dbPTM

JIP3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	JIP3_HUMAN
UniProt AC	Q9UPT6
Protein Name	C-Jun-amino-terminal kinase-interacting protein 3
Gene Name	MAPK8IP3
Organism	Homo sapiens (Human).
Sequence Length	1336
Subcellular Localization	Cytoplasm.
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 (By similarity)..
Protein Sequence	MMEIQMDEGGGVVVYQDDYCSGSVMSERVSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQVGGNSQTESSLPGRRKERPTSLNVFPLADGTVRAQIGGKLVPAGDHWHLSDLGQLQSSSSYQCPQDEMSESGQSSAAATPSTTGTKSNTPTSSVPSAAVTPLNESLQPLGDYGVGSKNSKRAREKRDSRNMEVQVTQEMRNVSIGMGSSDEWSDVQDIIDSTPELDMCPETRLDRTGSSPTQGIVNKAFGINTDSLYHELSTAGSEVIGDVDEGADLLGEFSVRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKRVKSEAIIARREPKEEAEDVSSYLCTESDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKKSTIWQFFSRLFSSSSSPPPAKRPYPSVNIHYKSPTTAGFSQRRNHAMCPISAGSRPLEFFPDDDCTSSARREQKREQYRQVREHVRNDDGRLQACGWSLPAKYKQLSPNGGQEDTRMKNVPVPVYCRPLVEKDPTMKLWCAAGVNLSGWRPNEDDAGNGVKPAPGRDPLTCDREGDGEPKSAHTSPEKKKAKELPEMDATSSRVWILTSTLTTSKVVIIDANQPGTVVDQFTVCNAHVLCISSIPAASDSDYPPGEMFLDSDVNPEDPGADGVLAGITLVGCATRCNVPRSNCSSRGDTPVLDKGQGEVATIANGKVNPSQSTEEATEATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQPGSENGPEPDSSSTRPEPEPSGDPTGAGSSAAPTMWLGAQNGWLYVHSAVANWKKCLHSIKLKDSVLSLVHVKGRVLVALADGTLAIFHRGEDGQWDLSNYHLMDLGHPHHSIRCMAVVYDRVWCGYKNKVHVIQPKTMQIEKSFDAHPRRESQVRQLAWIGDGVWVSIRLDSTLRLYHAHTHQHLQDVDIEPYVSKMLGTGKLGFSFVRITALLVAGSRLWVGTGNGVVISIPLTETVVLHRGQLLGLRANKTSPTSGEGARPGGIIHVYGDDSSDRAASSFIPYCSMAQAQLCFHGHRDAVKFFVSVPGNVLATLNGSVLDSPAEGPGPAAPASEVEGQKLRNVLVLSGGEGYIDFRIGDGEDDETEEGAGDMSQVKPVLSKAERSHIIVWQVSYTPE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
19	Phosphorylation	VVVYQDDYCSGSVMS EEEEECCCCCCCHHH	9.23	25954137
21	Phosphorylation	VYQDDYCSGSVMSER EEECCCCCCCHHHHH	28.07	25954137
23	Phosphorylation	QDDYCSGSVMSERVS ECCCCCCCHHHHHHH	9.80	25954137
26	Phosphorylation	YCSGSVMSERVSGLA CCCCCHHHHHHHHHH	21.79	25954137
35	Phosphorylation	RVSGLAGSIYREFER HHHHHHHHHHHHHHH	15.73	25954137
84	Methylation	EVELELLREDNEQLL EEEEHHHHHCHHHHH	62.94	18567435
101	Methylation	YEREKALRRQAEEKF HHHHHHHHHHHHHHH	33.26	18567447
102	Methylation	EREKALRRQAEEKFI HHHHHHHHHHHHHHH	40.69	18567459
107	Ubiquitination	LRRQAEEKFIEFEDA HHHHHHHHHHCHHHH	43.05	-
139	Sumoylation	QTRQLELKAKNYADQ HHHHHHHHHHHHHHH	48.19	-
139	Sumoylation	QTRQLELKAKNYADQ HHHHHHHHHHHHHHH	48.19	-
148	Phosphorylation	KNYADQISRLEERES HHHHHHHHHHHHHHH	25.77	25159151
159	Ubiquitination	ERESEMKKEYNALHQ HHHHHHHHHHHHHHH	65.21	-
169	Phosphorylation	NALHQRHTEMIQTYV HHHHHHHHHHHHHHH	29.45	24129246
174	Phosphorylation	RHTEMIQTYVEHIER HHHHHHHHHHHHHHH	20.71	24129246
175	Phosphorylation	HTEMIQTYVEHIERS HHHHHHHHHHHHHHH	6.35	24129246
183	Ubiquitination	VEHIERSKMQQVGGN HHHHHHHHCHHCCCC	47.12	-
191	Phosphorylation	MQQVGGNSQTESSLP CHHCCCCCCCCCCCC	41.58	27732954
193	Phosphorylation	QVGGNSQTESSLPGR HCCCCCCCCCCCCCC	37.34	27732954
195	Phosphorylation	GGNSQTESSLPGRRK CCCCCCCCCCCCCCC	40.33	27732954
196	Phosphorylation	GNSQTESSLPGRRKE CCCCCCCCCCCCCCC	32.14	27732954
206	Phosphorylation	GRRKERPTSLNVFPL CCCCCCCCCEEEEEC	52.66	28450419
207	Phosphorylation	RRKERPTSLNVFPLA CCCCCCCCEEEEECC	22.19	25394399
265	Phosphorylation	GQSSAAATPSTTGTK CCCCCCCCCCCCCCC	17.04	10629060
273	Phosphorylation	PSTTGTKSNTPTSSV CCCCCCCCCCCCCCC	45.86	23403867
275	Phosphorylation	TTGTKSNTPTSSVPS CCCCCCCCCCCCCCC	34.73	10629060
277	Phosphorylation	GTKSNTPTSSVPSAA CCCCCCCCCCCCCCE	31.43	23403867
278	Phosphorylation	TKSNTPTSSVPSAAV CCCCCCCCCCCCCEE	30.46	23403867
279	Phosphorylation	KSNTPTSSVPSAAVT CCCCCCCCCCCCEEC	40.29	23403867
282	Phosphorylation	TPTSSVPSAAVTPLN CCCCCCCCCEECCCC	27.06	23403867
286	Phosphorylation	SVPSAAVTPLNESLQ CCCCCEECCCCCCCC	19.82	10629060
291	Phosphorylation	AVTPLNESLQPLGDY EECCCCCCCCCCCCC	31.09	27732954
298	Phosphorylation	SLQPLGDYGVGSKNS CCCCCCCCCCCCCCC	16.35	27732954
302	Phosphorylation	LGDYGVGSKNSKRAR CCCCCCCCCCCHHHH	26.68	27732954
314	Phosphorylation	RAREKRDSRNMEVQV HHHHHHHHCCCEEEE	29.59	19036714
362	Phosphorylation	PETRLDRTGSSPTQG CCCCCCCCCCCCCCC	40.87	28176443
364	Phosphorylation	TRLDRTGSSPTQGIV CCCCCCCCCCCCCHH	32.31	30278072
365	Phosphorylation	RLDRTGSSPTQGIVN CCCCCCCCCCCCHHH	33.05	28355574
367	Phosphorylation	DRTGSSPTQGIVNKA CCCCCCCCCCHHHHH	41.18	28176443
552	Phosphorylation	LQEAVRWTEMIRASR HHHHHHHHHHHHHHC	12.71	28464451
558	Phosphorylation	WTEMIRASREHPSVQ HHHHHHHHCCCCCHH	28.49	28348404
563	O-linked_Glycosylation	RASREHPSVQEKKKS HHHCCCCCHHHHHHH	38.04	29351928
581	Phosphorylation	QFFSRLFSSSSSPPP HHHHHHHCCCCCCCC	33.62	30108239
582	Phosphorylation	FFSRLFSSSSSPPPA HHHHHHCCCCCCCCC	27.23	27794612
583	Phosphorylation	FSRLFSSSSSPPPAK HHHHHCCCCCCCCCC	33.37	27794612
584	Phosphorylation	SRLFSSSSSPPPAKR HHHHCCCCCCCCCCC	49.14	30631047
585	Phosphorylation	RLFSSSSSPPPAKRP HHHCCCCCCCCCCCC	43.29	28355574
593	Phosphorylation	PPPAKRPYPSVNIHY CCCCCCCCCCCEEEE	16.51	25262027
595	Phosphorylation	PAKRPYPSVNIHYKS CCCCCCCCCEEEECC	23.19	25262027
600	Phosphorylation	YPSVNIHYKSPTTAG CCCCEEEECCCCCCC	14.90	25262027
602	Phosphorylation	SVNIHYKSPTTAGFS CCEEEECCCCCCCCC	21.95	28152594
604	Phosphorylation	NIHYKSPTTAGFSQR EEEECCCCCCCCCCC	36.05	27732954
605	Phosphorylation	IHYKSPTTAGFSQRR EEECCCCCCCCCCCC	28.32	28152594
609	Phosphorylation	SPTTAGFSQRRNHAM CCCCCCCCCCCCCCC	23.12	28152594
676	Phosphorylation	PAKYKQLSPNGGQED CCCCCCCCCCCCCCC	17.52	20068231
684	Phosphorylation	PNGGQEDTRMKNVPV CCCCCCCCCCCCCCC	31.73	20068231
716	Phosphorylation	CAAGVNLSGWRPNED EEECCCCCCCCCCCC	30.98	20068231
750	Phosphorylation	EGDGEPKSAHTSPEK CCCCCCCCCCCCHHH	35.68	30177828
753	Phosphorylation	GEPKSAHTSPEKKKA CCCCCCCCCHHHHHH	45.77	30177828
754	Phosphorylation	EPKSAHTSPEKKKAK CCCCCCCCHHHHHHH	22.61	30177828
779	Phosphorylation	RVWILTSTLTTSKVV CEEEEEEEECCCEEE	23.92	-
860	Phosphorylation	TRCNVPRSNCSSRGD HHCCCCCCCCCCCCC	35.80	27732954
863	Phosphorylation	NVPRSNCSSRGDTPV CCCCCCCCCCCCCCC	27.59	27732954
864	Phosphorylation	VPRSNCSSRGDTPVL CCCCCCCCCCCCCCC	42.35	27732954
868	Phosphorylation	NCSSRGDTPVLDKGQ CCCCCCCCCCCCCCC	20.37	27732954
911	Phosphorylation	PGPSEPETATLRPGP CCCCCCCCCEECCCC	35.34	20068231
913	Phosphorylation	PSEPETATLRPGPLT CCCCCCCEECCCCCC	30.62	20068231
995	Phosphorylation	NWKKCLHSIKLKDSV CHHHHHHHCCCCCCC	14.41	29083192
997	Ubiquitination	KKCLHSIKLKDSVLS HHHHHHCCCCCCCHH	53.12	-
1004	Phosphorylation	KLKDSVLSLVHVKGR CCCCCCHHHEEECCC	26.62	-
1143	Phosphorylation	GTGKLGFSFVRITAL CCCCCCCCHHHHHHE	22.49	22617229
1174	Phosphorylation	ISIPLTETVVLHRGQ EEEECCCEEEEECCE	15.64	22210691
1190	Phosphorylation	LGLRANKTSPTSGEG EEEECCCCCCCCCCC	39.48	25307156
1191	Phosphorylation	GLRANKTSPTSGEGA EEECCCCCCCCCCCC	27.99	24117733
1193	Phosphorylation	RANKTSPTSGEGARP ECCCCCCCCCCCCCC	49.48	24117733
1194	Phosphorylation	ANKTSPTSGEGARPG CCCCCCCCCCCCCCC	37.93	24117733
1260	Phosphorylation	LNGSVLDSPAEGPGP ECCCCCCCCCCCCCC	23.11	24173317
1286	Phosphorylation	LRNVLVLSGGEGYID EEEEEEECCCCCEEE	36.95	-

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
265	T	Phosphorylation	Kinase	MAPK	-	Uniprot
275	T	Phosphorylation	Kinase	MAPK	-	Uniprot
286	T	Phosphorylation	Kinase	MAPK	-	Uniprot
314	S	Phosphorylation	Kinase	ROCK1	Q13464	Uniprot
364	S	Phosphorylation	Kinase	ROCK1	Q13464	Uniprot
365	S	Phosphorylation	Kinase	ROCK1	Q13464	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of JIP3_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 JIP3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KLC1_HUMAN	KLC1	physical	11106729
MK10_HUMAN	MAPK10	physical	10523642
RIC8A_HUMAN	RIC8A	physical	16169070
FAK1_HUMAN	PTK2	physical	12226752
MP2K1_HUMAN	MAP2K1	physical	11044439
RAF1_HUMAN	RAF1	physical	11044439
MK08_HUMAN	MAPK8	physical	10523642
MK09_HUMAN	MAPK9	physical	10523642
MP2K4_HUMAN	MAP2K4	physical	10523642
MP2K1_HUMAN	MAP2K1	physical	10523642
M3K1_HUMAN	MAP3K1	physical	10523642
RAF1_HUMAN	RAF1	physical	10523642
MK08_HUMAN	MAPK8	physical	10629060
MK09_HUMAN	MAPK9	physical	10629060
MK10_HUMAN	MAPK10	physical	10629060
MP2K7_HUMAN	MAP2K7	physical	10629060
M3K11_HUMAN	MAP3K11	physical	10629060
JIP2_HUMAN	MAPK8IP2	physical	10629060
KLC2_HUMAN	KLC2	physical	11106729
M3K5_HUMAN	MAP3K5	physical	12189133
MP2K4_HUMAN	MAP2K4	physical	12189133
MP2K7_HUMAN	MAP2K7	physical	12189133
MK10_HUMAN	MAPK10	physical	12189133
JIP2_HUMAN	MAPK8IP2	physical	28514442
TNKS2_HUMAN	TNKS2	physical	28514442
JIP1_HUMAN	MAPK8IP1	physical	28514442
JIP4_HUMAN	SPAG9	physical	28514442
TNKS1_HUMAN	TNKS	physical	28514442
DCTN6_HUMAN	DCTN6	physical	28514442
ARP10_HUMAN	ACTR10	physical	28514442
WDR54_HUMAN	WDR54	physical	28514442
DCTN4_HUMAN	DCTN4	physical	28514442

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 JIP3_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Identification of ROCK1 as an upstream activator of the JIP-3 to JNKsignaling axis in response to UVB damage."; Ongusaha P.P., Qi H.H., Raj L., Kim Y.B., Aaronson S.A., Davis R.J.,Shi Y., Liao J.K., Lee S.W.; Sci. Signal. 1:RA14-RA14(2008). Cited for: INTERACTION WITH ROCK1, AND PHOSPHORYLATION AT SER-314; SER-364 ANDSER-365.	19036714 [Abstract]
"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-585, AND MASSSPECTROMETRY.	15302935 [Abstract]