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UniProtKB/Swiss-Prot entry P27338


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AOFB_HUMAN
Primary accession number P27338
Secondary accession number Q7Z6S2
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 93)
Name and origin of the protein
Protein name Amine oxidase [flavin-containing] B
Synonyms EC 1.4.3.4
Monoamine oxidase type B
MAO-B
Gene name
Name: MAOB
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2023912 [NCBI, ExPASy, EBI, Israel, Japan]
Grimsby J., Chen K., Wang L.J., Lan N.C., Shih J.C.;
"Human monoamine oxidase A and B genes exhibit identical exon-intron organization.";
Proc. Natl. Acad. Sci. U.S.A. 88:3637-3641(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3387449 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"cDNA cloning of human liver monoamine oxidase A and B: molecular basis of differences in enzymatic properties.";
Proc. Natl. Acad. Sci. U.S.A. 85:4934-4938(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8515265 [NCBI, ExPASy, EBI, Israel, Japan]
Chen K., Wu H.F., Shih J.C.;
"The deduced amino acid sequences of human platelet and frontal cortex monoamine oxidase B are identical.";
J. Neurochem. 61:187-190(1993).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03440; PubMed=15772651 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
PubMed=1432104 [NCBI, ExPASy, EBI, Israel, Japan]
Zhu Q.S., Grimsby J.S., Chen K., Shih J.C.;
"Promoter organization and activity of human monoamine oxidase (MAO) A and B genes.";
J. Neurosci. 12:4437-4446(1992).
[6]
PROTEIN SEQUENCE OF 2-17, ACETYLATION AT SER-2, AND MASS SPECTROMETRY.
DOI=10.1006/prep.2000.1309; PubMed=11049757 [NCBI, ExPASy, EBI, Israel, Japan]
Newton-Vinson P., Hubalek F., Edmondson D.E.;
"High-level expression of human liver monoamine oxidase B in Pichia pastoris.";
Protein Expr. Purif. 20:334-345(2000).
[7]
PROTEIN SEQUENCE OF 371-391, AND MUTAGENESIS OF THR-158; HIS-382; LYS-386; CYS-389 AND SER-394.
PubMed=8665924 [NCBI, ExPASy, EBI, Israel, Japan]
Cesura A.M., Gottowik J., Lahm H.-W., Lang G., Imhof R., Malherbe P., Roethlisberger U., Da Prada M.;
"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.";
Eur. J. Biochem. 236:996-1002(1996).
[8]
MUTAGENESIS OF CYS-5; CYS-156; CYS-172; CYS-192; CYS-297; CYS-312; CYS-365; CYS-389 AND CYS-397.
PubMed=8316221 [NCBI, ExPASy, EBI, Israel, Japan]
Wu H.F., Chen K., Shih J.C.;
"Site-directed mutagenesis of monoamine oxidase A and B: role of cysteines.";
Mol. Pharmacol. 43:888-893(1993).
[9]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
DOI=10.1038/nsb732; PubMed=11753429 [NCBI, ExPASy, EBI, Israel, Japan]
Binda C., Newton-Vinson P., Hubalek F., Edmondson D.E., Mattevi A.;
"Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders.";
Nat. Struct. Biol. 9:22-26(2002).
[10]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH INHIBITORS.
DOI=10.1073/pnas.1633804100; PubMed=12913124 [NCBI, ExPASy, EBI, Israel, Japan]
Binda C., Li M., Hubalek F., Restelli N., Edmondson D.E., Mattevi A.;
"Insights into the mode of inhibition of human mitochondrial monoamine oxidase B from high-resolution crystal structures.";
Proc. Natl. Acad. Sci. U.S.A. 100:9750-9755(2003).
[11]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEXES WITH INHIBITORS.
DOI=10.1021/jm031087c; PubMed=15027868 [NCBI, ExPASy, EBI, Israel, Japan]
Binda C., Hubalek F., Li M., Herzig Y., Sterling J., Edmondson D.E., Mattevi A.;
"Crystal structures of monoamine oxidase B in complex with four inhibitors of the N-propargylaminoindan class.";
J. Med. Chem. 47:1767-1774(2004).
[12]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT PHE-199 IN COMPLEXES WITH INHIBITORS.
DOI=10.1074/jbc.M500949200; PubMed=15710600 [NCBI, ExPASy, EBI, Israel, Japan]
Hubalek F., Binda C., Khalil A., Li M., Mattevi A., Castagnoli N., Edmondson D.E.;
"Demonstration of isoleucine 199 as a structural determinant for the selective inhibition of human monoamine oxidase B by specific reversible inhibitors.";
J. Biol. Chem. 280:15761-15766(2005).
[13]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH INHIBITORS.
DOI=10.1021/jm0506266; PubMed=16366596 [NCBI, ExPASy, EBI, Israel, Japan]
Binda C., Hubalek F., Li M., Herzig Y., Sterling J., Edmondson D.E., Mattevi A.;
"Binding of rasagiline-related inhibitors to human monoamine oxidases: a kinetic and crystallographic analysis.";
J. Med. Chem. 48:8148-8154(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
S62734; AAB27229.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M69135; AAA59551.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M69177; AAA59550.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M89637; AAB46386.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL008709; CAD92552.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BX537148; CAD92552.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z95125; CAD92552.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BX537148; CAI42422.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL008709; CAI42422.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z95125; CAI42422.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z95125; CAI42522.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL008709; CAI42522.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BX537148; CAI42522.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JH0817; JH0817.
RefSeq NP_000889.3; -.
UniGene Hs.654473
3D structure databases
PDB
1GOS; X-ray; 3.00 A; A/B=1-520.[ExPASy / RCSB / EBI]
1H8R; Model; -; A=5-459.[ExPASy / RCSB / EBI]
1OJ9; X-ray; 2.30 A; A/B=1-520.[ExPASy / RCSB / EBI]
1OJA; X-ray; 1.70 A; A/B=1-520.[ExPASy / RCSB / EBI]
1OJB; X-ray; 2.20 A; A/B=1-520.[ExPASy / RCSB / EBI]
1OJC; X-ray; 2.40 A; A/B=1-520.[ExPASy / RCSB / EBI]
1OJD; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I/L=1-520.[ExPASy / RCSB / EBI]
1S2Q; X-ray; 2.07 A; A/B=1-520.[ExPASy / RCSB / EBI]
1S2Y; X-ray; 2.12 A; A/B=1-520.[ExPASy / RCSB / EBI]
1S3B; X-ray; 1.65 A; A/B=1-520.[ExPASy / RCSB / EBI]
1S3E; X-ray; 1.60 A; A/B=1-520.[ExPASy / RCSB / EBI]
2BK3; X-ray; 1.80 A; A/B=1-520.[ExPASy / RCSB / EBI]
2BK4; X-ray; 1.90 A; A/B=1-520.[ExPASy / RCSB / EBI]
2BK5; X-ray; 1.83 A; A/B=1-520.[ExPASy / RCSB / EBI]
2BYB; X-ray; 2.20 A; A/B=1-520.[ExPASy / RCSB / EBI]
2C64; X-ray; 2.20 A; A/B=1-520.[ExPASy / RCSB / EBI]
2C65; X-ray; 1.70 A; A/B=1-520.[ExPASy / RCSB / EBI]
2C66; X-ray; 2.50 A; A/B=1-520.[ExPASy / RCSB / EBI]
2C67; X-ray; 1.70 A; A/B=1-520.[ExPASy / RCSB / EBI]
2C70; X-ray; 2.06 A; A/B=1-520.[ExPASy / RCSB / EBI]
2C72; X-ray; 2.00 A; A/B=1-520.[ExPASy / RCSB / EBI]
2C73; X-ray; 2.20 A; A/B=1-520.[ExPASy / RCSB / EBI]
2C75; X-ray; 1.70 A; A/B=1-520.[ExPASy / RCSB / EBI]
2C76; X-ray; 1.70 A; A/B=1-520.[ExPASy / RCSB / EBI]
2V5Z; X-ray; 1.60 A; A/B=1-520.[ExPASy / RCSB / EBI]
2V60; X-ray; 2.00 A; A/B=1-520.[ExPASy / RCSB / EBI]
2V61; X-ray; 1.70 A; A/B=1-520.[ExPASy / RCSB / EBI]
2VRL; X-ray; 2.40 A; A/B=1-520.[ExPASy / RCSB / EBI]
2VRM; X-ray; 2.30 A; A/B=1-520.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1GOS; -.
1H8R; -.
1OJ9; -.
1OJA; -.
1OJB; -.
1OJC; -.
1OJD; -.
1S2Q; -.
1S2Y; -.
1S3B; -.
1S3E; -.
2BK3; -.
2BK4; -.
2BK5; -.
2BYB; -.
2C64; -.
2C65; -.
2C66; -.
2C67; -.
2C70; -.
2C72; -.
2C73; -.
2C75; -.
2C76; -.
2V5Z; -.
2V60; -.
2V61; -.
2VRL; -.
2VRM; -.
ModBase P27338.
Enzyme and pathway databases
BioCyc MetaCyc:MON-32; -.
Reactome REACT_2063; Metabolism of xenobiotics.
Organism-specific databases
H-InvDB HIX0016741; -.
HGNC HGNC:6834; MAOB.
GenAtlas MAOB.
HPA HPA002328; -.
MIM 309860; gene. [NCBI / EBI]
PharmGKB PA237; -.
GeneCards P27338.
Gene expression databases
ArrayExpress P27338; -.
CleanEx HS_MAOB; -.
GermOnline ENSG00000069535; Homo sapiens.
Ontologies
GO
GO:0005740; Cellular component: mitochondrial envelope (traceable author statement from ProtInc).
GO:0009055; Molecular function: electron carrier activity (traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR001613; Amineoxid_fl.
IPR002937; Amino_oxidase.
Graphical view of domain structure.
Pfam PF01593; Amino_oxidase; 1.
Pfam graphical view of domain structure.
PRINTS PR00757; AMINEOXDASEF.
BLOCKS P27338.
Genome annotation databases
Ensembl ENSG00000069535; Homo sapiens. [Contig view]
GeneID 4129; -.
KEGG hsa:4129; -.
NMPDR fig|9606.3.peg.32658; -.
Phylogenomic databases
HOGENOM P27338; -.
HOVERGEN P27338; -.
Other
DrugBank DB00915; 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.
SOURCE MAOB; Homo sapiens.
ProtoNet P27338.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Direct protein sequencing; FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion outer membrane; Oxidoreductase; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   520  519     Amine oxidase [flavin-containing] B. PRO_0000099859
TOPO_DOM   2   489  488     Cytoplasmic. 
TRANSMEM   490   516  27     Anchor for type IV membrane protein. 
TOPO_DOM   517   520  4     Mitochondrial intermembrane. 
COMPBIAS   36    52  17     Arg/Lys-rich (basic). 
SITE   156   156  1     Important for catalytic activity. 
SITE   365   365  1     Important for catalytic activity. 
SITE   382   382  1     Important for catalytic activity. 
MOD_RES   2     2        N-acetylserine. 
MOD_RES   52    52        N6-acetyllysine (By similarity). 
MOD_RES   397   397        S-8alpha-FAD cysteine. 
MUTAGEN   5     5        C->S: No loss of activity. 
MUTAGEN   156   156        C->S: Complete loss of activity. 
MUTAGEN   158   158        T->A: Dramatic loss of activity. 
MUTAGEN   172   172        C->S: No loss of activity. 
MUTAGEN   192   192        C->S: No loss of activity. 
MUTAGEN   199   199        I->F: Alters specificity towards synthetic inhibitors. 
MUTAGEN   297   297        C->S: No loss of activity. 
MUTAGEN   312   312        C->S: No loss of activity. 
MUTAGEN   365   365        C->S: Complete loss of activity. 
MUTAGEN   382   382        H->R: Significant loss of activity. 
MUTAGEN   386   386        K->M: No loss of activity. 
MUTAGEN   389   389        C->A: Complete loss of activity. 
MUTAGEN   389   389        C->S: No loss of activity. 
MUTAGEN   394   394        S->A: No loss of activity. 
MUTAGEN   397   397        C->S: Complete loss of activity. 
STRAND   6    10  5      
HELIX   14    25  12      
STRAND   30    33  4      
STRAND   35    40  6      
TURN   49    51  3      
STRAND   54    57  4      
HELIX   66    74  9      
STRAND   79    81  3      
STRAND   85    92  8      
STRAND   95    99  5      
STRAND   101   103  3      
HELIX   109   126  18      
HELIX   134   136  3      
HELIX   140   144  5      
STRAND   145   147  3      
HELIX   148   155  8      
HELIX   159   173  15      
TURN   177   179  3      
HELIX   182   190  9      
TURN   191   193  3      
HELIX   195   199  5      
STRAND   207   210  4      
HELIX   216   225  10      
HELIX   226   228  3      
STRAND   235   239  5      
STRAND   241   249  9      
STRAND   254   262  9      
HELIX   266   271  6      
STRAND   272   276  5      
HELIX   280   285  6      
STRAND   294   300  7      
HELIX   305   309  5      
STRAND   311   317  7      
STRAND   325   329  5      
STRAND   339   345  7      
HELIX   347   352  6      
HELIX   357   372  16      
HELIX