JIP4_MOUSE - dbPTM
JIP4_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID JIP4_MOUSE
UniProt AC Q58A65
Protein Name C-Jun-amino-terminal kinase-interacting protein 4
Gene Name Spag9
Organism Mus musculus (Mouse).
Sequence Length 1321
Subcellular Localization Cytoplasm. Cytoplasm, perinuclear region. Perinuclear distribution in response to stress signals such as UV radiation.
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..
Protein Sequence MELEDGVVYQEEPGGSGAVMSERVSGLAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLERTKLHQLSGSDQLEATAHSRIRKERPISLGIFPLPAGDGLLTPDTQKGGETPGSEQWKFQELSQPRSHTSLKVSHSPEPPKAVEQEDELSDISQGGSKATTPASTANSDVSAIPPDTPSKEDNEGFVKGTDTSNKSEISKHIEVQVAQETRNVSTESGENEEKSEVQAIIESTPELDMDKDLSGYKGSSTPTKGIENKAFDRNTESLFEELSSAGSGLIGDVDEGADLLGMGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKRSSIWQFFSRLFSSSSNATKKPEPPVNLKYNAPTSHVTPSVKKRSSTLSQLPGDKSKAFDFLSEETEASLASRREQKREQYRQVKAHVQKEDGRVQAFGWSLPQKYKQVANGQGETKMKNLPVPVYLRPLDEKDASMKLWCAVGVNLSGGKTRDGGSVVGASVFYKDIAGLDTEGSKQRSASQSSLDKLDQELKEQQKEFKNQEELSSQVWICTSTHSTTKVIIIDAVQPGNILDSFTVCNSHVLCIASVPGARETDYPAGEELSESGQVDKASLCGSMTSNSSAEMDSLLGGITVVGCSTEGLTGAATSPSTNGASPVIEKPPEMETENSEVDENIPTAEEATEATEGNAGSTEDTVDISQPGVYTEHVFTDPLGVQIPEDLSPVFQSSNDSDVYKDQISVLPNEQDLAREEAQKMSSLLPTMWLGAQNGCLYVHSSVAQWRKCLHSIKLKDSILSIVHVKGIVLVALADGTLAIFHRGVDGQWDLSNYHLLDLGRPHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVSIRLDSTLRLYHAHTYQHLQDVDIEPYVSKMLGTGKLGFSFVRITALMVSCNRLWVGTGNGVIISIPLTETNKTSGTPGNRPGSVIRVYGDENSDKVTPGTFIPYCSMAHAQLCFHGHRDAVKFFVAVPGQVISPQSSSGGADLTADKAGSSAQEPSSQTPLKSMLVISGGEGYIDFRMGDEGGESELLGEDLPLEPSVTKAERSHLIVWQVMCGNE
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		52.12-
25PhosphorylationAVMSERVSGLAGSIY
CHHCHHHHCHHHHHH		34.0218779572
30PhosphorylationRVSGLAGSIYREFER
HHHCHHHHHHHHHHH		15.7329176673
55 (in isoform 3)Ubiquitination-3.93-
60 (in isoform 3)Phosphorylation-45.0129514104
60 (in isoform 4)Phosphorylation-45.0129514104
73 (in isoform 6)Phosphorylation-11.0629514104
77 (in isoform 6)Phosphorylation-8.1127742792
79 (in isoform 6)Phosphorylation-62.9627742792
80 (in isoform 6)Phosphorylation-64.1625266776
86 (in isoform 6)Phosphorylation-1.9529514104
89 (in isoform 6)Phosphorylation-14.3325521595
93 (in isoform 6)Phosphorylation-59.9725521595
95 (in isoform 3)Phosphorylation-12.7229514104
95 (in isoform 4)Phosphorylation-12.7229514104
99 (in isoform 3)Phosphorylation-29.6727742792
99 (in isoform 4)Phosphorylation-29.6727742792
101 (in isoform 3)Phosphorylation-54.7927742792
101 (in isoform 4)Phosphorylation-54.7927742792
102 (in isoform 3)Phosphorylation-43.0525266776
102 (in isoform 4)Phosphorylation-43.0525266776
108 (in isoform 3)Phosphorylation-62.0229514104
108 (in isoform 4)Phosphorylation-62.0229514104
109PhosphorylationKFIEFEDSQEQEKKD
HCCCCCCCHHHHHHH		28.5526824392
111 (in isoform 3)Phosphorylation-65.7425521595
111 (in isoform 4)Phosphorylation-65.7425521595
115 (in isoform 3)Phosphorylation-64.0225521595
115 (in isoform 4)Phosphorylation-64.0225521595
178UbiquitinationMEHLERTKLHQLSGS
HHHHHHHCHHHCCCC		50.63-
183PhosphorylationRTKLHQLSGSDQLEA
HHCHHHCCCCHHHHH		29.6726824392
185PhosphorylationKLHQLSGSDQLEATA
CHHHCCCCHHHHHHH		20.8622942356
191PhosphorylationGSDQLEATAHSRIRK
CCHHHHHHHHHHHCC		18.6125619855
194PhosphorylationQLEATAHSRIRKERP
HHHHHHHHHHCCCCC		27.2629514104
198UbiquitinationTAHSRIRKERPISLG
HHHHHHCCCCCCEEE		56.56-
198 (in isoform 5)Ubiquitination-56.56-
203PhosphorylationIRKERPISLGIFPLP
HCCCCCCEEEEEEEC		24.1927087446
203 (in isoform 2)Phosphorylation-24.1924719451
203 (in isoform 5)Phosphorylation-24.1929514104
217PhosphorylationPAGDGLLTPDTQKGG
CCCCCCCCCCCCCCC		24.9425521595
220PhosphorylationDGLLTPDTQKGGETP
CCCCCCCCCCCCCCC		33.1222942356
226PhosphorylationDTQKGGETPGSEQWK
CCCCCCCCCCCHHCC		35.9025521595
229PhosphorylationKGGETPGSEQWKFQE
CCCCCCCCHHCCEEE		28.0226160508
233UbiquitinationTPGSEQWKFQELSQP
CCCCHHCCEEECCCC		36.54-
233 (in isoform 2)Ubiquitination-36.54-
238PhosphorylationQWKFQELSQPRSHTS
HCCEEECCCCCCCCC		37.0727149854
238 (in isoform 2)Phosphorylation-37.0729514104
238 (in isoform 5)Phosphorylation-37.0729514104
242PhosphorylationQELSQPRSHTSLKVS
EECCCCCCCCCEEEE		37.4926060331
242 (in isoform 2)Phosphorylation-37.4927742792
242 (in isoform 5)Phosphorylation-37.4927742792
244PhosphorylationLSQPRSHTSLKVSHS
CCCCCCCCCEEEECC		36.6817242355
244 (in isoform 2)Phosphorylation-36.6827742792
244 (in isoform 5)Phosphorylation-36.6827742792
245 (in isoform 2)Phosphorylation-22.2925266776
245 (in isoform 5)Phosphorylation-22.2925266776
251PhosphorylationTSLKVSHSPEPPKAV
CCEEEECCCCCCCCC		24.37-
251 (in isoform 2)Phosphorylation-24.3729514104
251 (in isoform 5)Phosphorylation-24.3729514104
254 (in isoform 2)Phosphorylation-38.7925521595
254 (in isoform 5)Phosphorylation-38.7925521595
258 (in isoform 2)Phosphorylation-11.0125521595
258 (in isoform 5)Phosphorylation-11.0125521595
265PhosphorylationVEQEDELSDISQGGS
CCCCHHHHCCCCCCC		30.7429550500
268PhosphorylationEDELSDISQGGSKAT
CHHHHCCCCCCCCCC		27.9723737553
272PhosphorylationSDISQGGSKATTPAS
HCCCCCCCCCCCCCC		26.4127180971
275PhosphorylationSQGGSKATTPASTAN
CCCCCCCCCCCCCCC		36.7325619855
276PhosphorylationQGGSKATTPASTANS
CCCCCCCCCCCCCCC		23.0125619855
279PhosphorylationSKATTPASTANSDVS
CCCCCCCCCCCCCCC		29.2925619855
280PhosphorylationKATTPASTANSDVSA
CCCCCCCCCCCCCCC		31.7825619855
283PhosphorylationTPASTANSDVSAIPP
CCCCCCCCCCCCCCC		36.6025619855
286PhosphorylationSTANSDVSAIPPDTP
CCCCCCCCCCCCCCC		26.0225619855
292PhosphorylationVSAIPPDTPSKEDNE
CCCCCCCCCCCCCCC		34.9225521595
294PhosphorylationAIPPDTPSKEDNEGF
CCCCCCCCCCCCCCC		51.2525619855
311PhosphorylationGTDTSNKSEISKHIE
CCCCCCHHHHHHHEE		44.40-
325PhosphorylationEVQVAQETRNVSTES
EEEEEEECCCCCCCC		18.5728066266
329PhosphorylationAQETRNVSTESGENE
EEECCCCCCCCCCCH		29.9727087446
330PhosphorylationQETRNVSTESGENEE
EECCCCCCCCCCCHH		29.8627087446
332PhosphorylationTRNVSTESGENEEKS
CCCCCCCCCCCHHHH		52.0425521595
334 (in isoform 2)Phosphorylation-71.41-
339PhosphorylationSGENEEKSEVQAIIE
CCCCHHHHHHHHHHH		46.4025168779
347PhosphorylationEVQAIIESTPELDMD
HHHHHHHCCCCCCCC		38.5623984901
348PhosphorylationVQAIIESTPELDMDK
HHHHHHCCCCCCCCC		14.1625168779
351 (in isoform 2)Phosphorylation-7.52-
358PhosphorylationLDMDKDLSGYKGSST
CCCCCCCCCCCCCCC		50.6526745281
360PhosphorylationMDKDLSGYKGSSTPT
CCCCCCCCCCCCCCC		14.5925168779
363PhosphorylationDLSGYKGSSTPTKGI
CCCCCCCCCCCCCCC		27.2126745281
364PhosphorylationLSGYKGSSTPTKGIE
CCCCCCCCCCCCCCC		47.2626745281
365PhosphorylationSGYKGSSTPTKGIEN
CCCCCCCCCCCCCCC		36.3527149854
367PhosphorylationYKGSSTPTKGIENKA
CCCCCCCCCCCCCCC		41.8326745281
418PhosphorylationENLILENTQLLETKN
HHHHHHCHHHHCHHH		15.9528066266
493PhosphorylationKAKDDDDSDIPTAQR
HCCCCCCCCCCHHHH		44.4223684622
505MethylationAQRKRFTRVEMARVL
HHHHHHHHHHHHHHH		21.4918959235
538PhosphorylationWTEMIRASRENPAMQ
HHHHHHHHCCCHHHH		30.2223737553
550PhosphorylationAMQEKKRSSIWQFFS
HHHHHHHHHHHHHHH		34.7528059163
551PhosphorylationMQEKKRSSIWQFFSR
HHHHHHHHHHHHHHH		31.7027600695
557PhosphorylationSSIWQFFSRLFSSSS
HHHHHHHHHHHCCCC		29.3928059163
561PhosphorylationQFFSRLFSSSSNATK
HHHHHHHCCCCCCCC		33.6228725479
562PhosphorylationFFSRLFSSSSNATKK
HHHHHHCCCCCCCCC		30.3729176673
563PhosphorylationFSRLFSSSSNATKKP
HHHHHCCCCCCCCCC		26.8117203969
567PhosphorylationFSSSSNATKKPEPPV
HCCCCCCCCCCCCCC		43.8017203969
578PhosphorylationEPPVNLKYNAPTSHV
CCCCCCEECCCCCCC		21.5229514104
582PhosphorylationNLKYNAPTSHVTPSV
CCEECCCCCCCCCCH		29.1125367039
583PhosphorylationLKYNAPTSHVTPSVK
CEECCCCCCCCCCHH		18.2023984901
586PhosphorylationNAPTSHVTPSVKKRS
CCCCCCCCCCHHHCC		12.3826824392
588PhosphorylationPTSHVTPSVKKRSST
CCCCCCCCHHHCCCC		36.8829472430
593PhosphorylationTPSVKKRSSTLSQLP
CCCHHHCCCCHHCCC		36.2327742792
594PhosphorylationPSVKKRSSTLSQLPG
CCHHHCCCCHHCCCC		37.0825521595
595PhosphorylationSVKKRSSTLSQLPGD
CHHHCCCCHHCCCCC		31.5125521595
597PhosphorylationKKRSSTLSQLPGDKS
HHCCCCHHCCCCCHH		29.7422324799
604PhosphorylationSQLPGDKSKAFDFLS
HCCCCCHHHHHHHHC		33.6830635358
653AcetylationFGWSLPQKYKQVANG
CCCCCCHHHHHHHCC		53.1023806337
700PhosphorylationVNLSGGKTRDGGSVV
EECCCCCCCCCCCEE		36.9523984901
705PhosphorylationGKTRDGGSVVGASVF
CCCCCCCCEEEEEEE		21.1125521595
710PhosphorylationGGSVVGASVFYKDIA
CCCEEEEEEEEHHHC		13.5628833060
719 (in isoform 2)Phosphorylation-5.6424719451
728PhosphorylationTEGSKQRSASQSSLD
CCCHHHHCCCHHHHH		29.7627087446
730PhosphorylationGSKQRSASQSSLDKL
CHHHHCCCHHHHHHH		31.6627087446
732PhosphorylationKQRSASQSSLDKLDQ
HHHCCCHHHHHHHHH		30.3027087446
733PhosphorylationQRSASQSSLDKLDQE
HHCCCHHHHHHHHHH		32.7127087446
766PhosphorylationWICTSTHSTTKVIII
EEEECCCCCCEEEEE		37.5522871156
804PhosphorylationSVPGARETDYPAGEE
ECCCCCCCCCCCCCC		34.9719655815
806PhosphorylationPGARETDYPAGEELS
CCCCCCCCCCCCCCC		11.4719655815
813PhosphorylationYPAGEELSESGQVDK
CCCCCCCCCCCCCCC		32.7525619855
815PhosphorylationAGEELSESGQVDKAS
CCCCCCCCCCCCCHH		31.0227742792
941PhosphorylationVFQSSNDSDVYKDQI
HCCCCCCCCHHHHHH		32.9723649490
949PhosphorylationDVYKDQISVLPNEQD
CHHHHHHCCCCCHHH		16.3923649490
1044 (in isoform 4)Phosphorylation-40.5229514104
1110PhosphorylationWVSIRLDSTLRLYHA
EEEEEECCEEEEEEC		33.6527149854
1174 (in isoform 2)Phosphorylation-59.0524719451
1181PhosphorylationETNKTSGTPGNRPGS
CCCCCCCCCCCCCCC		27.9925338131
1188PhosphorylationTPGNRPGSVIRVYGD
CCCCCCCCEEEEECC		19.6326824392
1227UbiquitinationHGHRDAVKFFVAVPG
CCCCCCEEEEEECCC		34.50-
1238PhosphorylationAVPGQVISPQSSSGG
ECCCCEECCCCCCCC		20.3120415495
1264PhosphorylationAQEPSSQTPLKSMLV
CCCCCCCCCCCEEEE		32.32-
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
351TPhosphorylationKinasePLK1P53350
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of JIP4_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FYV1_MOUSEPikfyvephysical
19056739
MK08_MOUSEMapk8physical
15767678
M3K5_MOUSEMap3k5physical
15767678
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of JIP4_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND SER-730, ANDMASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-244; THR-292 ANDSER-733, AND MASS SPECTROMETRY.
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-730 AND SER-733, ANDMASS SPECTROMETRY.
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-217 AND THR-365, ANDMASS SPECTROMETRY.

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