ADIPO_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ADIPO_HUMAN
• UniProt AC: Q15848
• Protein Name: Adiponectin
• Gene Name: ADIPOQ
• Organism: Homo sapiens (Human).
• Sequence Length: 244
• 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: MLLLGAVLLLLALPGHDQETTTQGPGVLLPLPKGACTGWMAGIPGHPGHNGAPGRDGRDGTPGEKGEKGDPGLIGPKGDIGETGVPGAEGPRGFPGIQGRKGEPGEGAYVYRSAFSVGLETYVTIPNMPIRFTKIFYNQQNHYDGSTGKFHCNIPGLYYFAYHITVYMKDVKVSLFKKDKAMLFTYDQYQENNVDQASGSVLLHLEVGDQVWLQVYGEGERNGLYADNDNDSTFTGFLLYHDTN

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
21	O-linked_Glycosylation	PGHDQETTTQGPGVL CCCCCCCCCCCCCEE	19.17	19855092
22	O-linked_Glycosylation	GHDQETTTQGPGVLL CCCCCCCCCCCCEEE	38.66	19855092
33	Hydroxylation	GVLLPLPKGACTGWM CEEEECCCCCCCCHH	67.81	-
36	Succinylation	LPLPKGACTGWMAGI EECCCCCCCCHHCCC	5.01	-
44	Hydroxylation	TGWMAGIPGHPGHNG CCHHCCCCCCCCCCC	33.84	16497731
47	Hydroxylation	MAGIPGHPGHNGAPG HCCCCCCCCCCCCCC	52.21	16497731
53	Hydroxylation	HPGHNGAPGRDGRDG CCCCCCCCCCCCCCC	39.49	16497731
65	O-linked_Glycosylation	RDGTPGEKGEKGDPG CCCCCCCCCCCCCCC	77.58	11912203
65	Hydroxylation	RDGTPGEKGEKGDPG CCCCCCCCCCCCCCC	77.58	16497731
68	Hydroxylation	TPGEKGEKGDPGLIG CCCCCCCCCCCCCCC	76.82	16497731
68	O-linked_Glycosylation	TPGEKGEKGDPGLIG CCCCCCCCCCCCCCC	76.82	11912203
71	Hydroxylation	EKGEKGDPGLIGPKG CCCCCCCCCCCCCCC	48.43	16497731
76	Hydroxylation	GDPGLIGPKGDIGET CCCCCCCCCCCCCCC	30.38	16497731
77	Hydroxylation	DPGLIGPKGDIGETG CCCCCCCCCCCCCCC	65.09	16497731
77	O-linked_Glycosylation	DPGLIGPKGDIGETG CCCCCCCCCCCCCCC	65.09	11912203
83	Phosphorylation	PKGDIGETGVPGAEG CCCCCCCCCCCCCCC	37.96	22985185
91	Hydroxylation	GVPGAEGPRGFPGIQ CCCCCCCCCCCCCCC	25.40	16497731
95	Hydroxylation	AEGPRGFPGIQGRKG CCCCCCCCCCCCCCC	41.63	16497731
101	Hydroxylation	FPGIQGRKGEPGEGA CCCCCCCCCCCCCCC	74.56	16497731
101	O-linked_Glycosylation	FPGIQGRKGEPGEGA CCCCCCCCCCCCCCC	74.56	11912203
116	Phosphorylation	YVYRSAFSVGLETYV EEEEEEEEEECEEEE	18.26	22210691
122	Phosphorylation	FSVGLETYVTIPNMP EEEECEEEEECCCCC	6.04	22210691
174	Phosphorylation	YMKDVKVSLFKKDKA EECCEEEEEEECCEE	23.52	24719451

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

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

Functions of PTM Sites

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

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PDGFB_HUMAN	PDGFB	physical	12070119
ADIPO_HUMAN	ADIPOQ	physical	12021245
ADIPO_HUMAN	ADIPOQ	physical	19855092
KASH5_HUMAN	CCDC155	physical	25416956
SYNE4_HUMAN	SYNE4	physical	25416956

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 612556: Adiponectin deficiency (ADPND)
• 125853: Diabetes mellitus, non-insulin-dependent (NIDDM)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Hydroxylation

"Adiponectin multimerization is dependent on conserved lysines in thecollagenous domain: evidence for regulation of multimerization byalterations in posttranslational modifications.";
Richards A.A., Stephens T., Charlton H.K., Jones A., Macdonald G.A.,Prins J.B., Whitehead J.P.;
Mol. Endocrinol. 20:1673-1687(2006).
Cited for: SUBUNIT, HYDROXYLATION AT PRO-44; PRO-47; PRO-53; LYS-65; LYS-68;PRO-71; PRO-76; LYS-77; PRO-91; PRO-95 AND LYS-101, GLYCOSYLATION ATLYS-65; LYS-68; LYS-77 AND LYS-101, DISULFIDE BOND, LACK OFHYDROXYLATION AT PRO-62; PRO-86 AND PRO-104, LACK OF GLYCOSYLATION ATASN-230, MUTAGENESIS OF LYS-33; CYS-36; LYS-65; LYS-68; LYS-77 ANDLYS-101, AND MASS SPECTROMETRY.
PubMed: 16497731

O-linked Glycosylation

"Adiponectin multimerization is dependent on conserved lysines in thecollagenous domain: evidence for regulation of multimerization byalterations in posttranslational modifications.";
Richards A.A., Stephens T., Charlton H.K., Jones A., Macdonald G.A.,Prins J.B., Whitehead J.P.;
Mol. Endocrinol. 20:1673-1687(2006).
Cited for: SUBUNIT, HYDROXYLATION AT PRO-44; PRO-47; PRO-53; LYS-65; LYS-68;PRO-71; PRO-76; LYS-77; PRO-91; PRO-95 AND LYS-101, GLYCOSYLATION ATLYS-65; LYS-68; LYS-77 AND LYS-101, DISULFIDE BOND, LACK OFHYDROXYLATION AT PRO-62; PRO-86 AND PRO-104, LACK OF GLYCOSYLATION ATASN-230, MUTAGENESIS OF LYS-33; CYS-36; LYS-65; LYS-68; LYS-77 ANDLYS-101, AND MASS SPECTROMETRY.
PubMed: 16497731

"Sialic acid modification of adiponectin is not required formultimerization or secretion but determines half-life incirculation.";
Richards A.A., Colgrave M.L., Zhang J., Webster J., Simpson F.,Preston E., Wilks D., Hoehn K.L., Stephenson M., Macdonald G.A.,Prins J.B., Cooney G.J., Xu A., Whitehead J.P.;
Mol. Endocrinol. 24:229-239(2010).
Cited for: GLYCOSYLATION AT THR-21 AND THR-22, SUBUNIT, MASS SPECTROMETRY, ANDMUTAGENESIS OF THR-20; THR-21 AND THR-22.
PubMed: 19855092