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Protein

Amine oxidase [flavin-containing] B

Gene

Maob

Organism
Mus musculus (Mouse)
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 (By similarity).By similarity

Catalytic activityi

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

Cofactori

FADBy similarity

Sites

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BRENDAi1.4.3.4. 3474.
ReactomeiREACT_284233. Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:96916. Maob.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 489488CytoplasmicBy similarityAdd
BLAST
Transmembranei490 – 51627Helical; Anchor for type IV membrane proteinBy similarityAdd
BLAST
Topological domaini517 – 5204Mitochondrial intermembraneBy similarity

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • mitochondrial inner membrane Source: MGI
  • mitochondrial outer membrane Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 520519Amine oxidase [flavin-containing] BPRO_0000099860Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei52 – 521N6-acetyllysine1 Publication
Modified residuei248 – 2481N6-acetyllysine1 Publication
Modified residuei397 – 3971S-8alpha-FAD cysteineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8BW75.
PaxDbiQ8BW75.
PRIDEiQ8BW75.

PTM databases

PhosphoSiteiQ8BW75.

Expressioni

Gene expression databases

BgeeiQ8BW75.
CleanExiMM_MAOB.
ExpressionAtlasiQ8BW75. baseline and differential.
GenevisibleiQ8BW75. MM.

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

IntActiQ8BW75. 2 interactions.
MINTiMINT-1861050.
STRINGi10090.ENSMUSP00000040550.

Structurei

3D structure databases

ProteinModelPortaliQ8BW75.
SMRiQ8BW75. Positions 3-495.
ModBaseiSearch...
MobiDBiSearch...

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.
InParanoidiQ8BW75.
KOiK00274.
OMAiVLYQMAS.
OrthoDBiEOG7K6PTP.
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.

Q8BW75-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNKSDVIVV GGGISGMAAA KLLHDCGLSV VVLEARDRVG GRTYTIRNKN
60 70 80 90 100
VKYVDLGGSY VGPTQNRILR LAKELGLETY KVNEVERLIH FVKGKSYAFR
110 120 130 140 150
GPFPPVWNPI TYLDNNNLWR TMDEMGQEIP SDAPWKAPLA EEWDYMTMKE
160 170 180 190 200
LLDKICWTKS TKQIATLFVN LCVTAETHEV SALWFLWYVK QCGGTTRIIS
210 220 230 240 250
TTNGGQERKF IGGSGQVSER IKDILGDRVK LERPVIHIDQ TGENVIVKTL
260 270 280 290 300
NHEIYEAKYV ISAIPPALGM KIHYSPPLPM LRNQLISRVP LGSVIKCMVY
310 320 330 340 350
YKEPFWRKKD FCGTMVIEGE EAPIAYTLDD TKPDGTYAAI MGFILAHKAR
360 370 380 390 400
KLVRLTKEER LRKLCELYAK VLNSQEALQP VHYEEKNWCE EQYSGGCYTT
410 420 430 440 450
YFPPGILTQY GRVLRQPVGK IFFAGTETAS HWSGYMEGAV EAGERAAREI
460 470 480 490 500
LHAIGKIPED EIWQPEPESL DVPARPITST FLERHLPSVP GLLKLFGLTT
510 520
ILSATALGFL AHKRGLFVHF
Length:520
Mass (Da):58,558
Last modified:July 27, 2011 - v4
Checksum:iA5982EBBF5C4BD62
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti408 – 4081T → S in BAC35634 (PubMed:16141072).Curated
Sequence conflicti482 – 4821L → M in BAC27571 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK031833 mRNA. Translation: BAC27571.1.
AK054050 mRNA. Translation: BAC35634.1.
AL732321, AL831729 Genomic DNA. Translation: CAM16088.1.
AL831729, AL732321 Genomic DNA. Translation: CAM26633.1.
CH466584 Genomic DNA. Translation: EDL35718.1.
BC113182 mRNA. Translation: AAI13183.1.
BC113788 mRNA. Translation: AAI13789.1.
CCDSiCCDS40882.1.
RefSeqiNP_766366.2. NM_172778.2.
UniGeneiMm.241656.

Genome annotation databases

EnsembliENSMUST00000040820; ENSMUSP00000040550; ENSMUSG00000040147.
GeneIDi109731.
KEGGimmu:109731.
UCSCiuc009ssb.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK031833 mRNA. Translation: BAC27571.1.
AK054050 mRNA. Translation: BAC35634.1.
AL732321, AL831729 Genomic DNA. Translation: CAM16088.1.
AL831729, AL732321 Genomic DNA. Translation: CAM26633.1.
CH466584 Genomic DNA. Translation: EDL35718.1.
BC113182 mRNA. Translation: AAI13183.1.
BC113788 mRNA. Translation: AAI13789.1.
CCDSiCCDS40882.1.
RefSeqiNP_766366.2. NM_172778.2.
UniGeneiMm.241656.

3D structure databases

ProteinModelPortaliQ8BW75.
SMRiQ8BW75. Positions 3-495.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8BW75. 2 interactions.
MINTiMINT-1861050.
STRINGi10090.ENSMUSP00000040550.

Chemistry

ChEMBLiCHEMBL3050.

PTM databases

PhosphoSiteiQ8BW75.

Proteomic databases

MaxQBiQ8BW75.
PaxDbiQ8BW75.
PRIDEiQ8BW75.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000040820; ENSMUSP00000040550; ENSMUSG00000040147.
GeneIDi109731.
KEGGimmu:109731.
UCSCiuc009ssb.2. mouse.

Organism-specific databases

CTDi4129.
MGIiMGI:96916. Maob.

Phylogenomic databases

eggNOGiCOG1231.
GeneTreeiENSGT00730000110903.
HOGENOMiHOG000221615.
HOVERGENiHBG004255.
InParanoidiQ8BW75.
KOiK00274.
OMAiVLYQMAS.
OrthoDBiEOG7K6PTP.
TreeFamiTF313314.

Enzyme and pathway databases

BRENDAi1.4.3.4. 3474.
ReactomeiREACT_284233. Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB.

Miscellaneous databases

NextBioi362651.
PROiQ8BW75.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BW75.
CleanExiMM_MAOB.
ExpressionAtlasiQ8BW75. baseline and differential.
GenevisibleiQ8BW75. MM.

Family and domain databases

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

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Medulla oblongata and Oviduct.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
  5. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-52 AND LYS-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiAOFB_MOUSE
AccessioniPrimary (citable) accession number: Q8BW75
Secondary accession number(s): Q14CG9, Q8C0B2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2004
Last sequence update: July 27, 2011
Last modified: July 22, 2015
This is version 102 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.