dbPTM

HBEGF_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HBEGF_HUMAN
UniProt AC	Q99075
Protein Name	Proheparin-binding EGF-like growth factor
Gene Name	HBEGF
Organism	Homo sapiens (Human).
Sequence Length	208
Subcellular Localization	Heparin-binding EGF-like growth factor: Secreted, extracellular space. Mature HB-EGF is released into the extracellular space and probably binds to a receptor. Proheparin-binding EGF-like growth factor: Cell membrane Single-pass type I membrane pro
Protein Description	Growth factor that mediates its effects via EGFR, ERBB2 and ERBB4. Required for normal cardiac valve formation and normal heart function. Promotes smooth muscle cell proliferation. May be involved in macrophage-mediated cellular proliferation. It is mitogenic for fibroblasts, but not endothelial cells. It is able to bind EGF receptor/EGFR with higher affinity than EGF itself and is a far more potent mitogen for smooth muscle cells than EGF. Also acts as a diphtheria toxin receptor..
Protein Sequence	MKLLPSVVLKLFLAAVLSALVTGESLERLRRGLAAGTSNPDPPTVSTDQLLPLGGGRDRKVRDLQEADLDLLRVTLSSKPQALATPNKEEHGKRKKKGKGLGKKRDPCLRKYKDFCIHGECKYVKELRAPSCICHPGYHGERCHGLSLPVENRLYTYDHTTILAVVAVVLSSVCLLVIVGLLMFRYHRRGGYDVENEEKVKLGMTNSH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MKLLPSVVLKLFL --CCCHHHHHHHHHH	25.48	23909892
37	O-linked_Glycosylation	RRGLAAGTSNPDPPT HHHHHCCCCCCCCCC	22.17	23234360
37	Phosphorylation	RRGLAAGTSNPDPPT HHHHHCCCCCCCCCC	22.17	22468782
38	O-linked_Glycosylation	RGLAAGTSNPDPPTV HHHHCCCCCCCCCCC	45.51	23234360
38	Phosphorylation	RGLAAGTSNPDPPTV HHHHCCCCCCCCCCC	45.51	22468782
44	O-linked_Glycosylation	TSNPDPPTVSTDQLL CCCCCCCCCCHHHCE	32.26	22171320
44	Phosphorylation	TSNPDPPTVSTDQLL CCCCCCCCCCHHHCE	32.26	-
46	O-linked_Glycosylation	NPDPPTVSTDQLLPL CCCCCCCCHHHCEEC	28.83	OGP
47	Phosphorylation	PDPPTVSTDQLLPLG CCCCCCCHHHCEECC	24.35	22468782
47	O-linked_Glycosylation	PDPPTVSTDQLLPLG CCCCCCCHHHCEECC	24.35	22171320
75	O-linked_Glycosylation	DLDLLRVTLSSKPQA CCHHHHHHCCCCCCC	17.94	UniProtKB CARBOHYD
75	O-linked_Glycosylation	DLDLLRVTLSSKPQA CCHHHHHHCCCCCCC	17.94	1556128
77	O-linked_Glycosylation	DLLRVTLSSKPQALA HHHHHHCCCCCCCCC	27.27	55828397
78	O-linked_Glycosylation	LLRVTLSSKPQALAT HHHHHCCCCCCCCCC	52.01	55828403
85	O-linked_Glycosylation	SKPQALATPNKEEHG CCCCCCCCCCHHHHC	28.39	55828409
85	O-linked_Glycosylation	SKPQALATPNKEEHG CCCCCCCCCCHHHHC	28.39	1556128
95	Acetylation	KEEHGKRKKKGKGLG HHHHCCCCCCCCCCC	63.42	88663
96	Acetylation	EEHGKRKKKGKGLGK HHHCCCCCCCCCCCC	71.44	70655
97	Acetylation	EHGKRKKKGKGLGKK HHCCCCCCCCCCCCC	69.74	61159
99	Acetylation	GKRKKKGKGLGKKRD CCCCCCCCCCCCCCC	60.90	70651
103	Acetylation	KKGKGLGKKRDPCLR CCCCCCCCCCCHHHH	50.07	70643
104	Acetylation	KGKGLGKKRDPCLRK CCCCCCCCCCHHHHH	61.30	70647
199	Ubiquitination	YDVENEEKVKLGMTN CCCCCHHHEECCCCC	38.19	29901268
207	Phosphorylation	VKLGMTNSH------ EECCCCCCC------	22.77	16557002

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 HBEGF_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
44	T	Glycosylation	22171320
Thr-47 is a minor glycosylation site compared to Thr-44.
47	T	Glycosylation	22171320
Thr-47 is a minor glycosylation site compared to Thr-44.

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 HBEGF_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ZBT16_HUMAN	ZBTB16	physical	14597771
ZBT16_HUMAN	ZBTB16	physical	15219838
EGFR_HUMAN	EGFR	physical	12725245
BAG1_HUMAN	BAG1	physical	11340068
BCL6_HUMAN	BCL6	physical	19337254
BCL6_HUMAN	BCL6	physical	17392284

Drug and Disease Associations

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

Regulatory Network of HBEGF_HUMAN

Related Literatures of Post-Translational Modification

O-linked Glycosylation
Reference	PubMed
"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD."; Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.; Mol. Cell. Proteomics 0:0-0(2011). Cited for: GLYCOSYLATION AT THR-44 AND THR-47, STRUCTURE OF CARBOHYDRATES, ANDMASS SPECTROMETRY.	22171320 [Abstract]
"Structure of heparin-binding EGF-like growth factor. Multiple forms,primary structure, and glycosylation of the mature protein."; Higashiyama S., Lau K., Besner G.E., Abraham J.A., Klagsbrun M.; J. Biol. Chem. 267:6205-6212(1992). Cited for: PROTEIN SEQUENCE OF 63-141 AND 143-148, AND GLYCOSYLATION AT THR-75AND THR-85.	1556128 [Abstract]

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