P21397 (AOFA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Amine oxidase [flavin-containing] A
EC=1.4.3.4

Alternative name(s):
Monoamine oxidase type A
Short name=MAO-A

Gene names

Name:

MAOA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	527 AA.
Sequence status	Complete.
Protein existence	Evidence 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. MAOA preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT), norepinephrine and epinephrine.
Catalytic activity	RCH2NHR' + H2O + O2 = RCHO + R'NH2 + H2O2.
Cofactor	FAD. Ref.17 Ref.18
Subunit structure	Monomer, homo- or heterodimer (containing two subunits of similar size). Each subunit contains a covalently bound flavin. Enzymatically active as monomer. Ref.17
Subcellular location	Mitochondrion outer membrane; Single-pass type IV membrane protein; Cytoplasmic side.
Tissue specificity	Heart, liver, duodenum, blood vessels and kidney.
Polymorphism	A polymorphism 1.2 kb upstream of the MAOA coding sequences consists of a 30-bp repeated sequence present in 3, 3.5, 4, or 5 copies. The polymorphism affect transcriptional activity of the MAOA gene promoter. Alleles with 3.5 or 4 copies of the repeat sequence are transcribed 2 to 10 times more efficiently than those with 3 or 5 copies of the repeat.
Involvement in disease	Brunner syndrome (BRUNS) [MIM:300615]: A form of X-linked non-dysmorphic mild mental retardation. Male patients are affected by borderline mental retardation and exhibit abnormal behavior, including disturbed regulation of impulsive aggression. Obligate female carriers have normal intelligence and behavior. Note: The disease is caused by mutations affecting the gene represented in this entry.
Sequence similarities	Belongs to the flavin monoamine oxidase family.
Mass spectrometry	Molecular mass is 60512±6 Da from positions 1 - 527. Determined by ESI. Ref.13

Ontologies

Keywords
Biological process	Catecholamine metabolism Neurotransmitter degradation
Cellular component	Membrane Mitochondrion Mitochondrion outer membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Mental retardation
Domain	Transmembrane Transmembrane helix
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	behavior Traceable author statement Ref.15. Source: ProtInc cellular biogenic amine metabolic process Traceable author statement Ref.15. Source: ProtInc dopamine catabolic process Inferred from electronic annotation. Source: Compara neurotransmitter biosynthetic process Traceable author statement. Source: Reactome neurotransmitter catabolic process Inferred from electronic annotation. Source: UniProtKB-KW neurotransmitter secretion Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome xenobiotic metabolic process Traceable author statement. Source: Reactome
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial outer membrane Traceable author statement. Source: Reactome
Molecular_function	primary amine oxidase activity Traceable author statement. Source: Reactome
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P21397-1)

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.

Isoform 2 (identifier: P21397-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 527

527

Amine oxidase [flavin-containing] A

PRO_0000099850

Regions

Topological domain

1 – 497

497

Cytoplasmic Ref.18

Transmembrane

498 – 518

21

Helical; Anchor for type IV membrane protein

Topological domain

519 – 527

9

Mitochondrial intermembrane Ref.18

Region

520 – 522

3

Interaction with membrane phospholipid headgroups Probable

Sites

Site

335

1

Important for substrate specificity By similarity

Site

374

1

Important for catalytic activity

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.13

Modified residue

406

1

S-8alpha-FAD cysteine

Natural variations

Alternative sequence

1 – 133

133

Missing in isoform 2.

VSP_045173

Natural variant

15

1

D → E in a breast cancer sample; somatic mutation. Ref.19

VAR_036545

Natural variant

188

1

E → K. Ref.20
Corresponds to variant rs77698881 [ dbSNP | Ensembl ].

VAR_064573

Natural variant

314

1

F → V.
Corresponds to variant rs1799835 [ dbSNP | Ensembl ].

VAR_014795

Natural variant

520

1

K → R.
Corresponds to variant rs1800466 [ dbSNP | Ensembl ].

VAR_014796

Experimental info

Mutagenesis

165

1

C → S: No loss of activity. Ref.14

Mutagenesis

266

1

C → S: No loss of activity. Ref.14

Mutagenesis

306

1

C → S: No loss of activity. Ref.14

Mutagenesis

321

1

C → S: No loss of activity. Ref.14

Mutagenesis

323

1

C → S: No loss of activity. Ref.14

Mutagenesis

374

1

C → S: Complete loss of activity. Ref.14

Mutagenesis

398

1

C → S: No loss of activity. Ref.14

Mutagenesis

406

1

C → S: Complete loss of activity. Ref.14

Sequence conflict

397

1

W → M AA sequence Ref.11

Secondary structure

1

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527

Helix Strand Turn

Details...

Beta strand

15 – 19

5

Helix

23 – 34

12

Beta strand

39 – 42

4

Beta strand

44 – 49

6

Beta strand

54 – 57

4

Turn

58 – 60

3

Beta strand

61 – 66

6

Helix

75 – 83

9

Beta strand

88 – 90

3

Beta strand

94 – 101

8

Beta strand

104 – 108

5

Beta strand

110 – 112

3

Helix

118 – 136

19

Helix

143 – 145

3

Helix

149 – 154

6

Helix

157 – 164

8

Helix

168 – 182

15

Turn

186 – 188

3

Helix

191 – 199

9

Turn

200 – 202

3

Helix

204 – 208

5

Beta strand

211 – 213

3

Beta strand

216 – 219

4

Helix

224 – 234

11

Helix

235 – 237

3

Beta strand

238 – 241

4

Beta strand

244 – 248

5

Beta strand

250 – 258

9

Beta strand

263 – 271

9

Helix

275 – 278

4

Beta strand

281 – 285

5

Helix

289 – 295

7

Beta strand

303 – 309

7

Helix

314 – 317

4

Beta strand

320 – 327

8

Beta strand

334 – 338

5

Beta strand

348 – 354

7

Helix

355 – 361

7

Helix

366 – 381

16

Helix

385 – 387

3

Beta strand

390 – 397

8

Turn

401 – 403

3

Beta strand

405 – 407

3

Helix

415 – 418

4

Helix

420 – 422

3

Beta strand

430 – 432

3

Helix

435 – 437

3

Beta strand

439 – 441

3

Helix

445 – 462

18

Beta strand

464 – 466

3

Helix

469 – 471

3

Beta strand

479 – 481

3

Helix

490 – 494

5

Helix

498 – 520

23

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1991. Version 1. Checksum: 4270E346928AE832	FASTA	527	59,682
	10 20 30 40 50 60 MENQEKASIA GHMFDVVVIG GGISGLSAAK LLTEYGVSVL VLEARDRVGG RTYTIRNEHV 70 80 90 100 110 120 DYVDVGGAYV GPTQNRILRL SKELGIETYK VNVSERLVQY VKGKTYPFRG AFPPVWNPIA 130 140 150 160 170 180 YLDYNNLWRT IDNMGKEIPT DAPWEAQHAD KWDKMTMKEL IDKICWTKTA RRFAYLFVNI 190 200 210 220 230 240 NVTSEPHEVS ALWFLWYVKQ CGGTTRIFSV TNGGQERKFV GGSGQVSERI MDLLGDQVKL 250 260 270 280 290 300 NHPVTHVDQS SDNIIIETLN HEHYECKYVI NAIPPTLTAK IHFRPELPAE RNQLIQRLPM 310 320 330 340 350 360 GAVIKCMMYY KEAFWKKKDY CGCMIIEDED APISITLDDT KPDGSLPAIM GFILARKADR 370 380 390 400 410 420 LAKLHKEIRK KKICELYAKV LGSQEALHPV HYEEKNWCEE QYSGGCYTAY FPPGIMTQYG 430 440 450 460 470 480 RVIRQPVGRI FFAGTETATK WSGYMEGAVE AGERAAREVL NGLGKVTEKD IWVQEPESKD 490 500 510 520 VPAVEITHTF WERNLPSVSG LLKIIGFSTS VTALGFVLYK YKLLPRS
	Isoform 2 [UniParc]. Checksum: CA2429F72CD7F231	FASTA	394	44,848
	10 20 30 40 50 60 MGKEIPTDAP WEAQHADKWD KMTMKELIDK ICWTKTARRF AYLFVNINVT SEPHEVSALW 70 80 90 100 110 120 FLWYVKQCGG TTRIFSVTNG GQERKFVGGS GQVSERIMDL LGDQVKLNHP VTHVDQSSDN 130 140 150 160 170 180 IIIETLNHEH YECKYVINAI PPTLTAKIHF RPELPAERNQ LIQRLPMGAV IKCMMYYKEA 190 200 210 220 230 240 FWKKKDYCGC MIIEDEDAPI SITLDDTKPD GSLPAIMGFI LARKADRLAK LHKEIRKKKI 250 260 270 280 290 300 CELYAKVLGS QEALHPVHYE EKNWCEEQYS GGCYTAYFPP GIMTQYGRVI RQPVGRIFFA 310 320 330 340 350 360 GTETATKWSG YMEGAVEAGE RAAREVLNGL GKVTEKDIWV QEPESKDVPA VEITHTFWER 370 380 390 NLPSVSGLLK IIGFSTSVTA LGFVLYKYKL LPRS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural features of human monoamine oxidase A elucidated from cDNA and peptide sequences." Hsu Y.-P.P., Weyler W., Chen S., Sims K.B., Rinehart W.B., Utterback M.C., Powell J.F., Breakefield X.O. J. Neurochem. 51:1321-1324(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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). Tissue: Liver.
[3]	"Structure of the human gene for monoamine oxidase type A." Chen Z.-Y., Hotamisligil G.S., Huang J.-K., Wen L., Ezzeddine D., Aydin-Muderrisoglu N., Powell J.F., Huang R.H., Breakefield X.O., Craig I., Hsu Y.-P.P. Nucleic Acids Res. 19:4537-4541(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"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].
[5]	"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] (ISOFORM 2). Tissue: Cerebellum.
[6]	"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].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Ovary.
[8]	"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 1-24.
[9]	"The promoter of the human monoamine oxidase A gene." Denney R.M. Prog. Brain Res. 106:57-66(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
[10]	"A new look at the promoter of the human monoamine oxidase A gene: mapping transcription initiation sites and capacity to drive luciferase expression." Denney R.M., Sharma A., Dave S.K., Waguespack A. J. Neurochem. 63:843-856(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
[11]	"Partial amino acid sequence analysis of human placenta monoamine oxidase A and bovine liver monoamine oxidase B." Chen S.-Y., Weyler W. Biochem. Biophys. Res. Commun. 156:445-450(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 31-45; 62-78; 109-129; 268-288; 298-315; 318-332; 336-352; 372-412; 430-440 AND 458-493. Tissue: Placenta.
[12]	"Monoamine oxidase A from human placenta and monoamine oxidase B from bovine liver both have one FAD per subunit." Weyler W. Biochem. J. 260:725-729(1989) [PubMed] [Europe PMC] [Abstract] Cited for: DETERMINATION OF PROTEIN-FAD RATIO. Tissue: Placenta.
[13]	"High-level expression of human liver monoamine oxidase A in Pichia pastoris: comparison with the enzyme expressed in Saccharomyces cerevisiae." Li M., Hubalek F., Newton-Vinson P., Edmondson D.E. Protein Expr. Purif. 24:152-162(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, ACETYLATION AT MET-1, MASS SPECTROMETRY.
[14]	"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-165; CYS-266; CYS-306; CYS-321; CYS-323; CYS-374; CYS-398 AND CYS-406.
[15]	"Abnormal behavior associated with a point mutation in the structural gene for monoamine oxidase A." Brunner H.G., Nelen M., Breakefield X.O., Ropers H.-H., van Oost B.A. Science 262:578-580(1993) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN BRUNNER SYNDROME.
[16]	"A functional polymorphism in the monoamine oxidase A gene promoter." Sabol S.Z., Hu S., Hamer D. Hum. Genet. 103:273-279(1998) [PubMed] [Europe PMC] [Abstract] Cited for: POLYMORPHISM IN THE PROMOTER REGION.
[17]	"Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO B." De Colibus L., Li M., Binda C., Lustig A., Edmondson D.E., Mattevi A. Proc. Natl. Acad. Sci. U.S.A. 102:12684-12689(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), COFACTOR, SUBUNIT.
[18]	"Structure of human monoamine oxidase A at 2.2-A resolution: the control of opening the entry for substrates/inhibitors." Son S.-Y., Ma J., Kondou Y., Yoshimura M., Yamashita E., Tsukihara T. Proc. Natl. Acad. Sci. U.S.A. 105:5739-5744(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS) OF 12-524 IN COMPLEX WITH FAD AND THE INHIBITOR HARMINE, COFACTOR, TOPOLOGY.
[19]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-15.
[20]	"A population-specific HTR2B stop codon predisposes to severe impulsivity." Bevilacqua L., Doly S., Kaprio J., Yuan Q., Tikkanen R., Paunio T., Zhou Z., Wedenoja J., Maroteaux L., Diaz S., Belmer A., Hodgkinson C.A., Dell'osso L., Suvisaari J., Coccaro E., Rose R.J., Peltonen L., Virkkunen M., Goldman D. Nature 468:1061-1066(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT LYS-188.
+	Additional computationally mapped references.

Web resources

GeneReviews

Wikipedia

Monoamine oxidase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M69226 mRNA. Translation: AAA59549.1.
M68840 mRNA. Translation: AAA59548.1.
X60806 Genomic DNA. No translation available.
X60807 Genomic DNA. No translation available.
X60808 Genomic DNA. No translation available.
X60809 Genomic DNA. No translation available.
X60810 Genomic DNA. No translation available.
X60811 Genomic DNA. No translation available.
X60812 Genomic DNA. No translation available.
X60813 Genomic DNA. No translation available.
X60814 Genomic DNA. No translation available.
X60815 Genomic DNA. No translation available.
X60816 Genomic DNA. No translation available.
X60817 Genomic DNA. No translation available.
X60818 Genomic DNA. No translation available.
X60819 Genomic DNA. No translation available.
M68857 , M68843, M68844, M68845, M68846, M68847, M68848, M68849, M68850, M68851, M68852, M68853, M68854, M68855, M68856 Genomic DNA. Translation: AAA59547.1.
AK293926 mRNA. Translation: BAG57307.1.
AL109855 Genomic DNA. No translation available.
BX530072 Genomic DNA. No translation available.
BX537147 Genomic DNA. No translation available.
BX537148 Genomic DNA. No translation available.
BC008064 mRNA. Translation: AAH08064.1.
M89636 Genomic DNA. Translation: AAB46385.1.
S81371 Genomic DNA. Translation: AAD14361.1.
S72704 Genomic DNA. Translation: AAD14113.1.

IPI

IPI00008483.

PIR

A36175.

RefSeq

NP_000231.1. NM_000240.3.
NP_001257387.1. NM_001270458.1.

UniGene

Hs.183109.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H8Q	model	-	A	14-468	[»]
2BXR	X-ray	3.00	A/B	1-527	[»]
2BXS	X-ray	3.15	A/B	1-527	[»]
2Z5X	X-ray	2.20	A	12-524	[»]
2Z5Y	X-ray	2.17	A	12-524	[»]

ProteinModelPortal

P21397.

ModBase

Search...

Protein-protein interaction databases

IntAct

P21397. 1 interaction.

MINT

MINT-4054607.

STRING

9606.ENSP00000340684.

PTM databases

PhosphoSite

P21397.

Polymorphism databases

DMDM

113978.

Proteomic databases

PaxDb

P21397.

PeptideAtlas

P21397.

PRIDE

P21397.

Protocols and materials databases

DNASU

4128.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000338702; ENSP00000340684; ENSG00000189221.
ENST00000542639; ENSP00000440846; ENSG00000189221.

GeneID

4128.

KEGG

hsa:4128.

UCSC

uc004dfy.3. human.

Organism-specific databases

CTD

4128.

GeneCards

GC0XP043515.

HGNC

HGNC:6833. MAOA.

HPA

CAB009437.

MIM

300615. phenotype.
309850. gene+phenotype.

neXtProt

NX_P21397.

Orphanet

3057. Monoamine oxidase-A deficiency.

PharmGKB

PA236.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1231.

HOGENOM

HOG000221615.

HOVERGEN

HBG004255.

InParanoid

P21397.

KO

K00274.

OMA

WTKTARR.

OrthoDB

EOG412M55.

PhylomeDB

P21397.

Enzyme and pathway databases

BioCyc

MetaCyc:HS01798-MONOMER.

BRENDA

1.4.3.4. 2681.

Reactome

REACT_111217. Metabolism.
REACT_13685. Neuronal System.

SABIO-RK

P21397.

Gene expression databases

ArrayExpress

P21397.

Bgee

P21397.

CleanEx

HS_MAOA.

Genevestigator

P21397.

GermOnline

ENSG00000189221. Homo sapiens.

Family and domain databases

InterPro

IPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
[Graphical view]

Pfam

PF01593. Amino_oxidase. 1 hit.
[Graphical view]

PRINTS

PR00757. AMINEOXDASEF.

ProtoNet

Search...

Other

BindingDB

P21397.

ChEMBL

CHEMBL1951.

DrugBank

DB00918. Almotriptan.
DB00190. Carbidopa.
DB01068. Clonazepam.
DB00988. Dopamine.
DB00176. Fluvoxamine.
DB01381. Ginkgo biloba.
DB00458. Imipramine.
DB01247. Isocarboxazid.
DB01235. Levodopa.
DB00601. Linezolid.
DB00186. Lorazepam.
DB01171. Moclobemide.
DB00184. Nicotine.
DB00368. Norepinephrine.
DB00780. Phenelzine.
DB00830. Phenmetrazine.
DB00191. Phentermine.
DB00388. Phenylephrine.
DB00397. Phenylpropanolamine.
DB00852. Pseudoephedrine.
DB01367. Rasagiline.
DB00140. Riboflavin.
DB00953. Rizatriptan.
DB01037. Selegiline.
DB00669. Sumatriptan.
DB00624. Testosterone.
DB00752. Tranylcypromine.
DB00315. Zolmitriptan.

EvolutionaryTrace

P21397.

GenomeRNAi

4128.

NextBio

16206.

SOURCE

Search...

Entry information

Entry name

AOFA_HUMAN

Accession

Primary (citable) accession number: P21397
Secondary accession number(s): B4DF46, Q16426

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	May 1, 1991
Last modified:	May 1, 2013
This is version 156 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.