Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Amine oxidase [flavin-containing] B

Gene

MAOB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.

Catalytic activityi

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

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei156 – 1561Important for catalytic activity
Sitei365 – 3651Important for catalytic activity
Sitei382 – 3821Important for catalytic activity

GO - Molecular functioni

  1. electron carrier activity Source: UniProtKB
  2. flavin adenine dinucleotide binding Source: Ensembl
  3. primary amine oxidase activity Source: Reactome

GO - Biological processi

  1. dopamine catabolic process Source: ParkinsonsUK-UCL
  2. hydrogen peroxide biosynthetic process Source: ParkinsonsUK-UCL
  3. negative regulation of serotonin secretion Source: Ensembl
  4. positive regulation of dopamine metabolic process Source: Ensembl
  5. response to aluminum ion Source: Ensembl
  6. response to corticosterone Source: Ensembl
  7. response to drug Source: Ensembl
  8. response to ethanol Source: Ensembl
  9. response to lipopolysaccharide Source: Ensembl
  10. response to selenium ion Source: Ensembl
  11. response to toxic substance Source: Ensembl
  12. small molecule metabolic process Source: Reactome
  13. substantia nigra development Source: UniProtKB
  14. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:HS00966-MONOMER.
BRENDAi1.4.3.4. 2681.
ReactomeiREACT_416. Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB.
SABIO-RKP27338.

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
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:6834. MAOB.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 489488CytoplasmicAdd
BLAST
Transmembranei490 – 51627Helical; Anchor for type IV membrane proteinAdd
BLAST
Topological domaini517 – 5204Mitochondrial intermembrane

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. integral component of membrane Source: UniProtKB-KW
  3. mitochondrial envelope Source: ProtInc
  4. mitochondrial inner membrane Source: Ensembl
  5. mitochondrial outer membrane Source: ParkinsonsUK-UCL
  6. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi5 – 51C → S: No loss of activity. 1 Publication
Mutagenesisi156 – 1561C → S: Complete loss of activity. 1 Publication
Mutagenesisi158 – 1581T → A: Dramatic loss of activity. 1 Publication
Mutagenesisi172 – 1721C → S: No loss of activity. 1 Publication
Mutagenesisi192 – 1921C → S: No loss of activity. 1 Publication
Mutagenesisi199 – 1991I → F: Alters specificity towards synthetic inhibitors.
Mutagenesisi297 – 2971C → S: No loss of activity. 1 Publication
Mutagenesisi312 – 3121C → S: No loss of activity. 1 Publication
Mutagenesisi365 – 3651C → S: Complete loss of activity. 1 Publication
Mutagenesisi382 – 3821H → R: Significant loss of activity. 1 Publication
Mutagenesisi386 – 3861K → M: No loss of activity. 1 Publication
Mutagenesisi389 – 3891C → A: Complete loss of activity. 2 Publications
Mutagenesisi389 – 3891C → S: No loss of activity. 2 Publications
Mutagenesisi394 – 3941S → A: No loss of activity. 1 Publication
Mutagenesisi397 – 3971C → S: Complete loss of activity. 1 Publication

Organism-specific databases

PharmGKBiPA237.

Chemistry

DrugBankiDB00915. Amantadine.
DB00182. Amphetamine.
DB00988. Dopamine.
DB01363. Ephedra.
DB03147. Flavin adenine dinucleotide.
DB00614. Furazolidone.
DB01247. Isocarboxazid.
DB00601. Linezolid.
DB01577. Methamphetamine.
DB01171. Moclobemide.
DB08804. Nandrolone decanoate.
DB00184. Nicotine.
DB01626. Pargyline.
DB00780. Phenelzine.
DB00191. Phentermine.
DB00721. Procaine.
DB01367. Rasagiline.
DB01037. Selegiline.
DB01104. Sertraline.
DB00752. Tranylcypromine.
DB00909. Zonisamide.

Polymorphism and mutation databases

BioMutaiMAOB.
DMDMi113980.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 520519Amine oxidase [flavin-containing] BPRO_0000099859Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei52 – 521N6-acetyllysineBy similarity
Modified residuei397 – 3971S-8alpha-FAD cysteine

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP27338.
PaxDbiP27338.
PRIDEiP27338.

PTM databases

PhosphoSiteiP27338.

Expressioni

Gene expression databases

BgeeiP27338.
CleanExiHS_MAOB.
ExpressionAtlasiP27338. baseline and differential.
GenevestigatoriP27338.

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

Protein-protein interaction databases

BioGridi110302. 5 interactions.
IntActiP27338. 3 interactions.
MINTiMINT-3010688.
STRINGi9606.ENSP00000367309.

Structurei

Secondary structure

1
520
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 105Combined sources
Helixi14 – 2512Combined sources
Beta strandi30 – 334Combined sources
Beta strandi35 – 406Combined sources
Beta strandi45 – 484Combined sources
Turni49 – 513Combined sources
Beta strandi54 – 574Combined sources
Helixi66 – 749Combined sources
Beta strandi79 – 813Combined sources
Beta strandi85 – 928Combined sources
Beta strandi95 – 995Combined sources
Beta strandi101 – 1033Combined sources
Helixi109 – 12618Combined sources
Helixi134 – 1363Combined sources
Helixi140 – 1445Combined sources
Beta strandi145 – 1473Combined sources
Helixi148 – 1558Combined sources
Helixi159 – 17315Combined sources
Turni177 – 1793Combined sources
Helixi182 – 1909Combined sources
Turni191 – 1933Combined sources
Helixi195 – 1995Combined sources
Beta strandi207 – 2104Combined sources
Helixi215 – 22511Combined sources
Helixi226 – 2283Combined sources
Beta strandi229 – 2324Combined sources
Beta strandi235 – 2395Combined sources
Beta strandi241 – 2499Combined sources
Beta strandi254 – 2629Combined sources
Helixi266 – 2716Combined sources
Beta strandi272 – 2765Combined sources
Helixi280 – 2856Combined sources
Beta strandi294 – 3007Combined sources
Helixi305 – 3095Combined sources
Beta strandi311 – 3177Combined sources
Beta strandi319 – 3213Combined sources
Beta strandi325 – 3295Combined sources
Beta strandi339 – 3457Combined sources
Helixi347 – 3526Combined sources
Helixi357 – 37216Combined sources
Helixi375 – 3784Combined sources
Beta strandi381 – 3877Combined sources
Helixi388 – 3903Combined sources
Turni392 – 3943Combined sources
Beta strandi396 – 3983Combined sources
Helixi406 – 4105Combined sources
Helixi411 – 4133Combined sources
Beta strandi421 – 4233Combined sources
Helixi426 – 4283Combined sources
Beta strandi430 – 4323Combined sources
Helixi436 – 45318Combined sources
Helixi459 – 4613Combined sources
Beta strandi470 – 4723Combined sources
Helixi481 – 4855Combined sources
Helixi489 – 50012Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP27338.
SMRiP27338. Positions 3-501.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27338.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi36 – 5217Arg/Lys-rich (basic)Add
BLAST

Sequence similaritiesi

Belongs to the flavin monoamine oxidase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1231.
GeneTreeiENSGT00730000110903.
HOGENOMiHOG000221615.
HOVERGENiHBG004255.
InParanoidiP27338.
KOiK00274.
OMAiWESRARM.
OrthoDBiEOG7K6PTP.
PhylomeDBiP27338.
TreeFamiTF313314.

Family and domain databases

InterProiIPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00757. AMINEOXDASEF.

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)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1616Missing in isoform 2. VSP_057047Add
BLAST
Alternative sequencei380 – 42748PVHYE…FAGTE → GSTPASGQDLLCRHRDCHTL ERLHGGGCRGRGESSPRDPA CHGEDSRG in isoform 2. 1 PublicationVSP_057048Add
BLAST
Alternative sequencei428 – 52093Missing in isoform 2. 1 PublicationVSP_057049Add
BLAST

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.4. human. [P27338-1]

Polymorphism and mutation databases

BioMutaiMAOB.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Monoamine oxidase entry

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP27338.
SMRiP27338. Positions 3-501.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110302. 5 interactions.
IntActiP27338. 3 interactions.
MINTiMINT-3010688.
STRINGi9606.ENSP00000367309.

Chemistry

BindingDBiP27338.
ChEMBLiCHEMBL2095205.
DrugBankiDB00915. Amantadine.
DB00182. Amphetamine.
DB00988. Dopamine.
DB01363. Ephedra.
DB03147. Flavin adenine dinucleotide.
DB00614. Furazolidone.
DB01247. Isocarboxazid.
DB00601. Linezolid.
DB01577. Methamphetamine.
DB01171. Moclobemide.
DB08804. Nandrolone decanoate.
DB00184. Nicotine.
DB01626. Pargyline.
DB00780. Phenelzine.
DB00191. Phentermine.
DB00721. Procaine.
DB01367. Rasagiline.
DB01037. Selegiline.
DB01104. Sertraline.
DB00752. Tranylcypromine.
DB00909. Zonisamide.
GuidetoPHARMACOLOGYi2490.

PTM databases

PhosphoSiteiP27338.

Polymorphism and mutation databases

BioMutaiMAOB.
DMDMi113980.

Proteomic databases

MaxQBiP27338.
PaxDbiP27338.
PRIDEiP27338.

Protocols and materials databases

DNASUi4129.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000378069; ENSP00000367309; ENSG00000069535. [P27338-1]
GeneIDi4129.
KEGGihsa:4129.
UCSCiuc004dfz.4. human. [P27338-1]

Organism-specific databases

CTDi4129.
GeneCardsiGC0XM043625.
HGNCiHGNC:6834. MAOB.
HPAiCAB037200.
HPA002328.
MIMi309860. gene.
neXtProtiNX_P27338.
PharmGKBiPA237.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1231.
GeneTreeiENSGT00730000110903.
HOGENOMiHOG000221615.
HOVERGENiHBG004255.
InParanoidiP27338.
KOiK00274.
OMAiWESRARM.
OrthoDBiEOG7K6PTP.
PhylomeDBiP27338.
TreeFamiTF313314.

Enzyme and pathway databases

BioCyciMetaCyc:HS00966-MONOMER.
BRENDAi1.4.3.4. 2681.
ReactomeiREACT_416. Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB.
SABIO-RKP27338.

Miscellaneous databases

ChiTaRSiMAOB. human.
EvolutionaryTraceiP27338.
GeneWikiiMonoamine_oxidase_B.
GenomeRNAii4129.
NextBioi16210.
PROiP27338.
SOURCEiSearch...

Gene expression databases

BgeeiP27338.
CleanExiHS_MAOB.
ExpressionAtlasiP27338. baseline and differential.
GenevestigatoriP27338.

Family and domain databases

InterProiIPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00757. AMINEOXDASEF.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human monoamine oxidase A and B genes exhibit identical exon-intron organization."
    Grimsby J., Chen K., Wang L.J., Lan N.C., Shih J.C.
    Proc. Natl. Acad. Sci. U.S.A. 88:3637-3641(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "cDNA cloning of human liver monoamine oxidase A and B: molecular basis of differences in enzymatic properties."
    Bach A.W.J., Lan N.C., Johnson D.L., Abell C.W., Bembenek M.E., Kwan S.W., Seeburg P.H., Shih J.C.
    Proc. Natl. Acad. Sci. U.S.A. 85:4934-4938(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "The deduced amino acid sequences of human platelet and frontal cortex monoamine oxidase B are identical."
    Chen K., Wu H.F., Shih J.C.
    J. Neurochem. 61:187-190(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
  5. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "Promoter organization and activity of human monoamine oxidase (MAO) A and B genes."
    Zhu Q.S., Grimsby J.S., Chen K., Shih J.C.
    J. Neurosci. 12:4437-4446(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
  8. "High-level expression of human liver monoamine oxidase B in Pichia pastoris."
    Newton-Vinson P., Hubalek F., Edmondson D.E.
    Protein Expr. Purif. 20:334-345(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-17, ACETYLATION AT SER-2, MASS SPECTROMETRY.
  9. "Investigation on the structure of the active site of monoamine oxidase-B by affinity labeling with the selective inhibitor lazabemide and by site-directed mutagenesis."
    Cesura A.M., Gottowik J., Lahm H.-W., Lang G., Imhof R., Malherbe P., Roethlisberger U., Da Prada M.
    Eur. J. Biochem. 236:996-1002(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 371-391, MUTAGENESIS OF THR-158; HIS-382; LYS-386; CYS-389 AND SER-394.
  10. "Site-directed mutagenesis of monoamine oxidase A and B: role of cysteines."
    Wu H.F., Chen K., Shih J.C.
    Mol. Pharmacol. 43:888-893(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-5; CYS-156; CYS-172; CYS-192; CYS-297; CYS-312; CYS-365; CYS-389 AND CYS-397.
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders."
    Binda C., Newton-Vinson P., Hubalek F., Edmondson D.E., Mattevi A.
    Nat. Struct. Biol. 9:22-26(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
  13. "Insights into the mode of inhibition of human mitochondrial monoamine oxidase B from high-resolution crystal structures."
    Binda C., Li M., Hubalek F., Restelli N., Edmondson D.E., Mattevi A.
    Proc. Natl. Acad. Sci. U.S.A. 100:9750-9755(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH INHIBITORS.
  14. "Crystal structures of monoamine oxidase B in complex with four inhibitors of the N-propargylaminoindan class."
    Binda C., Hubalek F., Li M., Herzig Y., Sterling J., Edmondson D.E., Mattevi A.
    J. Med. Chem. 47:1767-1774(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEXES WITH INHIBITORS.
  15. "Demonstration of isoleucine 199 as a structural determinant for the selective inhibition of human monoamine oxidase B by specific reversible inhibitors."
    Hubalek F., Binda C., Khalil A., Li M., Mattevi A., Castagnoli N., Edmondson D.E.
    J. Biol. Chem. 280:15761-15766(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT PHE-199 IN COMPLEXES WITH INHIBITORS.
  16. "Binding of rasagiline-related inhibitors to human monoamine oxidases: a kinetic and crystallographic analysis."
    Binda C., Hubalek F., Li M., Herzig Y., Sterling J., Edmondson D.E., Mattevi A.
    J. Med. Chem. 48:8148-8154(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH INHIBITORS.

Entry informationi

Entry nameiAOFB_HUMAN
AccessioniPrimary (citable) accession number: P27338
Secondary accession number(s): B2R6R3
, B7Z5H3, D3DWC3, Q7Z6S2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 164 of the entry and version 3 of the sequence. [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

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.