JIP1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: JIP1_MOUSE
• UniProt AC: Q9WVI9
• Protein Name: C-Jun-amino-terminal kinase-interacting protein 1
• Gene Name: Mapk8ip1
• Organism: Mus musculus (Mouse).
• Sequence Length: 707
• Subcellular Localization: Cytoplasm. Cytoplasm, perinuclear region. Nucleus. Endoplasmic reticulum membrane. Mitochondrion membrane. Accumulates in cell surface projections. Under certain stress conditions, translocates to the perinuclear region of neurons. In insulin-secreti
• 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. Required for JNK activation in response to excitotoxic stress. Cytoplasmic MAPK8IP1 causes inhibition of JNK-regulated activity by retaining JNK in the cytoplasm and thus inhibiting the JNK phosphorylation of c-Jun. May also participate in ApoER2-specific reelin signaling. Directly, or indirectly, regulates GLUT2 gene expression and beta-cell function. Appears to have a role in cell signaling in mature and developing nerve terminals. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins. Functions as an anti-apoptotic protein and whose level seems to influence the beta-cell death or survival response (By similarity)..
• Protein Sequence: MAERESGLGGGAASPPAASPFLGLHIASPPNFRLTHDISLEEFEDEDLSEITDECGISLQCKDTLSLRPPRAGLLSAGSSGSAGSRLQAEMLQMDLIDAAGDTPGAEDDEEEEDDELAAQRPGVGPPKAESNQDPAPRSQGQGPGTGSGDTYRPKRPTTLNLFPQVPRSQDTLNNNSLGKKHSWQDRVSRSSSPLKTGEQTPPHEHICLSDELPPQGSPVPTQDRGTSTDSPCRRSAATQMAPPSGPPATAPGGRGHSHRDRIHYQADVRLEATEEIYLTPVQRPPDPAEPTSTFMPPTESRMSVSSDPDPAAYSVTAGRPHPSISEEDEGFDCLSSPERAEPPGGGWRGSLGEPPPPPRASLSSDTSALSYDSVKYTLVVDEHAQLELVSLRPCFGDYSDESDSATVYDNCASASSPYESAIGEEYEEAPQPRPPTCLSEDSTPDEPDVHFSKKFLNVFMSGRSRSSSAESFGLFSCVINGEEHEQTHRAIFRFVPRHEDELELEVDDPLLVELQAEDYWYEAYNMRTGARGVFPAYYAIEVTKEPEHMAALAKNSDWIDQFRVKFLGSVQVPYHKGNDVLCAAMQKIATTRRLTVHFNPPSSCVLEISVRGVKIGVKADDALEAKGNKCSHFFQLKNISFCGYHPKNNKYFGFITKHPADHRFACHVFVSEDSTKALAESVGRAFQQFYKQFVEYTCPTEDIYLE

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
6	Phosphorylation	--MAERESGLGGGAA --CCCCCCCCCCCCC	45.60	24759943
14	Phosphorylation	GLGGGAASPPAASPF CCCCCCCCCCCCCCC	30.77	24925903
19	Phosphorylation	AASPPAASPFLGLHI CCCCCCCCCCCCEEE	20.49	24925903
28	Phosphorylation	FLGLHIASPPNFRLT CCCEEECCCCCEEEC	40.04	24925903
35	Phosphorylation	SPPNFRLTHDISLEE CCCCEEECCCCCHHH	17.16	29899451
39	Phosphorylation	FRLTHDISLEEFEDE EEECCCCCHHHHCCC	35.47	-
103	Phosphorylation	LIDAAGDTPGAEDDE HHHHCCCCCCCCCCC	23.78	-
148	Phosphorylation	GQGPGTGSGDTYRPK CCCCCCCCCCCCCCC	33.08	-
177	Phosphorylation	QDTLNNNSLGKKHSW CCCCCCCCCCCCCCH	40.39	25521595
183	Phosphorylation	NSLGKKHSWQDRVSR CCCCCCCCHHHHHCC	35.00	-
189	Phosphorylation	HSWQDRVSRSSSPLK CCHHHHHCCCCCCCC	27.60	-
191	Phosphorylation	WQDRVSRSSSPLKTG HHHHHCCCCCCCCCC	27.88	-
192	Phosphorylation	QDRVSRSSSPLKTGE HHHHCCCCCCCCCCC	34.56	-
201	Phosphorylation	PLKTGEQTPPHEHIC CCCCCCCCCCCCCEE	34.19	-
210	Phosphorylation	PHEHICLSDELPPQG CCCCEECCCCCCCCC	25.32	-
229	Phosphorylation	TQDRGTSTDSPCRRS CCCCCCCCCCCCHHH	40.09	29899451
231	Phosphorylation	DRGTSTDSPCRRSAA CCCCCCCCCCHHHHC	26.45	29899451
239	Phosphorylation	PCRRSAATQMAPPSG CCHHHHCCCCCCCCC	20.70	29899451
250	Phosphorylation	PPSGPPATAPGGRGH CCCCCCCCCCCCCCC	38.88	24719451
278	Phosphorylation	LEATEEIYLTPVQRP EEEECEEEEECCCCC	14.06	-
280	Phosphorylation	ATEEIYLTPVQRPPD EECEEEEECCCCCCC	12.39	-
304	Phosphorylation	PPTESRMSVSSDPDP CCCCCCCCCCCCCCC	20.10	28066266
306	Phosphorylation	TESRMSVSSDPDPAA CCCCCCCCCCCCCHH	23.01	28066266
307	Phosphorylation	ESRMSVSSDPDPAAY CCCCCCCCCCCCHHH	51.51	28066266
314	Phosphorylation	SDPDPAAYSVTAGRP CCCCCHHHEECCCCC	13.04	28066266
315	Phosphorylation	DPDPAAYSVTAGRPH CCCCHHHEECCCCCC	14.31	28066266
324	Phosphorylation	TAGRPHPSISEEDEG CCCCCCCCCCCCCCC	35.39	-
326	Phosphorylation	GRPHPSISEEDEGFD CCCCCCCCCCCCCCC	38.99	-
336	Phosphorylation	DEGFDCLSSPERAEP CCCCCCCCCCCCCCC	50.61	28066266
337	Phosphorylation	EGFDCLSSPERAEPP CCCCCCCCCCCCCCC	20.17	22817900
351	Phosphorylation	PGGGWRGSLGEPPPP CCCCCCCCCCCCCCC	25.32	28066266
362	Phosphorylation	PPPPPRASLSSDTSA CCCCCCCCCCCCCCC	30.02	-
362	O-linked_Glycosylation	PPPPPRASLSSDTSA CCCCCCCCCCCCCCC	30.02	55753
365	Phosphorylation	PPRASLSSDTSALSY CCCCCCCCCCCCCCC	50.64	-
403	Phosphorylation	FGDYSDESDSATVYD CCCCCCCCCCCEEEC	41.68	-
405	Phosphorylation	DYSDESDSATVYDNC CCCCCCCCCEEECCC	34.81	-
407	Phosphorylation	SDESDSATVYDNCAS CCCCCCCEEECCCCC	24.45	-
409	Phosphorylation	ESDSATVYDNCASAS CCCCCEEECCCCCCC	9.33	-
417	Phosphorylation	DNCASASSPYESAIG CCCCCCCCCCHHHCC	31.08	-
427	Phosphorylation	ESAIGEEYEEAPQPR HHHCCCCHHCCCCCC	18.11	-
440	Phosphorylation	PRPPTCLSEDSTPDE CCCCCCCCCCCCCCC	41.31	-
443	Phosphorylation	PTCLSEDSTPDEPDV CCCCCCCCCCCCCCC	37.48	-
444	Phosphorylation	TCLSEDSTPDEPDVH CCCCCCCCCCCCCCC	47.26	-
465	Phosphorylation	NVFMSGRSRSSSAES HHHHCCCCCCCCHHH	39.79	-
467	Phosphorylation	FMSGRSRSSSAESFG HHCCCCCCCCHHHHC	29.86	-
468	Phosphorylation	MSGRSRSSSAESFGL HCCCCCCCCHHHHCC	32.24	-
469	Phosphorylation	SGRSRSSSAESFGLF CCCCCCCCHHHHCCE	36.98	-
592	Phosphorylation	AMQKIATTRRLTVHF HHHHHHCCCEEEEEC	12.55	24719451
652	Phosphorylation	YHPKNNKYFGFITKH EECCCCEEEEEEECC	15.85	28059163
657	Phosphorylation	NKYFGFITKHPADHR CEEEEEEECCCCCCC	22.50	28059163
682	Phosphorylation	STKALAESVGRAFQQ HHHHHHHHHHHHHHH	25.02	-

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
103	T	Phosphorylation	Kinase	MAPK8	Q91Y86	Uniprot
103	T	Phosphorylation	Kinase	MAPK9	Q9WTU6	Uniprot
103	T	Phosphorylation	Kinase	MAPK10	Q61831	Uniprot
201	T	Phosphorylation	Kinase	MAPK8	Q91Y86	Uniprot
201	T	Phosphorylation	Kinase	MAPK9	Q9WTU6	Uniprot
201	T	Phosphorylation	Kinase	MAPK10	Q61831	Uniprot
278	Y	Phosphorylation	Kinase	ABL-FAMILY	-	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
103	T	Phosphorylation	Phosphorylation on Thr-103 is also necessary for the dissociation and activation of MAP3K12.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of JIP1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
M3K7_MOUSE	Map3k7	physical	17709393
TAB1_MOUSE	Tab1	physical	17709393
MK08_MOUSE	Mapk8	physical	17709393

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.