ERBB3_RAT - dbPTM
ERBB3_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ERBB3_RAT
UniProt AC Q62799
Protein Name Receptor tyrosine-protein kinase erbB-3
Gene Name Erbb3
Organism Rattus norvegicus (Rat).
Sequence Length 1339
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Tyrosine-protein kinase that plays an essential role as cell surface receptor for neuregulins. Binds to neuregulin-1 (NRG1) and is activated by it; ligand-binding increases phosphorylation on tyrosine residues and promotes its association with the p85 subunit of phosphatidylinositol 3-kinase. May also be activated by CSPG5..
Protein Sequence MRATGTLQVLCFLLSLARGSEMGNSQAVCPGTLNGLSVTGDADNQYQTLYKLYEKCEVVMGNLEIVLTGHNADLSFLQWIREVTGYVLVAMNEFSVLPLPNLRVVRGTQVYDGKFAIFVMLNYNTNSSHALRQLKFTQLTEILSGGVYIEKNDKLCHMDTIDWRDIVRVRGAEIVVKNNGANCPPCHEVCKGRCWGPGPDDCQILTKTICAPQCNGRCFGPNPNQCCHDECAGGCSGPQDTDCFACRRFNDSGACVPRCPEPLVYNKLTFQLEPNPHTKYQYGGVCVASCPHNFVVDQTFCVRACPPDKMEVDKHGLKMCEPCGGLCPKACEGTGSGSRYQTVDSSNIDGFVNCTKILGNLDFLITGLNVDPWHKIPALDPEKLNVFRTVREITGYLNIQSWPPHMHNFSVFSNLTTIGGRSLYNRGFSLLIMKNLNVTSLGFRSLKEISAGRVYISANQQLCYHHSLNWTRLLRGPSEERLDIKYDRPLGECLAEGKVCDPLCSSGGCWGPGPGQCLSCRNYSREGVCVTHCNFLQGEPREFVHEAQCFSCHPECLPMEGTSTCNGSGSDACARCAHFRDGPHCVNSCPHGILGAKGPIYKYPDAQNECRPCHENCTQGCNGPELQDCLGQAEVLMSKPHLVIAVTVGLAVILMILGGSFLYWRGRRIQNKRAMRRYLERGESIEPLDPSEKANKVLARIFKETELRKLKVLGSGVFGTVHKGIWIPEGESIKIPVCIKVIEDKSGRQSFQAVTDHMLAVGSLDHAHIVRLLGLCPGSSLQLVTQYLPLGSLLDHVKQHRETLGPQLLLNWGVQIAKGMYYLEEHSMVHRDLALRNVMLKSPSQVQVADFGVADLLPPDDKQLLHSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWELMTFGAEPYAGLRLAEIPDLLEKGERLAQPQICTIDVYMVMVKCWMIDENIRPTFKELANEFTRMARDPPRYLVIKRASGPGTPPAAEPSVLTTKELQEAELEPELDLDLDLEAEEEGLATSLGSALSLPTGTLTRPRGSQSLLSPSSGYMPMNQSSLGEACLDSAVLGGREQFSRPISLHPIPRGRPASESSEGHVTGSEAELQEKVSVCRSRSRSRSPRPRGDSAYHSQRHSLLTPVTPLSPPGLEEEDGNGYVMPDTHLRGASSSREGTLSSVGLSSVLGTEEEDEDEEYEYMNRKRRGSPPRPPRPGSLEELGYEYMDVGSDLSASLGSTQSCPLHPMAIVPSAGTTPDEDYEYMNRRRGAGGAGGDYAAMGACPAAEQGYEEMRAFQGPGHHAPHVRYARLKTLRSLEATDSAFDNPDYWHSRLFPKANAQRT
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 Orthologous
Protein Cluster
126N-linked_GlycosylationVMLNYNTNSSHALRQ
EEEECCCCCHHHHHH
37.57-
250N-linked_GlycosylationCFACRRFNDSGACVP
CEECCCCCCCCCCCC
40.50-
353N-linked_GlycosylationSNIDGFVNCTKILGN
CCCCCEEEHHHHHCC
26.02-
408N-linked_GlycosylationSWPPHMHNFSVFSNL
CCCCCCCCEECEECC
24.26-
414N-linked_GlycosylationHNFSVFSNLTTIGGR
CCEECEECCEEECCH
29.91-
437N-linked_GlycosylationLLIMKNLNVTSLGFR
EEEEECCCCCEECCC
44.40-
469N-linked_GlycosylationLCYHHSLNWTRLLRG
EEEECCCCHHHHCCC
40.88-
522N-linked_GlycosylationGQCLSCRNYSREGVC
CCCCCCCCCCCCCEE
43.38-
566N-linked_GlycosylationMEGTSTCNGSGSDAC
CCCCCCCCCCCCCHH
47.99-
616N-linked_GlycosylationECRPCHENCTQGCNG
CCCCCCCCCCCCCCC
15.52-
678PhosphorylationNKRAMRRYLERGESI
CHHHHHHHHHCCCCC
11.5323984901
684PhosphorylationRYLERGESIEPLDPS
HHHHCCCCCCCCCHH
34.7729779826
691PhosphorylationSIEPLDPSEKANKVL
CCCCCCHHHHHHHHH
51.9323984901
693UbiquitinationEPLDPSEKANKVLAR
CCCCHHHHHHHHHHH
62.69-
871PhosphorylationLLHSEAKTPIKWMAL
HCCCCCCCCCCEEEE
36.9822817900
924UbiquitinationEIPDLLEKGERLAQP
HCHHHHHHCCHHCCC
67.07-
980PhosphorylationYLVIKRASGPGTPPA
EEEEEECCCCCCCCC
49.9429779826
984PhosphorylationKRASGPGTPPAAEPS
EECCCCCCCCCCCCC
29.2727097102
991PhosphorylationTPPAAEPSVLTTKEL
CCCCCCCCCCCHHHH
22.6728689409
994PhosphorylationAAEPSVLTTKELQEA
CCCCCCCCHHHHHHC
33.4028689409
1051PhosphorylationLLSPSSGYMPMNQSS
CCCCCCCCCCCCHHH
10.4511546794
1080PhosphorylationEQFSRPISLHPIPRG
HHCCCCCCCCCCCCC
24.2528689409
1091PhosphorylationIPRGRPASESSEGHV
CCCCCCCCCCCCCCC
40.4722673903
1093PhosphorylationRGRPASESSEGHVTG
CCCCCCCCCCCCCCC
31.0622673903
1094PhosphorylationGRPASESSEGHVTGS
CCCCCCCCCCCCCCC
43.4722673903
1099PhosphorylationESSEGHVTGSEAELQ
CCCCCCCCCCHHHHH
29.3422673903
1101PhosphorylationSEGHVTGSEAELQEK
CCCCCCCCHHHHHHH
25.0328689409
1120PhosphorylationRSRSRSRSPRPRGDS
CCCCCCCCCCCCCCC
26.8922817900
1173PhosphorylationASSSREGTLSSVGLS
CCCCCCCCCCHHCHH
20.7927097102
1175PhosphorylationSSREGTLSSVGLSSV
CCCCCCCCHHCHHHC
23.8627097102
1176PhosphorylationSREGTLSSVGLSSVL
CCCCCCCHHCHHHCC
24.2627097102
1180PhosphorylationTLSSVGLSSVLGTEE
CCCHHCHHHCCCCCC
16.6927097102
1181PhosphorylationLSSVGLSSVLGTEEE
CCHHCHHHCCCCCCC
26.8027097102
1185PhosphorylationGLSSVLGTEEEDEDE
CHHHCCCCCCCCCHH
35.7427097102
1194PhosphorylationEEDEDEEYEYMNRKR
CCCCHHHHHHHHHHC
15.4311546794
1219PhosphorylationGSLEELGYEYMDVGS
CCHHHHCCEEEECCC
19.2611546794
1257PhosphorylationGTTPDEDYEYMNRRR
CCCCHHHHHHHHHCC
13.6011546794
1273PhosphorylationAGGAGGDYAAMGACP
CCCCCCCCHHHCCCC
10.2711546794
1286PhosphorylationCPAAEQGYEEMRAFQ
CCHHHHHHHHHHHHC
14.3811546794
1312PhosphorylationARLKTLRSLEATDSA
HHHHHHHHHHCCCCC
33.4022108457
1325PhosphorylationSAFDNPDYWHSRLFP
CCCCCCCHHHHHHCC
13.2830181290
1328PhosphorylationDNPDYWHSRLFPKAN
CCCCHHHHHHCCHHH
19.2830181290

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
871TPhosphorylationKinaseCDK5Q03114
PSP
1120SPhosphorylationKinaseCDK5Q03114
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ERBB3_RAT !!

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 ERBB3_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RL13A_HUMANRPL13Aphysical
10095121
L1CAM_RATL1camphysical
22815787

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ERBB3_RAT

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Related Literatures of Post-Translational Modification

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