dbPTM

AOC3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AOC3_HUMAN
UniProt AC	Q16853
Protein Name	Membrane primary amine oxidase
Gene Name	AOC3
Organism	Homo sapiens (Human).
Sequence Length	763
Subcellular Localization	Cell membrane Single-pass type II membrane protein .
Protein Description	Cell adhesion protein that participates in lymphocyte extravasation and recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin-independent fashion. Has semicarbazide-sensitive (SSAO) monoamine oxidase activity. May play a role in adipogenesis..
Protein Sequence	MNQKTILVLLILAVITIFALVCVLLVGRGGDGGEPSQLPHCPSVSPSAQPWTHPGQSQLFADLSREELTAVMRFLTQRLGPGLVDAAQARPSDNCVFSVELQLPPKAAALAHLDRGSPPPAREALAIVFFGRQPQPNVSELVVGPLPHPSYMRDVTVERHGGPLPYHRRPVLFQEYLDIDQMIFNRELPQASGLLHHCCFYKHRGRNLVTMTTAPRGLQSGDRATWFGLYYNISGAGFFLHHVGLELLVNHKALDPARWTIQKVFYQGRYYDSLAQLEAQFEAGLVNVVLIPDNGTGGSWSLKSPVPPGPAPPLQFYPQGPRFSVQGSRVASSLWTFSFGLGAFSGPRIFDVRFQGERLVYEISLQEALAIYGGNSPAAMTTRYVDGGFGMGKYTTPLTRGVDCPYLATYVDWHFLLESQAPKTIRDAFCVFEQNQGLPLRRHHSDLYSHYFGGLAETVLVVRSMSTLLNYDYVWDTVFHPSGAIEIRFYATGYISSAFLFGATGKYGNQVSEHTLGTVHTHSAHFKVDLDVAGLENWVWAEDMVFVPMAVPWSPEHQLQRLQVTRKLLEMEEQAAFLVGSATPRYLYLASNHSNKWGHPRGYRIQMLSFAGEPLPQNSSMARGFSWERYQLAVTQRKEEEPSSSSVFNQNDPWAPTVDFSDFINNETIAGKDLVAWVTAGFLHIPHAEDIPNTVTVGNGVGFFLRPYNFFDEDPSFYSADSIYFRGDQDAGACEVNPLACLPQAAACAPDLPAFSHGGFSHN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
47	O-linked_Glycosylation	HCPSVSPSAQPWTHP CCCCCCCCCCCCCCC	31.84	OGP
137	N-linked_Glycosylation	FGRQPQPNVSELVVG ECCCCCCCCCEEEEE	44.70	16046623
210	Phosphorylation	HRGRNLVTMTTAPRG CCCCCEEEEEECCCC	16.38	23532336
212	O-linked_Glycosylation	GRNLVTMTTAPRGLQ CCCEEEEEECCCCCC	15.50	16046623
232	N-linked_Glycosylation	TWFGLYYNISGAGFF EEEEEEEECCCCCHH	14.37	16046623
294	N-linked_Glycosylation	NVVLIPDNGTGGSWS EEEEECCCCCCCCCE	44.57	16046623
345	Phosphorylation	SFGLGAFSGPRIFDV EEECCCCCCCEEEEE	47.56	24719451
471	Other	SMSTLLNYDYVWDTV CHHHHHCCCEEEEEE	14.50	-
471	"2',4',5'-topaquinone"	SMSTLLNYDYVWDTV CHHHHHCCCEEEEEE	14.50	-
507	Phosphorylation	LFGATGKYGNQVSEH HHCCCCCCCCCCCCC	23.74	29083192
512	Phosphorylation	GKYGNQVSEHTLGTV CCCCCCCCCCCCEEE	17.56	29083192
515	Phosphorylation	GNQVSEHTLGTVHTH CCCCCCCCCEEEECC	23.88	29083192
518	Phosphorylation	VSEHTLGTVHTHSAH CCCCCCEEEECCCCE	16.54	29083192
583	Phosphorylation	AFLVGSATPRYLYLA HHHHCCCCHHEEEEC	15.25	46164783
592	N-linked_Glycosylation	RYLYLASNHSNKWGH HEEEECCCCCCCCCC	36.68	16046623
618	N-linked_Glycosylation	AGEPLPQNSSMARGF CCCCCCCCCCCCCCC	33.83	16046623
666	N-linked_Glycosylation	DFSDFINNETIAGKD CHHHHCCCCCCCCHH	42.86	16046623

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 AOC3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of AOC3_HUMAN !!

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 AOC3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TMG4_HUMAN	PRRG4	physical	21988832
AOC2_HUMAN	AOC2	physical	28514442
EXTL2_HUMAN	EXTL2	physical	28514442
SL9A1_HUMAN	SLC9A1	physical	28514442
MANEA_HUMAN	MANEA	physical	28514442
ERF_HUMAN	ERF	physical	28514442
AR6P6_HUMAN	ARL6IP6	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of AOC3_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Crystal structure of the human vascular adhesion protein-1: uniquestructural features with functional implications."; Airenne T.T., Nymalm Y., Kidron H., Smith D.J., Pihlavisto M.,Salmi M., Jalkanen S., Johnson M.S., Salminen T.A.; Protein Sci. 14:1964-1974(2005). Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH COPPER ANDCALCIUM IONS, DISULFIDE BONDS, TOPAQUINONE AT TYR-471, ANDGLYCOSYLATION AT ASN-137; THR-212; ASN-232; ASN-294; ASN-592; ASN-618AND ASN-666.	16046623 [Abstract]
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-137; ASN-294; ASN-592;ASN-618 AND ASN-666, AND MASS SPECTROMETRY.	19159218 [Abstract]
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-592; ASN-618 AND ASN-666,AND MASS SPECTROMETRY.	16335952 [Abstract]