dbPTM

JUNB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	JUNB_HUMAN
UniProt AC	P17275
Protein Name	Transcription factor jun-B
Gene Name	JUNB
Organism	Homo sapiens (Human).
Sequence Length	347
Subcellular Localization	Nucleus.
Protein Description	Transcription factor involved in regulating gene activity following the primary growth factor response. Binds to the DNA sequence 5'-TGA[CG]TCA-3'..
Protein Sequence	MCTKMEQPFYHDDSYTATGYGRAPGGLSLHDYKLLKPSLAVNLADPYRSLKAPGARGPGPEGGGGGSYFSGQGSDTGASLKLASSELERLIVPNSNGVITTTPTPPGQYFYPRGGGSGGGAGGAGGGVTEEQEGFADGFVKALDDLHKMNHVTPPNVSLGATGGPPAGPGGVYAGPEPPPVYTNLSSYSPASASSGGAGAAVGTGSSYPTTTISYLPHAPPFAGGHPAQLGLGRGASTFKEEPQTVPEARSRDATPPVSPINMEDQERIKVERKRLRNRLAATKCRKRKLERIARLEDKVKTLKAENAGLSSTAGLLREQVAQLKQKVMTHVSNGCQLLLGVKGHAF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Sumoylation	----MCTKMEQPFYH ----CCCCCCCCCCC	35.20	-
4	Sumoylation	----MCTKMEQPFYH ----CCCCCCCCCCC	35.20	28112733
10	Phosphorylation	TKMEQPFYHDDSYTA CCCCCCCCCCCCCCC	15.83	22210691
14	Phosphorylation	QPFYHDDSYTATGYG CCCCCCCCCCCCCCC	30.36	28555341
16	Phosphorylation	FYHDDSYTATGYGRA CCCCCCCCCCCCCCC	22.99	22210691
20	Phosphorylation	DSYTATGYGRAPGGL CCCCCCCCCCCCCCC	10.09	27642862
28	Phosphorylation	GRAPGGLSLHDYKLL CCCCCCCCHHHHHCC	27.25	28555341
32	Phosphorylation	GGLSLHDYKLLKPSL CCCCHHHHHCCCHHH	7.87	27642862
33	Sumoylation	GLSLHDYKLLKPSLA CCCHHHHHCCCHHHE	54.09	-
33	Sumoylation	GLSLHDYKLLKPSLA CCCHHHHHCCCHHHE	54.09	28112733
36	Acetylation	LHDYKLLKPSLAVNL HHHHHCCCHHHEEEC	42.89	23236377
36	Ubiquitination	LHDYKLLKPSLAVNL HHHHHCCCHHHEEEC	42.89	21906983
36	Sumoylation	LHDYKLLKPSLAVNL HHHHHCCCHHHEEEC	42.89	-
36	Sumoylation	LHDYKLLKPSLAVNL HHHHHCCCHHHEEEC	42.89	28112733
47	Phosphorylation	AVNLADPYRSLKAPG EEECCCCCHHCCCCC	17.24	20090780
49	Phosphorylation	NLADPYRSLKAPGAR ECCCCCHHCCCCCCC	28.51	27067055
51	Sumoylation	ADPYRSLKAPGARGP CCCCHHCCCCCCCCC	54.50	-
51	Sumoylation	ADPYRSLKAPGARGP CCCCHHCCCCCCCCC	54.50	-
68	Phosphorylation	EGGGGGSYFSGQGSD CCCCCCCCCCCCCCC	12.68	20090780
70	Phosphorylation	GGGGSYFSGQGSDTG CCCCCCCCCCCCCCC	23.21	28555341
74	Phosphorylation	SYFSGQGSDTGASLK CCCCCCCCCCCCCEE	24.90	25159151
76	Phosphorylation	FSGQGSDTGASLKLA CCCCCCCCCCCEEEC	36.02	22210691
79	Phosphorylation	QGSDTGASLKLASSE CCCCCCCCEEECCHH	27.64	22817900
81	Sumoylation	SDTGASLKLASSELE CCCCCCEEECCHHCC	39.24	28112733
84	O-linked_Glycosylation	GASLKLASSELERLI CCCEEECCHHCCCCC	34.48	30059200
85	O-linked_Glycosylation	ASLKLASSELERLIV CCEEECCHHCCCCCC	40.36	30059200
95	O-linked_Glycosylation	ERLIVPNSNGVITTT CCCCCCCCCCCEECC	28.96	30059200
100	O-linked_Glycosylation	PNSNGVITTTPTPPG CCCCCCEECCCCCCC	23.39	30059200
100	Phosphorylation	PNSNGVITTTPTPPG CCCCCCEECCCCCCC	23.39	27067055
101	Phosphorylation	NSNGVITTTPTPPGQ CCCCCEECCCCCCCC	21.47	22617229
101	O-linked_Glycosylation	NSNGVITTTPTPPGQ CCCCCEECCCCCCCC	21.47	30059200
102	Phosphorylation	SNGVITTTPTPPGQY CCCCEECCCCCCCCC	19.26	25159151
102	O-linked_Glycosylation	SNGVITTTPTPPGQY CCCCEECCCCCCCCC	19.26	30059200
104	Phosphorylation	GVITTTPTPPGQYFY CCEECCCCCCCCCCC	39.77	25159151
104	O-linked_Glycosylation	GVITTTPTPPGQYFY CCEECCCCCCCCCCC	39.77	30059200
109	Phosphorylation	TPTPPGQYFYPRGGG CCCCCCCCCCCCCCC	15.82	20090780
111	Phosphorylation	TPPGQYFYPRGGGSG CCCCCCCCCCCCCCC	6.26	20090780
117	Phosphorylation	FYPRGGGSGGGAGGA CCCCCCCCCCCCCCC	37.22	25159151
129	Phosphorylation	GGAGGGVTEEQEGFA CCCCCCCCHHHHCCC	36.76	23403867
129	O-linked_Glycosylation	GGAGGGVTEEQEGFA CCCCCCCCHHHHCCC	36.76	30059200
141	Sumoylation	GFADGFVKALDDLHK CCCHHHHHHHHHHHH	40.76	28112733
153	O-linked_Glycosylation	LHKMNHVTPPNVSLG HHHCCCCCCCCCCCC	26.02	30059200
158	O-linked_Glycosylation	HVTPPNVSLGATGGP CCCCCCCCCCCCCCC	27.94	30059200
162	O-linked_Glycosylation	PNVSLGATGGPPAGP CCCCCCCCCCCCCCC	40.65	30059200
173	Phosphorylation	PAGPGGVYAGPEPPP CCCCCCCCCCCCCCC	14.76	-
182	Phosphorylation	GPEPPPVYTNLSSYS CCCCCCCCCCHHHCC	8.83	-
188	Phosphorylation	VYTNLSSYSPASASS CCCCHHHCCCCCCCC	18.46	-
189	O-linked_Glycosylation	YTNLSSYSPASASSG CCCHHHCCCCCCCCC	18.88	30059200
194	O-linked_Glycosylation	SYSPASASSGGAGAA HCCCCCCCCCCCCCC	27.33	30059200
195	O-linked_Glycosylation	YSPASASSGGAGAAV CCCCCCCCCCCCCCC	40.75	30059200
204	O-linked_Glycosylation	GAGAAVGTGSSYPTT CCCCCCCCCCCCCCE	27.56	30059200
206	O-linked_Glycosylation	GAAVGTGSSYPTTTI CCCCCCCCCCCCEEE	26.91	30059200
207	O-linked_Glycosylation	AAVGTGSSYPTTTIS CCCCCCCCCCCEEEE	36.15	30059200
210	O-linked_Glycosylation	GTGSSYPTTTISYLP CCCCCCCCEEEECCC	28.48	30059200
211	O-linked_Glycosylation	TGSSYPTTTISYLPH CCCCCCCEEEECCCC	20.02	30059200
212	O-linked_Glycosylation	GSSYPTTTISYLPHA CCCCCCEEEECCCCC	15.48	30059200
214	O-linked_Glycosylation	SYPTTTISYLPHAPP CCCCEEEECCCCCCC	20.65	30059200
237	Phosphorylation	LGLGRGASTFKEEPQ CCCCCCCCCCCCCCC	36.88	28857561
238	Phosphorylation	GLGRGASTFKEEPQT CCCCCCCCCCCCCCC	37.89	25106551
240	Acetylation	GRGASTFKEEPQTVP CCCCCCCCCCCCCCC	62.35	23236377
240	Sumoylation	GRGASTFKEEPQTVP CCCCCCCCCCCCCCC	62.35	-
240	Sumoylation	GRGASTFKEEPQTVP CCCCCCCCCCCCCCC	62.35	25114211
240	Ubiquitination	GRGASTFKEEPQTVP CCCCCCCCCCCCCCC	62.35	21906983
245	Phosphorylation	TFKEEPQTVPEARSR CCCCCCCCCCCHHHC	49.06	23090842
251	Phosphorylation	QTVPEARSRDATPPV CCCCCHHHCCCCCCC	41.37	22167270
255	Phosphorylation	EARSRDATPPVSPIN CHHHCCCCCCCCCCC	32.20	29255136
259	Phosphorylation	RDATPPVSPINMEDQ CCCCCCCCCCCHHHH	26.32	29255136
304	Ubiquitination	EDKVKTLKAENAGLS HHHHHHHHHHHCCCH	59.91	-
304	Sumoylation	EDKVKTLKAENAGLS HHHHHHHHHHHCCCH	59.91	-
304	Sumoylation	EDKVKTLKAENAGLS HHHHHHHHHHHCCCH	59.91	-
311	Phosphorylation	KAENAGLSSTAGLLR HHHHCCCHHHHHHHH	25.40	20068231
312	Phosphorylation	AENAGLSSTAGLLRE HHHCCCHHHHHHHHH	27.58	20068231
313	Phosphorylation	ENAGLSSTAGLLREQ HHCCCHHHHHHHHHH	22.74	20068231
325	Ubiquitination	REQVAQLKQKVMTHV HHHHHHHHHHHHHHH	35.67	-
330	Phosphorylation	QLKQKVMTHVSNGCQ HHHHHHHHHHHCCCE	23.32	-
343	Sumoylation	CQLLLGVKGHAF--- CEEEEEECCCCC---	43.08	28112733

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
79	S	Phosphorylation	Kinase	MAPK14	Q16539	GPS
102	T	Phosphorylation	Kinase	JNK1	P45983	PSP
102	T	Phosphorylation	Kinase	MAPK8	Q91Y86	GPS
104	T	Phosphorylation	Kinase	JNK1	P45983	PSP
104	T	Phosphorylation	Kinase	MAPK8	Q91Y86	GPS
173	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
182	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
188	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
251	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
255	T	Phosphorylation	Kinase	GSK3B	P49841	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	FBXW7	Q969H0	PMID:24658274
-	K	Ubiquitination	E3 ubiquitin ligase	ITCH	Q96J02	PMID:11828324

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NINL_HUMAN	NINL	physical	16189514
FOSL1_HUMAN	FOSL1	physical	16189514
BRCA1_HUMAN	BRCA1	physical	12080089
BATF_HUMAN	BATF	physical	8954125
SMCA4_HUMAN	SMARCA4	physical	14673171
EP300_HUMAN	EP300	physical	15308641
EP300_HUMAN	EP300	physical	17510411
TYY1_HUMAN	YY1	physical	17510411
SMUF1_HUMAN	SMURF1	physical	20200942
TCL1A_HUMAN	TCL1A	physical	19064921
BATF3_HUMAN	BATF3	physical	23661758
BATF2_HUMAN	BATF2	physical	23661758
BATF_HUMAN	BATF	physical	23661758
ATF3_HUMAN	ATF3	physical	23661758
FOSL1_HUMAN	FOSL1	physical	23661758
FOS_HUMAN	FOS	physical	23661758
SET_HUMAN	SET	physical	21988832
NEUR1_HUMAN	NEU1	physical	21988832
MK06_HUMAN	MAPK6	physical	21988832
SAT1_HUMAN	SAT1	physical	21988832
TDG_HUMAN	TDG	physical	21988832
ZSWM9_HUMAN	C19orf68	physical	20195357
IPKA_HUMAN	PKIA	physical	20195357
MTAP2_HUMAN	MAP2	physical	20195357
TCRG1_HUMAN	TCERG1	physical	20195357
APLP2_HUMAN	APLP2	physical	20195357
UBP24_HUMAN	USP24	physical	20195357
BATF_HUMAN	BATF	physical	25416956
FOSL2_HUMAN	FOSL2	physical	28514442
ATF2_HUMAN	ATF2	physical	28514442
CREB5_HUMAN	CREB5	physical	28514442
ATF3_HUMAN	ATF3	physical	28514442
ATF7_HUMAN	ATF7	physical	28514442
BRCA1_HUMAN	BRCA1	physical	28514442
ARI1_HUMAN	ARIH1	physical	28514442
FOSB_HUMAN	FOSB	physical	28514442
JUND_HUMAN	JUND	physical	28514442
MYPT1_HUMAN	PPP1R12A	physical	28514442
NBR1_HUMAN	NBR1	physical	28514442
UBP4_HUMAN	USP4	physical	28514442
RAD18_HUMAN	RAD18	physical	28514442
JUN_HUMAN	JUN	physical	28514442
STK40_HUMAN	STK40	physical	28514442
CN080_HUMAN	C14orf80	physical	28514442
DET1_HUMAN	DET1	physical	28514442
CR025_HUMAN	C18orf25	physical	28514442
RFWD2_HUMAN	RFWD2	physical	28514442
NDE1_HUMAN	NDE1	physical	28514442
GOPC_HUMAN	GOPC	physical	28514442
NUCB2_HUMAN	NUCB2	physical	28514442
TRIB1_HUMAN	TRIB1	physical	28514442
CSN7B_HUMAN	COPS7B	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 JUNB_HUMAN

Related Literatures of Post-Translational Modification

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-251; THR-255 ANDSER-259, AND MASS SPECTROMETRY.	19690332 [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 THR-102; THR-104; SER-117;SER-251; THR-255 AND SER-259, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-255 AND SER-259, ANDMASS SPECTROMETRY.	17081983 [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-259, AND MASSSPECTROMETRY.	15302935 [Abstract]