JIP4_HUMAN - dbPTM
JIP4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID JIP4_HUMAN
UniProt AC O60271
Protein Name C-Jun-amino-terminal kinase-interacting protein 4
Gene Name SPAG9
Organism Homo sapiens (Human).
Sequence Length 1321
Subcellular Localization Cytoplasm. Cytoplasm, perinuclear region. Perinuclear distribution in response to stress signals such as UV radiation.
Isoform 5: Cytoplasmic vesicle, secretory vesicle, acrosome. Associated with the plasma membrane of the acrosomal compartment
Protein Description The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. Isoform 5 may play a role in spermatozoa-egg-interaction..
Protein Sequence MELEDGVVYQEEPGGSGAVMSERVSGLAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLERTKLHQLSGSDQLESTAHSRIRKERPISLGIFPLPAGDGLLTPDAQKGGETPGSEQWKFQELSQPRSHTSLKVSNSPEPQKAVEQEDELSDVSQGGSKATTPASTANSDVATIPTDTPLKEENEGFVKVTDAPNKSEISKHIEVQVAQETRNVSTGSAENEEKSEVQAIIESTPELDMDKDLSGYKGSSTPTKGIENKAFDRNTESLFEELSSAGSGLIGDVDEGADLLGMGREVENLILENTQLLETKNALNIVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEEKNRELEEELRKARAEAEDARQKAKDDDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKRSSIWQFFSRLFSSSSNTTKKPEPPVNLKYNAPTSHVTPSVKKRSSTLSQLPGDKSKAFDFLSEETEASLASRREQKREQYRQVKAHVQKEDGRVQAFGWSLPQKYKQVTNGQGENKMKNLPVPVYLRPLDEKDTSMKLWCAVGVNLSGGKTRDGGSVVGASVFYKDVAGLDTEGSKQRSASQSSLDKLDQELKEQQKELKNQEELSSLVWICTSTHSATKVLIIDAVQPGNILDSFTVCNSHVLCIASVPGARETDYPAGEDLSESGQVDKASLCGSMTSNSSAETDSLLGGITVVGCSAEGVTGAATSPSTNGASPVMDKPPEMEAENSEVDENVPTAEEATEATEGNAGSAEDTVDISQTGVYTEHVFTDPLGVQIPEDLSPVYQSSNDSDAYKDQISVLPNEQDLVREEAQKMSSLLPTMWLGAQNGCLYVHSSVAQWRKCLHSIKLKDSILSIVHVKGIVLVALADGTLAIFHRGVDGQWDLSNYHLLDLGRPHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVSIRLDSTLRLYHAHTYQHLQDVDIEPYVSKMLGTGKLGFSFVRITALMVSCNRLWVGTGNGVIISIPLTETNKTSGVPGNRPGSVIRVYGDENSDKVTPGTFIPYCSMAHAQLCFHGHRDAVKFFVAVPGQVISPQSSSSGTDLTGDKAGPSAQEPGSQTPLKSMLVISGGEGYIDFRMGDEGGESELLGEDLPLEPSVTKAERSHLIVWQVMYGNE
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
1Acetylation-------MELEDGVV
-------CCCCCCCE		52.1222814378
9PhosphorylationELEDGVVYQEEPGGS
CCCCCCEEECCCCCC		14.0624043423
16PhosphorylationYQEEPGGSGAVMSER
EECCCCCCCCHHCHH		29.5124043423
21PhosphorylationGGSGAVMSERVSGLA
CCCCCHHCHHHHCHH		18.6924043423
25PhosphorylationAVMSERVSGLAGSIY
CHHCHHHHCHHHHHH		34.0224043423
30PhosphorylationRVSGLAGSIYREFER
HHHCHHHHHHHHHHH		15.7324043423
32PhosphorylationSGLAGSIYREFERLI
HCHHHHHHHHHHHHH		13.0424043423
60 (in isoform 9)Phosphorylation-45.0128731282
95 (in isoform 9)Phosphorylation-12.7225849741
99 (in isoform 9)Phosphorylation-29.6725159151
101 (in isoform 9)Phosphorylation-54.7925159151
102UbiquitinationLRKHAEEKFIEFEDS
HHHHHHHHCCCCCCC		43.05-
102 (in isoform 9)Phosphorylation-43.0517525332
108 (in isoform 9)Phosphorylation-62.0217525332
109PhosphorylationKFIEFEDSQEQEKKD
HCCCCCCCHHHHHHH		28.5523401153
111 (in isoform 9)Phosphorylation-65.7417525332
1142-HydroxyisobutyrylationEDSQEQEKKDLQTRV
CCCHHHHHHHHHHHH		51.81-
115 (in isoform 9)Phosphorylation-64.0225849741
118 (in isoform 9)Phosphorylation-37.0825849741
119PhosphorylationQEKKDLQTRVESLES
HHHHHHHHHHHHHHH		43.9319413330
119 (in isoform 9)Phosphorylation-43.9325849741
123PhosphorylationDLQTRVESLESQTRQ
HHHHHHHHHHHHHHH		34.2823312004
134SumoylationQTRQLELKAKNYADQ
HHHHHHHHHHHHHHH		48.19-
134SumoylationQTRQLELKAKNYADQ
HHHHHHHHHHHHHHH		48.19-
143PhosphorylationKNYADQISRLEEREA
HHHHHHHHHHHHHHH		25.7725159151
154AcetylationEREAELKKEYNALHQ
HHHHHHHHHHHHHHH		77.4119413330
154UbiquitinationEREAELKKEYNALHQ
HHHHHHHHHHHHHHH		77.41-
164PhosphorylationNALHQRHTEMIHNYM
HHHHHHHHHHHHHHH		29.4526546556
177PhosphorylationYMEHLERTKLHQLSG
HHHHHHHHCHHHCCC		28.6920873877
178UbiquitinationMEHLERTKLHQLSGS
HHHHHHHCHHHCCCC		50.63-
183PhosphorylationRTKLHQLSGSDQLES
HHCHHHCCCCHHHCH		29.6723927012
183 (in isoform 2)Phosphorylation-29.6718669648
185PhosphorylationKLHQLSGSDQLESTA
CHHHCCCCHHHCHHH		20.8623927012
185 (in isoform 2)Phosphorylation-20.8618669648
190PhosphorylationSGSDQLESTAHSRIR
CCCHHHCHHHHHHHH		39.2123927012
191PhosphorylationGSDQLESTAHSRIRK
CCHHHCHHHHHHHHC		21.0025159151
194PhosphorylationQLESTAHSRIRKERP
HHCHHHHHHHHCCCC		27.2623927012
203PhosphorylationIRKERPISLGIFPLP
HHCCCCCEEEEEEEC		24.1929255136
203 (in isoform 2)Phosphorylation-24.1918669648
217PhosphorylationPAGDGLLTPDAQKGG
CCCCCCCCCCHHCCC		24.9429255136
217 (in isoform 2)Phosphorylation-24.9418669648
226PhosphorylationDAQKGGETPGSEQWK
CHHCCCCCCCCHHCC		35.9019664994
226 (in isoform 2)Phosphorylation-35.9018669648
229PhosphorylationKGGETPGSEQWKFQE
CCCCCCCCHHCCCEE		28.0225159151
233UbiquitinationTPGSEQWKFQELSQP
CCCCHHCCCEECCCC		36.5421890473
233UbiquitinationTPGSEQWKFQELSQP
CCCCHHCCCEECCCC		36.5421890473
233UbiquitinationTPGSEQWKFQELSQP
CCCCHHCCCEECCCC		36.5421890473
233 (in isoform 1)Ubiquitination-36.5421890473
233 (in isoform 2)Ubiquitination-36.5421890473
233 (in isoform 3)Ubiquitination-36.5421890473
233 (in isoform 4)Ubiquitination-36.5421890473
233 (in isoform 5)Ubiquitination-36.5421890473
238PhosphorylationQWKFQELSQPRSHTS
HCCCEECCCCCCCCC		37.0730266825
238 (in isoform 2)Phosphorylation-37.0725849741
238 (in isoform 4)Phosphorylation-37.0725849741
238 (in isoform 5)Phosphorylation-37.0725849741
242PhosphorylationQELSQPRSHTSLKVS
EECCCCCCCCCCCCC		37.4925159151
242 (in isoform 2)Phosphorylation-37.4925159151
242 (in isoform 4)Phosphorylation-37.4925159151
242 (in isoform 5)Phosphorylation-37.4925159151
244PhosphorylationLSQPRSHTSLKVSNS
CCCCCCCCCCCCCCC		36.6822199227
244 (in isoform 2)Phosphorylation-36.6825159151
244 (in isoform 4)Phosphorylation-36.6825159151
244 (in isoform 5)Phosphorylation-36.6825159151
245PhosphorylationSQPRSHTSLKVSNSP
CCCCCCCCCCCCCCC		22.2917525332
245 (in isoform 2)Phosphorylation-22.2917525332
245 (in isoform 4)Phosphorylation-22.2917525332
245 (in isoform 5)Phosphorylation-22.2917525332
249PhosphorylationSHTSLKVSNSPEPQK
CCCCCCCCCCCCHHH		29.9723401153
251PhosphorylationTSLKVSNSPEPQKAV
CCCCCCCCCCHHHHH		24.1229255136
251 (in isoform 2)Phosphorylation-24.1217525332
251 (in isoform 4)Phosphorylation-24.1217525332
251 (in isoform 5)Phosphorylation-24.1217525332
254 (in isoform 2)Phosphorylation-44.3417525332
254 (in isoform 4)Phosphorylation-44.3417525332
254 (in isoform 5)Phosphorylation-44.3417525332
258 (in isoform 2)Phosphorylation-11.4125849741
258 (in isoform 4)Phosphorylation-11.4125849741
258 (in isoform 5)Phosphorylation-11.4125849741
261 (in isoform 2)Phosphorylation-39.6925849741
261 (in isoform 4)Phosphorylation-39.6925849741
261 (in isoform 5)Phosphorylation-39.6925849741
262 (in isoform 2)Phosphorylation-62.9325849741
262 (in isoform 4)Phosphorylation-62.9325849741
262 (in isoform 5)Phosphorylation-62.9325849741
265PhosphorylationVEQEDELSDVSQGGS
HCCCHHHHCCCCCCC		33.6417525332
268PhosphorylationEDELSDVSQGGSKAT
CHHHHCCCCCCCCCC		28.2617525332
272PhosphorylationSDVSQGGSKATTPAS
HCCCCCCCCCCCCCC		26.4117525332
275PhosphorylationSQGGSKATTPASTAN
CCCCCCCCCCCCCCC		36.7329255136
276PhosphorylationQGGSKATTPASTANS
CCCCCCCCCCCCCCC		23.0129255136
279PhosphorylationSKATTPASTANSDVA
CCCCCCCCCCCCCCE		29.2929255136
280PhosphorylationKATTPASTANSDVAT
CCCCCCCCCCCCCEE		31.7829255136
283PhosphorylationTPASTANSDVATIPT
CCCCCCCCCCEECCC		30.8829255136
287PhosphorylationTANSDVATIPTDTPL
CCCCCCEECCCCCCC		27.6027794612
290PhosphorylationSDVATIPTDTPLKEE
CCCEECCCCCCCCCC		48.9729255136
292PhosphorylationVATIPTDTPLKEENE
CEECCCCCCCCCCCC		32.7629255136
297AcetylationTDTPLKEENEGFVKV
CCCCCCCCCCCCEEE		60.0219413330
305PhosphorylationNEGFVKVTDAPNKSE
CCCCEEEECCCCHHH		22.2622199227
310AcetylationKVTDAPNKSEISKHI
EEECCCCHHHHHHCE		48.7025953088
311AcetylationVTDAPNKSEISKHIE
EECCCCHHHHHHCEE		46.9619413330
311PhosphorylationVTDAPNKSEISKHIE
EECCCCHHHHHHCEE		46.9629255136
314PhosphorylationAPNKSEISKHIEVQV
CCCHHHHHHCEEEEE		17.7125159151
325PhosphorylationEVQVAQETRNVSTGS
EEEEEEEECCCCCCC		18.5729514088
329PhosphorylationAQETRNVSTGSAENE
EEEECCCCCCCCCCH		30.5129255136
330PhosphorylationQETRNVSTGSAENEE
EEECCCCCCCCCCHH		30.7629255136
332PhosphorylationTRNVSTGSAENEEKS
ECCCCCCCCCCHHHH		32.2829255136
339PhosphorylationSAENEEKSEVQAIIE
CCCCHHHHHHHHHHH		46.4025159151
347PhosphorylationEVQAIIESTPELDMD
HHHHHHHCCCCCCCC		38.5625159151
348PhosphorylationVQAIIESTPELDMDK
HHHHHHCCCCCCCCC		14.1625159151
358PhosphorylationLDMDKDLSGYKGSST
CCCCCCCCCCCCCCC		50.6525159151
360PhosphorylationMDKDLSGYKGSSTPT
CCCCCCCCCCCCCCC		14.5921712546
361UbiquitinationDKDLSGYKGSSTPTK
CCCCCCCCCCCCCCC		56.70-
363PhosphorylationDLSGYKGSSTPTKGI
CCCCCCCCCCCCCCC		27.2125159151
364PhosphorylationLSGYKGSSTPTKGIE
CCCCCCCCCCCCCCC		47.2623401153
365PhosphorylationSGYKGSSTPTKGIEN
CCCCCCCCCCCCCCC		36.3528355574
367PhosphorylationYKGSSTPTKGIENKA
CCCCCCCCCCCCCCC		41.8328176443
379PhosphorylationNKAFDRNTESLFEEL
CCCCCCCHHHHHHHH		28.0420068231
381PhosphorylationAFDRNTESLFEELSS
CCCCCHHHHHHHHHH		36.0020068231
387PhosphorylationESLFEELSSAGSGLI
HHHHHHHHHCCCCCC		22.7927422710
388PhosphorylationSLFEELSSAGSGLIG
HHHHHHHHCCCCCCC		49.6427422710
391PhosphorylationEELSSAGSGLIGDVD
HHHHHCCCCCCCCCC		30.0929743597
418PhosphorylationENLILENTQLLETKN
HHHHHHCHHHHCHHH		15.9517525332
423PhosphorylationENTQLLETKNALNIV
HCHHHHCHHHHHHHH		29.5729523821
424UbiquitinationNTQLLETKNALNIVK
CHHHHCHHHHHHHHH		30.7422053931
443GlutathionylationAKVDELTCEKDVLQG
HHHHHHHCCHHHHHH		10.7922555962
445UbiquitinationVDELTCEKDVLQGEL
HHHHHCCHHHHHHHH		56.11-
474MethylationRELEEELRKARAEAE
HHHHHHHHHHHHHHH		33.59115480725
493PhosphorylationKAKDDDDSDIPTAQR
HCCCCCCCCCCHHHH		44.4225159151
497PhosphorylationDDDSDIPTAQRKRFT
CCCCCCCHHHHHHHH		35.4428985074
523SulfoxidationNQYKERLMELQEAVR
HHHHHHHHHHHHHHH		6.3921406390
532PhosphorylationLQEAVRWTEMIRASR
HHHHHHHHHHHHHHC		12.7128464451
538PhosphorylationWTEMIRASRENPAMQ
HHHHHHHHCCCHHHH		30.2228348404
5472-HydroxyisobutyrylationENPAMQEKKRSSIWQ
CCHHHHHHHHHHHHH		36.27-
550PhosphorylationAMQEKKRSSIWQFFS
HHHHHHHHHHHHHHH		34.7529496963
551PhosphorylationMQEKKRSSIWQFFSR
HHHHHHHHHHHHHHH		31.7028555341
557PhosphorylationSSIWQFFSRLFSSSS
HHHHHHHHHHHCCCC		29.3929496963
561PhosphorylationQFFSRLFSSSSNTTK
HHHHHHHCCCCCCCC		33.6228857561
562PhosphorylationFFSRLFSSSSNTTKK
HHHHHHCCCCCCCCC		30.3726699800
563PhosphorylationFSRLFSSSSNTTKKP
HHHHHCCCCCCCCCC		26.8026699800
564PhosphorylationSRLFSSSSNTTKKPE
HHHHCCCCCCCCCCC		39.8926699800
566PhosphorylationLFSSSSNTTKKPEPP
HHCCCCCCCCCCCCC		41.7728857561
577MethylationPEPPVNLKYNAPTSH
CCCCCCCEECCCCCC		31.12115971577
577UbiquitinationPEPPVNLKYNAPTSH
CCCCCCCEECCCCCC		31.12-
578PhosphorylationEPPVNLKYNAPTSHV
CCCCCCEECCCCCCC		21.5223403867
582PhosphorylationNLKYNAPTSHVTPSV
CCEECCCCCCCCCCH		29.1130266825
583PhosphorylationLKYNAPTSHVTPSVK
CEECCCCCCCCCCHH		18.2030243723
586PhosphorylationNAPTSHVTPSVKKRS
CCCCCCCCCCHHHCC		12.3830266825
588PhosphorylationPTSHVTPSVKKRSST
CCCCCCCCHHHCCCC		36.8830266825
593PhosphorylationTPSVKKRSSTLSQLP
CCCHHHCCCCHHCCC		36.2323401153
594PhosphorylationPSVKKRSSTLSQLPG
CCHHHCCCCHHCCCC		37.0825159151
595PhosphorylationSVKKRSSTLSQLPGD
CHHHCCCCHHCCCCC		31.5119664994
597PhosphorylationKKRSSTLSQLPGDKS
HHCCCCHHCCCCCHH		29.7430266825
6032-HydroxyisobutyrylationLSQLPGDKSKAFDFL
HHCCCCCHHHHHHHH		60.82-
603UbiquitinationLSQLPGDKSKAFDFL
HHCCCCCHHHHHHHH		60.82-
605UbiquitinationQLPGDKSKAFDFLSE
CCCCCHHHHHHHHCH		59.83-
611PhosphorylationSKAFDFLSEETEASL
HHHHHHHCHHHHHHH		33.1228348404
614PhosphorylationFDFLSEETEASLASR
HHHHCHHHHHHHHHH		32.5721406692
617PhosphorylationLSEETEASLASRREQ
HCHHHHHHHHHHHHH		20.4521406692
620PhosphorylationETEASLASRREQKRE
HHHHHHHHHHHHHHH		36.8421406692
639UbiquitinationVKAHVQKEDGRVQAF
HHHHHHCCCCCEEEC		48.9121890473
639 (in isoform 4)Ubiquitination-48.9121890473
639 (in isoform 5)Ubiquitination-48.9121890473
643 (in isoform 2)Ubiquitination-6.1821890473
649PhosphorylationRVQAFGWSLPQKYKQ
CEEECCCCCCHHHEE		30.4728857561
653UbiquitinationFGWSLPQKYKQVTNG
CCCCCCHHHEECCCC		53.1021890473
653UbiquitinationFGWSLPQKYKQVTNG
CCCCCCHHHEECCCC		53.1021890473
653 (in isoform 1)Ubiquitination-53.1021890473
653 (in isoform 3)Ubiquitination-53.1021890473
654PhosphorylationGWSLPQKYKQVTNGQ
CCCCCHHHEECCCCC		11.0418083107
674PhosphorylationKNLPVPVYLRPLDEK
CCCCCCEEECCCCCC		7.3027642862
699UbiquitinationGVNLSGGKTRDGGSV
EEECCCCCCCCCCCE		43.86-
700PhosphorylationVNLSGGKTRDGGSVV
EECCCCCCCCCCCEE		36.9523186163
705PhosphorylationGKTRDGGSVVGASVF
CCCCCCCCEEEEEEE		21.1125159151
710PhosphorylationGGSVVGASVFYKDVA
CCCEEEEEEEEECCC		13.5628450419
713PhosphorylationVVGASVFYKDVAGLD
EEEEEEEEECCCCCC		12.2420068231
724PhosphorylationAGLDTEGSKQRSASQ
CCCCCCCHHHHCCCH		21.2728857561
728PhosphorylationTEGSKQRSASQSSLD
CCCHHHHCCCHHHHH		29.7623927012
730PhosphorylationGSKQRSASQSSLDKL
CHHHHCCCHHHHHHH		31.6629255136
732PhosphorylationKQRSASQSSLDKLDQ
HHHCCCHHHHHHHHH		30.3029255136
733PhosphorylationQRSASQSSLDKLDQE
HHCCCHHHHHHHHHH		32.7129255136
742AcetylationDKLDQELKEQQKELK
HHHHHHHHHHHHHHC		53.3718525921
746AcetylationQELKEQQKELKNQEE
HHHHHHHHHHCCHHH		65.7818525935
749AcetylationKEQQKELKNQEELSS
HHHHHHHCCHHHHHH		58.6418525949
806PhosphorylationPGARETDYPAGEDLS
CCCCCCCCCCCCCCC		11.4727251275
813PhosphorylationYPAGEDLSESGQVDK
CCCCCCCCCCCCCCH		41.8830278072
815PhosphorylationAGEDLSESGQVDKAS
CCCCCCCCCCCCHHH		31.0223401153
914PhosphorylationDISQTGVYTEHVFTD
EHHHCCEEEEEEEEC		14.04-
932PhosphorylationVQIPEDLSPVYQSSN
CCCCCCCCCCCCCCC		25.3322468782
949PhosphorylationDAYKDQISVLPNEQD
HHHHHHHCCCCCHHH		16.3925159151
996PhosphorylationQWRKCLHSIKLKDSI
HHHHHHHHCCCHHHH		14.4129083192
998UbiquitinationRKCLHSIKLKDSILS
HHHHHHCCCHHHHHH		53.12-
1036PhosphorylationVDGQWDLSNYHLLDL
CCCCCCCCCCEEECC		32.6328348404
1049PhosphorylationDLGRPHHSIRCMTVV
CCCCCCCEEEEEEEE		14.5428348404
1069PhosphorylationCGYRNKIYVVQPKAM
ECCCCEEEEECCCCE		9.0029496907
1080AcetylationPKAMKIEKSFDAHPR
CCCEECCHHCCCCCC		60.9525953088
1144PhosphorylationGTGKLGFSFVRITAL
CCCCCCCCCHHHHEE		22.4922617229
1178PhosphorylationPLTETNKTSGVPGNR
ECCCCCCCCCCCCCC		32.5523403867
1179PhosphorylationLTETNKTSGVPGNRP
CCCCCCCCCCCCCCC		39.1323403867
1188PhosphorylationVPGNRPGSVIRVYGD
CCCCCCCCEEEEECC		19.6325159151
1213UbiquitinationFIPYCSMAHAQLCFH
HHHCCHHCCHHHHHC		4.4121890473
1213 (in isoform 4)Ubiquitination-4.4121890473
1217 (in isoform 2)Ubiquitination-3.3221890473
1227UbiquitinationHGHRDAVKFFVAVPG
CCCCCCEEEEEECCC		34.5021890473
1227UbiquitinationHGHRDAVKFFVAVPG
CCCCCCEEEEEECCC		34.5021906983
1227 (in isoform 1)Ubiquitination-34.5021890473
1238PhosphorylationAVPGQVISPQSSSSG
ECCCCEECCCCCCCC		20.3129255136
1241PhosphorylationGQVISPQSSSSGTDL
CCEECCCCCCCCCCC		35.2629255136
1242PhosphorylationQVISPQSSSSGTDLT
CEECCCCCCCCCCCC		24.2326657352
1243PhosphorylationVISPQSSSSGTDLTG
EECCCCCCCCCCCCC		37.7329255136
1244PhosphorylationISPQSSSSGTDLTGD
ECCCCCCCCCCCCCC		47.8929255136
1246PhosphorylationPQSSSSGTDLTGDKA
CCCCCCCCCCCCCCC		29.7722199227
1249PhosphorylationSSSGTDLTGDKAGPS
CCCCCCCCCCCCCCC		46.2622199227
1256PhosphorylationTGDKAGPSAQEPGSQ
CCCCCCCCCCCCCCC		41.4929396449
1262PhosphorylationPSAQEPGSQTPLKSM
CCCCCCCCCCCCCEE		41.4129255136
1264PhosphorylationAQEPGSQTPLKSMLV
CCCCCCCCCCCEEEE		32.0829255136
1290PhosphorylationMGDEGGESELLGEDL
CCCCCCCCCCCCCCC		36.50-
1291 (in isoform 4)Ubiquitination-43.6521890473
1295 (in isoform 2)Ubiquitination-57.2421890473
1302PhosphorylationEDLPLEPSVTKAERS
CCCCCCCCCCHHHHH		32.8026657352
1304PhosphorylationLPLEPSVTKAERSHL
CCCCCCCCHHHHHCE		28.9528857561
1305UbiquitinationPLEPSVTKAERSHLI
CCCCCCCHHHHHCEE		46.2021906983
1305 (in isoform 1)Ubiquitination-46.2021890473
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
586TPhosphorylationKinaseCDK2P24941
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of JIP4_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 JIP4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MAX_HUMANMAXphysical
12391307
MK08_HUMANMAPK8physical
12391307
MK14_HUMANMAPK14physical
12391307
MP2K4_HUMANMAP2K4physical
12391307
M3K3_HUMANMAP3K3physical
12391307
NDRG1_HUMANNDRG1physical
22939629
NENF_HUMANNENFphysical
22939629
CD2AP_HUMANCD2APphysical
22863883
HUWE1_HUMANHUWE1physical
22863883
LARP7_HUMANLARP7physical
22863883
NOLC1_HUMANNOLC1physical
22863883
RABE2_HUMANRABEP2physical
22863883
TXND9_HUMANTXNDC9physical
22863883
ABL1_HUMANABL1physical
19470755
UBP15_HUMANUSP15physical
27173435
MCM2_HUMANMCM2physical
27173435
MCM4_HUMANMCM4physical
27173435
MCM6_HUMANMCM6physical
27173435
NS1BP_HUMANIVNS1ABPphysical
27173435
SMC1A_HUMANSMC1Aphysical
27173435
GAPD1_HUMANGAPVD1physical
27173435
ANK3_HUMANANK3physical
27173435
SMC3_HUMANSMC3physical
27173435
SBNO1_HUMANSBNO1physical
27173435
SOX4_HUMANSOX4physical
27173435
PP4R2_HUMANPPP4R2physical
27173435
HSF1_HUMANHSF1physical
27173435
K1468_HUMANKIAA1468physical
27173435
MCM7_HUMANMCM7physical
27173435
PLK1_HUMANPLK1physical
27173435
ATG2B_HUMANATG2Bphysical
27173435
P4R3A_HUMANSMEK1physical
27173435
WEE1_HUMANWEE1physical
27173435
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 JIP4_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 MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-226; SER-265; SER-268; THR-276; SER-728;SER-730; SER-733 AND THR-1264, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-203; THR-217 ANDSER-733, AND MASS 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 MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-226; SER-265; SER-268; THR-276; SER-728;SER-730; SER-733 AND THR-1264, AND MASS SPECTROMETRY.
"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 SER-183; SER-185; SER-203;THR-217; SER-238; SER-311; SER-329; SER-332; THR-418; THR-586; SER-733AND SER-1144, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND SER-185, ANDMASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-265; SER-268;THR-418 AND SER-730, AND MASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-594 AND THR-595, 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-183; SER-185; SER-203;THR-217; SER-387; SER-388 AND SER-391, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-730 AND SER-733, ANDMASS SPECTROMETRY.
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry.";
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.;
Anal. Chem. 76:2763-2772(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-732 AND SER-733, ANDMASS SPECTROMETRY.

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