JIP3_MOUSE - dbPTM
JIP3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID JIP3_MOUSE
UniProt AC Q9ESN9
Protein Name C-Jun-amino-terminal kinase-interacting protein 3
Gene Name Mapk8ip3
Organism Mus musculus (Mouse).
Sequence Length 1337
Subcellular Localization Cytoplasm. Golgi apparatus. Cytoplasmic vesicle. Cell projection, growth cone. Localized in the soma and growth cones of differentiated neurites and the Golgi and vesicles of the early secretory compartment of epithelial cells.
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. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins..
Protein Sequence MMEIQMDEGGGVVVYQDDYCSGSVMSERVSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQVGGSGQTESSLPGRSRKERPTSLNVFPLADGMVRAQMGGKLVPAGDHWHLSDLGQLQSSSSYQCPNDEMSESGQSSAAATPSTTGTKSNTPTSSVPSAAVTPLNESLQPLGDYVSVTKNNKQAREKRNSRNMEVQVTQEMRNVSIGMGSSDEWSDVQDIIDSTPELDVCPETRLERTGSSPTQGIVNKAFGINTDSLYHELSTAGSEVIGDVDEGADLLGEFSVRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTARREPREEVEDVSSYLCTELDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKKSTIWQFFSRLFSSSSSPPPAKRSYPSVNIHYKSPTAAGFSQRRSHALCQISAGSRPLEFFPDDDCTSSARREQKREQYRQVREHVRNDDGRLQACGWSLPAKYKQLSPNGGQEDTRMKNVPVPVYCRPLVEKDPSTKLWCAAGVNLSGWKPHEEDSSNGPKPVPGRDPLTCDREGEGEPKSTHPSPEKKKAKETPEADATSSRVWILTSTLTTSKVVIIDANQPGTIVDQFTVCNAHVLCISSIPAASDSDYPPGEMFLDSDVNPEDSGADGVLAGITLVGCATRCNVPRSNCSSRGDTPVLDKGQGDVATTANGKVNPSQSTEEATEATEVPDPGPSESEATTVRPGPLTEHVFTDPAPTPSSSTQPASENGSESNGTIVQPQVEPSGELSTTTSSAAPTMWLGAQNGWLYVHSAVANWKKCLHSIKLKDSVLSLVHVKGRVLVALADGTLAIFHRGEDGQWDLSNYHLMDLGHPHHSIRCMAVVNDRVWCGYKNKVHVIQPKTMQIEKSFDAHPRRESQVRQLAWIGDGVWVSIRLDSTLRLYHAHTHQHLQDVDIEPYVSKMLGTGKLGFSFVRITALLIAGNRLWVGTGNGVVISIPLTETVVLHRGQLLGLRANKTSPTSGEGTRPGGIIHVYGDDSSDKAASSFIPYCSMAQAQLCFHGHRDAVKFFVSVPGNVLATLNGSVLDSPSEGPGPAAPAADAEGQKLKNALVLSGGEGYIDFRIGDGEDDETEECAGDVNQTKPSLSKAERSHIIVWQVSYTPE
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
30PhosphorylationSVMSERVSGLAGSIY
CHHHHHHHHHHHHHH		34.0229176673
35PhosphorylationRVSGLAGSIYREFER
HHHHHHHHHHHHHHH		15.7329176673
148PhosphorylationKNYADQISRLEERES
HHHHHHHHHHHHHHH		25.77-
155PhosphorylationSRLEERESEMKKEYN
HHHHHHHHHHHHHHH		49.57-
183 (in isoform 6)Ubiquitination-47.1222790023
183UbiquitinationVEHIERSKMQQVGGS
HHHHHHHHCCCCCCC		47.1222790023
196 (in isoform 6)Phosphorylation-32.1428066266
196 (in isoform 3)Phosphorylation-32.1428066266
201 (in isoform 6)Phosphorylation-54.3326239621
201 (in isoform 3)Phosphorylation-54.3326239621
207PhosphorylationRSRKERPTSLNVFPL
CCCCCCCCCCEEEEC		52.6626239621
208PhosphorylationSRKERPTSLNVFPLA
CCCCCCCCCEEEECC		22.1926239621
216 (in isoform 6)Phosphorylation-54.1026824392
266PhosphorylationGQSSAAATPSTTGTK
CCCCCCCCCCCCCCC		17.0410629060
274PhosphorylationPSTTGTKSNTPTSSV
CCCCCCCCCCCCCCC		45.8626643407
276PhosphorylationTTGTKSNTPTSSVPS
CCCCCCCCCCCCCCC		34.7310629060
278PhosphorylationGTKSNTPTSSVPSAA
CCCCCCCCCCCCCCE		31.4326643407
279PhosphorylationTKSNTPTSSVPSAAV
CCCCCCCCCCCCCEE		30.4626643407
280PhosphorylationKSNTPTSSVPSAAVT
CCCCCCCCCCCCEEC		40.2926643407
283PhosphorylationTPTSSVPSAAVTPLN
CCCCCCCCCEECCCC		27.0626643407
287PhosphorylationSVPSAAVTPLNESLQ
CCCCCEECCCCCCCC		19.8210629060
315PhosphorylationQAREKRNSRNMEVQV
HHHHHHHHCCCEEEE		29.1226643407
330PhosphorylationTQEMRNVSIGMGSSD
EHHHHCCCCCCCCCC		19.5820415495
335PhosphorylationNVSIGMGSSDEWSDV
CCCCCCCCCCCHHCH		26.2320415495
336PhosphorylationVSIGMGSSDEWSDVQ
CCCCCCCCCCHHCHH		33.5420415495
340PhosphorylationMGSSDEWSDVQDIID
CCCCCCHHCHHHHHH		26.3420415495
363PhosphorylationPETRLERTGSSPTQG
CCCCCCCCCCCCCCC		31.8524925903
365PhosphorylationTRLERTGSSPTQGIV
CCCCCCCCCCCCCHH		32.3125521595
366PhosphorylationRLERTGSSPTQGIVN
CCCCCCCCCCCCHHH		33.0525521595
368PhosphorylationERTGSSPTQGIVNKA
CCCCCCCCCCHHHHH		41.1825521595
429PhosphorylationGNLLLENSQLLETKN
HHHHHHHHHHCCHHH		16.9028066266
434PhosphorylationENSQLLETKNALNVV
HHHHHCCHHHHHHHH		29.5728066266
435 (in isoform 6)Ubiquitination-30.7422790023
435UbiquitinationNSQLLETKNALNVVK
HHHHCCHHHHHHHHH		30.7422790023
443 (in isoform 6)Ubiquitination-37.40-
582PhosphorylationQFFSRLFSSSSSPPP
HHHHHHHCCCCCCCC		33.6226239621
583PhosphorylationFFSRLFSSSSSPPPA
HHHHHHCCCCCCCCC		27.2324925903
584PhosphorylationFSRLFSSSSSPPPAK
HHHHHCCCCCCCCCC		33.3726239621
585PhosphorylationSRLFSSSSSPPPAKR
HHHHCCCCCCCCCCC		49.1424925903
586PhosphorylationRLFSSSSSPPPAKRS
HHHCCCCCCCCCCCC		43.2925521595
596PhosphorylationPAKRSYPSVNIHYKS
CCCCCCCCCEEEECC		21.40-
601PhosphorylationYPSVNIHYKSPTAAG
CCCCEEEECCCCCCC		14.9023608596
603PhosphorylationSVNIHYKSPTAAGFS
CCEEEECCCCCCCCC		21.9523684622
605PhosphorylationNIHYKSPTAAGFSQR
EEEECCCCCCCCCCC		35.9123684622
610PhosphorylationSPTAAGFSQRRSHAL
CCCCCCCCCCCCCEE		23.1227149854
614PhosphorylationAGFSQRRSHALCQIS
CCCCCCCCCEEEEEC		18.4628066266
648PhosphorylationREQKREQYRQVREHV
HHHHHHHHHHHHHHH		9.77-
677PhosphorylationPAKYKQLSPNGGQED
CCCCCCCCCCCCCCC		17.5225521595
695PhosphorylationKNVPVPVYCRPLVEK
CCCCCCEEECCCCCC		4.08-
751PhosphorylationEGEGEPKSTHPSPEK
CCCCCCCCCCCCHHH		42.5421183079
752PhosphorylationGEGEPKSTHPSPEKK
CCCCCCCCCCCHHHH		43.8827841257
755PhosphorylationEPKSTHPSPEKKKAK
CCCCCCCCHHHHHCC		37.7824899341
764PhosphorylationEKKKAKETPEADATS
HHHHCCCCCCCCCCC		26.2325521595
770PhosphorylationETPEADATSSRVWIL
CCCCCCCCCCCEEEE		27.9929899451
861PhosphorylationTRCNVPRSNCSSRGD
HHCCCCCCCCCCCCC		35.8029899451
864PhosphorylationNVPRSNCSSRGDTPV
CCCCCCCCCCCCCCC		27.5921183079
865PhosphorylationVPRSNCSSRGDTPVL
CCCCCCCCCCCCCCC		42.3525521595
869PhosphorylationNCSSRGDTPVLDKGQ
CCCCCCCCCCCCCCC		20.3725521595
1038PhosphorylationGQWDLSNYHLMDLGH
CCEECCCCEECCCCC		7.9222871156
1049PhosphorylationDLGHPHHSIRCMAVV
CCCCCCCEEEEEEEE		14.5422871156
1110PhosphorylationWVSIRLDSTLRLYHA
EEEEEECCEEEEEEC		33.6527149854
1191PhosphorylationLGLRANKTSPTSGEG
EEEECCCCCCCCCCC		39.4825521595
1192PhosphorylationGLRANKTSPTSGEGT
EEECCCCCCCCCCCC		27.9924925903
1194PhosphorylationRANKTSPTSGEGTRP
ECCCCCCCCCCCCCC		49.4826643407
1195PhosphorylationANKTSPTSGEGTRPG
CCCCCCCCCCCCCCC		37.9326643407
1199PhosphorylationSPTSGEGTRPGGIIH
CCCCCCCCCCCEEEE		29.4126643407
1208PhosphorylationPGGIIHVYGDDSSDK
CCEEEEEECCCCCCH		10.7324925903
1212PhosphorylationIHVYGDDSSDKAASS
EEEECCCCCCHHHHC		45.2224925903
1213PhosphorylationHVYGDDSSDKAASSF
EEECCCCCCHHHHCC		50.5624925903
1245PhosphorylationDAVKFFVSVPGNVLA
CCEEEEEECCCCEEE		19.8920415495
1253PhosphorylationVPGNVLATLNGSVLD
CCCCEEEEECCCCCC		19.3220415495
1257PhosphorylationVLATLNGSVLDSPSE
EEEEECCCCCCCCCC		20.5920415495
1261PhosphorylationLNGSVLDSPSEGPGP
ECCCCCCCCCCCCCC		26.6019060867
1263PhosphorylationGSVLDSPSEGPGPAA
CCCCCCCCCCCCCCC		60.1720415495
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
266TPhosphorylationKinaseMAPK8P45983
GPS
266TPhosphorylationKinaseMAPK-Uniprot
276TPhosphorylationKinaseMAPK8P45983
GPS
276TPhosphorylationKinaseMAPK-Uniprot
287TPhosphorylationKinaseMAPK8P45983
GPS
287TPhosphorylationKinaseMAPK-Uniprot
315SPhosphorylationKinaseROCK1P70335
Uniprot
365SPhosphorylationKinaseROCK1P70335
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of JIP3_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 JIP3_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MK08_MOUSEMapk8physical
15767678
M3K5_MOUSEMap3k5physical
15767678
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of JIP3_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677, AND MASSSPECTROMETRY.
"Interaction of a mitogen-activated protein kinase signaling modulewith the neuronal protein JIP3.";
Kelkar N., Gupta S., Dickens M., Davis R.J.;
Mol. Cell. Biol. 20:1030-1043(2000).
Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS 1C AND 3A), FUNCTION, INDUCTION, TISSUESPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-266; THR-276AND THR-287, MUTAGENESIS OF ARG-205; PRO-206; THR-207; SER-208;LEU-209; THR-266; THR-276 AND THR-287, AND INTERACTION WITH MAPK8IP2;MAPK8; MAPK9; MAPK10; MAP2K7 AND MAP3K11.
"JSAP1, a novel jun N-terminal protein kinase (JNK)-binding proteinthat functions as a scaffold factor in the JNK signaling pathway.";
Ito M., Yoshioka K., Akechi M., Yamashita S., Takamatsu N.,Sugiyama K., Hibi M., Nakabeppu Y., Shiba T., Yamamoto K.;
Mol. Cell. Biol. 19:7539-7548(1999).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A), FUNCTION, PHOSPHORYLATION,AND INTERACTION WITH MAPK8; MAPK9; MAPK10; MAP2K4 AND MAP3K1.

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