AOFB_MOUSE - dbPTM
AOFB_MOUSE - PTM Information in dbPTM
Basic Information of Protein
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.
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MSNKSDVIV
------CCCCCCEEE
53.62-
2Phosphorylation------MSNKSDVIV
------CCCCCCEEE
53.6222871156
4Acetylation----MSNKSDVIVVG
----CCCCCCEEEEC
40.506566073
5Phosphorylation---MSNKSDVIVVGG
---CCCCCCEEEECC
41.1622871156
21AcetylationISGMAAAKLLHDCGL
HHHHHHHHHHHHCCC
47.0219819419
26S-palmitoylationAAKLLHDCGLSVVVL
HHHHHHHCCCEEEEE
4.0428526873
26S-nitrosylationAAKLLHDCGLSVVVL
HHHHHHHCCCEEEEE
4.0422178444
26S-nitrosocysteineAAKLLHDCGLSVVVL
HHHHHHHCCCEEEEE
4.04-
43PhosphorylationRDRVGGRTYTIRNKN
HHCCCCEEEEEECCC
28.4323984901
45PhosphorylationRVGGRTYTIRNKNVK
CCCCEEEEEECCCCE
16.9123984901
52AcetylationTIRNKNVKYVDLGGS
EEECCCCEEEECCCC
49.2923576753
52MalonylationTIRNKNVKYVDLGGS
EEECCCCEEEECCCC
49.2926320211
52UbiquitinationTIRNKNVKYVDLGGS
EEECCCCEEEECCCC
49.2927667366
73UbiquitinationNRILRLAKELGLETY
HHHHHHHHHHCCCEE
59.0522790023
81UbiquitinationELGLETYKVNEVERL
HHCCCEEEECHHHHH
46.10-
81SuccinylationELGLETYKVNEVERL
HHCCCEEEECHHHHH
46.1023954790
81AcetylationELGLETYKVNEVERL
HHCCCEEEECHHHHH
46.1023864654
93AcetylationERLIHFVKGKSYAFR
HHHHHHHCCCCCEEC
60.7323201123
93UbiquitinationERLIHFVKGKSYAFR
HHHHHHHCCCCCEEC
60.7327667366
95MalonylationLIHFVKGKSYAFRGP
HHHHHCCCCCEECCC
34.2826320211
95UbiquitinationLIHFVKGKSYAFRGP
HHHHHCCCCCEECCC
34.2827667366
136UbiquitinationIPSDAPWKAPLAEEW
CCCCCCCCCCCHHHC
38.7822790023
154UbiquitinationTMKELLDKICWTKST
CHHHHHHHHHCCCCH
39.4722790023
159UbiquitinationLDKICWTKSTKQIAT
HHHHHCCCCHHHHHH
31.4622790023
200PhosphorylationGGTTRIISTTNGGQE
CCEEEEEEECCCCCE
27.14-
201PhosphorylationGTTRIISTTNGGQER
CEEEEEEECCCCCEE
17.55-
209UbiquitinationTNGGQERKFIGGSGQ
CCCCCEEEEECCCCC
40.3522790023
222AcetylationGQVSERIKDILGDRV
CCHHHHHHHHHCCCC
44.9623864654
222UbiquitinationGQVSERIKDILGDRV
CCHHHHHHHHHCCCC
44.9627667366
222MalonylationGQVSERIKDILGDRV
CCHHHHHHHHHCCCC
44.9626320211
230UbiquitinationDILGDRVKLERPVIH
HHHCCCCEEECCEEE
45.5922790023
248AcetylationTGENVIVKTLNHEIY
CCCEEEEEECCCHHH
35.8523576753
248UbiquitinationTGENVIVKTLNHEIY
CCCEEEEEECCCHHH
35.8522790023
255PhosphorylationKTLNHEIYEAKYVIS
EECCCHHHHHHHHHH
13.5726032504
258UbiquitinationNHEIYEAKYVISAIP
CCHHHHHHHHHHCCC
28.2722790023
274PhosphorylationALGMKIHYSPPLPML
HHCCEEEECCCCHHH
26.7523140645
275PhosphorylationLGMKIHYSPPLPMLR
HCCEEEECCCCHHHH
13.0923140645
302AcetylationIKCMVYYKEPFWRKK
EHHEEEECCCCCCCC
41.0223201123
363AcetylationTKEERLRKLCELYAK
CHHHHHHHHHHHHHH
63.1823576753
363UbiquitinationTKEERLRKLCELYAK
CHHHHHHHHHHHHHH
63.18-
363MalonylationTKEERLRKLCELYAK
CHHHHHHHHHHHHHH
63.1826320211
365S-nitrosocysteineEERLRKLCELYAKVL
HHHHHHHHHHHHHHH
3.67-
365S-nitrosylationEERLRKLCELYAKVL
HHHHHHHHHHHHHHH
3.6721278135
365S-palmitoylationEERLRKLCELYAKVL
HHHHHHHHHHHHHHH
3.6728526873
370AcetylationKLCELYAKVLNSQEA
HHHHHHHHHHCCHHH
33.4323864654
370UbiquitinationKLCELYAKVLNSQEA
HHHHHHHHHHCCHHH
33.4322790023
386AcetylationQPVHYEEKNWCEEQY
CCCCCCCCCCCCHHC
43.7523864654
397OtherEEQYSGGCYTTYFPP
CHHCCCCCCCCCCCC
2.88-
397S-8alpha-FAD cysteineEEQYSGGCYTTYFPP
CHHCCCCCCCCCCCC
2.88-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AOFB_MOUSE !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of AOFB_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AOFB_MOUSE

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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.

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