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P27338 (AOFB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 156. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Amine oxidase [flavin-containing] B

EC=1.4.3.4
Alternative name(s):
Monoamine oxidase type B
Short name=MAO-B
Gene names
Name:MAOB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length520 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

FAD.

Subunit structure

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

Subcellular location

Mitochondrion outer membrane; Single-pass type IV membrane protein; Cytoplasmic side.

Sequence similarities

Belongs to the flavin monoamine oxidase family.

Mass spectrometry

Molecular mass is 59474±14.0 Da from positions 2 - 520. Determined by ESI. Ref.8

Ontologies

Keywords
   Cellular componentMembrane
Mitochondrion
Mitochondrion outer membrane
   DomainTransmembrane
Transmembrane helix
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of serotonin secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of dopamine metabolic process

Inferred from electronic annotation. Source: Ensembl

response to aluminum ion

Inferred from electronic annotation. Source: Ensembl

response to corticosterone

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to selenium ion

Inferred from electronic annotation. Source: Ensembl

response to toxic substance

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

substantia nigra development

Inferred from expression pattern PubMed 22926577. Source: UniProt

xenobiotic metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial envelope

Traceable author statement PubMed 7063850. Source: ProtInc

mitochondrial inner membrane

Inferred from electronic annotation. Source: Ensembl

mitochondrial outer membrane

Traceable author statement. Source: Reactome

mitochondrion

Inferred from direct assay PubMed 20833797. Source: UniProt

   Molecular_functionelectron carrier activity

Traceable author statement PubMed 8602220. Source: UniProtKB

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: Ensembl

primary amine oxidase activity

Traceable author statement. Source: Reactome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 520519Amine oxidase [flavin-containing] B
PRO_0000099859

Regions

Topological domain2 – 489488Cytoplasmic
Transmembrane490 – 51627Helical; Anchor for type IV membrane protein
Topological domain517 – 5204Mitochondrial intermembrane
Compositional bias36 – 5217Arg/Lys-rich (basic)

Sites

Site1561Important for catalytic activity
Site3651Important for catalytic activity
Site3821Important for catalytic activity

Amino acid modifications

Modified residue21N-acetylserine Ref.8
Modified residue521N6-acetyllysine By similarity
Modified residue3971S-8alpha-FAD cysteine

Experimental info

Mutagenesis51C → S: No loss of activity. Ref.10
Mutagenesis1561C → S: Complete loss of activity. Ref.10
Mutagenesis1581T → A: Dramatic loss of activity. Ref.9
Mutagenesis1721C → S: No loss of activity. Ref.10
Mutagenesis1921C → S: No loss of activity. Ref.10
Mutagenesis1991I → F: Alters specificity towards synthetic inhibitors.
Mutagenesis2971C → S: No loss of activity. Ref.10
Mutagenesis3121C → S: No loss of activity. Ref.10
Mutagenesis3651C → S: Complete loss of activity. Ref.10
Mutagenesis3821H → R: Significant loss of activity. Ref.9
Mutagenesis3861K → M: No loss of activity. Ref.9
Mutagenesis3891C → A: Complete loss of activity. Ref.9 Ref.10
Mutagenesis3891C → S: No loss of activity. Ref.9 Ref.10
Mutagenesis3941S → A: No loss of activity. Ref.9
Mutagenesis3971C → S: Complete loss of activity. Ref.10

Secondary structure

...................................................................................................... 520
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27338 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 358D1025F5BCA604

FASTA52058,763
        10         20         30         40         50         60 
MSNKCDVVVV GGGISGMAAA KLLHDSGLNV VVLEARDRVG GRTYTLRNQK VKYVDLGGSY 

        70         80         90        100        110        120 
VGPTQNRILR LAKELGLETY KVNEVERLIH HVKGKSYPFR GPFPPVWNPI TYLDHNNFWR 

       130        140        150        160        170        180 
TMDDMGREIP SDAPWKAPLA EEWDNMTMKE LLDKLCWTES AKQLATLFVN LCVTAETHEV 

       190        200        210        220        230        240 
SALWFLWYVK QCGGTTRIIS TTNGGQERKF VGGSGQVSER IMDLLGDRVK LERPVIYIDQ 

       250        260        270        280        290        300 
TRENVLVETL NHEMYEAKYV ISAIPPTLGM KIHFNPPLPM MRNQMITRVP LGSVIKCIVY 

       310        320        330        340        350        360 
YKEPFWRKKD YCGTMIIDGE EAPVAYTLDD TKPEGNYAAI MGFILAHKAR KLARLTKEER 

       370        380        390        400        410        420 
LKKLCELYAK VLGSLEALEP VHYEEKNWCE EQYSGGCYTT YFPPGILTQY GRVLRQPVDR 

       430        440        450        460        470        480 
IYFAGTETAT HWSGYMEGAV EAGERAAREI LHAMGKIPED EIWQSEPESV DVPAQPITTT 

       490        500        510        520 
FLERHLPSVP GLLRLIGLTT IFSATALGFL AHKRGLLVRV 

« Hide

References

« Hide 'large scale' references
[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].
[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].
[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. expand/collapse author list , 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].
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"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).
[12]"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.
[13]"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.
[14]"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.
[15]"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.
+Additional computationally mapped references.

Web resources

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Monoamine oxidase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S62734 mRNA. Translation: AAB27229.1.
M69135 Genomic DNA. Translation: AAA59551.1.
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.
Z95125 Genomic DNA. No translation available.
CH471141 Genomic DNA. Translation: EAW59378.1.
CH471141 Genomic DNA. Translation: EAW59380.1.
CCDSCCDS14261.1.
PIRJH0817.
RefSeqNP_000889.3. NM_000898.4.
UniGeneHs.654473.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP27338.
SMRP27338. Positions 3-501.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110302. 4 interactions.
IntActP27338. 3 interactions.
MINTMINT-3010688.
STRING9606.ENSP00000367309.

Chemistry

BindingDBP27338.
ChEMBLCHEMBL2039.
DrugBankDB00915. Amantadine.
DB01156. Bupropion.
DB00190. Carbidopa.
DB00215. Citalopram.
DB00988. Dopamine.
DB00494. Entacapone.
DB00614. Furazolidone.
DB01381. Ginkgo biloba.
DB01050. Ibuprofen.
DB00458. Imipramine.
DB04818. Iproniazid.
DB01247. Isocarboxazid.
DB01235. Levodopa.
DB00934. Maprotiline.
DB00737. Meclizine.
DB01171. Moclobemide.
DB00184. Nicotine.
DB01626. Pargyline.
DB00780. Phenelzine.
DB00191. Phentermine.
DB01367. Rasagiline.
DB01037. Selegiline.
DB00752. Tranylcypromine.
GuidetoPHARMACOLOGY2490.

PTM databases

PhosphoSiteP27338.

Polymorphism databases

DMDM113980.

Proteomic databases

MaxQBP27338.
PaxDbP27338.
PRIDEP27338.

Protocols and materials databases

DNASU4129.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000378069; ENSP00000367309; ENSG00000069535.
GeneID4129.
KEGGhsa:4129.
UCSCuc004dfz.4. human.

Organism-specific databases

CTD4129.
GeneCardsGC0XM043625.
HGNCHGNC:6834. MAOB.
HPACAB037200.
HPA002328.
MIM309860. gene.
neXtProtNX_P27338.
PharmGKBPA237.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1231.
HOGENOMHOG000221615.
HOVERGENHBG004255.
InParanoidP27338.
KOK00274.
OMAWDKMSMQ.
OrthoDBEOG7K6PTP.
PhylomeDBP27338.
TreeFamTF313314.

Enzyme and pathway databases

BioCycMetaCyc:HS00966-MONOMER.
BRENDA1.4.3.4. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKP27338.

Gene expression databases

ArrayExpressP27338.
BgeeP27338.
CleanExHS_MAOB.
GenevestigatorP27338.

Family and domain databases

InterProIPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
[Graphical view]
PfamPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSPR00757. AMINEOXDASEF.
ProtoNetSearch...

Other

ChiTaRSMAOB. human.
EvolutionaryTraceP27338.
GeneWikiMonoamine_oxidase_B.
GenomeRNAi4129.
NextBio16210.
PROP27338.
SOURCESearch...

Entry information

Entry nameAOFB_HUMAN
AccessionPrimary (citable) accession number: P27338
Secondary accession number(s): B2R6R3, D3DWC3, Q7Z6S2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 156 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM