPSVPGLLRLIGLTTIFSATALGFLAHKRGLLVRV
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
2Acetylation------MSNKCDVVV
------CCCCCCEEE		45.0211049757
26PhosphorylationAAKLLHDSGLNVVVL
HHHHHHHCCCCEEEE		34.1428258704
43PhosphorylationRDRVGGRTYTLRNQK
CCCCCCEEEEECCCE		24.92-
44PhosphorylationDRVGGRTYTLRNQKV
CCCCCEEEEECCCEE		11.4724719451
45PhosphorylationRVGGRTYTLRNQKVK
CCCCEEEEECCCEEE		20.7324719451
52AcetylationTLRNQKVKYVDLGGS
EECCCEEEEEECCCC		46.74-
52UbiquitinationTLRNQKVKYVDLGGS
EECCCEEEEEECCCC		46.7421906983
53PhosphorylationLRNQKVKYVDLGGSY
ECCCEEEEEECCCCC		11.37-
59PhosphorylationKYVDLGGSYVGPTQN
EEEECCCCCCCCHHH		18.1728857561
60PhosphorylationYVDLGGSYVGPTQNR
EEECCCCCCCCHHHH		16.83-
64PhosphorylationGGSYVGPTQNRILRL
CCCCCCCHHHHHHHH		32.3328857561
73UbiquitinationNRILRLAKELGLETY
HHHHHHHHHHCCCEE		59.0521906983
81UbiquitinationELGLETYKVNEVERL
HHCCCEEEHHHHHHH		46.1021906983
93UbiquitinationERLIHHVKGKSYPFR
HHHHHHHCCCCCCCC		57.15-
131PhosphorylationDMGREIPSDAPWKAP
HHCCCCCCCCCCCCC		52.6622673903
136UbiquitinationIPSDAPWKAPLAEEW
CCCCCCCCCCCHHHH		38.7821906983
181PhosphorylationTAETHEVSALWFLWY
CCCHHHHHHHHHHHH		18.0526074081
188PhosphorylationSALWFLWYVKQCGGT
HHHHHHHHHHHCCCE		10.4226074081
195PhosphorylationYVKQCGGTTRIISTT
HHHHCCCEEEEEEEC		9.7426074081
196PhosphorylationVKQCGGTTRIISTTN
HHHCCCEEEEEEECC		24.1226074081
200PhosphorylationGGTTRIISTTNGGQE
CCEEEEEEECCCCCE		27.1426074081
201PhosphorylationGTTRIISTTNGGQER
CEEEEEEECCCCCEE		17.5526074081
202PhosphorylationTTRIISTTNGGQERK
EEEEEEECCCCCEEE		25.6926074081
209UbiquitinationTNGGQERKFVGGSGQ
CCCCCEEEEECCCCH		43.5821906983
214PhosphorylationERKFVGGSGQVSERI
EEEEECCCCHHHHHH		21.8126074081
218PhosphorylationVGGSGQVSERIMDLL
ECCCCHHHHHHHHHH		17.1722210691
230UbiquitinationDLLGDRVKLERPVIY
HHHCCCCCCCCCEEE		45.5921906983
337PhosphorylationDTKPEGNYAAIMGFI
CCCCCCCHHHHHHHH		14.31-
370UbiquitinationKLCELYAKVLGSLEA
HHHHHHHHHHHCHHH		25.16-
374PhosphorylationLYAKVLGSLEALEPV
HHHHHHHCHHHHCCC		20.9020833797
383PhosphorylationEALEPVHYEEKNWCE
HHHCCCCCCCCCCCC		26.47-
397OtherEEQYSGGCYTTYFPP
CHHCCCCCCCCCCCC		2.8811753429
397S-8alpha-FAD cysteineEEQYSGGCYTTYFPP
CHHCCCCCCCCCCCC		2.88-
456UbiquitinationEILHAMGKIPEDEIW
HHHHHCCCCCHHHHH		41.8421906983
465PhosphorylationPEDEIWQSEPESVDV
CHHHHHHCCCCCCCC		39.8728857561
469PhosphorylationIWQSEPESVDVPAQP
HHHCCCCCCCCCCCC		34.0428857561
478PhosphorylationDVPAQPITTTFLERH
CCCCCCCCHHHHHHC		26.8527251275
479PhosphorylationVPAQPITTTFLERHL
CCCCCCCHHHHHHCC		19.1027251275
480PhosphorylationPAQPITTTFLERHLP
CCCCCCHHHHHHCCC		19.9927251275
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

Oops, there are no upstream regulatory protein records of AOFB_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AOFB_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 AOFB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRPK1_HUMANSRPK1physical
21988832
NFYB_HUMANNFYBphysical
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
D00095 Adrenaline (JP16); Epinephrine (USP/INN); Adrenalin (TN); Auvi-q (TN); Epipen (TN)
D00346 Isoniazid (JP16/USP/INN); Laniazid (TN)
D00505 Phenelzine sulfate (USP); Nardil (TN)
D00633 Dopamine hydrochloride (JP16/USP); Actopamin (TN); Intropin (TN)
D00785 Selegiline hydrochloride (JAN/USP); Eldepryl (TN)
D00826 Tranylcypromine sulfate (USP XXI); Parnate (TN)
D01097 Lazabemide hydrochloride (JAN/USAN); Tempium (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
D02562 Rasagiline mesylate (USAN); Azilect (TN)
D02564 Pargyline hydrochloride (USAN); Eutonyl (TN)
D02579 Iproniazid (INN)
D02580 Isocarboxazid (INN); Marplan (TN)
D03239 Ladostigil tartrate (USAN)
D03409 Caroxazone (USAN/INN)
D03731 Selegiline (USAN/INN); Emsam (TN)
D03733 Mofegiline hydrochloride (USAN)
D04092 Etryptamine acetate (USAN)
D04681 Lazabemide (USAN/INN)
D05033 Milacemide hydrochloride (USAN)
D07337 Nialamide (INN); Niamid (TN)
D07338 Iproclozide (INN); Iproclozide (TN)
D07870 Dopamine (INN); Medopa (TN)
D08085 Iproniazid phosphate; Marsilid (TN)
D08349 Phenelzine (BAN)
D08453 Pargyline (INN)
D08469 Rasagiline (USAN/INN); Azilect (TN)
D08625 Tranylcypromine (INN); Parnate (TN)
D09773 Isoniazid glucuronate sodium (JAN)
D10158 Safinamide (USAN/INN)
D10191 Safinamide mesylate (USAN)
DrugBank
DB00915Amantadine
DB00182Amphetamine
DB00988Dopamine
DB01363Ephedra
DB03147Flavin adenine dinucleotide
DB00614Furazolidone
DB01247Isocarboxazid
DB00601Linezolid
DB01577Methamphetamine
DB01171Moclobemide
DB08804Nandrolone decanoate
DB00184Nicotine
DB01626Pargyline
DB00780Phenelzine
DB00191Phentermine
DB00721Procaine
DB01367Rasagiline
DB01037Selegiline
DB01104Sertraline
DB00752Tranylcypromine
DB00909Zonisamide
Regulatory Network of AOFB_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"High-level expression of human liver monoamine oxidase B in Pichiapastoris.";
Newton-Vinson P., Hubalek F., Edmondson D.E.;
Protein Expr. Purif. 20:334-345(2000).
Cited for: PROTEIN SEQUENCE OF 2-17, ACETYLATION AT SER-2, AND MASS SPECTROMETRY.

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