dbPTM

JIP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	JIP1_HUMAN
UniProt AC	Q9UQF2
Protein Name	C-Jun-amino-terminal kinase-interacting protein 1
Gene Name	MAPK8IP1
Organism	Homo sapiens (Human).
Sequence Length	711
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 inhibiting 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 (By similarity). Functions as an anti-apoptotic protein and whose level seems to influence the beta-cell death or survival response..
Protein Sequence	MAERESGGLGGGAASPPAASPFLGLHIASPPNFRLTHDISLEEFEDEDLSEITDECGISLQCKDTLSLRPPRAGLLSAGGGGAGSRLQAEMLQMDLIDATGDTPGAEDDEEDDDEERAARRPGAGPPKAESGQEPASRGQGQSQGQSQGPGSGDTYRPKRPTTLNLFPQVPRSQDTLNNNSLGKKHSWQDRVSRSSSPLKTGEQTPPHEHICLSDELPPQSGPAPTTDRGTSTDSPCRRSTATQMAPPGGPPAAPPGGRGHSHRDRIHYQADVRLEATEEIYLTPVQRPPDAAEPTSAFLPPTESRMSVSSDPDPAAYPSTAGRPHPSISEEEEGFDCLSSPERAEPPGGGWRGSLGEPPPPPRASLSSDTSALSYDSVKYTLVVDEHAQLELVSLRPCFGDYSDESDSATVYDNCASVSSPYESAIGEEYEEAPRPQPPACLSEDSTPDEPDVHFSKKFLNVFMSGRSRSSSAESFGLFSCIINGEEQEQTHRAIFRFVPRHEDELELEVDDPLLVELQAEDYWYEAYNMRTGARGVFPAYYAIEVTKEPEHMAALAKNSDWVDQFRVKFLGSVQVPYHKGNDVLCAAMQKIATTRRLTVHFNPPSSCVLEISVRGVKIGVKADDSQEAKGNKCSHFFQLKNISFCGYHPKNNKYFGFITKHPADHRFACHVFVSEDSTKALAESVGRAFQQFYKQFVEYTCPTEDIYLE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MAERESGGLGGGA --CCCCCCCCCCCCC	44.36	23312004
15	Phosphorylation	GLGGGAASPPAASPF CCCCCCCCCCCCCCC	30.77	22817900
20	Phosphorylation	AASPPAASPFLGLHI CCCCCCCCCCCCEEE	20.49	23312004
29	Phosphorylation	FLGLHIASPPNFRLT CCCEEECCCCCEEEC	40.04	22817900
40	Phosphorylation	FRLTHDISLEEFEDE EEECCCCCHHHHCCC	35.47	22817900
67	Phosphorylation	LQCKDTLSLRPPRAG EEEECCCCCCCCCCE	25.15	24719451
86	Dimethylation	GGGGAGSRLQAEMLQ CCCCHHHHHHHHHHC	29.87	-
86	Methylation	GGGGAGSRLQAEMLQ CCCCHHHHHHHHHHC	29.87	24380957
100	Phosphorylation	QMDLIDATGDTPGAE CCCCHHCCCCCCCCC	31.66	-
103	Phosphorylation	LIDATGDTPGAEDDE CHHCCCCCCCCCCCC	25.60	22817900
128	Acetylation	RPGAGPPKAESGQEP CCCCCCCCCCCCCCC	68.84	30589565
152	Phosphorylation	GQSQGPGSGDTYRPK CCCCCCCCCCCCCCC	36.31	22817900
181	Phosphorylation	QDTLNNNSLGKKHSW CCCCCCCCCCCCCCH	40.39	22817900
187	Phosphorylation	NSLGKKHSWQDRVSR CCCCCCCCHHHHHCC	35.00	22817900
193	Phosphorylation	HSWQDRVSRSSSPLK CCHHHHHCCCCCCCC	27.60	22817900
195	Phosphorylation	WQDRVSRSSSPLKTG HHHHHCCCCCCCCCC	27.88	22817900
196	Phosphorylation	QDRVSRSSSPLKTGE HHHHCCCCCCCCCCC	34.56	22817900
197	Phosphorylation	DRVSRSSSPLKTGEQ HHHCCCCCCCCCCCC	35.18	22817900
201	Phosphorylation	RSSSPLKTGEQTPPH CCCCCCCCCCCCCCC	54.34	-
205	Phosphorylation	PLKTGEQTPPHEHIC CCCCCCCCCCCCCEE	34.19	22817900
214	Phosphorylation	PHEHICLSDELPPQS CCCCEECCCCCCCCC	25.32	22817900
231	Phosphorylation	APTTDRGTSTDSPCR CCCCCCCCCCCCCCC	29.37	22468782
233	Phosphorylation	TTDRGTSTDSPCRRS CCCCCCCCCCCCCCC	40.09	22468782
235	Phosphorylation	DRGTSTDSPCRRSTA CCCCCCCCCCCCCCC	26.45	22817900
240	Phosphorylation	TDSPCRRSTATQMAP CCCCCCCCCCCCCCC	11.75	-
241	Phosphorylation	DSPCRRSTATQMAPP CCCCCCCCCCCCCCC	31.73	-
243	Phosphorylation	PCRRSTATQMAPPGG CCCCCCCCCCCCCCC	20.97	-
284	Phosphorylation	ATEEIYLTPVQRPPD EECEEEEEECCCCCC	12.39	22817900
305	Phosphorylation	AFLPPTESRMSVSSD CCCCCCCCCCCCCCC	35.44	26074081
308	Phosphorylation	PPTESRMSVSSDPDP CCCCCCCCCCCCCCC	20.10	26074081
310	Phosphorylation	TESRMSVSSDPDPAA CCCCCCCCCCCCCCC	23.01	26074081
311	Phosphorylation	ESRMSVSSDPDPAAY CCCCCCCCCCCCCCC	51.51	26074081
328	Phosphorylation	TAGRPHPSISEEEEG CCCCCCCCCCCCCCC	35.39	30576142
330	Phosphorylation	GRPHPSISEEEEGFD CCCCCCCCCCCCCCC	43.20	30576142
340	Phosphorylation	EEGFDCLSSPERAEP CCCCCCCCCCCCCCC	50.61	29691806
341	Phosphorylation	EGFDCLSSPERAEPP CCCCCCCCCCCCCCC	20.17	20363803
355	Phosphorylation	PGGGWRGSLGEPPPP CCCCCCCCCCCCCCC	25.32	27732954
366	Phosphorylation	PPPPPRASLSSDTSA CCCCCCCCCCCCCCC	30.02	22817900
366	O-linked_Glycosylation	PPPPPRASLSSDTSA CCCCCCCCCCCCCCC	30.02	28657654
369	Phosphorylation	PPRASLSSDTSALSY CCCCCCCCCCCCCCC	50.64	22817900
395	Phosphorylation	HAQLELVSLRPCFGD CCEEEEEEEECCCCC	31.14	24719451
407	Phosphorylation	FGDYSDESDSATVYD CCCCCCCCCCCEEEC	41.68	22817900
409	Phosphorylation	DYSDESDSATVYDNC CCCCCCCCCEEECCC	34.81	22817900
411	Phosphorylation	SDESDSATVYDNCAS CCCCCCCEEECCCCC	24.45	22817900
421	Phosphorylation	DNCASVSSPYESAIG CCCCCCCCCCHHHCC	29.37	22817900
444	Phosphorylation	PQPPACLSEDSTPDE CCCCCCCCCCCCCCC	38.96	27732954
447	Phosphorylation	PACLSEDSTPDEPDV CCCCCCCCCCCCCCC	37.48	27732954
448	Phosphorylation	ACLSEDSTPDEPDVH CCCCCCCCCCCCCCC	47.26	27732954
469	Phosphorylation	NVFMSGRSRSSSAES HHHHCCCCCCCCCHH	39.79	22817900
471	Phosphorylation	FMSGRSRSSSAESFG HHCCCCCCCCCHHHC	29.86	22817900
472	Phosphorylation	MSGRSRSSSAESFGL HCCCCCCCCCHHHCC	32.24	22817900
473	Phosphorylation	SGRSRSSSAESFGLF CCCCCCCCCHHHCCE	36.98	10700186
574	Phosphorylation	FRVKFLGSVQVPYHK EEEEEEEEEECCCCC	16.12	28348404
596	Phosphorylation	AMQKIATTRRLTVHF HHHHHHCCCEEEEEC	12.55	24719451
702	Phosphorylation	YKQFVEYTCPTEDIY HHHHHHHCCCCHHCC	9.86	20044836

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
15	S	Phosphorylation	Kinase	JNK-SUBFAMILY	-	GPS
15	S	Phosphorylation	Kinase	JNK_GROUP	-	PhosphoELM
29	S	Phosphorylation	Kinase	JNK-SUBFAMILY	-	GPS
29	S	Phosphorylation	Kinase	JNK_GROUP	-	PhosphoELM
103	T	Phosphorylation	Kinase	MK08	P45983	PhosphoELM
103	T	Phosphorylation	Kinase	MK09	P45984	PhosphoELM
103	T	Phosphorylation	Kinase	MAPK10	P53779	Uniprot
197	S	Phosphorylation	Kinase	JNK-SUBFAMILY	-	GPS
197	S	Phosphorylation	Kinase	JNK_GROUP	-	PhosphoELM
205	T	Phosphorylation	Kinase	MAPK9	P45984	Uniprot
205	T	Phosphorylation	Kinase	MAPK10	P53779	Uniprot
205	T	Phosphorylation	Kinase	JNK-SUBFAMILY	-	GPS
205	T	Phosphorylation	Kinase	JNK_GROUP	-	PhosphoELM
205	T	Phosphorylation	Kinase	JNK1	P45983	PSP
284	T	Phosphorylation	Kinase	JNK-SUBFAMILY	-	GPS
284	T	Phosphorylation	Kinase	JNK_GROUP	-	PhosphoELM
341	S	Phosphorylation	Kinase	JNK-SUBFAMILY	-	GPS
341	S	Phosphorylation	Kinase	JNK_GROUP	-	PhosphoELM
421	S	Phosphorylation	Kinase	JNK_GROUP	-	PhosphoELM
421	S	Phosphorylation	Kinase	JNK-SUBFAMILY	-	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
103	T	Phosphorylation		12756254
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.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of JIP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LRP2_HUMAN	LRP2	physical	10827173
LRP1_HUMAN	LRP1	physical	10827173
JIP1_HUMAN	MAPK8IP1	physical	10490659
JIP2_HUMAN	MAPK8IP2	physical	10490659
DUS16_HUMAN	DUSP16	physical	12524447
MK08_HUMAN	MAPK8	physical	9733513
MK09_HUMAN	MAPK9	physical	9733513
PAX2_HUMAN	PAX2	physical	11700324
MK08_HUMAN	MAPK8	physical	11700324
M3K13_HUMAN	MAP3K13	physical	11726277
AKT1_HUMAN	AKT1	physical	15998799
MP2K7_HUMAN	MAP2K7	physical	16840345
VRK2_HUMAN	VRK2	physical	18286207
MK08_HUMAN	MAPK8	physical	18286207
M3K7_HUMAN	MAP3K7	physical	18286207
MP2K7_HUMAN	MAP2K7	physical	18286207
TAB1_HUMAN	TAB1	physical	18286207
A4_HUMAN	APP	physical	12917434
A4_HUMAN	APP	physical	16301330
JUN_HUMAN	JUN	physical	16343492
TTLL4_HUMAN	TTLL4	physical	28514442
JIP2_HUMAN	MAPK8IP2	physical	28514442
ANK3_HUMAN	ANK3	physical	28514442
MK08_HUMAN	MAPK8	physical	28514442
MK09_HUMAN	MAPK9	physical	28514442
FEM1B_HUMAN	FEM1B	physical	28514442
HXC8_HUMAN	HOXC8	physical	28514442
ANK2_HUMAN	ANK2	physical	28514442
SENP5_HUMAN	SENP5	physical	28514442
SETX_HUMAN	SETX	physical	28514442
TBB3_HUMAN	TUBB3	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
125853	Diabetes mellitus, non-insulin-dependent (NIDDM)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of JIP1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Recruitment of JNK to JIP1 and JNK-dependent JIP1 phosphorylationregulates JNK module dynamics and activation."; Nihalani D., Wong H.N., Holzman L.B.; J. Biol. Chem. 278:28694-28702(2003). Cited for: PHOSPHORYLATION AT THR-103 AND THR-205, AND MUTAGENESIS OF ARG-160 ANDPRO-161.	12756254 [Abstract]

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