NEDD4_RAT - dbPTM
NEDD4_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NEDD4_RAT
UniProt AC Q62940
Protein Name E3 ubiquitin-protein ligase NEDD4
Gene Name Nedd4
Organism Rattus norvegicus (Rat).
Sequence Length 887
Subcellular Localization Cytoplasm . Cell membrane
Peripheral membrane protein. Recruited to the plasma membrane by GRB10. Once complexed with GRB10 and IGF1R, follows IGF1R internalization, remaining associated with early endosomes. Uncouples from IGF1R-containing endosome
Protein Description E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Specifically ubiquitinates 'Lys-63' in target proteins (By similarity). Monoubiquitinates IGF1R at multiple sites, thus leading to receptor internalization and degradation in lysosomes. Ubiquitinates FGFR1, leading to receptor internalization and degradation in lysosomes. Promotes ubiquitination of RAPGEF2. Involved in the pathway leading to the degradation of VEGFR-2/KDFR, independently of its ubiquitin-ligase activity. Is involved in ubiquitination of ERBB4 intracellular domain E4ICD. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. Ubiquitinates TNK2 and regulates EGF-induced degradation of EGFR and TNF2 (By similarity). Involved in the ubiquitination of ebola virus VP40 protein and this ubiquitination plays a role in facilitating viral budding. Ubiquitinates BRAT1 and this ubiquitination is enhanced in the presence of NDFIP1 (By similarity)..
Protein Sequence MAADDTEAPVLSEDEVWEFCLDKNEEGGGSPGSDVTDTCEPPCGCWELNPSSLEEEHVLFTAESIISSFNNDDTRVVRVKVIAGIGLAKKDILGASDPYVRVTLYDPMSGVLTSVQTKTIKKSLNPKWNEEILFRVLPQQHRILFEVFDENRLTRDDFLGQVDVPLYPLPTENPRMERPYTFKDFVLHPRSHKSRVKGYLRLKMTYLPKNGSDDENADQAEELEPGWVVLDQPDAATHLQHPPEPSPLPPGWEERQDVLGRTYYVNHESRTTQWKRPSPEDDLTDDENGDIQLQAHGAFTTRRQISEDVDGPDNHESPENWEIVREDENTIYSGQAVQSPPSGHPDVQVRLAEELDTRLTMYGNPATSQPVTSSNHSSRGGSSQTCIFEEQPTLPVLLPTSSGLPPGWEEKQDDRGRSYYVDHNSKTTTWSKPTMQDDPRSKIPAHLRGKTPVDSNDLGPLPPGWEERTHTDGRVFFINHNIKKTQWEDPRMQNVAITGPAEPYSRDYKRKYEFFRRKLKKQTDIPNKFEMKLRRANILEDSYRRIMGVKRADFLKARLWIEFDGEKGLDYGGVAREWFFLISKEMFNPYYGLFEYSATEDNYTLQINPNSGLCNEDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLQKLITLHDMESVDSEYYSSLRWILENDPTELDLRFIIDEELFGQTHQHELKTGGSEVVVTNKNKKEYIYLVIQWRFVNRIQKQMAAFKEGFFELIPQDLIKIFDENELELLMCGLGDVDVNDWREHTKYKNGYSLNHQVIHWFWKAVLMMDSEKRIRLLQFVTGTSRVPMNGFAELYGSNGPQSFTVEQWGTPDKLPRAHTCFNRLDLPPYESFDELWDKLQMAIENTQGFDGVD
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
99PhosphorylationILGASDPYVRVTLYD
HCCCCCCEEEEEEEC
13.0926022182
105PhosphorylationPYVRVTLYDPMSGVL
CEEEEEEECCCCCCE
14.5026022182
109PhosphorylationVTLYDPMSGVLTSVQ
EEEECCCCCCEEEEE
31.0126022182
113PhosphorylationDPMSGVLTSVQTKTI
CCCCCCEEEEEEECC
25.1726022182
114PhosphorylationPMSGVLTSVQTKTIK
CCCCCEEEEEEECCH
14.2026022182
212PhosphorylationTYLPKNGSDDENADQ
EECCCCCCCCCCHHH
51.8121630457
263PhosphorylationQDVLGRTYYVNHESR
HCCCCCEEEECCCCC
12.21-
278PhosphorylationTTQWKRPSPEDDLTD
CCCCCCCCCCCCCCC
44.9823712012
284PhosphorylationPSPEDDLTDDENGDI
CCCCCCCCCCCCCCE
48.6921630457
306PhosphorylationFTTRRQISEDVDGPD
EECCCCCCCCCCCCC
21.2927097102
317PhosphorylationDGPDNHESPENWEIV
CCCCCCCCCCCCEEE
29.9327097102
339PhosphorylationYSGQAVQSPPSGHPD
ECCEECCCCCCCCCC
31.9830240740
362PhosphorylationLDTRLTMYGNPATSQ
HCCCEEECCCCCCCC
14.44-
377PhosphorylationPVTSSNHSSRGGSSQ
CCCCCCCCCCCCCCC
26.44-
382PhosphorylationNHSSRGGSSQTCIFE
CCCCCCCCCCEEEEC
23.3023984901
383PhosphorylationHSSRGGSSQTCIFEE
CCCCCCCCCEEEECC
32.5523984901
385PhosphorylationSRGGSSQTCIFEEQP
CCCCCCCEEEECCCC
14.9825575281
393PhosphorylationCIFEEQPTLPVLLPT
EEECCCCCCCEEEEC
43.3125575281
543PhosphorylationANILEDSYRRIMGVK
HHHCHHHHHHHHCCC
19.07-
571PhosphorylationDGEKGLDYGGVAREW
CCCCCCCCCCHHHHH
22.33-

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 NEDD4_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NEDD4_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 NEDD4_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KCNQ2_RATKcnq2physical
17322297
FOXJ2_HUMANFOXJ2physical
19953087
PLS3_HUMANPLSCR3physical
19953087
WBP2_HUMANWBP2physical
19953087
ABL1_HUMANABL1physical
19953087
FGF12_HUMANFGF12physical
19953087
FKBP3_HUMANFKBP3physical
19953087
ANXA9_HUMANANXA9physical
19953087
IF5_HUMANEIF5physical
19953087
MAPK5_HUMANMAPKAPK5physical
19953087
TYY1_HUMANYY1physical
19953087
MTAP2_HUMANMAP2physical
19953087
M3K20_HUMANZAKphysical
19953087
S23A2_HUMANSLC23A2physical
19953087
BEAN1_HUMANBEAN1physical
19953087
AKT3_HUMANAKT3physical
19953087
AQP9_HUMANAQP9physical
19953087
MAPK3_HUMANMAPKAPK3physical
19953087
VGFR1_HUMANFLT1physical
19953087
BRAF_HUMANBRAFphysical
19953087
TIM10_HUMANTIMM10physical
19953087
HEP2_HUMANSERPIND1physical
19953087
CUED1_HUMANCUEDC1physical
19953087
KCC1D_HUMANCAMK1Dphysical
19953087
SGK2_HUMANSGK2physical
19953087
M3K3_HUMANMAP3K3physical
19953087
TEC_HUMANTECphysical
19953087
CDK5_HUMANCDK5physical
19953087
AKT1_HUMANAKT1physical
19953087
PGFRA_HUMANPDGFRAphysical
19953087
M3K8_HUMANMAP3K8physical
19953087
TRPT1_HUMANTRPT1physical
19953087
BLK_HUMANBLKphysical
19953087
KPCD_HUMANPRKCDphysical
19953087
FYN_HUMANFYNphysical
19953087
MP2K1_HUMANMAP2K1physical
19953087
BMR1B_HUMANBMPR1Bphysical
19953087
KTU_HUMANDNAAF2physical
19953087
MK12_HUMANMAPK12physical
19953087
RGS3_HUMANRGS3physical
19953087
KLC4_HUMANKLC4physical
19953087
NTRK2_HUMANNTRK2physical
19953087
BTK_HUMANBTKphysical
19953087
EGFR_HUMANEGFRphysical
19953087
RPC4_HUMANPOLR3Dphysical
19953087
CSK21_HUMANCSNK2A1physical
19953087
STK16_HUMANSTK16physical
19953087
ARBK1_HUMANADRBK1physical
19953087
DDX54_HUMANDDX54physical
19953087
TRI41_HUMANTRIM41physical
19953087
HMCES_HUMANHMCESphysical
19953087
TAF1B_HUMANTAF1Bphysical
19953087
FGF21_HUMANFGF21physical
19953087
STAC_HUMANSTACphysical
19953087
H10_HUMANH1F0physical
19953087
ADAP2_HUMANADAP2physical
19953087
UBC12_HUMANUBE2Mphysical
19953087
TMG1_HUMANPRRG1physical
19953087
KCAB2_HUMANKCNAB2physical
19953087
BMR1A_HUMANBMPR1Aphysical
19953087
PPID_HUMANPPIDphysical
19953087
RBX2_HUMANRNF7physical
19953087
NHP2_HUMANNHP2physical
19953087
SIVA_HUMANSIVA1physical
19953087
RSLBB_HUMANRASL11Bphysical
19953087
TIRR_HUMANNUDT16L1physical
19953087
CG050_HUMANC7orf50physical
19953087
TCAL2_HUMANTCEAL2physical
19953087
MOB3A_HUMANMOB3Aphysical
19953087
TCP1L_HUMANTCP10Lphysical
19953087
CU077_HUMANTCP10Lphysical
19953087
DIRA1_HUMANDIRAS1physical
19953087
TEANC_HUMANTCEANCphysical
19953087
KCAB1_HUMANKCNAB1physical
19953087
PTGR3_HUMANZADH2physical
19953087
PPARD_HUMANPPARDphysical
19953087
RNF37_HUMANUBOX5physical
19953087
1433F_RATYwhahphysical
15677482
1433B_RATYwhabphysical
15677482
1433G_RATYwhagphysical
15677482
1433E_RATYwhaephysical
15677482
1433T_RATYwhaqphysical
15677482
SCNNG_RATScnn1gphysical
11805112
SCNNA_RATScnn1aphysical
8665844
SCNNB_RATScnn1bphysical
9923703
SCNNB_RATScnn1bphysical
12654927
CXA1_RATGja1physical
26841867

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NEDD4_RAT

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Related Literatures of Post-Translational Modification

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