ADIPO_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ADIPO_MOUSE
• UniProt AC: Q60994
• Protein Name: Adiponectin
• Gene Name: Adipoq
• Organism: Mus musculus (Mouse).
• Sequence Length: 247
• Subcellular Localization: Secreted.
• Protein Description: Important adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion. Antagonizes TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. Inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. May play a role in cell growth, angiogenesis and tissue remodeling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex, LMW, MMW or HMW..
• Protein Sequence: MLLLQALLFLLILPSHAEDDVTTTEELAPALVPPPKGTCAGWMAGIPGHPGHNGTPGRDGRDGTPGEKGEKGDAGLLGPKGETGDVGMTGAEGPRGFPGTPGRKGEPGEAAYVYRSAFSVGLETRVTVPNVPIRFTKIFYNQQNHYDGSTGKFYCNIPGLYYFSYHITVYMKDVKVSLFKKDKAVLFTYDQYQEKNVDQASGSVLLHLEVGDQVWLQVYGDGDHNGLYADNVNDSTFTGFLLYHDTN

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
23	O-linked_Glycosylation	HAEDDVTTTEELAPA CCCCCCCCHHHHHHH	31.87	19855092
24	O-linked_Glycosylation	AEDDVTTTEELAPAL CCCCCCCHHHHHHHH	20.35	19855092
36	Hydroxylation	PALVPPPKGTCAGWM HHHCCCCCCCCCCHH	73.04	-
39	Succinylation	VPPPKGTCAGWMAGI CCCCCCCCCCHHCCC	4.49	19592500
47	Hydroxylation	AGWMAGIPGHPGHNG CCHHCCCCCCCCCCC	33.84	-
50	Hydroxylation	MAGIPGHPGHNGTPG HCCCCCCCCCCCCCC	52.21	-
56	Hydroxylation	HPGHNGTPGRDGRDG CCCCCCCCCCCCCCC	36.90	-
68	O-linked_Glycosylation	RDGTPGEKGEKGDAG CCCCCCCCCCCCCCC	77.58	23209641
68	Hydroxylation	RDGTPGEKGEKGDAG CCCCCCCCCCCCCCC	77.58	23209641
71	O-linked_Glycosylation	TPGEKGEKGDAGLLG CCCCCCCCCCCCCCC	71.42	23209641
71	Hydroxylation	TPGEKGEKGDAGLLG CCCCCCCCCCCCCCC	71.42	23209641
80	O-linked_Glycosylation	DAGLLGPKGETGDVG CCCCCCCCCCCCCCC	68.53	23209641
80	Hydroxylation	DAGLLGPKGETGDVG CCCCCCCCCCCCCCC	68.53	23209641
89	Phosphorylation	ETGDVGMTGAEGPRG CCCCCCCCCCCCCCC	27.58	28059163
94	Hydroxylation	GMTGAEGPRGFPGTP CCCCCCCCCCCCCCC	25.40	11912203
100	Phosphorylation	GPRGFPGTPGRKGEP CCCCCCCCCCCCCCC	23.86	28059163
104	Hydroxylation	FPGTPGRKGEPGEAA CCCCCCCCCCCCCEE	73.81	23209641
104	O-linked_Glycosylation	FPGTPGRKGEPGEAA CCCCCCCCCCCCCEE	73.81	23209641

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

Oops, there are no upstream regulatory protein records of ADIPO_MOUSE !!

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ADIPO_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CAD13_MOUSE	Cdh13	physical	15210937
ADIPO_MOUSE	Adipoq	physical	19855092

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Hydroxylation

"Hydroxylation and glycosylation of the four conserved lysine residuesin the collagenous domain of adiponectin. Potential role in themodulation of its insulin-sensitizing activity.";
Wang Y., Xu A., Knight C., Xu L.Y., Cooper G.J.S.;
J. Biol. Chem. 277:19521-19529(2002).
Cited for: PROTEIN SEQUENCE OF 18-25, HYDROXYLATION AT LYS-68; LYS-71; LYS-80;PRO-94 AND LYS-104, GLYCOSYLATION AT LYS-68; LYS-71; LYS-80 ANDLYS-104, GLYCAN STRUCTURE, ABSENCE OF HYDROXYLATION AT PRO-79; PRO-98AND PRO-107, ABSENCE OF GLYCOSYLATION AT ASN-233, AND MASSSPECTROMETRY.
PubMed: 11912203

O-linked Glycosylation

"Hydroxylation and glycosylation of the four conserved lysine residuesin the collagenous domain of adiponectin. Potential role in themodulation of its insulin-sensitizing activity.";
Wang Y., Xu A., Knight C., Xu L.Y., Cooper G.J.S.;
J. Biol. Chem. 277:19521-19529(2002).
Cited for: PROTEIN SEQUENCE OF 18-25, HYDROXYLATION AT LYS-68; LYS-71; LYS-80;PRO-94 AND LYS-104, GLYCOSYLATION AT LYS-68; LYS-71; LYS-80 ANDLYS-104, GLYCAN STRUCTURE, ABSENCE OF HYDROXYLATION AT PRO-79; PRO-98AND PRO-107, ABSENCE OF GLYCOSYLATION AT ASN-233, AND MASSSPECTROMETRY.
PubMed: 11912203