WWP1_HUMAN - dbPTM
WWP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WWP1_HUMAN
UniProt AC Q9H0M0
Protein Name NEDD4-like E3 ubiquitin-protein ligase WWP1
Gene Name WWP1
Organism Homo sapiens (Human).
Sequence Length 922
Subcellular Localization Cytoplasm. Cell membrane
Peripheral membrane protein. Nucleus.
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. Ubiquitinates ERBB4 isoforms JM-A CYT-1 and JM-B CYT-1, KLF2, KLF5 and TP63 and promotes their proteasomal degradation. Ubiquitinates RNF11 without targeting it for degradation. Ubiquitinates and promotes degradation of TGFBR1; the ubiquitination is enhanced by SMAD7. Ubiquitinates SMAD6 and SMAD7. Ubiquitinates and promotes degradation of SMAD2 in response to TGF-beta signaling, which requires interaction with TGIF..
Protein Sequence MATASPRSDTSNNHSGRLQLQVTVSSAKLKRKKNWFGTAIYTEVVVDGEITKTAKSSSSSNPKWDEQLTVNVTPQTTLEFQVWSHRTLKADALLGKATIDLKQALLIHNRKLERVKEQLKLSLENKNGIAQTGELTVVLDGLVIEQENITNCSSSPTIEIQENGDALHENGEPSARTTARLAVEGTNGIDNHVPTSTLVQNSCCSYVVNGDNTPSSPSQVAARPKNTPAPKPLASEPADDTVNGESSSFAPTDNASVTGTPVVSEENALSPNCTSTTVEDPPVQEILTSSENNECIPSTSAELESEARSILEPDTSNSRSSSAFEAAKSRQPDGCMDPVRQQSGNANTETLPSGWEQRKDPHGRTYYVDHNTRTTTWERPQPLPPGWERRVDDRRRVYYVDHNTRTTTWQRPTMESVRNFEQWQSQRNQLQGAMQQFNQRYLYSASMLAAENDPYGPLPPGWEKRVDSTDRVYFVNHNTKTTQWEDPRTQGLQNEEPLPEGWEIRYTREGVRYFVDHNTRTTTFKDPRNGKSSVTKGGPQIAYERGFRWKLAHFRYLCQSNALPSHVKINVSRQTLFEDSFQQIMALKPYDLRRRLYVIFRGEEGLDYGGLAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASTINPDHLSYFCFIGRFIAMALFHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFSVDMEILGKVTSHDLKLGGSNILVTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQEVDLADWQRNTVYRHYTRNSKQIIWFWQFVKETDNEVRMRLLQFVTGTCRLPLGGFAELMGSNGPQKFCIEKVGKDTWLPRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFGQE
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
3Phosphorylation-----MATASPRSDT
-----CCCCCCCCCC		26.77-
23PhosphorylationGRLQLQVTVSSAKLK
CEEEEEEEECHHHHH		11.1726657352
25PhosphorylationLQLQVTVSSAKLKRK
EEEEEEECHHHHHCC		18.4025849741
26PhosphorylationQLQVTVSSAKLKRKK
EEEEEECHHHHHCCC		25.7027050516
53PhosphorylationVDGEITKTAKSSSSS
ECCEEEEECCCCCCC		30.5726657352
56PhosphorylationEITKTAKSSSSSNPK
EEEEECCCCCCCCCC		32.7526657352
59PhosphorylationKTAKSSSSSNPKWDE
EECCCCCCCCCCCCC		35.7618510355
60PhosphorylationTAKSSSSSNPKWDEQ
ECCCCCCCCCCCCCC		60.1326657352
89UbiquitinationVWSHRTLKADALLGK
EEECCCHHHHHHHCC		43.5429901268
96UbiquitinationKADALLGKATIDLKQ
HHHHHHCCCEECHHH		42.1829967540
110 (in isoform 6)Ubiquitination-30.6721890473
120UbiquitinationERVKEQLKLSLENKN
HHHHHHHHHHHCCCC		35.4129967540
122PhosphorylationVKEQLKLSLENKNGI
HHHHHHHHHCCCCCE		31.8624702127
149UbiquitinationLVIEQENITNCSSSP
EEEEEECCCCCCCCC		2.6323000965
198 (in isoform 3)Ubiquitination-3.6021890473
213PhosphorylationYVVNGDNTPSSPSQV
EEECCCCCCCCHHHH		29.3223898821
215PhosphorylationVNGDNTPSSPSQVAA
ECCCCCCCCHHHHCC		53.4923898821
216PhosphorylationNGDNTPSSPSQVAAR
CCCCCCCCHHHHCCC		29.7628348404
260PhosphorylationDNASVTGTPVVSEEN
CCCCCCCCCEECCCC		11.9822468782
285UbiquitinationVEDPPVQEILTSSEN
CCCCCHHHHHCCCCC		39.9521890473
309PhosphorylationELESEARSILEPDTS
HHHHHHHHHCCCCCC		38.2828674419
315PhosphorylationRSILEPDTSNSRSSS
HHHCCCCCCCCCCCH		40.2928555341
316PhosphorylationSILEPDTSNSRSSSA
HHCCCCCCCCCCCHH		39.9428555341
318PhosphorylationLEPDTSNSRSSSAFE
CCCCCCCCCCCHHHH		33.0527251275
320PhosphorylationPDTSNSRSSSAFEAA
CCCCCCCCCHHHHHH		28.5927251275
321PhosphorylationDTSNSRSSSAFEAAK
CCCCCCCCHHHHHHH		25.2827251275
322PhosphorylationTSNSRSSSAFEAAKS
CCCCCCCHHHHHHHH		37.9227251275
327UbiquitinationSSSAFEAAKSRQPDG
CCHHHHHHHHCCCCC		11.8023000965
328UbiquitinationSSAFEAAKSRQPDGC
CHHHHHHHHCCCCCC		53.9023000965
328 (in isoform 1)Ubiquitination-53.9021890473
343PhosphorylationMDPVRQQSGNANTET
CCHHHCCCCCCCCCC		26.1925072903
348PhosphorylationQQSGNANTETLPSGW
CCCCCCCCCCCCCCC		28.1225072903
350PhosphorylationSGNANTETLPSGWEQ
CCCCCCCCCCCCCHH		41.7625072903
352UbiquitinationNANTETLPSGWEQRK
CCCCCCCCCCCHHCC		37.9123000965
353PhosphorylationANTETLPSGWEQRKD
CCCCCCCCCCHHCCC		60.7025072903
357UbiquitinationTLPSGWEQRKDPHGR
CCCCCCHHCCCCCCC		51.7423000965
365PhosphorylationRKDPHGRTYYVDHNT
CCCCCCCEEEEECCC		24.64-
366PhosphorylationKDPHGRTYYVDHNTR
CCCCCCEEEEECCCC		10.5127642862
367PhosphorylationDPHGRTYYVDHNTRT
CCCCCEEEEECCCCE		9.9727642862
375PhosphorylationVDHNTRTTTWERPQP
EECCCCEECCCCCCC		26.9928348404
376PhosphorylationDHNTRTTTWERPQPL
ECCCCEECCCCCCCC		25.3928348404
463UbiquitinationGPLPPGWEKRVDSTD
CCCCCCHHHCCCCCC		36.5821890473
464UbiquitinationPLPPGWEKRVDSTDR
CCCCCHHHCCCCCCE		51.7321890473
468PhosphorylationGWEKRVDSTDRVYFV
CHHHCCCCCCEEEEE		29.3828674151
469PhosphorylationWEKRVDSTDRVYFVN
HHHCCCCCCEEEEEE		24.3028674151
481UbiquitinationFVNHNTKTTQWEDPR
EEECCCCCCCCCCCC		23.3721890473
486UbiquitinationTKTTQWEDPRTQGLQ
CCCCCCCCCCCCCCC		34.7122817900
505UbiquitinationLPEGWEIRYTREGVR
CCCCEEEEEEECCEE		18.4321890473
510UbiquitinationEIRYTREGVRYFVDH
EEEEEECCEEEEEEC		13.1022817900
519PhosphorylationRYFVDHNTRTTTFKD
EEEEECCCCEEEEEC		26.4420068231
521PhosphorylationFVDHNTRTTTFKDPR
EEECCCCEEEEECCC		28.3126657352
523PhosphorylationDHNTRTTTFKDPRNG
ECCCCEEEEECCCCC		28.2426657352
530UbiquitinationTFKDPRNGKSSVTKG
EEECCCCCCCCCCCC		32.2823000965
531UbiquitinationFKDPRNGKSSVTKGG
EECCCCCCCCCCCCC		43.0123000965
535UbiquitinationRNGKSSVTKGGPQIA
CCCCCCCCCCCCCEE		26.3923000965
536UbiquitinationNGKSSVTKGGPQIAY
CCCCCCCCCCCCEEH		60.7723000965
543PhosphorylationKGGPQIAYERGFRWK
CCCCCEEHHCCCCCC		14.05-
572PhosphorylationSHVKINVSRQTLFED
CCEEEECCCCHHHHH		17.7420873877
575PhosphorylationKINVSRQTLFEDSFQ
EEECCCCHHHHHHHH		32.1020873877
580PhosphorylationRQTLFEDSFQQIMAL
CCHHHHHHHHHHHCC		20.1120068231
597PhosphorylationYDLRRRLYVIFRGEE
HHCCCCEEEEEECCC		6.9530108239
639PhosphorylationEYAGKNNYCLQINPA
EECCCCCEEEEECCC		12.16-
660UbiquitinationHLSYFCFIGRFIAMA
HHHHHHHHHHHHHHH		3.9921890473
665UbiquitinationCFIGRFIAMALFHGK
HHHHHHHHHHHHCCC		3.7222817900
682 (in isoform 6)Ubiquitination-15.8521890473
683UbiquitinationTGFSLPFYKRMLSKK
CCCCHHHHHHHHCCC		8.8521890473
684UbiquitinationGFSLPFYKRMLSKKL
CCCHHHHHHHHCCCC		31.5421890473
688UbiquitinationPFYKRMLSKKLTIKD
HHHHHHHCCCCCHHH		20.5722817900
689UbiquitinationFYKRMLSKKLTIKDL
HHHHHHCCCCCHHHH		48.0922817900
692PhosphorylationRMLSKKLTIKDLESI
HHHCCCCCHHHHHHC		34.5624719451
697UbiquitinationKLTIKDLESIDTEFY
CCCHHHHHHCCHHHH		56.6421890473
721UbiquitinationNIEECGLEMYFSVDM
CCCCCCCEEEEEECH		19.6821890473
770 (in isoform 3)Ubiquitination-39.6521890473
822PhosphorylationNTVYRHYTRNSKQII
CCHHHHHCCCCHHEE		19.7617081983
876UbiquitinationGPQKFCIEKVGKDTW
CCCEEEEEECCCCCC		42.7621890473
877UbiquitinationPQKFCIEKVGKDTWL
CCEEEEEECCCCCCC		36.05-
899UbiquitinationNRLDLPPYKSYEQLK
CCCCCCCCCCHHHHH		15.6121890473
900UbiquitinationRLDLPPYKSYEQLKE
CCCCCCCCCHHHHHH		52.9522817900
900UbiquitinationRLDLPPYKSYEQLKE
CCCCCCCCCHHHHHH		52.9521890473
900 (in isoform 1)Ubiquitination-52.9521890473
906UbiquitinationYKSYEQLKEKLLFAI
CCCHHHHHHHHHHHH		53.1229901268
908UbiquitinationSYEQLKEKLLFAIEE
CHHHHHHHHHHHHHH		49.2329901268
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
-KUbiquitinationE3 ubiquitin ligaseWWP1Q9H0M0
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WWP1_HUMAN !!
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 WWP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZN638_HUMANZNF638physical
16189514
DIDO1_HUMANDIDO1physical
16189514
KLF2_HUMANKLF2physical
11375995
RTN4_HUMANRTN4physical
19035836
KLF5_HUMANKLF5physical
16223724
SKIL_HUMANSKILphysical
15221015
ERBB4_HUMANERBB4physical
19561640
ESR2_HUMANESR2physical
21487105
KLF5_HUMANKLF5physical
21487105
RNF11_HUMANRNF11physical
18724389
PSPC_HUMANSFTPCphysical
19366705
P63_HUMANTP63physical
20951678
KLF5_HUMANKLF5physical
20694673
RUNX2_HUMANRUNX2physical
16728642
SPART_HUMANSPG20physical
19307600
SMAD7_HUMANSMAD7physical
15359284
SMAD2_HUMANSMAD2physical
15359284
SMAD3_HUMANSMAD3physical
15359284
SMAD4_HUMANSMAD4physical
15359284
SMAD6_HUMANSMAD6physical
15359284
SMAD1_HUMANSMAD1physical
15359284
ERBB4_HUMANERBB4physical
19047365
P63_HUMANTP63physical
18806757
UB2L3_HUMANUBE2L3physical
20951678
AAPK2_HUMANPRKAA2physical
23293026
FXL15_HUMANFBXL15physical
21572392
NOTC1_HUMANNOTCH1physical
16785210
WWP1_HUMANWWP1physical
17996703
UB2L3_HUMANUBE2L3physical
17996703
FXL18_HUMANFBXL18physical
25416956
UBC_HUMANUBCphysical
25723849
UB2D1_HUMANUBE2D1physical
25723849
UB2D2_HUMANUBE2D2physical
25723849
UB2D3_HUMANUBE2D3physical
25723849
UB2L3_HUMANUBE2L3physical
25723849
WWP1_HUMANWWP1physical
26152726
UB2L3_HUMANUBE2L3physical
26152726
DVL2_HUMANDVL2physical
26701932
WWP1_HUMANWWP1physical
26949039
UB2L3_HUMANUBE2L3physical
26949039
WWP1_HUMANWWP1physical
28475870
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of WWP1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-822, AND MASSSPECTROMETRY.

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