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Protein

Amine oxidase [flavin-containing] B

Gene

MAOB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.

Caution

Catalytic activityi

RCH2NHR' + H2O + O2 = RCHO + R'NH2 + H2O2.

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei156Important for catalytic activity1
Sitei365Important for catalytic activity1
Sitei382Important for catalytic activity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
LigandFAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:HS00966-MONOMER
BRENDAi1.4.3.4 2681
ReactomeiR-HSA-141333 Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB
SABIO-RKiP27338
SIGNORiP27338

Names & Taxonomyi

Protein namesi
Recommended name:
Amine oxidase [flavin-containing] B (EC:1.4.3.4)
Alternative name(s):
Monoamine oxidase type B
Short name:
MAO-B
Gene namesi
Name:MAOB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

EuPathDBiHostDB:ENSG00000069535.13
HGNCiHGNC:6834 MAOB
MIMi309860 gene
neXtProtiNX_P27338

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 489CytoplasmicAdd BLAST488
Transmembranei490 – 516Helical; Anchor for type IV membrane proteinAdd BLAST27
Topological domaini517 – 520Mitochondrial intermembrane4

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi5C → S: No loss of activity. 1 Publication1
Mutagenesisi156C → S: Complete loss of activity. 1 Publication1
Mutagenesisi158T → A: Dramatic loss of activity. 1 Publication1
Mutagenesisi172C → S: No loss of activity. 1 Publication1
Mutagenesisi192C → S: No loss of activity. 1 Publication1
Mutagenesisi199I → F: Alters specificity towards synthetic inhibitors. 1
Mutagenesisi297C → S: No loss of activity. 1 Publication1
Mutagenesisi312C → S: No loss of activity. 1 Publication1
Mutagenesisi365C → S: Complete loss of activity. 1 Publication1
Mutagenesisi382H → R: Significant loss of activity. 1 Publication1
Mutagenesisi386K → M: No loss of activity. 1 Publication1
Mutagenesisi389C → A: Complete loss of activity. 2 Publications1
Mutagenesisi389C → S: No loss of activity. 2 Publications1
Mutagenesisi394S → A: No loss of activity. 1 Publication1
Mutagenesisi397C → S: Complete loss of activity. 1 Publication1

Organism-specific databases

DisGeNETi4129
OpenTargetsiENSG00000069535
PharmGKBiPA237

Chemistry databases

ChEMBLiCHEMBL2039
DrugBankiDB08176 (1Z)-4-(4-FLUOROPHENYL)-2-METHYLIDENEBUTAN-1-IMINE
DB08516 (S)-(+)-2-[4-(FLUOROBENZYLOXY-BENZYLAMINO)PROPIONAMIDE]
DB08480 4-HYDROXY-N-PROPARGYL-1(R)-AMINOINDAN
DB01472 4-Methoxyamphetamine
DB04307 5-Hydroxy-N-Propargyl-1(R)-Aminoindan
DB07512 7-[(3-CHLOROBENZYL)OXY]-2-OXO-2H-CHROMENE-4-CARBALDEHYDE
DB07513 7-[(3-CHLOROBENZYL)OXY]-4-[(METHYLAMINO)METHYL]-2H-CHROMEN-2-ONE
DB00915 Amantadine
DB00182 Amphetamine
DB04889 Bicifadine
DB01445 Bufotenine
DB00988 Dopamine
DB01363 Ephedra
DB02509 Farnesol
DB03147 Flavin adenine dinucleotide
DB00614 Furazolidone
DB04818 Iproniazid
DB02095 Isatin
DB01247 Isocarboxazid
DB04147 Lauryl Dimethylamine-N-Oxide
DB00601 Linezolid
DB01577 Methamphetamine
DB01442 MMDA
DB01171 Moclobemide
DB08082 N-(2-AMINOETHYL)-P-CHLOROBENZAMIDE
DB04677 N-METHYL-N-[(1R)-1-METHYL-2-PHENYLETHYL]PROP-2-EN-1-AMINE
DB02211 N-Methyl-N-Propargyl-1(R)-Aminoindan
DB03894 N-Propargyl-1(S)-Aminoindan
DB08804 Nandrolone decanoate
DB04820 Nialamide
DB00184 Nicotine
DB04821 Nomifensine
DB01626 Pargyline
DB00780 Phenelzine
DB00191 Phentermine
DB00721 Procaine
DB01168 Procarbazine
DB01367 Rasagiline
DB06654 Safinamide
DB01037 Selegiline
DB01104 Sertraline
DB00752 Tranylcypromine
DB04832 Zimelidine
DB00909 Zonisamide
GuidetoPHARMACOLOGYi2490

Polymorphism and mutation databases

BioMutaiMAOB
DMDMi113980

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000998592 – 520Amine oxidase [flavin-containing] BAdd BLAST519

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine1 Publication1
Modified residuei52N6-acetyllysineBy similarity1
Modified residuei397S-8alpha-FAD cysteine1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP27338
MaxQBiP27338
PaxDbiP27338
PeptideAtlasiP27338
PRIDEiP27338

PTM databases

CarbonylDBiP27338
iPTMnetiP27338
PhosphoSitePlusiP27338

Expressioni

Gene expression databases

BgeeiENSG00000069535
CleanExiHS_MAOB
GenevisibleiP27338 HS

Organism-specific databases

HPAiCAB037200
HPA002328

Interactioni

Subunit structurei

Monomer, homo- or heterodimer (containing two subunits of similar size). Each subunit contains a covalently bound flavin. Enzymatically active as monomer (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi1103025 interactors.
IntActiP27338 3 interactors.
MINTiP27338
STRINGi9606.ENSP00000367309

Chemistry databases

BindingDBiP27338

Structurei

Secondary structure

1520
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 10Combined sources5
Helixi14 – 25Combined sources12
Beta strandi30 – 33Combined sources4
Beta strandi35 – 40Combined sources6
Beta strandi45 – 48Combined sources4
Turni49 – 51Combined sources3
Beta strandi54 – 57Combined sources4
Helixi66 – 74Combined sources9
Beta strandi79 – 81Combined sources3
Beta strandi85 – 92Combined sources8
Beta strandi95 – 99Combined sources5
Beta strandi101 – 103Combined sources3
Helixi109 – 126Combined sources18
Helixi134 – 136Combined sources3
Helixi140 – 144Combined sources5
Beta strandi145 – 147Combined sources3
Helixi148 – 155Combined sources8
Helixi159 – 173Combined sources15
Turni177 – 179Combined sources3
Helixi182 – 190Combined sources9
Turni191 – 193Combined sources3
Helixi195 – 199Combined sources5
Beta strandi207 – 210Combined sources4
Helixi215 – 225Combined sources11
Helixi226 – 228Combined sources3
Beta strandi229 – 232Combined sources4
Beta strandi235 – 239Combined sources5
Beta strandi241 – 249Combined sources9
Beta strandi254 – 262Combined sources9
Helixi266 – 271Combined sources6
Beta strandi272 – 276Combined sources5
Helixi280 – 285Combined sources6
Beta strandi294 – 300Combined sources7
Helixi305 – 309Combined sources5
Beta strandi311 – 317Combined sources7
Beta strandi319 – 321Combined sources3
Beta strandi325 – 329Combined sources5
Beta strandi339 – 345Combined sources7
Helixi347 – 352Combined sources6
Helixi357 – 372Combined sources16
Helixi375 – 378Combined sources4
Beta strandi381 – 387Combined sources7
Helixi388 – 390Combined sources3
Turni392 – 394Combined sources3
Beta strandi396 – 398Combined sources3
Helixi406 – 410Combined sources5
Helixi411 – 413Combined sources3
Beta strandi421 – 423Combined sources3
Helixi426 – 428Combined sources3
Beta strandi430 – 432Combined sources3
Helixi436 – 453Combined sources18
Helixi459 – 461Combined sources3
Beta strandi470 – 472Combined sources3
Helixi481 – 485Combined sources5
Helixi489 – 500Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GOSX-ray3.00A/B2-520[»]
1H8Rmodel-A5-459[»]
1OJ9X-ray2.30A/B2-520[»]
1OJAX-ray1.70A/B2-520[»]
1OJCX-ray2.40A/B2-520[»]
1OJDX-ray3.10A/B/C/D/E/F/G/H/I/L2-520[»]
1S2QX-ray2.07A/B1-520[»]
1S2YX-ray2.12A/B1-520[»]
1S3BX-ray1.65A/B1-520[»]
1S3EX-ray1.60A/B1-520[»]
2BK3X-ray1.80A/B2-520[»]
2BK4X-ray1.90A/B2-520[»]
2BK5X-ray1.83A/B1-520[»]
2BYBX-ray2.20A/B2-520[»]
2C64X-ray2.20A/B2-520[»]
2C65X-ray1.70A/B2-520[»]
2C66X-ray2.50A/B2-520[»]
2C67X-ray1.70A/B2-520[»]
2C70X-ray2.06A/B2-520[»]
2C72X-ray2.00A/B2-520[»]
2C73X-ray2.20A/B2-520[»]
2C75X-ray1.70A/B2-520[»]
2C76X-ray1.70A/B2-520[»]
2V5ZX-ray1.60A/B2-520[»]
2V60X-ray2.00A/B2-520[»]
2V61X-ray1.70A/B2-520[»]
2VRLX-ray2.40A/B1-520[»]
2VRMX-ray2.30A/B1-520[»]
2VZ2X-ray2.30A/B1-520[»]
2XCGX-ray1.90A/B1-520[»]
2XFNX-ray1.60A/B1-520[»]
2XFOX-ray2.10A/B1-520[»]
2XFPX-ray1.66A/B1-520[»]
2XFQX-ray2.20A/B1-520[»]
2XFUX-ray2.20A/B2-520[»]
3PO7X-ray1.80A/B1-520[»]
3ZYXX-ray2.20A/B2-520[»]
4A79X-ray1.89A/B1-520[»]
4A7AX-ray1.70A/B1-520[»]
4CRTX-ray1.80A/B1-520[»]
5MRLX-ray2.42A/B1-520[»]
ProteinModelPortaliP27338
SMRiP27338
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27338

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi36 – 52Arg/Lys-rich (basic)Add BLAST17

Sequence similaritiesi

Belongs to the flavin monoamine oxidase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0029 Eukaryota
ENOG410XSNC LUCA
GeneTreeiENSGT00730000110903
HOGENOMiHOG000221615
HOVERGENiHBG004255
InParanoidiP27338
KOiK00274
OMAiPWKAPLA
OrthoDBiEOG091G0G7P
PhylomeDBiP27338
TreeFamiTF313314

Family and domain databases

Gene3Di3.50.50.604 hits
InterProiView protein in InterPro
IPR002937 Amino_oxidase
IPR036188 FAD/NAD-bd_sf
IPR001613 Flavin_amine_oxidase
PfamiView protein in Pfam
PF01593 Amino_oxidase, 1 hit
PRINTSiPR00757 AMINEOXDASEF
SUPFAMiSSF51905 SSF51905, 2 hits

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P27338-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSNKCDVVVV GGGISGMAAA KLLHDSGLNV VVLEARDRVG GRTYTLRNQK
60 70 80 90 100
VKYVDLGGSY VGPTQNRILR LAKELGLETY KVNEVERLIH HVKGKSYPFR
110 120 130 140 150
GPFPPVWNPI TYLDHNNFWR TMDDMGREIP SDAPWKAPLA EEWDNMTMKE
160 170 180 190 200
LLDKLCWTES AKQLATLFVN LCVTAETHEV SALWFLWYVK QCGGTTRIIS
210 220 230 240 250
TTNGGQERKF VGGSGQVSER IMDLLGDRVK LERPVIYIDQ TRENVLVETL
260 270 280 290 300
NHEMYEAKYV ISAIPPTLGM KIHFNPPLPM MRNQMITRVP LGSVIKCIVY
310 320 330 340 350
YKEPFWRKKD YCGTMIIDGE EAPVAYTLDD TKPEGNYAAI MGFILAHKAR
360 370 380 390 400
KLARLTKEER LKKLCELYAK VLGSLEALEP VHYEEKNWCE EQYSGGCYTT
410 420 430 440 450
YFPPGILTQY GRVLRQPVDR IYFAGTETAT HWSGYMEGAV EAGERAAREI
460 470 480 490 500
LHAMGKIPED EIWQSEPESV DVPAQPITTT FLERHLPSVP GLLRLIGLTT
510 520
IFSATALGFL AHKRGLLVRV
Length:520
Mass (Da):58,763
Last modified:January 23, 2007 - v3
Checksum:i358D1025F5BCA604
GO
Isoform 2 (identifier: P27338-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: Missing.
     380-427: PVHYEEKNWC...VDRIYFAGTE → GSTPASGQDL...PACHGEDSRG
     428-520: Missing.

Note: No experimental confirmation available.
Show »
Length:411
Mass (Da):46,539
Checksum:iCDF2F7AD6D7EC66F
GO

Mass spectrometryi

Molecular mass is 59474±14.0 Da from positions 2 - 520. Determined by ESI. 1 Publication

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0570471 – 16Missing in isoform 2. Add BLAST16
Alternative sequenceiVSP_057048380 – 427PVHYE…FAGTE → GSTPASGQDLLCRHRDCHTL ERLHGGGCRGRGESSPRDPA CHGEDSRG in isoform 2. 1 PublicationAdd BLAST48
Alternative sequenceiVSP_057049428 – 520Missing in isoform 2. 1 PublicationAdd BLAST93

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S62734 mRNA Translation: AAB27229.1
M69135 Genomic DNA Translation: AAA59551.1
AK298942 mRNA Translation: BAH12909.1
AK312679 mRNA Translation: BAG35560.1
M69177 mRNA Translation: AAA59550.1
M89637 Genomic DNA Translation: AAB46386.1
AL008709 Genomic DNA No translation available.
AL020990 Genomic DNA No translation available.
BX537148 Genomic DNA No translation available.
Z95125 Genomic DNA No translation available.
CH471141 Genomic DNA Translation: EAW59378.1
CH471141 Genomic DNA Translation: EAW59380.1
CCDSiCCDS14261.1 [P27338-1]
PIRiJH0817
RefSeqiNP_000889.3, NM_000898.4 [P27338-1]
UniGeneiHs.654473

Genome annotation databases

EnsembliENST00000378069; ENSP00000367309; ENSG00000069535 [P27338-1]
GeneIDi4129
KEGGihsa:4129
UCSCiuc004dfz.5 human [P27338-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiAOFB_HUMAN
AccessioniPrimary (citable) accession number: P27338
Secondary accession number(s): B2R6R3
, B7Z5H3, D3DWC3, Q7Z6S2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: February 28, 2018
This is version 188 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome