ERBB2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ERBB2_MOUSE
• UniProt AC: P70424
• Protein Name: Receptor tyrosine-protein kinase erbB-2
• Gene Name: Erbb2
• Organism: Mus musculus (Mouse).
• Sequence Length: 1256
• Subcellular Localization: Cell membrane; Single-pass type I membrane protein. Cytoplasm, perinuclear region. Nucleus.
• Protein Description: Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization (By similarity).; In the nucleus is involved in transcriptional regulation. Associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter and activates its transcription. Implicated in transcriptional activation of CDKN1A; the function involves STAT3 and SRC. Involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell growth (By similarity)..
• Protein Sequence: MELAAWCRWGFLLALLSPGAAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPANASLSFLQDIQEVQGYMLIAHNRVKHVPLQRLRIVRGTQLFEDKYALAVLDNRDPLDNVTTAAPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVLRKNNQLAPVDMDTNRSRACPPCAPTCKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALITYNTDTFESMLNPEGRYTFGASCVTTCPYNYLSTEVGSCTLVCPPNNQEVTAEDGTQRCEKCSKPCAGVCYGLGMEHLRGARAITSDNIQEFAGCKKIFGSLAFLPESFDGNPSSGVAPLKPEHLQVFETLEEITGYLYISAWPESFQDLSVFQNLRVIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNTHLCFVNTVPWDQLFRNPHQALLHSGNRPEEACGLEGLVCNSLCARGHCWGPGPTQCVNCSQFLRGQECVEECRVWKGLPREYVRGKHCLPCHPECQPQNSSETCYGSEADQCEACAHYKDSSSCVARCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDERGCPAEQRASPVTFIIATVVGVLLFLIIVVVIGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAVPNQAQMRILKETELRKLKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGELVDAEEYLVPQQGFFSPDPALGTGSTAHRRHRSSSARSGGGELTLGLEPSEEEPPRSPLAPSEGAGSDVFDGDLAVGVTKGLQSLSPHDLSPLQRYSEDPTLPLPPETDGYVAPLACSPQPEYVNQPEVRPQSPLTPEGPPPPIRPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLAPRAGTASQPHPSPAFSPAFDNLYYWDQNSSEQGPPPSTFEGTPTAENPEYLGLDVPV

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
68	N-linked_Glycosylation	ELTYLPANASLSFLQ EEEEECCCCCCHHHH	28.29	-
125	N-linked_Glycosylation	DNRDPLDNVTTAAPG CCCCCCCCCCCCCCC	40.49	-
188	N-linked_Glycosylation	APVDMDTNRSRACPP CCCCCCCCCCCCCCC	35.35	-
260	N-linked_Glycosylation	CLACLHFNHSGICEL CEEECCCCCCCCEEE	20.05	-
531	N-linked_Glycosylation	PGPTQCVNCSQFLRG CCCCCCCCHHHHHCC	27.61	-
572	N-linked_Glycosylation	HPECQPQNSSETCYG CCCCCCCCCCCCCCC	54.94	-
630	N-linked_Glycosylation	ICQPCPINCTHSCVD CCCCCCCCCCCCCEE	15.13	-
687	Phosphorylation	RQKIRKYTMRRLLQE HHHHHHHHHHHHHHH	13.77	19878607
702	Phosphorylation	TELVEPLTPSGAVPN HCCCCCCCCCCCCCC	26.56	27180971
704	Phosphorylation	LVEPLTPSGAVPNQA CCCCCCCCCCCCCHH	33.86	22942356
725	Ubiquitination	ETELRKLKVLGSGAF HHHHHHCEEECCCCC	38.15	-
729	Phosphorylation	RKLKVLGSGAFGTVY HHCEEECCCCCCCEE	23.84	29514104
734	Phosphorylation	LGSGAFGTVYKGIWI ECCCCCCCEEEEEEC	17.76	20469934
736	Phosphorylation	SGAFGTVYKGIWIPD CCCCCCEEEEEECCC	11.88	29514104
748	Ubiquitination	IPDGENVKIPVAIKV CCCCCCEEEEEEHHH	53.53	-
878	Phosphorylation	LDIDETEYHADGGKV CCCCCCEEECCCCCC	15.10	14647453
924	Phosphorylation	MTFGAKPYDGIPARE HHCCCCCCCCCCHHH	26.54	-
938	Ubiquitination	EIPDLLEKGERLPQP HCHHHHHCCCCCCCC	67.07	-
998	Phosphorylation	QNEDLGPSSPMDSTF ECCCCCCCCCCCCHH	45.32	25338131
999	Phosphorylation	NEDLGPSSPMDSTFY CCCCCCCCCCCCHHH	27.64	29514104
1055	Phosphorylation	HRSSSARSGGGELTL HCCCCCCCCCCEEEE	41.32	27180971
1061	Phosphorylation	RSGGGELTLGLEPSE CCCCCEEEECCCCCC	17.93	25338131
1074	Phosphorylation	SEEEPPRSPLAPSEG CCCCCCCCCCCCCCC	30.00	21743459
1079	Phosphorylation	PRSPLAPSEGAGSDV CCCCCCCCCCCCCCC	42.95	21743459
1084	Phosphorylation	APSEGAGSDVFDGDL CCCCCCCCCCCCCCE	30.02	21743459
1103	Phosphorylation	TKGLQSLSPHDLSPL CCCHHHCCHHCCCCC	25.99	24899341
1108	Phosphorylation	SLSPHDLSPLQRYSE HCCHHCCCCCHHCCC	29.62	24899341
1113	Phosphorylation	DLSPLQRYSEDPTLP CCCCCHHCCCCCCCC	11.94	19878607
1114	Phosphorylation	LSPLQRYSEDPTLPL CCCCHHCCCCCCCCC	37.40	19878607
1140	Phosphorylation	ACSPQPEYVNQPEVR CCCCCCHHCCCCCCC	16.04	-
1167	Phosphorylation	PIRPAGATLERPKTL CCCCCCCCCCCCCCC	28.38	-
1173	Phosphorylation	ATLERPKTLSPGKNG CCCCCCCCCCCCCCC	34.84	-
1175	Phosphorylation	LERPKTLSPGKNGVV CCCCCCCCCCCCCCE	36.52	29514104
1197	Phosphorylation	GAVENPEYLAPRAGT CCCCCHHHHCCCCCC	14.93	22817900
1222	Phosphorylation	SPAFDNLYYWDQNSS CCCCCCEEEECCCCC	14.57	19878607
1223	Phosphorylation	PAFDNLYYWDQNSSE CCCCCEEEECCCCCC	12.99	19878607
1249	Phosphorylation	PTAENPEYLGLDVPV CCCCCCCCCCCCCCC	13.81	19878607

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ERBB2_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ERBB2_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ERBB2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ERBIN_HUMAN	ERBB2IP	physical	11279080
CBL_MOUSE	Cbl	physical	10940298
P85A_MOUSE	Pik3r1	physical	10940298
SHC1_MOUSE	Shc1	physical	10940298

Drug and Disease Associations

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