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P27338

- AOFB_HUMAN

UniProt

P27338 - AOFB_HUMAN

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Protein
Amine oxidase [flavin-containing] B
Gene
MAOB
Organism
Homo sapiens (Human)
Status
Reviewed - 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

FAD.

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
Complete GO annotation...

GO - Biological processi

  1. negative regulation of serotonin secretion Source: Ensembl
  2. positive regulation of dopamine metabolic process Source: Ensembl
  3. response to aluminum ion Source: Ensembl
  4. response to corticosterone Source: Ensembl
  5. response to drug Source: Ensembl
  6. response to ethanol Source: Ensembl
  7. response to lipopolysaccharide Source: Ensembl
  8. response to selenium ion Source: Ensembl
  9. response to toxic substance Source: Ensembl
  10. small molecule metabolic process Source: Reactome
  11. substantia nigra development Source: UniProt
  12. 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. Monoamines are oxidized to aldehydes by MAOA and MAOB, producing NH3 and H2O2.
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: Chromosome X

Organism-specific databases

HGNCiHGNC:6834. MAOB.

Subcellular locationi

Topology

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

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. integral component of membrane Source: UniProtKB-KW
  3. mitochondrial envelope Source: ProtInc
  4. mitochondrial inner membrane Source: Ensembl
  5. mitochondrial outer membrane Source: Reactome
  6. mitochondrion Source: UniProt
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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 520519Amine oxidase [flavin-containing] B
PRO_0000099859Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP27338.
PaxDbiP27338.
PRIDEiP27338.

PTM databases

PhosphoSiteiP27338.

Expressioni

Gene expression databases

ArrayExpressiP27338.
BgeeiP27338.
CleanExiHS_MAOB.
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.

Protein-protein interaction databases

BioGridi110302. 4 interactions.
IntActiP27338. 3 interactions.
MINTiMINT-3010688.
STRINGi9606.ENSP00000367309.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP27338.

Family & Domainsi

Compositional bias

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

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1231.
HOGENOMiHOG000221615.
HOVERGENiHBG004255.
InParanoidiP27338.
KOiK00274.
OMAiWDKMSMQ.
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.

Sequencei

Sequence statusi: Complete.

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

P27338-1 [UniParc]FASTAAdd to Basket

« Hide

MSNKCDVVVV GGGISGMAAA KLLHDSGLNV VVLEARDRVG GRTYTLRNQK    50
VKYVDLGGSY VGPTQNRILR LAKELGLETY KVNEVERLIH HVKGKSYPFR 100
GPFPPVWNPI TYLDHNNFWR TMDDMGREIP SDAPWKAPLA EEWDNMTMKE 150
LLDKLCWTES AKQLATLFVN LCVTAETHEV SALWFLWYVK QCGGTTRIIS 200
TTNGGQERKF VGGSGQVSER IMDLLGDRVK LERPVIYIDQ TRENVLVETL 250
NHEMYEAKYV ISAIPPTLGM KIHFNPPLPM MRNQMITRVP LGSVIKCIVY 300
YKEPFWRKKD YCGTMIIDGE EAPVAYTLDD TKPEGNYAAI MGFILAHKAR 350
KLARLTKEER LKKLCELYAK VLGSLEALEP VHYEEKNWCE EQYSGGCYTT 400
YFPPGILTQY GRVLRQPVDR IYFAGTETAT HWSGYMEGAV EAGERAAREI 450
LHAMGKIPED EIWQSEPESV DVPAQPITTT FLERHLPSVP GLLRLIGLTT 500
IFSATALGFL AHKRGLLVRV 520
Length:520
Mass (Da):58,763
Last modified:January 23, 2007 - v3
Checksum:i358D1025F5BCA604
GO

Mass spectrometryi

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS14261.1.
PIRiJH0817.
RefSeqiNP_000889.3. NM_000898.4.
UniGeneiHs.654473.

Genome annotation databases

EnsembliENST00000378069; ENSP00000367309; ENSG00000069535.
GeneIDi4129.
KEGGihsa:4129.
UCSCiuc004dfz.4. human.

Polymorphism databases

DMDMi113980.

Cross-referencesi

Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Monoamine oxidase entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS14261.1.
PIRi JH0817.
RefSeqi NP_000889.3. NM_000898.4.
UniGenei Hs.654473.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GOS X-ray 3.00 A/B 2-520 [» ]
1H8R model - A 5-459 [» ]
1OJ9 X-ray 2.30 A/B 2-520 [» ]
1OJA X-ray 1.70 A/B 2-520 [» ]
1OJC X-ray 2.40 A/B 2-520 [» ]
1OJD X-ray 3.10 A/B/C/D/E/F/G/H/I/L 2-520 [» ]
1S2Q X-ray 2.07 A/B 1-520 [» ]
1S2Y X-ray 2.12 A/B 1-520 [» ]
1S3B X-ray 1.65 A/B 1-520 [» ]
1S3E X-ray 1.60 A/B 1-520 [» ]
2BK3 X-ray 1.80 A/B 2-520 [» ]
2BK4 X-ray 1.90 A/B 2-520 [» ]
2BK5 X-ray 1.83 A/B 1-520 [» ]
2BYB X-ray 2.20 A/B 2-520 [» ]
2C64 X-ray 2.20 A/B 2-520 [» ]
2C65 X-ray 1.70 A/B 2-520 [» ]
2C66 X-ray 2.50 A/B 2-520 [» ]
2C67 X-ray 1.70 A/B 2-520 [» ]
2C70 X-ray 2.06 A/B 2-520 [» ]
2C72 X-ray 2.00 A/B 2-520 [» ]
2C73 X-ray 2.20 A/B 2-520 [» ]
2C75 X-ray 1.70 A/B 2-520 [» ]
2C76 X-ray 1.70 A/B 2-520 [» ]
2V5Z X-ray 1.60 A/B 2-520 [» ]
2V60 X-ray 2.00 A/B 2-520 [» ]
2V61 X-ray 1.70 A/B 2-520 [» ]
2VRL X-ray 2.40 A/B 1-520 [» ]
2VRM X-ray 2.30 A/B 1-520 [» ]
2VZ2 X-ray 2.30 A/B 1-520 [» ]
2XCG X-ray 1.90 A/B 1-520 [» ]
2XFN X-ray 1.60 A/B 1-520 [» ]
2XFO X-ray 2.10 A/B 1-520 [» ]
2XFP X-ray 1.66 A/B 1-520 [» ]
2XFQ X-ray 2.20 A/B 1-520 [» ]
2XFU X-ray 2.20 A/B 2-520 [» ]
3PO7 X-ray 1.80 A/B 1-520 [» ]
3ZYX X-ray 2.20 A/B 2-520 [» ]
4A79 X-ray 1.89 A/B 1-520 [» ]
4A7A X-ray 1.70 A/B 1-520 [» ]
4CRT X-ray 1.80 A/B 1-520 [» ]
ProteinModelPortali P27338.
SMRi P27338. Positions 3-501.
ModBasei Search...

Protein-protein interaction databases

BioGridi 110302. 4 interactions.
IntActi P27338. 3 interactions.
MINTi MINT-3010688.
STRINGi 9606.ENSP00000367309.

Chemistry

BindingDBi P27338.
ChEMBLi CHEMBL2039.
DrugBanki 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.
GuidetoPHARMACOLOGYi 2490.

PTM databases

PhosphoSitei P27338.

Polymorphism databases

DMDMi 113980.

Proteomic databases

MaxQBi P27338.
PaxDbi P27338.
PRIDEi P27338.

Protocols and materials databases

DNASUi 4129.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000378069 ; ENSP00000367309 ; ENSG00000069535 .
GeneIDi 4129.
KEGGi hsa:4129.
UCSCi uc004dfz.4. human.

Organism-specific databases

CTDi 4129.
GeneCardsi GC0XM043625.
HGNCi HGNC:6834. MAOB.
HPAi CAB037200.
HPA002328.
MIMi 309860. gene.
neXtProti NX_P27338.
PharmGKBi PA237.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1231.
HOGENOMi HOG000221615.
HOVERGENi HBG004255.
InParanoidi P27338.
KOi K00274.
OMAi WDKMSMQ.
OrthoDBi EOG7K6PTP.
PhylomeDBi P27338.
TreeFami TF313314.

Enzyme and pathway databases

BioCyci MetaCyc:HS00966-MONOMER.
BRENDAi 1.4.3.4. 2681.
Reactomei REACT_416. Monoamines are oxidized to aldehydes by MAOA and MAOB, producing NH3 and H2O2.
SABIO-RK P27338.

Miscellaneous databases

ChiTaRSi MAOB. human.
EvolutionaryTracei P27338.
GeneWikii Monoamine_oxidase_B.
GenomeRNAii 4129.
NextBioi 16210.
PROi P27338.
SOURCEi Search...

Gene expression databases

ArrayExpressi P27338.
Bgeei P27338.
CleanExi HS_MAOB.
Genevestigatori P27338.

Family and domain databases

InterProi IPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
[Graphical view ]
Pfami PF01593. Amino_oxidase. 1 hit.
[Graphical view ]
PRINTSi PR00757. AMINEOXDASEF.
ProtoNeti Search...

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].
  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.
    , 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.
    , 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. "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.

Entry informationi

Entry nameiAOFB_HUMAN
AccessioniPrimary (citable) accession number: P27338
Secondary accession number(s): B2R6R3, D3DWC3, Q7Z6S2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 157 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

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