dbPTM

EGLN_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EGLN_HUMAN
UniProt AC	P17813
Protein Name	Endoglin
Gene Name	ENG
Organism	Homo sapiens (Human).
Sequence Length	658
Subcellular Localization	Cell membrane Single-pass type I membrane protein .
Protein Description	Vascular endothelium glycoprotein that plays an important role in the regulation of angiogenesis. [PubMed: 21737454]
Protein Sequence	MDRGTLPLAVALLLASCSLSPTSLAETVHCDLQPVGPERGEVTYTTSQVSKGCVAQAPNAILEVHVLFLEFPTGPSQLELTLQASKQNGTWPREVLLVLSVNSSVFLHLQALGIPLHLAYNSSLVTFQEPPGVNTTELPSFPKTQILEWAAERGPITSAAELNDPQSILLRLGQAQGSLSFCMLEASQDMGRTLEWRPRTPALVRGCHLEGVAGHKEAHILRVLPGHSAGPRTVTVKVELSCAPGDLDAVLILQGPPYVSWLIDANHNMQIWTTGEYSFKIFPEKNIRGFKLPDTPQGLLGEARMLNASIVASFVELPLASIVSLHASSCGGRLQTSPAPIQTTPPKDTCSPELLMSLIQTKCADDAMTLVLKKELVAHLKCTITGLTFWDPSCEAEDRGDKFVLRSAYSSCGMQVSASMISNEAVVNILSSSSPQRKKVHCLNMDSLSFQLGLYLSPHFLQASNTIEPGQQSFVQVRVSPSVSEFLLQLDSCHLDLGPEGGTVELIQGRAAKGNCVSLLSPSPEGDPRFSFLLHFYTVPIPKTGTLSCTVALRPKTGSQDQEVHRTVFMRLNIISPDLSGCTSKGLVLPAVLGITFGAFLIGALLTAALWYIYSHTRSPSKREPVVAVAAPASSESSSTNHSIGSTQSTPCSTSSMA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
43	Phosphorylation	GPERGEVTYTTSQVS CCCCCEEEEEECCCC	15.73	23532336
88	N-linked_Glycosylation	TLQASKQNGTWPREV EEEHHHHCCCCCCEE	54.31	UniProtKB CARBOHYD
102	N-linked_Glycosylation	VLLVLSVNSSVFLHL EEEEEECCCHHHHHH	25.78	UniProtKB CARBOHYD
121	N-linked_Glycosylation	IPLHLAYNSSLVTFQ CCEEEEECCCCEEEC	21.37	UniProtKB CARBOHYD
134	N-linked_Glycosylation	FQEPPGVNTTELPSF ECCCCCCCCCCCCCC	47.39	19159218
307	N-linked_Glycosylation	LGEARMLNASIVASF HHHHHHHCHHHHHHH	23.46	UniProtKB CARBOHYD
336	O-linked_Glycosylation	SCGGRLQTSPAPIQT HCCCCCCCCCCCCCC	41.07	OGP
337	O-linked_Glycosylation	CGGRLQTSPAPIQTT CCCCCCCCCCCCCCC	13.20	OGP
343	O-linked_Glycosylation	TSPAPIQTTPPKDTC CCCCCCCCCCCCCCC	41.83	OGP
344	O-linked_Glycosylation	SPAPIQTTPPKDTCS CCCCCCCCCCCCCCC	22.63	OGP
612	Phosphorylation	LLTAALWYIYSHTRS HHHHHHHHHHHCCCC	7.28	-
614	Phosphorylation	TAALWYIYSHTRSPS HHHHHHHHHCCCCCC	4.44	-
617 (in isoform 2)	Phosphorylation	-	27.23	24719451
619	Phosphorylation	YIYSHTRSPSKREPV HHHHCCCCCCCCCCE	34.38	23403867
634	Phosphorylation	VAVAAPASSESSSTN EEEEECCCCCCCCCC	33.31	22817900
635	Phosphorylation	AVAAPASSESSSTNH EEEECCCCCCCCCCC	43.53	23403867
637	Phosphorylation	AAPASSESSSTNHSI EECCCCCCCCCCCCC	31.38	23403867
638	Phosphorylation	APASSESSSTNHSIG ECCCCCCCCCCCCCC	36.81	28857561
639	Phosphorylation	PASSESSSTNHSIGS CCCCCCCCCCCCCCC	42.37	28857561
640	Phosphorylation	ASSESSSTNHSIGST CCCCCCCCCCCCCCC	38.61	28857561
643	Phosphorylation	ESSSTNHSIGSTQST CCCCCCCCCCCCCCC	30.62	28857561
646	Phosphorylation	STNHSIGSTQSTPCS CCCCCCCCCCCCCCC	22.92	20042635
647	Phosphorylation	TNHSIGSTQSTPCST CCCCCCCCCCCCCCC	22.71	28857561
649	Phosphorylation	HSIGSTQSTPCSTSS CCCCCCCCCCCCCCC	34.11	20042635
650	Phosphorylation	SIGSTQSTPCSTSSM CCCCCCCCCCCCCCC	20.63	25159151
654	Phosphorylation	TQSTPCSTSSMA--- CCCCCCCCCCCC---	31.38	16785228

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
612	Y	Phosphorylation	Kinase	SRC	P12931	PSP
614	Y	Phosphorylation	Kinase	SRC	P12931	PSP
634	S	Phosphorylation	Kinase	TGFBR2	P37173	PSP
635	S	Phosphorylation	Kinase	TGFBR2	P37173	PSP
640	T	Phosphorylation	Kinase	ACVRL1	P37023	GPS
646	S	Phosphorylation	Kinase	ACVRL1	P37023	GPS
646	S	Phosphorylation	Kinase	TGFBR1	P36897	Uniprot
649	S	Phosphorylation	Kinase	ACVRL1	P37023	GPS
649	S	Phosphorylation	Kinase	TGFBR1	P36897	Uniprot
654	T	Phosphorylation	Kinase	ACVRL1	P37023	GPS

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TGFR1_HUMAN	TGFBR1	physical	12015308
TGFR2_HUMAN	TGFBR2	physical	12015308
TGFR1_HUMAN	TGFBR1	physical	9872992
TGFR2_HUMAN	TGFBR2	physical	9872992
ACVR1_HUMAN	ACVR1	physical	9872992
AVR2B_HUMAN	ACVR2B	physical	9872992
BMP7_HUMAN	BMP7	physical	9872992
BMP2_HUMAN	BMP2	physical	9872992
AVR2A_HUMAN	ACVR2A	physical	9872992
TGFR1_HUMAN	TGFBR1	physical	18974388
ACVL1_HUMAN	ACVRL1	physical	15702480
TGFR1_HUMAN	TGFBR1	physical	15702480
TGFR2_HUMAN	TGFBR2	physical	15702480
TGFB3_HUMAN	TGFB3	physical	1326540
TGFB1_HUMAN	TGFB1	physical	1326540
EGLN_HUMAN	ENG	physical	1537377

Drug and Disease Associations

Kegg Disease
H00533	Hereditary hemorrhagic telangiectasia (HHT)
OMIM Disease
187300	Telangiectasia, hereditary hemorrhagic, 1 (HHT1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of EGLN_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-134, AND MASSSPECTROMETRY.	19159218 [Abstract]