dbPTM

JUN_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	JUN_HUMAN
UniProt AC	P05412
Protein Name	Transcription factor AP-1
Gene Name	JUN
Organism	Homo sapiens (Human).
Sequence Length	331
Subcellular Localization	Nucleus.
Protein Description	Transcription factor that recognizes and binds to the enhancer heptamer motif 5'-TGA[CG]TCA-3'. Promotes activity of NR5A1 when phosphorylated by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation. Involved in activated KRAS-mediated transcriptional activation of USP28 in colorectal cancer (CRC) cells. [PubMed: 24623306 Binds to the USP28 promoter in colorectal cancer (CRC) cells]
Protein Sequence	MTAKMETTFYDDALNASFLPSESGPYGYSNPKILKQSMTLNLADPVGSLKPHLRAKNSDLLTSPDVGLLKLASPELERLIIQSSNGHITTTPTPTQFLCPKNVTDEQEGFAEGFVRALAELHSQNTLPSVTSAAQPVNGAGMVAPAVASVAGGSGSGGFSASLHSEPPVYANLSNFNPGALSSGGGAPSYGAAGLAFPAQPQQQQQPPHHLPQQMPVQHPRLQALKEEPQTVPEMPGETPPLSPIDMESQERIKAERKRMRNRIAASKCRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNHVNSGCQLMLTQQLQTF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MTAKMETTF ------CCCCCCCCC	34.68	21177766
8	Phosphorylation	MTAKMETTFYDDALN CCCCCCCCCCHHHHC	13.59	21177766
21	Phosphorylation	LNASFLPSESGPYGY HCCCCCCCCCCCCCC	46.68	30576142
28	Phosphorylation	SESGPYGYSNPKILK CCCCCCCCCCHHHHH	10.22	30576142
29	Phosphorylation	ESGPYGYSNPKILKQ CCCCCCCCCHHHHHH	42.15	30576142
35	Sumoylation	YSNPKILKQSMTLNL CCCHHHHHHHEECCC	43.74	28112733
37	Phosphorylation	NPKILKQSMTLNLAD CHHHHHHHEECCCCC	16.49	-
48	Phosphorylation	NLADPVGSLKPHLRA CCCCCCCCCCHHHHH	33.19	-
50	Ubiquitination	ADPVGSLKPHLRAKN CCCCCCCCHHHHHCC	31.89	21890473
50	Ubiquitination	ADPVGSLKPHLRAKN CCCCCCCCHHHHHCC	31.89	22817900
50	Sumoylation	ADPVGSLKPHLRAKN CCCCCCCCHHHHHCC	31.89	28112733
50	Acetylation	ADPVGSLKPHLRAKN CCCCCCCCHHHHHCC	31.89	23236377
56	Sumoylation	LKPHLRAKNSDLLTS CCHHHHHCCCCCCCC	51.02	-
56	Ubiquitination	LKPHLRAKNSDLLTS CCHHHHHCCCCCCCC	51.02	32015554
56	Acetylation	LKPHLRAKNSDLLTS CCHHHHHCCCCCCCC	51.02	-
56	Sumoylation	LKPHLRAKNSDLLTS CCHHHHHCCCCCCCC	51.02	28112733
58	Phosphorylation	PHLRAKNSDLLTSPD HHHHHCCCCCCCCCC	29.00	30266825
62	Phosphorylation	AKNSDLLTSPDVGLL HCCCCCCCCCCCCHH	45.57	22322096
63	Phosphorylation	KNSDLLTSPDVGLLK CCCCCCCCCCCCHHH	21.05	22322096
70	Ubiquitination	SPDVGLLKLASPELE CCCCCHHHHCCHHHH	47.23	32015554
70	Sumoylation	SPDVGLLKLASPELE CCCCCHHHHCCHHHH	47.23	28112733
73	O-linked_Glycosylation	VGLLKLASPELERLI CCHHHHCCHHHHHEE	29.37	23301498
73	Phosphorylation	VGLLKLASPELERLI CCHHHHCCHHHHHEE	29.37	19664994
83	O-linked_Glycosylation	LERLIIQSSNGHITT HHHEEEECCCCCEEC	18.50	23301498
83	Phosphorylation	LERLIIQSSNGHITT HHHEEEECCCCCEEC	18.50	28450419
84	O-linked_Glycosylation	ERLIIQSSNGHITTT HHEEEECCCCCEECC	30.38	23301498
84	Phosphorylation	ERLIIQSSNGHITTT HHEEEECCCCCEECC	30.38	28450419
89	Phosphorylation	QSSNGHITTTPTPTQ ECCCCCEECCCCCCE	20.95	21177766
90	O-linked_Glycosylation	SSNGHITTTPTPTQF CCCCCEECCCCCCEE	30.12	23301498
90	Phosphorylation	SSNGHITTTPTPTQF CCCCCEECCCCCCEE	30.12	28450419
91	Phosphorylation	SNGHITTTPTPTQFL CCCCEECCCCCCEEE	19.26	7744008
91	O-linked_Glycosylation	SNGHITTTPTPTQFL CCCCEECCCCCCEEE	19.26	23301498
93	Phosphorylation	GHITTTPTPTQFLCP CCEECCCCCCEEECC	36.55	7744008
95	Phosphorylation	ITTTPTPTQFLCPKN EECCCCCCEEECCCC	34.14	28450419
95	O-linked_Glycosylation	ITTTPTPTQFLCPKN EECCCCCCEEECCCC	34.14	23301498
170	Phosphorylation	LHSEPPVYANLSNFN CCCCCCEEECCCCCC	8.78	14757045
226	Ubiquitination	HPRLQALKEEPQTVP CHHHHHHHHCCCCCC	64.15	32015554
226	Sumoylation	HPRLQALKEEPQTVP CHHHHHHHHCCCCCC	64.15	28112733
226	Acetylation	HPRLQALKEEPQTVP CHHHHHHHHCCCCCC	64.15	26051181
226	Sumoylation	HPRLQALKEEPQTVP CHHHHHHHHCCCCCC	64.15	-
231	Phosphorylation	ALKEEPQTVPEMPGE HHHHCCCCCCCCCCC	49.06	30266825
239	Phosphorylation	VPEMPGETPPLSPID CCCCCCCCCCCCCCC	35.80	30266825
243	Phosphorylation	PGETPPLSPIDMESQ CCCCCCCCCCCHHHH	26.11	16023596
249	Phosphorylation	LSPIDMESQERIKAE CCCCCHHHHHHHHHH	30.61	30266825
254	Sumoylation	MESQERIKAERKRMR HHHHHHHHHHHHHHH	50.87	-
254	Sumoylation	MESQERIKAERKRMR HHHHHHHHHHHHHHH	50.87	-
268	Acetylation	RNRIAASKCRKRKLE HHHHHHHHHHHHHHH	33.07	16214953
268	Ubiquitination	RNRIAASKCRKRKLE HHHHHHHHHHHHHHH	33.07	32015554
269	S-nitrosylation	NRIAASKCRKRKLER HHHHHHHHHHHHHHH	6.01	9108029
269	Glutathionylation	NRIAASKCRKRKLER HHHHHHHHHHHHHHH	6.01	22833525
271	Acetylation	IAASKCRKRKLERIA HHHHHHHHHHHHHHH	64.45	11689449
273	Acetylation	ASKCRKRKLERIARL HHHHHHHHHHHHHHH	58.70	16214953
286	Phosphorylation	RLEEKVKTLKAQNSE HHHHHHHHHHHHCHH	36.16	28112733
288	Ubiquitination	EEKVKTLKAQNSELA HHHHHHHHHHCHHHH	53.83	32015554
296	Phosphorylation	AQNSELASTANMLRE HHCHHHHHHHHHHHH	40.45	28258704
297	Phosphorylation	QNSELASTANMLREQ HCHHHHHHHHHHHHH	19.22	28258704
309	Ubiquitination	REQVAQLKQKVMNHV HHHHHHHHHHHHHHH	35.67	33845483
318	Phosphorylation	KVMNHVNSGCQLMLT HHHHHHHHHHHHHHH	39.60	26552605
320	S-nitrosylation	MNHVNSGCQLMLTQQ HHHHHHHHHHHHHHH	2.56	9108029
325	Phosphorylation	SGCQLMLTQQLQTF- HHHHHHHHHHHHCC-	10.58	26552605
330	Phosphorylation	MLTQQLQTF------ HHHHHHHCC------	39.65	26552605

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
2	T	Phosphorylation	Kinase	PAK2	Q13177	Uniprot
8	T	Phosphorylation	Kinase	PAK2	Q13177	Uniprot
58	S	Phosphorylation	Kinase	PKD-FAMILY	-	GPS
63	S	Phosphorylation	Kinase	VRK1	Q99986	PSP
63	S	Phosphorylation	Kinase	PBK	Q96KB5	PSP
63	S	Phosphorylation	Kinase	PLK3	Q9H4B4	Uniprot
63	S	Phosphorylation	Kinase	CDK3	Q00526	PSP
63	S	Phosphorylation	Kinase	MAPK15	Q8TD08	GPS
63	S	Phosphorylation	Kinase	PRKD1	Q15139	PSP
63	S	Phosphorylation	Kinase	ERK2	P28482	PSP
63	S	Phosphorylation	Kinase	MAPK9	P45984	GPS
63	S	Phosphorylation	Kinase	ERK1	P27361	PSP
63	S	Phosphorylation	Kinase	MK08	P45983	PhosphoELM
73	S	Phosphorylation	Kinase	VRK1	Q99986	PSP
73	S	Phosphorylation	Kinase	PBK	Q96KB5	PSP
73	S	Phosphorylation	Kinase	PLK3	Q9H4B4	Uniprot
73	S	Phosphorylation	Kinase	CDK3	Q00526	PSP
73	S	Phosphorylation	Kinase	MAPK15	Q8TD08	GPS
73	S	Phosphorylation	Kinase	MAPK9	P45984	GPS
73	S	Phosphorylation	Kinase	MK08	P45983	PhosphoELM
73	S	Phosphorylation	Kinase	ERK1	P27361	PSP
73	S	Phosphorylation	Kinase	ERK2	P28482	PSP
89	T	Phosphorylation	Kinase	PAK2	Q13177	Uniprot
91	T	Phosphorylation	Kinase	MAPK8	P45983	GPS
93	T	Phosphorylation	Kinase	MAPK8	P45983	GPS
93	T	Phosphorylation	Kinase	PAK2	Q13177	Uniprot
170	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
231	T	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
231	T	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
231	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
239	T	Phosphorylation	Kinase	GSK3A	P49840	PhosphoELM
239	T	Phosphorylation	Kinase	GSK-FAMILY	-	GPS
239	T	Phosphorylation	Kinase	GSK3B	P49841	PSP
239	T	Phosphorylation	Kinase	GSK-3_GROUP	-	PhosphoELM
243	S	Phosphorylation	Kinase	GSK3A	P49840	PhosphoELM
243	S	Phosphorylation	Kinase	DYRK2	Q92630	Uniprot
243	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
243	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
243	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
243	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
249	S	Phosphorylation	Kinase	PRKDC	P78527	PhosphoELM
249	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
249	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
249	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
249	S	Phosphorylation	Kinase	GSK3B	P49841	GPS
286	T	Phosphorylation	Kinase	PAK2	Q13177	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	FBXW7	Q969H0	PMID:14739463
-	K	Ubiquitination	E3 ubiquitin ligase	SPOP	O43791	PMID:19164706
-	K	Ubiquitination	E3 ubiquitin ligase	ITCH	Q96J02	PMID:11828324
-	K	Ubiquitination	E3 ubiquitin ligase	MAP3K1	Q13233	PMID:17101801
-	K	Ubiquitination	E3 ubiquitin ligase	DET1	Q7L5Y6	PMID:14739464
-	K	Ubiquitination	E3 ubiquitin ligase	SAG	P10523	PMID:23136067
-	K	Ubiquitination	E3 ubiquitin ligase	DET1#COP1	Q7L5Y6#Q8NHY2	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	COP1	Q8NHY2	PMID:12615916

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
2	T	Phosphorylation	1846781
Phosphorylated by PAK2 at Thr-2, Thr-8, Thr-89, Thr-93 and Thr-286 thereby promoting JUN-mediated cell proliferation and transformation.
8	T	Phosphorylation	21177766
Phosphorylated by PAK2 at Thr-2, Thr-8, Thr-89, Thr-93 and Thr-286 thereby promoting JUN-mediated cell proliferation and transformation.
89	T	Phosphorylation	21177766
Phosphorylated by PAK2 at Thr-2, Thr-8, Thr-89, Thr-93 and Thr-286 thereby promoting JUN-mediated cell proliferation and transformation.
93	T	Phosphorylation	14739463
Phosphorylated by PAK2 at Thr-2, Thr-8, Thr-89, Thr-93 and Thr-286 thereby promoting JUN-mediated cell proliferation and transformation.
239	T	Phosphorylation	1846781
Phosphorylated at Thr-239, Ser-243 and Ser-249 by GSK3B; phosphorylation reduces its ability to bind DNA.
239	T	Phosphorylation	1846781
Phosphorylated by DYRK2 at Ser-243; this primes the protein for subsequent phosphorylation by GSK3B at Thr-239.
243	S	Phosphorylation	1846781
Phosphorylated at Thr-239, Ser-243 and Ser-249 by GSK3B; phosphorylation reduces its ability to bind DNA.
243	S	Phosphorylation	1846781
Phosphorylated by DYRK2 at Ser-243; this primes the protein for subsequent phosphorylation by GSK3B at Thr-239.
249	S	Phosphorylation	1846781
Phosphorylated at Thr-239, Ser-243 and Ser-249 by GSK3B; phosphorylation reduces its ability to bind DNA.
271	K	Acetylation	11689449
Acetylated at Lys-271 by EP300.
286	T	Phosphorylation	21177766
Phosphorylated by PAK2 at Thr-2, Thr-8, Thr-89, Thr-93 and Thr-286 thereby promoting JUN-mediated cell proliferation and transformation.

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 JUN_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ANDR_HUMAN	AR	physical	9211894
ATF2_HUMAN	ATF2	physical	8027667
RFWD2_HUMAN	RFWD2	physical	12615916
SNF5_MOUSE	Smarcb1	physical	11053448
SMCA2_MOUSE	Smarca2	physical	11053448
BCL3_HUMAN	BCL3	physical	10497212
CSK21_HUMAN	CSNK2A1	physical	9685505
CBP_HUMAN	CREBBP	physical	9786917
FOSL1_HUMAN	FOSL1	physical	9160889
FOS_HUMAN	FOS	physical	9160889
ERG_HUMAN	ERG	physical	11278640
SKI_HUMAN	SKI	physical	12034730
CSN5_HUMAN	COPS5	physical	8837781
JUN_HUMAN	JUN	physical	7848298
TF2B_HUMAN	GTF2B	physical	7848298
TBP_HUMAN	TBP	physical	7848298
FOS_HUMAN	FOS	physical	7816143
JUN_HUMAN	JUN	physical	10488148
FOS_HUMAN	FOS	physical	10488148
TCF20_HUMAN	TCF20	physical	8663478
PIT1_HUMAN	POU1F1	physical	8663380
DHX9_HUMAN	DHX9	physical	11823437
HNRPM_HUMAN	HNRNPM	physical	11823437
DDX21_HUMAN	DDX21	physical	11823437
MK08_HUMAN	MAPK8	physical	8137421
PIN1_HUMAN	PIN1	physical	11432833
SENP2_MOUSE	Senp2	genetic	12419228
HIF1A_HUMAN	HIF1A	physical	11739718
T2EB_HUMAN	GTF2E2	physical	8628277
T2FB_HUMAN	GTF2F2	physical	8628277
T2FA_HUMAN	GTF2F1	physical	8628277
JUN_HUMAN	JUN	physical	8440710
FOS_HUMAN	FOS	physical	8440710
MK08_HUMAN	MAPK8	physical	12052834
STAT4_HUMAN	STAT4	physical	11801649
STAT1_HUMAN	STAT1	physical	10490649
STAT3_HUMAN	STAT3	physical	10490649
MYOD1_HUMAN	MYOD1	physical	1310896
FOS_HUMAN	FOS	physical	8380166
NF2L1_HUMAN	NFE2L1	physical	9872330
NF2L2_HUMAN	NFE2L2	physical	9872330
NCOR2_HUMAN	NCOR2	physical	10777532
PP4C_HUMAN	PPP4C	physical	9837938
ETS1_HUMAN	ETS1	physical	8557686
NCOA1_HUMAN	NCOA1	physical	9642216
RB_HUMAN	RB1	physical	10026157
STF1_HUMAN	NR5A1	physical	10478848
TAF1_HUMAN	TAF1	physical	11316804
MK08_HUMAN	MAPK8	physical	8586671
BCL6_HUMAN	BCL6	physical	12165517
TOP2A_HUMAN	TOP2A	physical	8387155
ESR1_HUMAN	ESR1	physical	11477071
UBC9_HUMAN	UBE2I	physical	8733011
PP2BB_HUMAN	PPP3CB	physical	17952113
FOS_HUMAN	FOS	physical	11431474
FOSL1_HUMAN	FOSL1	physical	11431474
MK01_HUMAN	MAPK1	physical	11431474
MK08_HUMAN	MAPK8	physical	16983342
CDN1A_HUMAN	CDKN1A	physical	20102411
CSK_HUMAN	CSK	physical	16740711
DACH1_HUMAN	DACH1	physical	17182846
APLP2_HUMAN	APLP2	physical	20936779
ARRB1_HUMAN	ARRB1	physical	20936779
ATF4_HUMAN	ATF4	physical	20936779
FOS_HUMAN	FOS	physical	20936779
HS90A_HUMAN	HSP90AA1	physical	20936779
UBC_HUMAN	UBC	physical	20936779
MACF1_HUMAN	MACF1	physical	20936779
KMT2C_HUMAN	KMT2C	physical	20936779
HDAC1_HUMAN	HDAC1	physical	17056544
KAT7_HUMAN	KAT7	physical	16880509
EDF1_HUMAN	EDF1	physical	16880509
UBC_HUMAN	UBC	physical	15469925
SUMO1_HUMAN	SUMO1	physical	15469925
HDAC9_HUMAN	HDAC9	physical	16611996
HMGA1_HUMAN	HMGA1	physical	10428834
ESR1_HUMAN	ESR1	physical	17317669
STAT6_HUMAN	STAT6	physical	21357535
FOS_HUMAN	FOS	physical	20410304
MBD3_HUMAN	MBD3	physical	21196933
CHD3_HUMAN	CHD3	physical	21196933
MTA3_HUMAN	MTA3	physical	21196933
MYC_HUMAN	MYC	physical	20232342
NF2L2_HUMAN	NFE2L2	physical	20232342
RACK1_HUMAN	GNB2L1	physical	21860413
RN187_HUMAN	RNF187	physical	20852630
HIF1A_HUMAN	HIF1A	physical	19738058
CBP_HUMAN	CREBBP	physical	10327051
EP300_HUMAN	EP300	physical	10327051
ITCH_HUMAN	ITCH	physical	19806201
FOS_HUMAN	FOS	physical	21675959
JUN_HUMAN	JUN	physical	21675959
GAG_HV1H2	gag	physical	17538020
NEDD4_HUMAN	NEDD4	physical	17538020
TS101_HUMAN	TSG101	physical	17538020
FOS_HUMAN	FOS	physical	16055710
MPRD_HUMAN	M6PR	physical	15044437
SMAD3_HUMAN	SMAD3	physical	21829441
ABL1_HUMAN	ABL1	physical	19818398
CSK_HUMAN	CSK	physical	19818398
ITCH_HUMAN	ITCH	physical	19818398
MK08_HUMAN	MAPK8	physical	14701799
PML_HUMAN	PML	physical	10620019
CSN5_HUMAN	COPS5	physical	10766246
FOS_HUMAN	FOS	physical	11090181
PML_HUMAN	PML	physical	15626733
PML_HUMAN	PML	physical	16916642
EPN4_HUMAN	CLINT1	physical	14675752
FOS_HUMAN	FOS	physical	15319445
MK08_HUMAN	MAPK8	physical	8001819
MK09_HUMAN	MAPK9	physical	8001819
RB_HUMAN	RB1	physical	9545246
NFAC2_HUMAN	NFATC2	physical	20557936
TAF4_HUMAN	TAF4	physical	20557936
TCL1A_HUMAN	TCL1A	physical	19064921
RN187_HUMAN	RNF187	physical	23624934
BATF3_HUMAN	BATF3	physical	23661758
BATF2_HUMAN	BATF2	physical	23661758
BATF_HUMAN	BATF	physical	23661758
ATF3_HUMAN	ATF3	physical	23661758
ATF4_HUMAN	ATF4	physical	23661758
FOSL1_HUMAN	FOSL1	physical	23661758
FOS_HUMAN	FOS	physical	23661758
ATF2_HUMAN	ATF2	physical	23661758
FOS_HUMAN	FOS	physical	15718494
EP300_HUMAN	EP300	physical	14630807
FOS_HUMAN	FOS	physical	17440114
NCOR1_HUMAN	NCOR1	physical	17440114
IMA1_HUMAN	KPNA2	physical	21988832
MK10_HUMAN	MAPK10	physical	21988832
NAT14_HUMAN	NAT14	physical	21988832
CBP_HUMAN	CREBBP	physical	15994313
FOS_HUMAN	FOS	physical	20195357
ATF2_HUMAN	ATF2	physical	20195357
CREB3_HUMAN	CREB3	physical	20195357
STRN4_HUMAN	STRN4	physical	20195357
MARE3_HUMAN	MAPRE3	physical	20195357
BBS7_HUMAN	BBS7	physical	20195357
PRC2A_HUMAN	PRRC2A	physical	20195357
A4_HUMAN	APP	physical	20195357
HSP7C_HUMAN	HSPA8	physical	20195357
HS90A_HUMAN	HSP90AA1	physical	20195357
GOPC_HUMAN	GOPC	physical	20195357
APLP2_HUMAN	APLP2	physical	20195357
ATF2_HUMAN	ATF2	physical	15546613
EP300_HUMAN	EP300	physical	21268080
PP2BA_HUMAN	PPP3CA	physical	17215518
SP1_HUMAN	SP1	physical	17215518
EWS_HUMAN	EWSR1	physical	14550555
ETV1_HUMAN	ETV1	physical	14550555
TRIP4_HUMAN	TRIP4	physical	12077347
ATF3_HUMAN	ATF3	physical	26496610
ATF2_HUMAN	ATF2	physical	26496610
FOSL2_HUMAN	FOSL2	physical	26496610
I5P2_HUMAN	INPP5B	physical	26496610
CREB5_HUMAN	CREB5	physical	26496610
ATF7_HUMAN	ATF7	physical	26496610
KLF5_HUMAN	KLF5	physical	19628677
ATF7_HUMAN	ATF7	physical	25609649
CREB5_HUMAN	CREB5	physical	25609649
ATF2_HUMAN	ATF2	physical	25609649
ATF3_HUMAN	ATF3	physical	25609649
FOSB_HUMAN	FOSB	physical	25609649
JDP2_HUMAN	JDP2	physical	25609649
NFAC1_HUMAN	NFATC1	physical	25609649
CEBPB_HUMAN	CEBPB	physical	25609649
FOSL2_HUMAN	FOSL2	physical	25609649
APOA2_HUMAN	APOA2	physical	25609649
BATF3_HUMAN	BATF3	physical	25609649
COE3_HUMAN	EBF3	physical	25609649
MEF2A_HUMAN	MEF2A	physical	25609649
RFWD2_HUMAN	RFWD2	physical	25609649
AP2A_HUMAN	TFAP2A	physical	25609649
NFIX_HUMAN	NFIX	physical	25609649
BANP_HUMAN	BANP	physical	25609649
CREB1_HUMAN	CREB1	physical	25609649
HXB9_HUMAN	HOXB9	physical	25609649
DNLI3_HUMAN	LIG3	physical	25609649
MEF2D_HUMAN	MEF2D	physical	25609649
SNF5_HUMAN	SMARCB1	physical	25609649
SYVC_HUMAN	VARS	physical	25609649
GOPC_HUMAN	GOPC	physical	25609649
JUND_HUMAN	JUND	physical	25609649
EF1D_HUMAN	EEF1D	physical	25609649
BEND4_HUMAN	BEND4	physical	25609649
SYDC_HUMAN	DARS	physical	25609649
SYIC_HUMAN	IARS	physical	25609649
NBR1_HUMAN	NBR1	physical	25609649
NKRF_HUMAN	NKRF	physical	25609649
TMED1_HUMAN	TMED1	physical	25609649
SMAD4_HUMAN	SMAD4	physical	25609649
NFAC4_HUMAN	NFATC4	physical	25609649
NR2F6_HUMAN	NR2F6	physical	25609649
TRI33_HUMAN	TRIM33	physical	25609649
NFAC2_HUMAN	NFATC2	physical	25609649
RAGP1_HUMAN	RANGAP1	physical	25609649
FOS_HUMAN	FOS	physical	25609649
HXD13_HUMAN	HOXD13	physical	25609649
SMRC1_HUMAN	SMARCC1	physical	25609649
ARI3B_HUMAN	ARID3B	physical	25609649
FUBP2_HUMAN	KHSRP	physical	25609649
NKX25_HUMAN	NKX2-5	physical	25609649
PDS5A_HUMAN	PDS5A	physical	25609649
SATB1_HUMAN	SATB1	physical	25609649
SATB2_HUMAN	SATB2	physical	25609649
SIX4_HUMAN	SIX4	physical	25609649
SMRC2_HUMAN	SMARCC2	physical	25609649
SMCE1_HUMAN	SMARCE1	physical	25609649
FBXW7_HUMAN	FBXW7	physical	14739463
ARNT_HUMAN	ARNT	physical	19203995
NFAT5_HUMAN	NFAT5	physical	18056707
EP300_HUMAN	EP300	physical	12471036
ZBT7C_HUMAN	ZBTB7C	physical	27646874
ESR1_HUMAN	ESR1	physical	23747343
BMAL1_HUMAN	ARNTL	physical	27173435
RPR1A_HUMAN	RPRD1A	physical	27173435
HAUS6_HUMAN	HAUS6	physical	27173435
CAVN1_HUMAN	PTRF	physical	27173435
UBP6_HUMAN	USP6	physical	29061731
MK08_HUMAN	MAPK8	physical	9032244
LYRIC_HUMAN	MTDH	physical	27956703
EP300_HUMAN	EP300	physical	27956703
BLM_HUMAN	BLM	physical	23750012

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
DB01169	Arsenic trioxide
DB01029	Irbesartan
DB00852	Pseudoephedrine
DB00570	Vinblastine

Regulatory Network of JUN_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"A specific lysine in c-Jun is required for transcriptional repressionby E1A and is acetylated by p300."; Vries R.G., Prudenziati M., Zwartjes C., Verlaan M., Kalkhoven E.,Zantema A.; EMBO J. 20:6095-6103(2001). Cited for: ACETYLATION AT LYS-271 BY EP300.	11689449 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63 AND SER-243, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62; SER-63; THR-239;SER-243 AND SER-249, AND MASS SPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-63; SER-73;THR-239 AND SER-243, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Activation of Polo-like kinase 3 by hypoxic stresses."; Wang L., Gao J., Dai W., Lu L.; J. Biol. Chem. 283:25928-25935(2008). Cited for: PHOSPHORYLATION AT SER-63 AND SER-73.	18650425 [Abstract]
"Stress-induced c-Jun activation mediated by Polo-like kinase 3 incorneal epithelial cells."; Wang L., Dai W., Lu L.; J. Biol. Chem. 282:32121-32127(2007). Cited for: PHOSPHORYLATION AT SER-63 AND SER-73.	17804415 [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-73, AND MASSSPECTROMETRY.	15302935 [Abstract]
"Activation of protein kinase C decreases phosphorylation of c-Jun atsites that negatively regulate its DNA-binding activity."; Boyle W.J., Smeal T., Defize L.H., Angel P., Woodgett J.R., Karin M.,Hunter T.; Cell 64:573-584(1991). Cited for: PHOSPHORYLATION AT THR-239; SER-243 AND SER-249 BY GSK3B.	1846781 [Abstract]
"P21-activated protein kinase (PAK2)-mediated c-Jun phosphorylation at5 threonine sites promotes cell transformation."; Li T., Zhang J., Zhu F., Wen W., Zykova T., Li X., Liu K., Peng C.,Ma W., Shi G., Dong Z., Bode A.M., Dong Z.; Carcinogenesis 32:659-666(2011). Cited for: PHOSPHORYLATION AT THR-2; THR-8; THR-89; THR-93 AND THR-286, ANDMUTAGENESIS OF THR-2; THR-8; THR-89; THR-93 AND THR-286.	21177766 [Abstract]

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