dbPTM

TF65_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TF65_HUMAN
UniProt AC	Q04206
Protein Name	Transcription factor p65
Gene Name	RELA
Organism	Homo sapiens (Human).
Sequence Length	551
Subcellular Localization	Nucleus. Cytoplasm. Colocalized with DDX1 in the nucleus upon TNF-alpha induction (By similarity). Nuclear, but also found in the cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B). Colocalizes with GFI1 in the nucleus after LPS stim
Protein Description	NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and p65-c-Rel complexes are transcriptional activators. The NF-kappa-B p65-p65 complex appears to be involved in invasin-mediated activation of IL-8 expression. The inhibitory effect of I-kappa-B upon NF-kappa-B the cytoplasm is exerted primarily through the interaction with p65. p65 shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappa-B complex. Associates with chromatin at the NF-kappa-B promoter region via association with DDX1. Essential for cytokine gene expression in T-cells. [PubMed: 15790681]
Protein Sequence	MDELFPLIFPAEPAQASGPYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINGYTGPGTVRISLVTKDPPHRPHPHELVGKDCRDGFYEAELCPDRCIHSFQNLGIQCVKKRDLEQAISQRIQTNNNPFQVPIEEQRGDYDLNAVRLCFQVTVRDPSGRPLRLPPVLSHPIFDNRAPNTAELKICRVNRNSGSCLGGDEIFLLCDKVQKEDIEVYFTGPGWEARGSFSQADVHRQVAIVFRTPPYADPSLQAPVRVSMQLRRPSDRELSEPMEFQYLPDTDDRHRIEEKRKRTYETFKSIMKKSPFSGPTDPRPPPRRIAVPSRSSASVPKPAPQPYPFTSSLSTINYDEFPTMVFPSGQISQASALAPAPPQVLPQAPAPAPAPAMVSALAQAPAPVPVLAPGPPQAVAPPAPKPTQAGEGTLSEALLQLQFDDEDLGALLGNSTDPAVFTDLASVDNSEFQQLLNQGIPVAPHTTEPMLMEYPEAITRLVTGAQRPPDPAPAPLGAPGLPNGLLSGDEDFSSIADMDFSALLSQISS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDELFPLI -------CCCCCCCE	9.01	22814378
36	Phosphorylation	QRGMRFRYKCEGRSA HCCCCEEEEECCCCC	19.78	26074081
37	Methylation	RGMRFRYKCEGRSAG CCCCEEEEECCCCCC	22.89	19864627
37	Sumoylation	RGMRFRYKCEGRSAG CCCCEEEEECCCCCC	22.89	22649547
37	Sumoylation	RGMRFRYKCEGRSAG CCCCEEEEECCCCCC	22.89	-
38	Cysteine persulfide	GMRFRYKCEGRSAGS CCCEEEEECCCCCCC	5.06	-
38	Glutathionylation	GMRFRYKCEGRSAGS CCCEEEEECCCCCCC	5.06	22833525
38	Sulfhydration	GMRFRYKCEGRSAGS CCCEEEEECCCCCCC	5.06	-
38	S-nitrosylation	GMRFRYKCEGRSAGS CCCEEEEECCCCCCC	5.06	22178444
42	Phosphorylation	RYKCEGRSAGSIPGE EEEECCCCCCCCCCC	48.08	26074081
45	Phosphorylation	CEGRSAGSIPGERST ECCCCCCCCCCCCCC	25.90	25262027
56	Ubiquitination	ERSTDTTKTHPTIKI CCCCCCCCCCCEEEE	47.10	21706061
62	Ubiquitination	TKTHPTIKINGYTGP CCCCCEEEECCEECC	32.37	-
62	Acetylation	TKTHPTIKINGYTGP CCCCCEEEECCEECC	32.37	25953088
62	Malonylation	TKTHPTIKINGYTGP CCCCCEEEECCEECC	32.37	26320211
66	Phosphorylation	PTIKINGYTGPGTVR CEEEECCEECCCEEE	12.20	29496907
66	Nitration	PTIKINGYTGPGTVR CEEEECCEECCCEEE	12.20	-
66	Nitrated tyrosine	PTIKINGYTGPGTVR CEEEECCEECCCEEE	12.20	-
71	Phosphorylation	NGYTGPGTVRISLVT CCEECCCEEEEEEEE	15.11	-
79	Ubiquitination	VRISLVTKDPPHRPH EEEEEEECCCCCCCC	61.84	21706061
93	Ubiquitination	HPHELVGKDCRDGFY CCHHCCCCCCCCCCE	46.29	-
112	Phosphorylation	CPDRCIHSFQNLGIQ CCHHHHHHHHHCCCE	14.49	27251275
122	Ubiquitination	NLGIQCVKKRDLEQA HCCCEEEECCCHHHH	50.12	21706061
122	Acetylation	NLGIQCVKKRDLEQA HCCCEEEECCCHHHH	50.12	12419806
123	Ubiquitination	LGIQCVKKRDLEQAI CCCEEEECCCHHHHH	30.65	21706061
123	Acetylation	LGIQCVKKRDLEQAI CCCEEEECCCHHHHH	30.65	12419806
131	Phosphorylation	RDLEQAISQRIQTNN CCHHHHHHHHHHHCC	19.20	20873877
136	Phosphorylation	AISQRIQTNNNPFQV HHHHHHHHCCCCCCC	37.23	-
152	Nitration	IEEQRGDYDLNAVRL CHHHCCCCCCHHEEE	25.75	-
152	Nitrated tyrosine	IEEQRGDYDLNAVRL CHHHCCCCCCHHEEE	25.75	-
160	Glutathionylation	DLNAVRLCFQVTVRD CCHHEEEEEEEEEEC	1.25	22833525
164	Phosphorylation	VRLCFQVTVRDPSGR EEEEEEEEEECCCCC	10.07	24719451
174	Dimethylation	DPSGRPLRLPPVLSH CCCCCCCCCCCCCCC	48.08	-
174	Methylation	DPSGRPLRLPPVLSH CCCCCCCCCCCCCCC	48.08	108442399
180	Phosphorylation	LRLPPVLSHPIFDNR CCCCCCCCCCCCCCC	27.70	23312004
187	Methylation	SHPIFDNRAPNTAEL CCCCCCCCCCCCCEE	53.95	115484907
191	Phosphorylation	FDNRAPNTAELKICR CCCCCCCCCEEEEEE	22.05	28060719
195	Acetylation	APNTAELKICRVNRN CCCCCEEEEEEECCC	31.12	25953088
195	Ubiquitination	APNTAELKICRVNRN CCCCCEEEEEEECCC	31.12	19706600
203	Phosphorylation	ICRVNRNSGSCLGGD EEEECCCCCCCCCCC	28.93	23403867
205	Phosphorylation	RVNRNSGSCLGGDEI EECCCCCCCCCCCEE	13.14	23403867
215	Methylation	GGDEIFLLCDKVQKE CCCEEEEEECCCCHH	2.18	12456660
215	Acetylation	GGDEIFLLCDKVQKE CCCEEEEEECCCCHH	2.18	12456660
216	Glutathionylation	GDEIFLLCDKVQKED CCEEEEEECCCCHHC	5.31	22833525
218	Acetylation	EIFLLCDKVQKEDIE EEEEEECCCCHHCEE	45.64	12456660
218	Ubiquitination	EIFLLCDKVQKEDIE EEEEEECCCCHHCEE	45.64	12456660
218	Methylation	EIFLLCDKVQKEDIE EEEEEECCCCHHCEE	45.64	12456660
221	Acetylation	LLCDKVQKEDIEVYF EEECCCCHHCEEEEE	61.41	12456660
221	Methylation	LLCDKVQKEDIEVYF EEECCCCHHCEEEEE	61.41	12456660
238	Phosphorylation	PGWEARGSFSQADVH CCCHHCCCCHHHHHC	19.03	25849741
240	Phosphorylation	WEARGSFSQADVHRQ CHHCCCCHHHHHCCC	26.59	30266825
254	Phosphorylation	QVAIVFRTPPYADPS CEEEEEECCCCCCCC	19.70	14690596
261	Phosphorylation	TPPYADPSLQAPVRV CCCCCCCCCCCCEEE	33.39	-
269	O-linked_Glycosylation	LQAPVRVSMQLRRPS CCCCEEEEEEECCCC	7.11	29706631
269	Phosphorylation	LQAPVRVSMQLRRPS CCCCEEEEEEECCCC	7.11	-
276	Phosphorylation	SMQLRRPSDRELSEP EEEECCCCCCCCCCC	47.70	20516073
281	Phosphorylation	RPSDRELSEPMEFQY CCCCCCCCCCCCCEE	34.60	18223231
284	Sulfoxidation	DRELSEPMEFQYLPD CCCCCCCCCCEECCC	7.66	30846556
305	O-linked_Glycosylation	IEEKRKRTYETFKSI HHHHHHHHHHHHHHH	28.83	29706631
305	Phosphorylation	IEEKRKRTYETFKSI HHHHHHHHHHHHHHH	28.83	29496907
306	Phosphorylation	EEKRKRTYETFKSIM HHHHHHHHHHHHHHH	19.60	28674419
307	Acetylation	EKRKRTYETFKSIMK HHHHHHHHHHHHHHH	47.34	12456660
307	Methylation	EKRKRTYETFKSIMK HHHHHHHHHHHHHHH	47.34	12456660
307	Ubiquitination	EKRKRTYETFKSIMK HHHHHHHHHHHHHHH	47.34	12456660
308	Phosphorylation	KRKRTYETFKSIMKK HHHHHHHHHHHHHHH	26.42	-
310	Ubiquitination	KRTYETFKSIMKKSP HHHHHHHHHHHHHCC	46.63	17000776
310	Methylation	KRTYETFKSIMKKSP HHHHHHHHHHHHHCC	46.63	17000776
310	Acetylation	KRTYETFKSIMKKSP HHHHHHHHHHHHHCC	46.63	17000776
311	Phosphorylation	RTYETFKSIMKKSPF HHHHHHHHHHHHCCC	24.59	21515635
314	Ubiquitination	ETFKSIMKKSPFSGP HHHHHHHHHCCCCCC	48.72	21706061
314	Acetylation	ETFKSIMKKSPFSGP HHHHHHHHHCCCCCC	48.72	18263619
314	Methylation	ETFKSIMKKSPFSGP HHHHHHHHHCCCCCC	48.72	19262565
315	Acetylation	TFKSIMKKSPFSGPT HHHHHHHHCCCCCCC	46.08	18263619
315	Methylation	TFKSIMKKSPFSGPT HHHHHHHHCCCCCCC	46.08	19262565
315	Ubiquitination	TFKSIMKKSPFSGPT HHHHHHHHCCCCCCC	46.08	2170606
316	Phosphorylation	FKSIMKKSPFSGPTD HHHHHHHCCCCCCCC	26.17	26055452
319	O-linked_Glycosylation	IMKKSPFSGPTDPRP HHHHCCCCCCCCCCC	47.44	29706631
319	Phosphorylation	IMKKSPFSGPTDPRP HHHHCCCCCCCCCCC	47.44	29214152
322	Phosphorylation	KSPFSGPTDPRPPPR HCCCCCCCCCCCCCC	63.26	26270265
322	O-linked_Glycosylation	KSPFSGPTDPRPPPR HCCCCCCCCCCCCCC	63.26	32114385
335	Phosphorylation	PRRIAVPSRSSASVP CCCEECCCCCCCCCC	37.89	28348404
337	Phosphorylation	RIAVPSRSSASVPKP CEECCCCCCCCCCCC	34.29	28348404
337	O-linked_Glycosylation	RIAVPSRSSASVPKP CEECCCCCCCCCCCC	34.29	29706631
338	Phosphorylation	IAVPSRSSASVPKPA EECCCCCCCCCCCCC	24.37	28348404
340	Phosphorylation	VPSRSSASVPKPAPQ CCCCCCCCCCCCCCC	40.68	28348404
352	O-linked_Glycosylation	APQPYPFTSSLSTIN CCCCCCCCCCCCCCC	16.95	32114385
374	O-linked_Glycosylation	VFPSGQISQASALAP EECCCCCCCCCCCCC	16.29	29706631
377	O-linked_Glycosylation	SGQISQASALAPAPP CCCCCCCCCCCCCCC	19.04	128453829
435	Phosphorylation	PTQAGEGTLSEALLQ CCCCCCCCHHHHHHH	23.86	20001970
468	Phosphorylation	AVFTDLASVDNSEFQ CHHHCCCCCCHHHHH	36.98	16046471
472	Phosphorylation	DLASVDNSEFQQLLN CCCCCCHHHHHHHHH	35.01	-
483 (in isoform 2)	Phosphorylation	-	24.04	23879269
492 (in isoform 2)	Phosphorylation	-	4.53	23879269
505	Phosphorylation	EAITRLVTGAQRPPD HHHHHHHHCCCCCCC	31.24	21737676
529	Phosphorylation	GLPNGLLSGDEDFSS CCCCCCCCCCCCHHH	49.60	15856023
536	Phosphorylation	SGDEDFSSIADMDFS CCCCCHHHHHHCCHH	23.07	15100319
543	Phosphorylation	SIADMDFSALLSQIS HHHHCCHHHHHHHHC	17.47	10938077
547	Phosphorylation	MDFSALLSQISS--- CCHHHHHHHHCC---	26.73	-

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
42	S	Phosphorylation	Kinase	IKBKB	O14920	GPS
42	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
45	S	Phosphorylation	Kinase	IKBKB	O14920	GPS
45	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
131	S	Phosphorylation	Kinase	IKBKB	O14920	GPS
261	S	Phosphorylation	Kinase	IKBKB	O14920	GPS
276	S	Phosphorylation	Kinase	PKACA	P17612	PSP
276	S	Phosphorylation	Kinase	KS6A5	O75582	PhosphoELM
276	S	Phosphorylation	Kinase	MSK2	O75676	PSP
276	S	Phosphorylation	Kinase	RSK2	P51812	PSP
276	S	Phosphorylation	Kinase	P90RSK	Q15418	PSP
276	S	Phosphorylation	Kinase	PIM1	P11309	PSP
276	S	Phosphorylation	Kinase	PRKACA	P05132	GPS
276	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
311	S	Phosphorylation	Kinase	IKBKB	O14920	GPS
311	S	Phosphorylation	Kinase	KPCZ	Q05513	PhosphoELM
316	S	Phosphorylation	Kinase	CSNK1A1	P48729	GPS
435	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
468	S	Phosphorylation	Kinase	IKBKE	Q14164	GPS
468	S	Phosphorylation	Kinase	IKBKB	O14920	GPS
468	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
505	T	Phosphorylation	Kinase	CHK1	O14757	PSP
529	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
529	S	Phosphorylation	Kinase	CK2	-	Uniprot
529	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
529	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
536	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
536	S	Phosphorylation	Kinase	CAMK4	Q16566	PSP
536	S	Phosphorylation	Kinase	TBK1	Q9UHD2	PSP
536	S	Phosphorylation	Kinase	CSNK1G1	Q9HCP0	GPS
536	S	Phosphorylation	Kinase	IKK-FAMILY	-	GPS
536	S	Phosphorylation	Kinase	IKBKE	Q14164	GPS
536	S	Phosphorylation	Kinase	IKBKB	O14920	GPS
536	S	Phosphorylation	Kinase	CHUK	O15111	GPS
536	S	Phosphorylation	Kinase	IKK_GROUP	-	PhosphoELM
-	K	Ubiquitination	E3 ubiquitin ligase	PPARG	P37231	PMID:23250430
-	K	Ubiquitination	E3 ubiquitin ligase	ING4	Q9UNL4	PMID:23624912
-	K	Ubiquitination	E3 ubiquitin ligase	PDLIM2	Q96JY6	PMID:17468759
-	K	Ubiquitination	E3 ubiquitin ligase	SOCS1	O15524	PMID:19339690
-	K	Ubiquitination	E3 ubiquitin ligase	TRIM21	P19474	PMID:32232831

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
38	C	S-nitrosylation	-
S-nitrosylation of Cys-38 inactivates the enzyme activity.
122	K	Acetylation	12419806
Acetylation at Lys-122 enhances DNA binding and impairs association with NFKBIA.
276	S	Phosphorylation	12628924
Phosphorylation at Ser-276 by RPS6KA4 and RPS6KA5 promotes its transactivation and transcriptional activities.
310	K	Methylation	12456660
Phosphorylation at Ser-311 disrupts the interaction with EHMT1 without preventing monomethylation at Lys-310 and relieves the repression of target genes (By similarity).
310	K	Phosphorylation	12456660
Phosphorylation on Ser-536 stimulates acetylation on Lys-310 and interaction with CBP; the phosphorylated and acetylated forms show enhanced transcriptional activity.
310	K	Phosphorylation	12456660
Phosphorylation at Ser-311 disrupts the interaction with EHMT1 without preventing monomethylation at Lys-310 and relieves the repression of target genes (By similarity).
310	K	Methylation	12456660
Monomethylation at Lys-310 is recognized by the ANK repeats of EHMT1 and promotes the formation of repressed chromatin at target genes, leading to down-regulation of NF-kappa-B transcription factor activity.
310	K	Methylation	12456660
Monomethylated at Lys-310 by SETD6.
310	K	Acetylation	12456660
Phosphorylation on Ser-536 stimulates acetylation on Lys-310 and interaction with CBP; the phosphorylated and acetylated forms show enhanced transcriptional activity.
310	K	Acetylation	12456660
Lys-310 is deacetylated by SIRT2.
310	K	Acetylation	12456660
Interaction with BRMS1 promotes deacetylation of Lys-310.
310	K	Acetylation	12456660
Acetylation at Lys-310 promotes interaction with BRD4.
310	K	Acetylation	12456660
Acetylation at Lys-310 is required for full transcriptional activity in the absence of effects on DNA binding and NFKBIA association.
311	S	Methylation	-
Phosphorylation at Ser-311 disrupts the interaction with EHMT1 without preventing monomethylation at Lys-310 and relieves the repression of target genes (By similarity).
311	S	Phosphorylation	16135789
Phosphorylation at Ser-311 disrupts the interaction with EHMT1 and promotes transcription factor activity (By similarity).
311	S	Phosphorylation	-
Phosphorylation at Ser-311 disrupts the interaction with EHMT1 without preventing monomethylation at Lys-310 and relieves the repression of target genes (By similarity).
536	S	Acetylation	10521409
Phosphorylation on Ser-536 stimulates acetylation on Lys-310 and interaction with CBP; the phosphorylated and acetylated forms show enhanced transcriptional activity.
536	S	Phosphorylation	10521409
Phosphorylation on Ser-536 stimulates acetylation on Lys-310 and interaction with CBP; the phosphorylated and acetylated forms show enhanced transcriptional activity.

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 TF65_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FOS_HUMAN	FOS	physical	10488148
PIAS3_HUMAN	PIAS3	physical	15140884
RNF25_HUMAN	RNF25	physical	12748188
IASPP_HUMAN	PPP1R13L	physical	10336463
IQGA2_HUMAN	IQGAP2	physical	14743216
AKP8L_HUMAN	AKAP8L	physical	14743216
TNIP2_HUMAN	TNIP2	physical	14743216
TRIB3_HUMAN	TRIB3	physical	12736262
BRCA1_HUMAN	BRCA1	physical	12700228
HMGB1_HUMAN	HMGB1	physical	12665595
HDAC3_HUMAN	HDAC3	physical	11533489
HDAC1_HUMAN	HDAC1	physical	12419806
HDAC2_HUMAN	HDAC2	physical	12419806
IKBA_HUMAN	NFKBIA	physical	12419806
HDAC1_HUMAN	HDAC1	physical	11931769
CBP_HUMAN	CREBBP	physical	11931769
HDAC1_HUMAN	HDAC1	physical	11564889
CBP_HUMAN	CREBBP	physical	9548485
CBP_HUMAN	CREBBP	genetic	9548485
CBP_HUMAN	CREBBP	genetic	9482849
CBP_HUMAN	CREBBP	genetic	9096323
EP300_HUMAN	EP300	genetic	9096323
JUN_HUMAN	JUN	physical	10488148
FOS_HUMAN	FOS	genetic	10488148
JUN_HUMAN	JUN	genetic	10488148
MEN1_HUMAN	MEN1	physical	11526476
PP2AA_HUMAN	PPP2CA	physical	11591705
PP2AB_HUMAN	PPP2CB	physical	11591705
CDK9_HUMAN	CDK9	physical	12173051
NOTC1_HUMAN	NOTCH1	physical	8642313
ETHE1_HUMAN	ETHE1	physical	12398897
AHR_HUMAN	AHR	physical	11114727
PPARA_HUMAN	PPARA	physical	10542237
TERT_HUMAN	TERT	physical	12517770
APBA2_HUMAN	APBA2	physical	10777610
RFC1_HUMAN	RFC1	physical	12509469
FBW1A_HUMAN	BTRC	physical	9990853
IKBA_HUMAN	NFKBIA	physical	9990853
RXRA_HUMAN	RXRA	physical	10075655
SP1_HUMAN	SP1	physical	7933095
AES_HUMAN	AES	physical	10660609
IKBB_HUMAN	NFKBIB	physical	8816457
IKBA_HUMAN	NFKBIA	physical	8139561
REL_HUMAN	REL	physical	8139561
IKBA_HUMAN	NFKBIA	physical	9738011
NCOR2_HUMAN	NCOR2	physical	10777532
PP4C_HUMAN	PPP4C	physical	9837938
PARP1_HUMAN	PARP1	physical	11590148
MTPN_HUMAN	MTPN	physical	11971907
NFKB2_HUMAN	NFKB2	physical	8413211
PO2F1_HUMAN	POU2F1	physical	12019209
TAF1_HUMAN	TAF1	physical	9584164
TBP_HUMAN	TBP	physical	9584164
TAF6_HUMAN	TAF6	physical	9584164
TAF11_HUMAN	TAF11	physical	9584164
TWST1_HUMAN	TWIST1	physical	12553906
TBP_HUMAN	TBP	physical	7706261
TF2B_HUMAN	GTF2B	physical	7706261
TBP_HUMAN	TBP	genetic	7706261
TF65_HUMAN	RELA	physical	10336463
TAF4B_HUMAN	TAF4B	physical	9724652
HDAC2_HUMAN	HDAC2	physical	12138131
EGR1_HUMAN	EGR1	physical	10671503
CEBPB_HUMAN	CEBPB	physical	9570146
CEBPD_HUMAN	CEBPD	physical	9570146
GCR_HUMAN	NR3C1	physical	10995388
GCR_HUMAN	NR3C1	physical	7659084
IRF8_HUMAN	IRF8	physical	8550813
IRF2_HUMAN	IRF2	physical	8550813
IRF9_HUMAN	IRF9	physical	8550813
DHX9_HUMAN	DHX9	physical	15355351
TBP_HUMAN	TBP	physical	10839990
ETHE1_HUMAN	ETHE1	physical	17353187
ING4_HUMAN	ING4	physical	18779315
SOCS1_HUMAN	SOCS1	physical	17183367
KDM2A_HUMAN	KDM2A	physical	20080798
NSD1_HUMAN	NSD1	physical	20080798
SIR6_HUMAN	SIRT6	physical	19135889
HDAC1_HUMAN	HDAC1	physical	20001970
USF2_HUMAN	USF2	physical	20936779
BRMS1_HUMAN	BRMS1	physical	17000776
HDAC1_HUMAN	HDAC1	physical	17000776
CARM1_HUMAN	CARM1	physical	16497732
HDAC1_HUMAN	HDAC1	physical	16483679
NFKB1_HUMAN	NFKB1	physical	16319923
ATF3_HUMAN	ATF3	physical	16291753
PARP1_HUMAN	PARP1	physical	16204234
NFKB1_HUMAN	NFKB1	physical	16204234
IKBA_HUMAN	NFKBIA	physical	7878004
CARM1_HUMAN	CARM1	physical	15616592
EP300_HUMAN	EP300	physical	11585920
ANM1_HUMAN	PRMT1	physical	18280497
TF65_HUMAN	RELA	physical	18280497
EP300_HUMAN	EP300	physical	18280497
PARP1_HUMAN	PARP1	physical	18280497
CARM1_HUMAN	CARM1	physical	18280497
HDAC2_HUMAN	HDAC2	physical	11395507
SP1_HUMAN	SP1	physical	18249093
HDAC2_HUMAN	HDAC2	physical	10958685
CBP_HUMAN	CREBBP	physical	10542243
EP300_HUMAN	EP300	physical	15192014
HDAC1_HUMAN	HDAC1	physical	15192014
HDAC3_HUMAN	HDAC3	physical	15192014
RS3_HUMAN	RPS3	physical	18045535
EP300_HUMAN	EP300	physical	10235267
CBP_HUMAN	CREBBP	physical	10235267
MED15_HUMAN	MED15	physical	10235267
MED23_HUMAN	MED23	physical	10235267
MED7_HUMAN	MED7	physical	10235267
PSD10_HUMAN	PSMD10	physical	17904523
HDAC1_HUMAN	HDAC1	physical	17827154
HDAC2_HUMAN	HDAC2	physical	17827154
CBP_HUMAN	CREBBP	physical	17362989
IKBA_HUMAN	NFKBIA	physical	8887633
IKBA_HUMAN	NFKBIA	physical	8978697
IKBA_HUMAN	NFKBIA	physical	7628694
IKBA_HUMAN	NFKBIA	physical	20065107
COMD1_HUMAN	COMMD1	physical	19270718
CUL2_HUMAN	CUL2	physical	19270718
IKBA_HUMAN	NFKBIA	physical	20551178
KAT2A_HUMAN	KAT2A	physical	19339690
AFF1_HUMAN	AFF1	physical	21030982
KEAP1_HUMAN	KEAP1	physical	21262351
P63_HUMAN	TP63	physical	22020940
RL13_HUMAN	RPL13	physical	21900206
MK14_HUMAN	MAPK14	physical	21900206
IKBB_HUMAN	NFKBIB	physical	22081069
IKBA_HUMAN	NFKBIA	physical	22081069
SOCS1_HUMAN	SOCS1	physical	21084693
ZBT7B_HUMAN	ZBTB7B	physical	22139845
SP3_HUMAN	SP3	physical	22139845
SP1_HUMAN	SP1	physical	22139845
NFKB1_HUMAN	NFKB1	physical	22139845
CEBPZ_HUMAN	CEBPZ	physical	22139845
IKBA_HUMAN	NFKBIA	physical	8657102
SETD6_HUMAN	SETD6	physical	21131967
EHMT1_HUMAN	EHMT1	physical	21131967
RELB_HUMAN	RELB	physical	21884980
EZH2_HUMAN	EZH2	physical	21884980
SUZ12_HUMAN	SUZ12	physical	21884980
DPF3_HUMAN	DPF3	physical	22334708
SMCA2_HUMAN	SMARCA2	physical	22334708
KAT5_HUMAN	KAT5	physical	22249179
NFKB1_HUMAN	NFKB1	physical	14690596
IKBA_HUMAN	NFKBIA	physical	14690596
ACTS_HUMAN	ACTA1	physical	14690596
SOCS1_HUMAN	SOCS1	physical	14690596
STAT3_HUMAN	STAT3	physical	14593105
NFKB1_HUMAN	NFKB1	physical	15799966
COMD1_HUMAN	COMMD1	physical	15799966
IKBA_HUMAN	NFKBIA	physical	15799966
TBL1X_HUMAN	TBL1X	physical	21189284
CHFR_HUMAN	CHFR	physical	19448676
NFKB2_HUMAN	NFKB2	physical	16009713
DNJA3_HUMAN	DNAJA3	physical	15601829
SOCS3_HUMAN	SOCS3	physical	21451109
ZBT7A_HUMAN	ZBTB7A	physical	15917220
CBP_HUMAN	CREBBP	physical	14597638
CEBPB_HUMAN	CEBPB	physical	16785565
ESR1_HUMAN	ESR1	physical	16331275
OGT1_HUMAN	OGT	physical	17882263
UBP7_HUMAN	USP7	physical	23267096
HIF1A_HUMAN	HIF1A	physical	23123196
PPARG_HUMAN	PPARG	physical	23250430
IKBA_HUMAN	NFKBIA	physical	8887627
IKBB_HUMAN	NFKBIB	physical	8887627
LYRIC_HUMAN	MTDH	physical	18316612
IKBA_HUMAN	NFKBIA	physical	23563313
ANM5_HUMAN	PRMT5	physical	23904475
NFKB1_HUMAN	NFKB1	physical	20154269
EP300_HUMAN	EP300	physical	20154269
DHSO_HUMAN	SORD	physical	21988832
SMAD3_HUMAN	SMAD3	physical	21988832
SMAD4_HUMAN	SMAD4	physical	21988832
RNAS1_HUMAN	RNASE1	physical	21988832
SAT1_HUMAN	SAT1	physical	21988832
RU17_HUMAN	SNRNP70	physical	21988832
TELT_HUMAN	TCAP	physical	21988832
SOCS6_HUMAN	SOCS6	physical	21988832
TRIP4_HUMAN	TRIP4	physical	21988832
RL23_HUMAN	RPL23	physical	21988832
RIOK2_HUMAN	RIOK2	physical	21988832
CBP_HUMAN	CREBBP	physical	9806899
IKBA_HUMAN	NFKBIA	physical	7739549
IKBA_HUMAN	NFKBIA	physical	9572494
HSP7C_HUMAN	HSPA8	physical	24175631
NFKB1_HUMAN	NFKB1	physical	24175631
KC1G1_HUMAN	CSNK1G1	physical	24442433
CUL2_HUMAN	CUL2	physical	24442433
STAT3_HUMAN	STAT3	physical	23335796
EP300_HUMAN	EP300	physical	17692505
TF65_HUMAN	RELA	physical	25331947
DCD_HUMAN	DCD	physical	25331947
K2C5_HUMAN	KRT5	physical	25331947
GRP78_HUMAN	HSPA5	physical	25331947
POTEJ_HUMAN	POTEJ	physical	25331947
IL1RA_HUMAN	IL1RN	physical	25331947
POTEE_HUMAN	POTEE	physical	25331947
PLMN_HUMAN	PLG	physical	25331947
SRSF7_HUMAN	SRSF7	physical	25331947
M3K8_HUMAN	MAP3K8	physical	25331947
DI3L2_HUMAN	DIS3L2	physical	25331947
GAN_HUMAN	GAN	physical	25331947
PRKDC_HUMAN	PRKDC	physical	25331947
PIWL4_HUMAN	PIWIL4	physical	25331947
ABCA1_HUMAN	ABCA1	physical	25331947
S31A3_HUMAN	SPATA31A3	physical	25331947
PEX1_HUMAN	PEX1	physical	25331947
REV1_HUMAN	REV1	physical	25331947
CDN2A_HUMAN	CDKN2A	physical	25331947
ARF_HUMAN	CDKN2A	physical	25331947
CDK4_HUMAN	CDK4	physical	25331947
CCND1_HUMAN	CCND1	physical	25331947
ITF2_HUMAN	TCF4	physical	25416956
EP300_HUMAN	EP300	physical	17982102
CBP_HUMAN	CREBBP	physical	17434128
P53_HUMAN	TP53	physical	17434128
IKKA_HUMAN	CHUK	physical	17434128
EP300_HUMAN	EP300	physical	18397880
TF65_HUMAN	RELA	physical	12456660
CENPJ_HUMAN	CENPJ	physical	15687488
ECSIT_HUMAN	ECSIT	physical	25355951
NFKB1_HUMAN	NFKB1	physical	25355951
PPARG_HUMAN	PPARG	physical	18556801
PPARG_HUMAN	PPARG	physical	17312272
ING4_HUMAN	ING4	physical	23624912
MDM2_HUMAN	MDM2	physical	23839035
EP300_HUMAN	EP300	physical	25074812
NFKB1_HUMAN	NFKB1	physical	22261743
IKBA_HUMAN	NFKBIA	physical	10085161
ANDR_HUMAN	AR	genetic	9482849
CASK_HUMAN	CSN3	physical	25486460
UBC_HUMAN	UBC	physical	25486460
EP300_HUMAN	EP300	physical	23999430
TRIP4_HUMAN	TRIP4	physical	12077347
EP300_HUMAN	EP300	physical	25400040
SNAI1_HUMAN	SNAI1	physical	25314079
IKBA_HUMAN	NFKBIA	physical	25520503
KAISO_HUMAN	ZBTB33	physical	26183023
IKBA_HUMAN	NFKBIA	physical	25609694
IKBA_HUMAN	NFKBIA	physical	26463447
DNM3L_HUMAN	DNMT3L	physical	24952347
DNM3B_HUMAN	DNMT3B	physical	24952347
HERC3_HUMAN	HERC3	physical	26476452
PRS7_HUMAN	PSMC2	physical	26476452
IKBA_HUMAN	NFKBIA	physical	26476452
NPM_HUMAN	NPM1	physical	19074833
SP1_HUMAN	SP1	physical	19074833
EP300_HUMAN	EP300	physical	16135789
IKKA_HUMAN	CHUK	physical	22689577
IKKB_HUMAN	IKBKB	physical	22689577
CDX2_HUMAN	CDX2	physical	17876541
CDX2_HUMAN	CDX2	physical	15013430
EP300_HUMAN	EP300	physical	12471036
LOX5_HUMAN	ALOX5	physical	9681993
IKBA_HUMAN	NFKBIA	physical	27923823

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 TF65_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-310, AND MASS SPECTROMETRY.	19608861 [Abstract]
"Breast cancer metastasis suppressor 1 functions as a corepressor byenhancing histone deacetylase 1-mediated deacetylation of RelA/p65 andpromoting apoptosis."; Liu Y., Smith P.W., Jones D.R.; Mol. Cell. Biol. 26:8683-8696(2006). Cited for: INTERACTION WITH BRMS1, FUNCTION, AND ACETYLATION AT LYS-310.	17000776 [Abstract]
"NF-kappaB RelA phosphorylation regulates RelA acetylation."; Chen L.F., Williams S.A., Mu Y., Nakano H., Duerr J.M., Buckbinder L.,Greene W.C.; Mol. Cell. Biol. 25:7966-7975(2005). Cited for: ACETYLATION AT LYS-310.	16135789 [Abstract]
"Post-activation turn-off of NF-kappa B-dependent transcription isregulated by acetylation of p65."; Kiernan R., Bres V., Ng R.W., Coudart M.-P., El Messaoudi S.,Sardet C., Jin D.-Y., Emiliani S., Benkirane M.; J. Biol. Chem. 278:2758-2766(2003). Cited for: ACETYLATION AT LYS-122 AND LYS-123.	12419806 [Abstract]
"Acetylation of RelA at discrete sites regulates distinct nuclearfunctions of NF-kappaB."; Chen L.F., Mu Y., Greene W.C.; EMBO J. 21:6539-6548(2002). Cited for: ACETYLATION AT LYS-218; LYS-221 AND LYS-310.	12456660 [Abstract]
Phosphorylation
Reference	PubMed
"Inducible phosphorylation of NF-kappa B p65 at serine 468 by T cellcostimulation is mediated by IKK epsilon."; Mattioli I., Geng H., Sebald A., Hodel M., Bucher C., Kracht M.,Schmitz M.L.; J. Biol. Chem. 281:6175-6183(2006). Cited for: PHOSPHORYLATION AT SER-468.	16407239 [Abstract]
"IKKbeta phosphorylates p65 at S468 in transactivaton domain 2."; Schwabe R.F., Sakurai H.; FASEB J. 19:1758-1760(2005). Cited for: PHOSPHORYLATION AT SER-468.	16046471 [Abstract]
"Transcriptional activation of the NF-kappaB p65 subunit by mitogen-and stress-activated protein kinase-1 (MSK1)."; Vermeulen L., De Wilde G., Van Damme P., Vanden Berghe W.,Haegeman G.; EMBO J. 22:1313-1324(2003). Cited for: INTERACTION WITH RPS6KA5, MUTAGENESIS OF SER-276, AND PHOSPHORYLATIONAT SER-276.	12628924 [Abstract]
"Tumor necrosis factor alpha-induced phosphorylation of RelA/p65 onSer529 is controlled by casein kinase II."; Wang D., Westerheide S.D., Hanson J.L., Baldwin A.S. Jr.; J. Biol. Chem. 275:32592-32597(2000). Cited for: PHOSPHORYLATION AT SER-529.	10938077 [Abstract]
"IkappaB kinases phosphorylate NF-kappaB p65 subunit on serine 536 inthe transactivation domain."; Sakurai H., Chiba H., Miyoshi H., Sugita T., Toriumi W.; J. Biol. Chem. 274:30353-30356(1999). Cited for: PHOSPHORYLATION AT SER-536.	10521409 [Abstract]
"Regulation of NF-kappaB and p53 through activation of ATR and Chk1 bythe ARF tumour suppressor."; Rocha S., Garrett M.D., Campbell K.J., Schumm K., Perkins N.D.; EMBO J. 24:1157-1169(2005). Cited for: PHOSPHORYLATION AT THR-505.	15775976 [Abstract]
"Suppression of MEK/ERK signaling pathway enhances cisplatin-inducedNF-kappaB activation by protein phosphatase 4-mediated NF-kappaB p65Thr dephosphorylation."; Yeh P.Y., Yeh K.H., Chuang S.E., Song Y.C., Cheng A.L.; J. Biol. Chem. 279:26143-26148(2004). Cited for: PHOSPHORYLATION AT THR-435.	15073167 [Abstract]
"Regulation of NF-kappaB signaling by Pin1-dependent prolylisomerization and ubiquitin-mediated proteolysis of p65/RelA."; Ryo A., Suizu F., Yoshida Y., Perrem K., Liou Y.C., Wulf G.,Rottapel R., Yamaoka S., Lu K.P.; Mol. Cell 12:1413-1426(2003). Cited for: PHOSPHORYLATION AT THR-254, INTERACTION WITH PIN1 AND SOCS1, ANDMUTAGENESIS OF THR-254.	14690596 [Abstract]

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