NED4L_HUMAN - dbPTM
NED4L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NED4L_HUMAN
UniProt AC Q96PU5
Protein Name E3 ubiquitin-protein ligase NEDD4-like
Gene Name NEDD4L
Organism Homo sapiens (Human).
Sequence Length 975
Subcellular Localization Cytoplasm . Golgi apparatus . Endosome, multivesicular body . May be recruited to exosomes by NDFIP1.
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. Inhibits TGF-beta signaling by triggering SMAD2 and TGFBR1 ubiquitination and proteasome-dependent degradation. Promotes ubiquitination and internalization of various plasma membrane channels such as ENaC, SCN2A/Nav1.2, SCN3A/Nav1.3, SCN5A/Nav1.5, SCN9A/Nav1.7, SCN10A/Nav1.8, KCNA3/Kv1.3, KCNH2, EAAT1, KCNQ2/Kv7.2, KCNQ3/Kv7.3 or CLC5. [PubMed: 26363003]
Protein Sequence MATGLGEPVYGLSEDEGESRILRVKVVSGIDLAKKDIFGASDPYVKLSLYVADENRELALVQTKTIKKTLNPKWNEEFYFRVNPSNHRLLFEVFDENRLTRDDFLGQVDVPLSHLPTEDPTMERPYTFKDFLLRPRSHKSRVKGFLRLKMAYMPKNGGQDEENSDQRDDMEHGWEVVDSNDSASQHQEELPPPPLPPGWEEKVDNLGRTYYVNHNNRTTQWHRPSLMDVSSESDNNIRQINQEAAHRRFRSRRHISEDLEPEPSEGGDVPEPWETISEEVNIAGDSLGLALPPPPASPGSRTSPQELSEELSRRLQITPDSNGEQFSSLIQREPSSRLRSCSVTDAVAEQGHLPPPSAPAGRARSSTVTGGEEPTPSVAYVHTTPGLPSGWEERKDAKGRTYYVNHNNRTTTWTRPIMQLAEDGASGSATNSNNHLIEPQIRRPRSLSSPTVTLSAPLEGAKDSPVRRAVKDTLSNPQSPQPSPYNSPKPQHKVTQSFLPPGWEMRIAPNGRPFFIDHNTKTTTWEDPRLKFPVHMRSKTSLNPNDLGPLPPGWEERIHLDGRTFYIDHNSKITQWEDPRLQNPAITGPAVPYSREFKQKYDYFRKKLKKPADIPNRFEMKLHRNNIFEESYRRIMSVKRPDVLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDNYTLQINPNSGLCNEDHLSYFTFIGRVAGLAVFHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWILENDPTELDLMFCIDEENFGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLIKIFDENELELLMCGLGDVDVNDWRQHSIYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELYGSNGPQLFTIEQWGSPEKLPRAHTCFNRLDLPPYETFEDLREKLLMAVENAQGFEGVD
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
2Acetylation------MATGLGEPV
------CCCCCCCCC		15.4622814378
3Phosphorylation-----MATGLGEPVY
-----CCCCCCCCCC		31.4729759185
8UbiquitinationMATGLGEPVYGLSED
CCCCCCCCCCCCCCC		23.8821890473
10PhosphorylationTGLGEPVYGLSEDEG
CCCCCCCCCCCCCCC		24.0626852163
13PhosphorylationGEPVYGLSEDEGESR
CCCCCCCCCCCCCCC		38.3422199227
19PhosphorylationLSEDEGESRILRVKV
CCCCCCCCCEEEEEE		35.1626852163
25UbiquitinationESRILRVKVVSGIDL
CCCEEEEEEEECCCH		30.41-
28PhosphorylationILRVKVVSGIDLAKK
EEEEEEEECCCHHHC		32.7826471730
113PhosphorylationGQVDVPLSHLPTEDP
CCCCCCHHHCCCCCC		19.5322210691
121 (in isoform 6)Ubiquitination-43.9421890473
121 (in isoform 7)Ubiquitination-43.9421890473
129UbiquitinationMERPYTFKDFLLRPR
CCCCCCHHHHHCCCC		39.5121890473
129 (in isoform 1)Ubiquitination-39.5121890473
129 (in isoform 2)Ubiquitination-39.5121890473
129 (in isoform 3)Ubiquitination-39.5121890473
129 (in isoform 5)Ubiquitination-39.5121890473
140PhosphorylationLRPRSHKSRVKGFLR
CCCCCCCHHHHHHEE		36.5628555341
149UbiquitinationVKGFLRLKMAYMPKN
HHHHEEEEEEECCCC		18.30-
155UbiquitinationLKMAYMPKNGGQDEE
EEEEECCCCCCCCCC		52.25-
179PhosphorylationHGWEVVDSNDSASQH
HCEEEECCCCCHHHC		30.8126471730
182PhosphorylationEVVDSNDSASQHQEE
EEECCCCCHHHCHHC		33.7926471730
184PhosphorylationVDSNDSASQHQEELP
ECCCCCHHHCHHCCC		31.9522468782
219 (in isoform 9)Phosphorylation-26.8227273156
221 (in isoform 9)Phosphorylation-6.3326657352
223 (in isoform 9)Phosphorylation-21.3929116813
225PhosphorylationTTQWHRPSLMDVSSE
CCEEECCCHHCCCCC		35.9628857561
230PhosphorylationRPSLMDVSSESDNNI
CCCHHCCCCCCCCCH		24.9127251275
231PhosphorylationPSLMDVSSESDNNIR
CCHHCCCCCCCCCHH		40.7527251275
233PhosphorylationLMDVSSESDNNIRQI
HHCCCCCCCCCHHHH		47.8128857561
236 (in isoform 9)Phosphorylation-35.4920873877
239 (in isoform 9)Phosphorylation-34.8820873877
242 (in isoform 9)Phosphorylation-43.2520873877
243 (in isoform 9)Phosphorylation-43.2520873877
248 (in isoform 9)Phosphorylation-22.8220873877
256O-linked_GlycosylationFRSRRHISEDLEPEP
HHHCCCCCCCCCCCC		20.9530169966
256PhosphorylationFRSRRHISEDLEPEP
HHHCCCCCCCCCCCC		20.9520873877
264PhosphorylationEDLEPEPSEGGDVPE
CCCCCCCCCCCCCCC		47.4120873877
275PhosphorylationDVPEPWETISEEVNI
CCCCCCHHCCHHCCC		26.4020873877
277PhosphorylationPEPWETISEEVNIAG
CCCCHHCCHHCCCCC		34.8120873877
286PhosphorylationEVNIAGDSLGLALPP
HCCCCCCCCCCCCCC		24.3426074081
297PhosphorylationALPPPPASPGSRTSP
CCCCCCCCCCCCCCH		35.2529496963
300PhosphorylationPPPASPGSRTSPQEL
CCCCCCCCCCCHHHH		35.4520873877
302PhosphorylationPASPGSRTSPQELSE
CCCCCCCCCHHHHHH		46.5930266825
303PhosphorylationASPGSRTSPQELSEE
CCCCCCCCHHHHHHH		24.3929255136
308PhosphorylationRTSPQELSEELSRRL
CCCHHHHHHHHHHHC		28.4228985074
312PhosphorylationQELSEELSRRLQITP
HHHHHHHHHHCCCCC		20.7327470641
318PhosphorylationLSRRLQITPDSNGEQ
HHHHCCCCCCCCCHH		14.2130266825
321PhosphorylationRLQITPDSNGEQFSS
HCCCCCCCCCHHHHH		48.1930266825
327PhosphorylationDSNGEQFSSLIQREP
CCCCHHHHHHHHCCC		24.7530266825
328PhosphorylationSNGEQFSSLIQREPS
CCCHHHHHHHHCCCC		30.6830266825
330UbiquitinationGEQFSSLIQREPSSR
CHHHHHHHHCCCCHH		3.8121890473
332 (in isoform 6)Phosphorylation-51.2927273156
334 (in isoform 6)Phosphorylation-39.5326657352
335PhosphorylationSLIQREPSSRLRSCS
HHHHCCCCHHCCCCC		24.2821712546
336PhosphorylationLIQREPSSRLRSCSV
HHHCCCCHHCCCCCH		46.1527422710
336 (in isoform 6)Phosphorylation-46.1529116813
340PhosphorylationEPSSRLRSCSVTDAV
CCCHHCCCCCHHHHH		18.4822617229
340 (in isoform 5)Phosphorylation-18.4827273156
341 (in isoform 4)Ubiquitination-2.8321890473
342PhosphorylationSSRLRSCSVTDAVAE
CHHCCCCCHHHHHHH		29.3330278072
342 (in isoform 5)Phosphorylation-29.3326657352
344PhosphorylationRLRSCSVTDAVAEQG
HCCCCCHHHHHHHCC		11.2730278072
344 (in isoform 5)Phosphorylation-11.2729116813
349 (in isoform 6)Phosphorylation-50.9620873877
350 (in isoform 4)Ubiquitination-34.5621890473
352 (in isoform 6)Phosphorylation-34.5520873877
355 (in isoform 6)Phosphorylation-41.6720873877
356 (in isoform 6)Phosphorylation-40.9820873877
357PhosphorylationQGHLPPPSAPAGRAR
CCCCCCCCCCCCCCC		53.2923186163
357 (in isoform 5)Phosphorylation-53.2920873877
360 (in isoform 5)Phosphorylation-21.5920873877
361 (in isoform 6)Phosphorylation-23.7920873877
363 (in isoform 5)Phosphorylation-18.1320873877
364 (in isoform 5)Phosphorylation-29.7620873877
365PhosphorylationAPAGRARSSTVTGGE
CCCCCCCCCCCCCCC		29.4030576142
366PhosphorylationPAGRARSSTVTGGEE
CCCCCCCCCCCCCCC		22.7318669648
367PhosphorylationAGRARSSTVTGGEEP
CCCCCCCCCCCCCCC		24.2725159151
367 (in isoform 3)Ubiquitination-24.2721890473
369PhosphorylationRARSSTVTGGEEPTP
CCCCCCCCCCCCCCC		39.2928857561
369 (in isoform 5)Phosphorylation-39.2920873877
375PhosphorylationVTGGEEPTPSVAYVH
CCCCCCCCCCEEEEE		31.3228857561
377PhosphorylationGGEEPTPSVAYVHTT
CCCCCCCCEEEEECC		23.1225159151
380UbiquitinationEPTPSVAYVHTTPGL
CCCCCEEEEECCCCC		7.2121890473
380PhosphorylationEPTPSVAYVHTTPGL
CCCCCEEEEECCCCC		7.2123312004
383PhosphorylationPSVAYVHTTPGLPSG
CCEEEEECCCCCCCC		25.3325159151
384PhosphorylationSVAYVHTTPGLPSGW
CEEEEECCCCCCCCH		10.6525159151
389PhosphorylationHTTPGLPSGWEERKD
ECCCCCCCCHHHCCC		62.6723186163
390UbiquitinationTTPGLPSGWEERKDA
CCCCCCCCHHHCCCC		33.6021890473
398 (in isoform 2)Ubiquitination-60.0921890473
400 (in isoform 4)Ubiquitination-20.8821890473
407 (in isoform 2)Ubiquitination-34.1821890473
410PhosphorylationYVNHNNRTTTWTRPI
EEECCCCEEEECCCC		30.6028348404
410 (in isoform 4)Ubiquitination-30.6021890473
411PhosphorylationVNHNNRTTTWTRPIM
EECCCCEEEECCCCH		19.6628348404
412PhosphorylationNHNNRTTTWTRPIMQ
ECCCCEEEECCCCHH		24.9928348404
417 (in isoform 3)Ubiquitination-2.1821890473
418 (in isoform 4)Ubiquitination-2.7121890473
425 (in isoform 2)Ubiquitination-24.04-
426PhosphorylationQLAEDGASGSATNSN
HHHHCCCCCCCCCCC		38.5219664995
427 (in isoform 3)Ubiquitination-22.2921890473
428PhosphorylationAEDGASGSATNSNNH
HHCCCCCCCCCCCCC		29.4419664995
429 (in isoform 2)Ubiquitination-17.83-
434 (in isoform 6)Ubiquitination-31.0321890473
435 (in isoform 3)Ubiquitination-32.2221890473
442 (in isoform 5)Ubiquitination-36.9921890473
443 (in isoform 6)Ubiquitination-32.3921890473
446PhosphorylationPQIRRPRSLSSPTVT
CCCCCCCCCCCCEEE		34.9722167270
448PhosphorylationIRRPRSLSSPTVTLS
CCCCCCCCCCEEEEE		35.2029255136
449PhosphorylationRRPRSLSSPTVTLSA
CCCCCCCCCEEEEEC		29.8629255136
451PhosphorylationPRSLSSPTVTLSAPL
CCCCCCCEEEEECCC		28.2422167270
451 (in isoform 5)Ubiquitination-28.2421890473
453O-linked_GlycosylationSLSSPTVTLSAPLEG
CCCCCEEEEECCCCC		19.9230169966
453PhosphorylationSLSSPTVTLSAPLEG
CCCCCEEEEECCCCC		19.9222167270
454 (in isoform 7)Ubiquitination-3.4121890473
455PhosphorylationSSPTVTLSAPLEGAK
CCCEEEEECCCCCCC		20.6222167270
457 (in isoform 2)Ubiquitination-27.8021890473
462UbiquitinationSAPLEGAKDSPVRRA
ECCCCCCCCCHHHHH		70.3821906983
462 (in isoform 1)Ubiquitination-70.3821890473
463 (in isoform 7)Ubiquitination-58.6021890473
464PhosphorylationPLEGAKDSPVRRAVK
CCCCCCCCHHHHHHH		25.2923927012
467 (in isoform 2)Ubiquitination-24.9921890473
471UbiquitinationSPVRRAVKDTLSNPQ
CHHHHHHHHHHCCCC		43.9721890473
471 (in isoform 1)Ubiquitination-43.9721890473
473PhosphorylationVRRAVKDTLSNPQSP
HHHHHHHHHCCCCCC		26.7721945579
475PhosphorylationRAVKDTLSNPQSPQP
HHHHHHHCCCCCCCC		48.8625159151
475 (in isoform 2)Ubiquitination-48.8621890473
479PhosphorylationDTLSNPQSPQPSPYN
HHHCCCCCCCCCCCC		27.1023927012
483PhosphorylationNPQSPQPSPYNSPKP
CCCCCCCCCCCCCCC		34.4723927012
485PhosphorylationQSPQPSPYNSPKPQH
CCCCCCCCCCCCCCC		32.3921945579
487PhosphorylationPQPSPYNSPKPQHKV
CCCCCCCCCCCCCCC		28.5823927012
489UbiquitinationPSPYNSPKPQHKVTQ
CCCCCCCCCCCCCCC		58.07-
493UbiquitinationNSPKPQHKVTQSFLP
CCCCCCCCCCCCCCC		41.55-
493 (in isoform 6)Ubiquitination-41.5521890473
501 (in isoform 5)Ubiquitination-63.7821890473
503 (in isoform 6)Ubiquitination-11.2821890473
508 (in isoform 2)Ubiquitination-4.91-
511 (in isoform 5)Ubiquitination-37.2621890473
511 (in isoform 6)Ubiquitination-37.2621890473
513 (in isoform 7)Ubiquitination-29.8721890473
519 (in isoform 5)Ubiquitination-39.2521890473
521UbiquitinationFFIDHNTKTTTWEDP
EEEECCCCCCCCCCC		49.5521890473
521 (in isoform 1)Ubiquitination-49.5521890473
523 (in isoform 7)Ubiquitination-31.3121890473
524PhosphorylationDHNTKTTTWEDPRLK
ECCCCCCCCCCCCCC		31.8927470641
531UbiquitinationTWEDPRLKFPVHMRS
CCCCCCCCCCEECCC		49.2321890473
531 (in isoform 1)Ubiquitination-49.2321890473
531 (in isoform 7)Ubiquitination-49.2321890473
535 (in isoform 4)Ubiquitination-13.2321890473
538PhosphorylationKFPVHMRSKTSLNPN
CCCEECCCCCCCCCC		32.4829514088
539UbiquitinationFPVHMRSKTSLNPND
CCEECCCCCCCCCCC		31.5921906983
539 (in isoform 1)Ubiquitination-31.5921890473
540PhosphorylationPVHMRSKTSLNPNDL
CEECCCCCCCCCCCC		39.4323312004
541PhosphorylationVHMRSKTSLNPNDLG
EECCCCCCCCCCCCC		29.8623312004
552 (in isoform 3)Ubiquitination-69.1121890473
571PhosphorylationTFYIDHNSKITQWED
EEEEECCCCCCCCCC		23.24-
572UbiquitinationFYIDHNSKITQWEDP
EEEECCCCCCCCCCC		55.90-
592 (in isoform 2)Ubiquitination-24.4021890473
628 (in isoform 6)Ubiquitination-10.4121890473
631PhosphorylationRNNIFEESYRRIMSV
HCCCCHHHHHHHHCC		19.4227499020
636 (in isoform 5)Ubiquitination-3.4121890473
637PhosphorylationESYRRIMSVKRPDVL
HHHHHHHCCCCHHHE		23.3224719451
639UbiquitinationYRRIMSVKRPDVLKA
HHHHHCCCCHHHEEE		51.40-
648 (in isoform 7)Ubiquitination-6.8921890473
656UbiquitinationWIEFESEKGLDYGGV
EEEEECCCCCCCCHH		74.242190698
656 (in isoform 1)Ubiquitination-74.2421890473
660PhosphorylationESEKGLDYGGVAREW
ECCCCCCCCHHHHHH		22.33-
795PhosphorylationVDLKPNGSEIMVTNE
EECCCCCCEEEEECC		30.5021501591
903PhosphorylationIRLLQFVTGTSRVPM
HHHHHHHHCCCCCCC		35.71-
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
342SPhosphorylationKinaseWNK4Q96J92
Uniprot
342SPhosphorylationKinaseSGK_GROUP-PhosphoELM
342SPhosphorylationKinasePKA_GROUP-PhosphoELM
342SPhosphorylationKinaseSGK-FAMILY-GPS
342SPhosphorylationKinasePKA-FAMILY-GPS
342SPhosphorylationKinaseWNK1Q9H4A3
Uniprot
342SPhosphorylationKinaseSGK1Q9WVC6
PSP
342SPhosphorylationKinaseSGK1O00141
PSP
342SPhosphorylationKinasePRKACAP17612
GPS
367TPhosphorylationKinaseSGK1O00141
Uniprot
367TPhosphorylationKinaseSGK_GROUP-PhosphoELM
367TPhosphorylationKinaseSGK1Q9WVC6
PSP
367TPhosphorylationKinasePRKACAP17612
GPS
367TPhosphorylationKinasePKA_GROUP-PhosphoELM
367TPhosphorylationKinasePKA-FAMILY-GPS
367TPhosphorylationKinaseSGK-FAMILY-GPS
448SPhosphorylationKinasePKA-FAMILY-GPS
448SPhosphorylationKinaseSGK_GROUP-PhosphoELM
448SPhosphorylationKinasePKA_GROUP-PhosphoELM
448SPhosphorylationKinasePKA-Uniprot
448SPhosphorylationKinaseSGK-FAMILY-GPS
448SPhosphorylationKinasePRKACAP17612
GPS
448SPhosphorylationKinaseSGK1O00141
Uniprot
448SPhosphorylationKinaseSGK1Q9WVC6
PSP
449SPhosphorylationKinaseWNK4Q96J92
Uniprot
449SPhosphorylationKinaseWNK1Q9H4A3
Uniprot
795SPhosphorylationKinaseAMPKB1Q9Y478
PSP
795SPhosphorylationKinaseAMPKA1Q13131
PSP
795SPhosphorylationKinaseAMPKG2Q9UGJ0
PSP
-KUbiquitinationE3 ubiquitin ligaseNEDD4LQ96PU5
PMID:18498246
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NED4L_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 NED4L_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GCR_HUMANNR3C1physical
9649342
NED4L_HUMANNEDD4Lphysical
19153599
NED4L_HUMANNEDD4Lphysical
18498246
PSMD4_HUMANPSMD4physical
20542005
NED4L_HUMANNEDD4Lphysical
20542005
1433B_HUMANYWHABphysical
20338996
ACK1_HUMANTNK2physical
19144635
APBB1_HUMANAPBB1physical
19381069
APBB1_RATApbb1physical
19381069
KCNB1_HUMANKCNB1physical
19953087
MAPK3_HUMANMAPKAPK3physical
19953087
CLIC2_HUMANCLIC2physical
19953087
FBLN4_HUMANEFEMP2physical
19953087
HGS_HUMANHGSphysical
19953087
NFIP2_HUMANNDFIP2physical
19953087
M3K3_HUMANMAP3K3physical
19953087
VDAC2_HUMANVDAC2physical
19953087
ZDHC3_HUMANZDHHC3physical
19953087
KCC1D_HUMANCAMK1Dphysical
19953087
RBP10_HUMANRANBP10physical
19953087
CDK5_HUMANCDK5physical
19953087
ABL1_HUMANABL1physical
19953087
MAGB1_HUMANMAGEB1physical
19953087
DEMA_HUMANDMTNphysical
19953087
AICDA_HUMANAICDAphysical
19953087
MARK2_HUMANMARK2physical
19953087
KCAB1_HUMANKCNAB1physical
19953087
FKBP3_HUMANFKBP3physical
19953087
DAPK3_HUMANDAPK3physical
19953087
BRAF_HUMANBRAFphysical
19953087
M3K5_HUMANMAP3K5physical
19953087
DDX54_HUMANDDX54physical
19953087
M3K20_HUMANZAKphysical
19953087
KCAB3_HUMANKCNAB3physical
19953087
NTRK1_HUMANNTRK1physical
19953087
CUED1_HUMANCUEDC1physical
19953087
KS6B2_HUMANRPS6KB2physical
19953087
ABL2_HUMANABL2physical
19953087
CACB1_HUMANCACNB1physical
19953087
TYY1_HUMANYY1physical
19953087
M3K2_HUMANMAP3K2physical
19953087
BBX_HUMANBBXphysical
19953087
PRKX_HUMANPRKXphysical
19953087
ACV1B_HUMANACVR1Bphysical
19953087
ADAP2_HUMANADAP2physical
19953087
BMR1A_HUMANBMPR1Aphysical
19953087
AKT3_HUMANAKT3physical
19953087
MINK1_HUMANMINK1physical
19953087
AURKC_HUMANAURKCphysical
19953087
NSRP1_HUMANNSRP1physical
19953087
PYM1_HUMANWIBGphysical
19953087
SGK2_HUMANSGK2physical
19953087
UBAC1_HUMANUBAC1physical
19953087
RL30_HUMANRPL30physical
19953087
MERTK_HUMANMERTKphysical
19953087
SRMS_HUMANSRMSphysical
19953087
PEDF_HUMANSERPINF1physical
19953087
DYRK3_HUMANDYRK3physical
19953087
IFRD2_HUMANIFRD2physical
19953087
ACOD_HUMANSCDphysical
19953087
ROBO3_HUMANROBO3physical
19953087
TRI41_HUMANTRIM41physical
19953087
TMA16_HUMANTMA16physical
19953087
TAF1B_HUMANTAF1Bphysical
19953087
SPAG8_HUMANSPAG8physical
19953087
STAC_HUMANSTACphysical
19953087
H10_HUMANH1F0physical
19953087
LARGN_HUMANPRR16physical
19953087
KIFC3_HUMANKIFC3physical
19953087
RSLAB_HUMANRASL10Bphysical
19953087
TMG1_HUMANPRRG1physical
19953087
CDK3_HUMANCDK3physical
19953087
KCAB2_HUMANKCNAB2physical
19953087
FGF12_HUMANFGF12physical
19953087
RBX2_HUMANRNF7physical
19953087
APEX2_HUMANAPEX2physical
19953087
RM19_HUMANMRPL19physical
19953087
TGFI1_HUMANTGFB1I1physical
19953087
TBCD7_HUMANTBC1D7physical
19953087
NHP2_HUMANNHP2physical
19953087
PP4P2_HUMANTMEM55Aphysical
19953087
CP26B_HUMANCYP26B1physical
19953087
DECR2_HUMANDECR2physical
19953087
SENP2_HUMANSENP2physical
19953087
SIVA_HUMANSIVA1physical
19953087
RSLBB_HUMANRASL11Bphysical
19953087
MTAP2_HUMANMAP2physical
19953087
STK40_HUMANSTK40physical
19953087
TIRR_HUMANNUDT16L1physical
19953087
CG050_HUMANC7orf50physical
19953087
TCAL2_HUMANTCEAL2physical
19953087
ZCCHL_HUMANZC3HAV1Lphysical
19953087
MOB3A_HUMANMOB3Aphysical
19953087
TRBP2_HUMANTARBP2physical
19953087
PTGR3_HUMANZADH2physical
19953087
1433F_HUMANYWHAHphysical
16716084
SCNNG_HUMANSCNN1Gphysical
16716084
SCNNB_HUMANSCNN1Bphysical
19380724
RAF1_HUMANRAF1physical
19380724
SCNNA_HUMANSCNN1Aphysical
12876068
SCNNB_HUMANSCNN1Bphysical
12876068
SCNNG_HUMANSCNN1Gphysical
12876068
AMOL1_HUMANAMOTL1physical
22558212
SCNNA_HUMANSCNN1Aphysical
15328345
SCNNB_HUMANSCNN1Bphysical
15328345
SCNNG_HUMANSCNN1Gphysical
15328345
SMAD3_HUMANSMAD3physical
19917253
1433T_HUMANYWHAQphysical
21900244
SCNNG_RATScnn1gphysical
11502596
SCNNA_HUMANSCNN1Aphysical
16844684
SCNNB_HUMANSCNN1Bphysical
16844684
SCNNG_HUMANSCNN1Gphysical
16844684
SCNNB_HUMANSCNN1Bphysical
11802777
SCNNA_HUMANSCNN1Aphysical
11802777
SCNNG_HUMANSCNN1Gphysical
11802777
NFIP2_HUMANNDFIP2physical
12050153
SCNNG_RATScnn1gphysical
15140763
NPC2_HUMANNPC2physical
19664597
MT2_HUMANMT2Aphysical
19664597
AT1B1_HUMANATP1B1physical
19664597
CYBR1_HUMANCYBRD1physical
19664597
YLAT1_HUMANSLC7A7physical
19664597
PBX1_HUMANPBX1physical
19664597
ACY3_HUMANACY3physical
19664597
HAX1_HUMANHAX1physical
19664597
KIF3B_HUMANKIF3Bphysical
19664597
CAV3_HUMANCAV3physical
22879586
NED4L_HUMANNEDD4Lphysical
22496338
UBC_HUMANUBCphysical
22496338
UB2D2_HUMANUBE2D2physical
20542005
UB2L3_HUMANUBE2L3physical
18498246
UBE2K_HUMANUBE2Kphysical
17429078
UB2D1_HUMANUBE2D1physical
9575161
UB2L3_HUMANUBE2L3physical
9575161
UB2D2_HUMANUBE2D2physical
22496338
UB2E3_HUMANUBE2E3physical
22496338
UB2J2_HUMANUBE2J2physical
22496338
UB2R1_HUMANCDC34physical
22496338
UBE2K_HUMANUBE2Kphysical
22496338
UB2D2_HUMANUBE2D2physical
19953087
FXL15_HUMANFBXL15physical
21572392
SGK3_HUMANSGK3physical
23589291
UBC_HUMANUBCphysical
23644597
NOTC1_HUMANNOTCH1physical
23886940
SNA3_YEASTSNA3physical
23936628
SMAD3_HUMANSMAD3physical
24071738
UB2D1_HUMANUBE2D1physical
24071738
UBE2N_HUMANUBE2Nphysical
24071738
HCN1_HUMANHCN1physical
24451387
SYUA_HUMANSNCAphysical
24831002
UB2D1_HUMANUBE2D1physical
21396940
NED4L_HUMANNEDD4Lphysical
21396940
P4K2A_MOUSEPi4k2aphysical
23146885
NED4L_HUMANNEDD4Lphysical
17719543
HGS_HUMANHGSphysical
20675381
NED4L_HUMANNEDD4Lphysical
25527291
UB2L3_HUMANUBE2L3physical
25527291
UBC_HUMANUBCphysical
25752577
UB2L3_HUMANUBE2L3physical
25752577
AMOT_HUMANAMOTphysical
25633977
WNK1_HUMANWNK1physical
26241057
NED4L_HUMANNEDD4Lphysical
26949039
UB2L3_HUMANUBE2L3physical
26949039
RHOB_HUMANRHOBphysical
26949039
CRYAB_HUMANCRYABphysical
26961874
GRB10_HUMANGRB10physical
27146988
KCNA3_HUMANKCNA3physical
27146988
ULK1_HUMANULK1physical
27932573
UB2D2_HUMANUBE2D2physical
27932573
ERBB3_HUMANERBB3physical
27793840
FAK2_HUMANPTK2Bphysical
27793840
GRIA1_HUMANGRIA1physical
28212375
LPAR1_HUMANLPAR1physical
27448760
UB2D1_HUMANUBE2D1physical
28972136
UB2D2_HUMANUBE2D2physical
28972136
UB2D3_HUMANUBE2D3physical
28972136
UB2E1_HUMANUBE2E1physical
28972136
UB2E3_HUMANUBE2E3physical
28972136
UB2E2_HUMANUBE2E2physical
28972136
UB2L6_HUMANUBE2L6physical
28972136
NED4L_HUMANNEDD4Lphysical
28972136
PK3CA_HUMANPIK3CAphysical
27339899
UB2D3_HUMANUBE2D3physical
27339899
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 NED4L_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-448; SER-479; SER-483 AND SER-487, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Serum and glucocorticoid-induced kinase (SGK) 1 and the epithelialsodium channel are regulated by multiple with no lysine (WNK) familymembers.";
Heise C.J., Xu B.E., Deaton S.L., Cha S.K., Cheng C.J., Earnest S.,Sengupta S., Juang Y.C., Stippec S., Xu Y., Zhao Y., Huang C.L.,Cobb M.H.;
J. Biol. Chem. 285:25161-25167(2010).
Cited for: PHOSPHORYLATION AT SER-342 AND SER-449, AND INTERACTION WITH WNK1.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303 AND SER-446, ANDMASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-448; SER-479; SER-483 AND SER-487, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318; SER-342; SER-446;SER-449; SER-464; SER-479; SER-483 AND SER-487, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448 AND SER-449, ANDMASS SPECTROMETRY.
"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 SER-479; SER-483 ANDSER-487, AND MASS SPECTROMETRY.
"cAMP and serum and glucocorticoid-inducible kinase (SGK) regulate theepithelial Na(+) channel through convergent phosphorylation of Nedd4-2.";
Snyder P.M., Olson D.R., Kabra R., Zhou R., Steines J.C.;
J. Biol. Chem. 279:45753-45758(2004).
Cited for: PHOSPHORYLATION AT SER-342; THR-367 AND SER-448.
"14-3-3 proteins modulate the expression of epithelial Na+ channels byphosphorylation-dependent interaction with Nedd4-2 ubiquitin ligase.";
Ichimura T., Yamamura H., Sasamoto K., Tominaga Y., Taoka M.,Kakiuchi K., Shinkawa T., Takahashi N., Shimada S., Isobe T.;
J. Biol. Chem. 280:13187-13194(2005).
Cited for: PROTEIN SEQUENCE OF 448-462, INTERACTION WITH YWHAB; YWHAG; YWHAE;YWHAQ AND YWHAH, PHOSPHORYLATION AT SER-448, MUTAGENESIS OF SER-448,AND MASS SPECTROMETRY.

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