| Id: | acc4057 |
| Group: | 1sens |
| Protein: | ErbB2 |
| Gene Symbol: | Erbb2 |
| Protein Id: | P06494 |
| Protein Name: | ERBB2_RAT |
| PTM: | phosphorylation |
| Site: | Tyr877 |
| Site Sequence: | LARLLDIDETEYHADGGKVPI |
| Disease Category: | Endocrine and metabolic diseases |
| Disease: | Diabetes Mellitus |
| Disease Subtype: | ischemia-reperfusion injury |
| Disease Cellline: | |
| Disease Info: | |
| Drug: | EGF |
| Drug Info: | "EGF stands for Epidermal Growth Factor, which is a protein that stimulates cell growth and differentiation." |
| Effect: | modulate |
| Effect Info: | "EGF treatment can reverse the inhibition of ERK1/2, p38 MAPK, and AKT signaling pathways caused by diabetes and ischemia, that is, activate the pathways and increase the phosphorylation level." |
| Note: | |
| Score: | 4.0 |
| Pubmed(PMID): | 22720029 |
| Sentence Index: | 22720029_7 |
| Sentence: | Losartan treatment improved cardiac function in diabetes but also impaired EGFR phosphorylation in diabetic heart. |
Sequence & Structure:
MELAAWCRWGFLLALLPPGIAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYVPANASLSFLQDIQEVQGYMLIAHNQVKRVPLQRLRIVRGTQLFEDKYALAVLDNRDPQDNVAASTPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVFRKNNQLAPVDIDTNRSRACPPCAPACKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMHNPEGRYTFGASCVTTCPYNYLSTEVGSCTLVCPPNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLRGARAITSDNVQEFDGCKKIFGSLAFLPESFDGDPSSGIAPLRPEQLQVFETLEEITGYLYISAWPDSLRDLSVFQNLRIIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNAHLCFVHTVPWDQLFRNPHQALLHSGNRPEEDLCVSSGLVCNSLCAHGHCWGPGPTQCVNCSHFLRGQECVEECRVWKGLPREYVSDKRCLPCHPECQPQNSSETCFGSEADQCAACAHYKDSSSCVARCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDERGCPAEQRASPVTFIIATVVGVLLFLILVVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFSPDPTPGTGSTAHRRHRSSSTRSGGGELTLGLEPSEEGPPRSPLAPSEGAGSDVFDGDLAMGVTKGLQSLSPHDLSPLQRYSEDPTLPLPPETDGYVAPLACSPQPEYVNQSEVQPQPPLTPEGPLPPVRPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLVPREGTASPPHPSPAFSPAFDNLYYWDQNSSEQGPPPSNFEGTPTAENPEYLGLDVPV
Select PDB:
No data.
Protein Tractability:
source: Open TargetsNo data.
PTM Intensity:
source: CPTACNo data.
PTM-Disease Association:
source: PTMD| Residue | Position | State | Disease | Class | PMID |
|---|---|---|---|---|---|
| Y | 1253 | U | Breast cancer | Phosphorylation | 9461599 |
State Note: Based on the distinct PTM states in diseases, PTMD classified all disease-associated PTMs into six classes, including whether the up-regulation (U) or down-regulation (D) of PTM levels, the absence (A) or presence (P) of PTMs, and the creation (C) or disruption (N) of PTM sites are associated with diseases.
PTM-Drug Perturbation Response:
source: DecryptMNo data.
Function score:
source: funscoRNo data.
