dbPTM

ANGL3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ANGL3_HUMAN
UniProt AC	Q9Y5C1
Protein Name	Angiopoietin-related protein 3
Gene Name	ANGPTL3
Organism	Homo sapiens (Human).
Sequence Length	460
Subcellular Localization	Secreted . Cell projection, lamellipodium . Colocalized with HSPG2 and activated ITGB3 on podocytes.
Protein Description	Acts in part as a hepatokine that is involved in regulation of lipid and glucose metabolism. [PubMed: 11788823]
Protein Sequence	MFTIKLLLFIVPLVISSRIDQDNSSFDSLSPEPKSRFAMLDDVKILANGLLQLGHGLKDFVHKTKGQINDIFQKLNIFDQSFYDLSLQTSEIKEEEKELRRTTYKLQVKNEEVKNMSLELNSKLESLLEEKILLQQKVKYLEEQLTNLIQNQPETPEHPEVTSLKTFVEKQDNSIKDLLQTVEDQYKQLNQQHSQIKEIENQLRRTSIQEPTEISLSSKPRAPRTTPFLQLNEIRNVKHDGIPAECTTIYNRGEHTSGMYAIRPSNSQVFHVYCDVISGSPWTLIQHRIDGSQNFNETWENYKYGFGRLDGEFWLGLEKIYSIVKQSNYVLRIELEDWKDNKHYIEYSFYLGNHETNYTLHLVAITGNVPNAIPENKDLVFSTWDHKAKGHFNCPEGYSGGWWWHDECGENNLNGKYNKPRAKSKPERRRGLSWKSQNGRLYSIKSTKMLIHPTDSESFE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
17	Phosphorylation	IVPLVISSRIDQDNS HHHHHHHCCCCCCCC	23.33	24719451
24	Phosphorylation	SRIDQDNSSFDSLSP CCCCCCCCCCCCCCC	40.44	24505115
25	Phosphorylation	RIDQDNSSFDSLSPE CCCCCCCCCCCCCCC	39.05	19824718
28	Phosphorylation	QDNSSFDSLSPEPKS CCCCCCCCCCCCCCH	28.83	24505115
115	N-linked_Glycosylation	VKNEEVKNMSLELNS ECCHHHHHCCHHHHH	30.37	10644446
122	O-linked_Glycosylation	NMSLELNSKLESLLE HCCHHHHHHHHHHHH	51.77	29351928
126	Phosphorylation	ELNSKLESLLEEKIL HHHHHHHHHHHHHHH	49.00	24719451
206	Phosphorylation	IENQLRRTSIQEPTE HHHHHHHCCCCCCCC	24.61	68700725
206	O-linked_Glycosylation	IENQLRRTSIQEPTE HHHHHHHCCCCCCCC	24.61	OGP
207	Phosphorylation	ENQLRRTSIQEPTEI HHHHHHCCCCCCCCC	22.06	68700731
212	O-linked_Glycosylation	RTSIQEPTEISLSSK HCCCCCCCCCCCCCC	45.24	OGP
215	O-linked_Glycosylation	IQEPTEISLSSKPRA CCCCCCCCCCCCCCC	18.90	OGP
217	O-linked_Glycosylation	EPTEISLSSKPRAPR CCCCCCCCCCCCCCC	29.53	OGP
218	O-linked_Glycosylation	PTEISLSSKPRAPRT CCCCCCCCCCCCCCC	52.55	OGP
225	O-linked_Glycosylation	SKPRAPRTTPFLQLN CCCCCCCCCCCCCHH	37.45	OGP
226	O-linked_Glycosylation	KPRAPRTTPFLQLNE CCCCCCCCCCCCHHH	17.21	20837471
296	N-linked_Glycosylation	IDGSQNFNETWENYK CCCCCCCCHHHHHHC	54.03	16335952
357	N-linked_Glycosylation	YLGNHETNYTLHLVA EECCCCCCEEEEEEE	25.47	16335952
436	Phosphorylation	RRGLSWKSQNGRLYS HCCCCEECCCCCEEE	23.71	101546011
442	Phosphorylation	KSQNGRLYSIKSTKM ECCCCCEEEEEECEE	13.64	22210691
443	Phosphorylation	SQNGRLYSIKSTKML CCCCCEEEEEECEEE	28.29	24719451
446	Phosphorylation	GRLYSIKSTKMLIHP CCEEEEEECEEEECC	31.43	24719451
447	Phosphorylation	RLYSIKSTKMLIHPT CEEEEEECEEEECCC	18.57	24719451
456	Phosphorylation	MLIHPTDSESFE--- EEECCCCCCCCC---	37.30	24505115
458	Phosphorylation	IHPTDSESFE----- ECCCCCCCCC-----	38.33	24505115

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 ANGL3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
226	T	Glycosylation		20837471
O-glycosylated at Thr-226 by GALNT2; blocks processing and activation by proprotein convertases.

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 ANGL3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CCD91_HUMAN	CCDC91	physical	28514442
GULP1_HUMAN	GULP1	physical	28514442
FBX28_HUMAN	FBXO28	physical	28514442
BIRC6_HUMAN	BIRC6	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
605019	Hypobetalipoproteinemia, familial, 2 (FHBL2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ANGL3_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"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-296, AND MASSSPECTROMETRY.	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-115; ASN-296 AND ASN-357,AND MASS SPECTROMETRY.	16335952 [Abstract]
"Identification of a mammalian angiopoietin-related protein expressedspecifically in liver."; Conklin D., Gilbertson D., Taft D.W., Maurer M.F., Whitmore T.E.,Smith D.L., Walker K.M., Chen L.H., Wattler S., Nehls M., Lewis K.B.; Genomics 62:477-482(1999). Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND GLYCOSYLATION ATASN-115.	10644446 [Abstract]

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