dbPTM

EGF_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EGF_HUMAN
UniProt AC	P01133
Protein Name	Pro-epidermal growth factor
Gene Name	EGF
Organism	Homo sapiens (Human).
Sequence Length	1207
Subcellular Localization	Membrane Single-pass type I membrane protein.
Protein Description	EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. Magnesiotropic hormone that stimulates magnesium reabsorption in the renal distal convoluted tubule via engagement of EGFR and activation of the magnesium channel TRPM6. Can induce neurite outgrowth in motoneurons of the pond snail Lymnaea stagnalis in vitro. [PubMed: 10964941]
Protein Sequence	MLLTLIILLPVVSKFSFVSLSAPQHWSCPEGTLAGNGNSTCVGPAPFLIFSHGNSIFRIDTEGTNYEQLVVDAGVSVIMDFHYNEKRIYWVDLERQLLQRVFLNGSRQERVCNIEKNVSGMAINWINEEVIWSNQQEGIITVTDMKGNNSHILLSALKYPANVAVDPVERFIFWSSEVAGSLYRADLDGVGVKALLETSEKITAVSLDVLDKRLFWIQYNREGSNSLICSCDYDGGSVHISKHPTQHNLFAMSLFGDRIFYSTWKMKTIWIANKHTGKDMVRINLHSSFVPLGELKVVHPLAQPKAEDDTWEPEQKLCKLRKGNCSSTVCGQDLQSHLCMCAEGYALSRDRKYCEDVNECAFWNHGCTLGCKNTPGSYYCTCPVGFVLLPDGKRCHQLVSCPRNVSECSHDCVLTSEGPLCFCPEGSVLERDGKTCSGCSSPDNGGCSQLCVPLSPVSWECDCFPGYDLQLDEKSCAASGPQPFLLFANSQDIRHMHFDGTDYGTLLSQQMGMVYALDHDPVENKIYFAHTALKWIERANMDGSQRERLIEEGVDVPEGLAVDWIGRRFYWTDRGKSLIGRSDLNGKRSKIITKENISQPRGIAVHPMAKRLFWTDTGINPRIESSSLQGLGRLVIASSDLIWPSGITIDFLTDKLYWCDAKQSVIEMANLDGSKRRRLTQNDVGHPFAVAVFEDYVWFSDWAMPSVMRVNKRTGKDRVRLQGSMLKPSSLVVVHPLAKPGADPCLYQNGGCEHICKKRLGTAWCSCREGFMKASDGKTCLALDGHQLLAGGEVDLKNQVTPLDILSKTRVSEDNITESQHMLVAEIMVSDQDDCAPVGCSMYARCISEGEDATCQCLKGFAGDGKLCSDIDECEMGVPVCPPASSKCINTEGGYVCRCSEGYQGDGIHCLDIDECQLGEHSCGENASCTNTEGGYTCMCAGRLSEPGLICPDSTPPPHLREDDHHYSVRNSDSECPLSHDGYCLHDGVCMYIEALDKYACNCVVGYIGERCQYRDLKWWELRHAGHGQQQKVIVVAVCVVVLVMLLLLSLWGAHYYRTQKLLSKNPKNPYEESSRDVRSRRPADTEDGMSSCPQPWFVVIKEHQDLKNGGQPVAGEDGQAADGSMQPTSWRQEPQLCGMGTEQGCWIPVSSDKGSCPQVMERSFHMPSYGTQTLEGGVEKPHSLLSANPLWQQRALDPPHQMELTQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
38	N-linked_Glycosylation	GTLAGNGNSTCVGPA CCCCCCCCCCCCCCC	37.84	UniProtKB CARBOHYD
104	N-linked_Glycosylation	LLQRVFLNGSRQERV HHHHHHHCCCCCEEE	34.62	UniProtKB CARBOHYD
117	N-linked_Glycosylation	RVCNIEKNVSGMAIN EECCCCCCCCCEEEE	22.01	UniProtKB CARBOHYD
148	N-linked_Glycosylation	TVTDMKGNNSHILLS EEEECCCCCCEEEHH	41.11	UniProtKB CARBOHYD
203	Phosphorylation	LETSEKITAVSLDVL HHCCCCEEEEEHHHH	31.88	30301811
206	Phosphorylation	SEKITAVSLDVLDKR CCCEEEEEHHHHCCE	19.18	30301811
262	Phosphorylation	FGDRIFYSTWKMKTI HCCCEEEEECCEEEE	19.62	-
276	Phosphorylation	IWIANKHTGKDMVRI EEEEECCCCCCCEEE	47.76	22210691
278	Ubiquitination	IANKHTGKDMVRINL EEECCCCCCCEEEEE	43.75	-
296	Ubiquitination	FVPLGELKVVHPLAQ CCCCCCCEEEEECCC	37.60	-
324	N-linked_Glycosylation	LCKLRKGNCSSTVCG HHHHCCCCCCCCCCC	26.07	UniProtKB CARBOHYD
348	Phosphorylation	CAEGYALSRDRKYCE HHHHCHHHCCHHHCC	24.78	-
404	N-linked_Glycosylation	QLVSCPRNVSECSHD EHHCCCCCHHHCCCC	27.15	UniProtKB CARBOHYD
596	N-linked_Glycosylation	SKIITKENISQPRGI CEEEECCCCCCCCCE	40.54	UniProtKB CARBOHYD
807	Phosphorylation	VTPLDILSKTRVSED CCHHHHHHCCCCCCC	32.11	21815630
815	N-linked_Glycosylation	KTRVSEDNITESQHM CCCCCCCCCCHHHEE	38.74	UniProtKB CARBOHYD
891	Phosphorylation	ASSKCINTEGGYVCR CCCCCEECCCCEEEE	18.98	29083192
895	Phosphorylation	CINTEGGYVCRCSEG CEECCCCEEEECCCC	13.77	29083192
926	N-linked_Glycosylation	GEHSCGENASCTNTE CCCCCCCCCCCCCCC	23.57	UniProtKB CARBOHYD
954	O-linked_Glycosylation	PGLICPDSTPPPHLR CCCCCCCCCCCCCCC	28.14	UniProtKB CARBOHYD
955	O-linked_Glycosylation	GLICPDSTPPPHLRE CCCCCCCCCCCCCCC	47.39	UniProtKB CARBOHYD
1071	Phosphorylation	SKNPKNPYEESSRDV CCCCCCCCCCCCCCH	41.54	29116813
1074	Phosphorylation	PKNPYEESSRDVRSR CCCCCCCCCCCHHHC	20.80	27535140
1164	Phosphorylation	CPQVMERSFHMPSYG CCCHHHEEECCCCCC	13.24	25072903
1169	Phosphorylation	ERSFHMPSYGTQTLE HEEECCCCCCCEEEE	28.72	25072903
1170	Phosphorylation	RSFHMPSYGTQTLEG EEECCCCCCCEEEEC	20.51	22817900
1172	Phosphorylation	FHMPSYGTQTLEGGV ECCCCCCCEEEECCC	15.33	25072903
1174	Phosphorylation	MPSYGTQTLEGGVEK CCCCCCEEEECCCCC	26.98	25072903

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 EGF_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
954	S	Glycosylation	22171320
It is uncertain if Ser-954 or Thr-955 is O-glycosylated.
955	T	Glycosylation	22171320
It is uncertain if Ser-954 or Thr-955 is O-glycosylated.

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 EGF_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EGF_HUMAN	EGF	physical	11438527
EGFR_HUMAN	EGFR	physical	12093292
ERBB2_HUMAN	ERBB2	physical	12093292
ERBB3_HUMAN	ERBB3	physical	12093292
LMNA_HUMAN	LMNA	physical	16248985
PCGF2_HUMAN	PCGF2	physical	19727227

Drug and Disease Associations

Kegg Disease
H00018	Gastric cancer
H01210	Hypomagnesemia
OMIM Disease
611718	Hypomagnesemia 4 (HOMG4)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of EGF_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 SER-954 AND THR-955, STRUCTURE OF CARBOHYDRATES, ANDMASS SPECTROMETRY.	22171320 [Abstract]

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