APOC3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: APOC3_HUMAN
• UniProt AC: P02656
• Protein Name: Apolipoprotein C-III
• Gene Name: APOC3
• Organism: Homo sapiens (Human).
• Sequence Length: 99
• Subcellular Localization: Secreted .
• Protein Description: Component of triglyceride-rich very low density lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma. [PubMed: 18201179]
• Protein Sequence: MQPRVLLVVALLALLASARASEAEDASLLSFMQGYMKHATKTAKDALSSVQESQVAQQARGWVTDGFSSLKDYWSTVKDKFSEFWDLDPEVRPTSAVAA

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
17	Phosphorylation	ALLALLASARASEAE HHHHHHHHHHCCHHH	20.46	-
44	Acetylation	KHATKTAKDALSSVQ HHHHHHHHHHHHHHH	49.09	23236377
44	Ubiquitination	KHATKTAKDALSSVQ HHHHHHHHHHHHHHH	49.09	-
44	Succinylation	KHATKTAKDALSSVQ HHHHHHHHHHHHHHH	49.09	23954790
48	Phosphorylation	KTAKDALSSVQESQV HHHHHHHHHHHHHHH	30.13	23911959
49	Phosphorylation	TAKDALSSVQESQVA HHHHHHHHHHHHHHH	28.77	30622161
53	Phosphorylation	ALSSVQESQVAQQAR HHHHHHHHHHHHHHH	16.92	23911959
53	O-linked_Glycosylation	ALSSVQESQVAQQAR HHHHHHHHHHHHHHH	16.92	OGP
64	O-linked_Glycosylation	QQARGWVTDGFSSLK HHHHCCHHCCCHHHH	24.72	OGP
76	O-linked_Glycosylation	SLKDYWSTVKDKFSE HHHHHHHHHHHHHHH	19.89	OGP
82	Phosphorylation	STVKDKFSEFWDLDP HHHHHHHHHHHCCCC	37.31	19413330
94	O-linked_Glycosylation	LDPEVRPTSAVAA-- CCCCCCCCCCCCC--	20.82	4846755
94	Phosphorylation	LDPEVRPTSAVAA-- CCCCCCCCCCCCC--	20.82	19838169
94	O-linked_Glycosylation	LDPEVRPTSAVAA-- CCCCCCCCCCCCC--	20.82	19413330
95	Phosphorylation	DPEVRPTSAVAA--- CCCCCCCCCCCC---	24.35	19413330
95	O-linked_Glycosylation	DPEVRPTSAVAA--- CCCCCCCCCCCC---	24.35	OGP

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

Oops, there are no upstream regulatory protein records of APOC3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
94	T	Glycosylation	O-glycosylated on Thr-94 with a core 1 or possibly core 8 glycan.	19838169

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
17	Phosphorylation	19 (2)	R ⇒ G;*	rs76353203	Triglyceride levels	28548082

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ARFG1_HUMAN	ARFGAP1	physical	21988832
SOX4_HUMAN	SOX4	physical	25969425

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 614028: Hyperalphalipoproteinemia 2 (HALP2)
• 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

O-linked Glycosylation

"Molecular cloning of a human apoC-III variant: Thr 74-->Ala 74mutation prevents O-glycosylation.";
Maeda H., Hashimoto R.K., Oguro T., Hiraga S., Uzawa H.;
J. Lipid Res. 28:1405-1409(1987).
Cited for: VARIANT C-III-0 ALA-94, AND GLYCOSYLATION AT THR-94.
PubMed: 3123586

"Enrichment of glycopeptides for glycan structure and attachment siteidentification.";
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,Brinkmalm G., Larson G.;
Nat. Methods 6:809-811(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-94, STRUCTURE OFCARBOHYDRATES, AND MASS SPECTROMETRY.
PubMed: 19838169