UniProt ID | AOFB_MOUSE | |
---|---|---|
UniProt AC | Q8BW75 | |
Protein Name | Amine oxidase [flavin-containing] B | |
Gene Name | Maob | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 520 | |
Subcellular Localization |
Mitochondrion outer membrane Single-pass type IV membrane protein Cytoplasmic side. |
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Protein Description | 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).. | |
Protein Sequence | MSNKSDVIVVGGGISGMAAAKLLHDCGLSVVVLEARDRVGGRTYTIRNKNVKYVDLGGSYVGPTQNRILRLAKELGLETYKVNEVERLIHFVKGKSYAFRGPFPPVWNPITYLDNNNLWRTMDEMGQEIPSDAPWKAPLAEEWDYMTMKELLDKICWTKSTKQIATLFVNLCVTAETHEVSALWFLWYVKQCGGTTRIISTTNGGQERKFIGGSGQVSERIKDILGDRVKLERPVIHIDQTGENVIVKTLNHEIYEAKYVISAIPPALGMKIHYSPPLPMLRNQLISRVPLGSVIKCMVYYKEPFWRKKDFCGTMVIEGEEAPIAYTLDDTKPDGTYAAIMGFILAHKARKLVRLTKEERLRKLCELYAKVLNSQEALQPVHYEEKNWCEEQYSGGCYTTYFPPGILTQYGRVLRQPVGKIFFAGTETASHWSGYMEGAVEAGERAAREILHAIGKIPEDEIWQPEPESLDVPARPITSTFLERHLPSVPGLLKLFGLTTILSATALGFLAHKRGLFVHF | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Acetylation | ------MSNKSDVIV ------CCCCCCEEE | 53.62 | - | |
2 | Phosphorylation | ------MSNKSDVIV ------CCCCCCEEE | 53.62 | 22871156 | |
4 | Acetylation | ----MSNKSDVIVVG ----CCCCCCEEEEC | 40.50 | 6566073 | |
5 | Phosphorylation | ---MSNKSDVIVVGG ---CCCCCCEEEECC | 41.16 | 22871156 | |
21 | Acetylation | ISGMAAAKLLHDCGL HHHHHHHHHHHHCCC | 47.02 | 19819419 | |
26 | S-palmitoylation | AAKLLHDCGLSVVVL HHHHHHHCCCEEEEE | 4.04 | 28526873 | |
26 | S-nitrosylation | AAKLLHDCGLSVVVL HHHHHHHCCCEEEEE | 4.04 | 22178444 | |
26 | S-nitrosocysteine | AAKLLHDCGLSVVVL HHHHHHHCCCEEEEE | 4.04 | - | |
43 | Phosphorylation | RDRVGGRTYTIRNKN HHCCCCEEEEEECCC | 28.43 | 23984901 | |
45 | Phosphorylation | RVGGRTYTIRNKNVK CCCCEEEEEECCCCE | 16.91 | 23984901 | |
52 | Acetylation | TIRNKNVKYVDLGGS EEECCCCEEEECCCC | 49.29 | 23576753 | |
52 | Malonylation | TIRNKNVKYVDLGGS EEECCCCEEEECCCC | 49.29 | 26320211 | |
52 | Ubiquitination | TIRNKNVKYVDLGGS EEECCCCEEEECCCC | 49.29 | 27667366 | |
73 | Ubiquitination | NRILRLAKELGLETY HHHHHHHHHHCCCEE | 59.05 | 22790023 | |
81 | Ubiquitination | ELGLETYKVNEVERL HHCCCEEEECHHHHH | 46.10 | - | |
81 | Succinylation | ELGLETYKVNEVERL HHCCCEEEECHHHHH | 46.10 | 23954790 | |
81 | Acetylation | ELGLETYKVNEVERL HHCCCEEEECHHHHH | 46.10 | 23864654 | |
93 | Acetylation | ERLIHFVKGKSYAFR HHHHHHHCCCCCEEC | 60.73 | 23201123 | |
93 | Ubiquitination | ERLIHFVKGKSYAFR HHHHHHHCCCCCEEC | 60.73 | 27667366 | |
95 | Malonylation | LIHFVKGKSYAFRGP HHHHHCCCCCEECCC | 34.28 | 26320211 | |
95 | Ubiquitination | LIHFVKGKSYAFRGP HHHHHCCCCCEECCC | 34.28 | 27667366 | |
136 | Ubiquitination | IPSDAPWKAPLAEEW CCCCCCCCCCCHHHC | 38.78 | 22790023 | |
154 | Ubiquitination | TMKELLDKICWTKST CHHHHHHHHHCCCCH | 39.47 | 22790023 | |
159 | Ubiquitination | LDKICWTKSTKQIAT HHHHHCCCCHHHHHH | 31.46 | 22790023 | |
200 | Phosphorylation | GGTTRIISTTNGGQE CCEEEEEEECCCCCE | 27.14 | - | |
201 | Phosphorylation | GTTRIISTTNGGQER CEEEEEEECCCCCEE | 17.55 | - | |
209 | Ubiquitination | TNGGQERKFIGGSGQ CCCCCEEEEECCCCC | 40.35 | 22790023 | |
222 | Acetylation | GQVSERIKDILGDRV CCHHHHHHHHHCCCC | 44.96 | 23864654 | |
222 | Ubiquitination | GQVSERIKDILGDRV CCHHHHHHHHHCCCC | 44.96 | 27667366 | |
222 | Malonylation | GQVSERIKDILGDRV CCHHHHHHHHHCCCC | 44.96 | 26320211 | |
230 | Ubiquitination | DILGDRVKLERPVIH HHHCCCCEEECCEEE | 45.59 | 22790023 | |
248 | Acetylation | TGENVIVKTLNHEIY CCCEEEEEECCCHHH | 35.85 | 23576753 | |
248 | Ubiquitination | TGENVIVKTLNHEIY CCCEEEEEECCCHHH | 35.85 | 22790023 | |
255 | Phosphorylation | KTLNHEIYEAKYVIS EECCCHHHHHHHHHH | 13.57 | 26032504 | |
258 | Ubiquitination | NHEIYEAKYVISAIP CCHHHHHHHHHHCCC | 28.27 | 22790023 | |
274 | Phosphorylation | ALGMKIHYSPPLPML HHCCEEEECCCCHHH | 26.75 | 23140645 | |
275 | Phosphorylation | LGMKIHYSPPLPMLR HCCEEEECCCCHHHH | 13.09 | 23140645 | |
302 | Acetylation | IKCMVYYKEPFWRKK EHHEEEECCCCCCCC | 41.02 | 23201123 | |
363 | Acetylation | TKEERLRKLCELYAK CHHHHHHHHHHHHHH | 63.18 | 23576753 | |
363 | Ubiquitination | TKEERLRKLCELYAK CHHHHHHHHHHHHHH | 63.18 | - | |
363 | Malonylation | TKEERLRKLCELYAK CHHHHHHHHHHHHHH | 63.18 | 26320211 | |
365 | S-nitrosocysteine | EERLRKLCELYAKVL HHHHHHHHHHHHHHH | 3.67 | - | |
365 | S-nitrosylation | EERLRKLCELYAKVL HHHHHHHHHHHHHHH | 3.67 | 21278135 | |
365 | S-palmitoylation | EERLRKLCELYAKVL HHHHHHHHHHHHHHH | 3.67 | 28526873 | |
370 | Acetylation | KLCELYAKVLNSQEA HHHHHHHHHHCCHHH | 33.43 | 23864654 | |
370 | Ubiquitination | KLCELYAKVLNSQEA HHHHHHHHHHCCHHH | 33.43 | 22790023 | |
386 | Acetylation | QPVHYEEKNWCEEQY CCCCCCCCCCCCHHC | 43.75 | 23864654 | |
397 | Other | EEQYSGGCYTTYFPP CHHCCCCCCCCCCCC | 2.88 | - | |
397 | S-8alpha-FAD cysteine | EEQYSGGCYTTYFPP CHHCCCCCCCCCCCC | 2.88 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of AOFB_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AOFB_MOUSE !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of AOFB_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of AOFB_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-52, AND MASS SPECTROMETRY. |