dbPTM

REL_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	REL_HUMAN
UniProt AC	Q04864
Protein Name	Proto-oncogene c-Rel
Gene Name	REL
Organism	Homo sapiens (Human).
Sequence Length	619
Subcellular Localization	Nucleus.
Protein Description	Proto-oncogene that may play a role in differentiation and lymphopoiesis. NF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed 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. 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. The NF-kappa-B heterodimer RELA/p65-c-Rel is a transcriptional activator..
Protein Sequence	MASGAYNPYIEIIEQPRQRGMRFRYKCEGRSAGSIPGEHSTDNNRTYPSIQIMNYYGKGKVRITLVTKNDPYKPHPHDLVGKDCRDGYYEAEFGQERRPLFFQNLGIRCVKKKEVKEAIITRIKAGINPFNVPEKQLNDIEDCDLNVVRLCFQVFLPDEHGNLTTALPPVVSNPIYDNRAPNTAELRICRVNKNCGSVRGGDEIFLLCDKVQKDDIEVRFVLNDWEAKGIFSQADVHRQVAIVFKTPPYCKAITEPVTVKMQLRRPSDQEVSESMDFRYLPDEKDTYGNKAKKQKTTLLFQKLCQDHVETGFRHVDQDGLELLTSGDPPTLASQSAGITVNFPERPRPGLLGSIGEGRYFKKEPNLFSHDAVVREMPTGVSSQAESYYPSPGPISSGLSHHASMAPLPSSSWSSVAHPTPRSGNTNPLSSFSTRTLPSNSQGIPPFLRIPVGNDLNASNACIYNNADDIVGMEASSMPSADLYGISDPNMLSNCSVNMMTTSSDSMGETDNPRLLSMNLENPSCNSVLDPRDLRQLHQMSSSSMSAGANSNTTVFVSQSDAFEGSDFSCADNSMINESGPSNSTNPNSHGFVQDSQYSGIGSMQNEQLSDSFPYEFFQV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASGAYNPY ------CCCCCCCCC	19.37	22814378
3	Phosphorylation	-----MASGAYNPYI -----CCCCCCCCCE	23.74	23186163
6	Phosphorylation	--MASGAYNPYIEII --CCCCCCCCCEEEE	21.86	24719451
26	Sumoylation	RGMRFRYKCEGRSAG CCCCEEEEECCCCCC	22.89	-
26	Sumoylation	RGMRFRYKCEGRSAG CCCCEEEEECCCCCC	22.89	-
31	Phosphorylation	RYKCEGRSAGSIPGE EEEECCCCCCCCCCC	48.08	20873877
34	Phosphorylation	CEGRSAGSIPGEHST ECCCCCCCCCCCCCC	25.90	24719451
46	Phosphorylation	HSTDNNRTYPSIQIM CCCCCCCCCCEEEEE	41.74	29507054
47	Phosphorylation	STDNNRTYPSIQIMN CCCCCCCCCEEEEEE	7.55	24043423
49	Phosphorylation	DNNRTYPSIQIMNYY CCCCCCCEEEEEEEE	19.40	24043423
55	Phosphorylation	PSIQIMNYYGKGKVR CEEEEEEEECCCEEE	9.01	24043423
56	Phosphorylation	SIQIMNYYGKGKVRI EEEEEEEECCCEEEE	13.83	24043423
68	Acetylation	VRITLVTKNDPYKPH EEEEEEECCCCCCCC	52.45	25953088
82	Ubiquitination	HPHDLVGKDCRDGYY CCCCCCCCCCCCCCE	46.29	29967540
88	Phosphorylation	GKDCRDGYYEAEFGQ CCCCCCCCEECCCCC	11.47	22817900
89	Phosphorylation	KDCRDGYYEAEFGQE CCCCCCCEECCCCCC	17.75	22817900
176	Phosphorylation	PVVSNPIYDNRAPNT CCCCCCCCCCCCCCC	14.39	28064214
210	Ubiquitination	EIFLLCDKVQKDDIE EEEEEECCCCCCCCE	45.64	29967540
210	Acetylation	EIFLLCDKVQKDDIE EEEEEECCCCCCCCE	45.64	25953088
254	O-linked_Glycosylation	PPYCKAITEPVTVKM CCCCCCCCCCEEEEE	38.81	27454154
258	O-linked_Glycosylation	KAITEPVTVKMQLRR CCCCCCEEEEEEECC	25.73	27454154
267	Phosphorylation	KMQLRRPSDQEVSES EEEECCCCCHHHHHH	50.55	21082442
350 (in isoform 2)	O-linked_Glycosylation	-	5.62	27454154
359	Phosphorylation	GSIGEGRYFKKEPNL CCCCCCCCCCCCCCC	30.52	22817900
368	Phosphorylation	KKEPNLFSHDAVVRE CCCCCCCCCCEEEEE	24.51	28555341
378	O-linked_Glycosylation	AVVREMPTGVSSQAE EEEEECCCCCCCCCH	49.24	27454154
382	O-linked_Glycosylation	EMPTGVSSQAESYYP ECCCCCCCCCHHCCC	30.88	27454154
386	Phosphorylation	GVSSQAESYYPSPGP CCCCCCHHCCCCCCC	32.74	-
387	Phosphorylation	VSSQAESYYPSPGPI CCCCCHHCCCCCCCC	15.76	-
409	O-linked_Glycosylation	ASMAPLPSSSWSSVA CCCCCCCCCCCCCCC	44.69	27454154
421	Methylation	SVAHPTPRSGNTNPL CCCCCCCCCCCCCCC	60.72	115386197
422	Phosphorylation	VAHPTPRSGNTNPLS CCCCCCCCCCCCCCC	37.28	28555341
425	Phosphorylation	PTPRSGNTNPLSSFS CCCCCCCCCCCCCCC	41.56	28555341
425	O-linked_Glycosylation	PTPRSGNTNPLSSFS CCCCCCCCCCCCCCC	41.56	27454154
429	Phosphorylation	SGNTNPLSSFSTRTL CCCCCCCCCCCCCCC	30.51	28857561
430	Phosphorylation	GNTNPLSSFSTRTLP CCCCCCCCCCCCCCC	30.79	28857561
433	Phosphorylation	NPLSSFSTRTLPSNS CCCCCCCCCCCCCCC	26.18	-
435	Phosphorylation	LSSFSTRTLPSNSQG CCCCCCCCCCCCCCC	43.01	28555341
438	Phosphorylation	FSTRTLPSNSQGIPP CCCCCCCCCCCCCCC	52.83	28555341
492	Phosphorylation	ISDPNMLSNCSVNMM CCCHHHHCCCEEEEE	25.64	16585559
503	Phosphorylation	VNMMTTSSDSMGETD EEEEECCCCCCCCCC	31.45	10823840
516	Phosphorylation	TDNPRLLSMNLENPS CCCCCEEEECCCCCC	15.37	28348404
523	Phosphorylation	SMNLENPSCNSVLDP EECCCCCCCCCCCCH	37.20	16585559
526	Phosphorylation	LENPSCNSVLDPRDL CCCCCCCCCCCHHHH	28.52	16585559
557	Phosphorylation	SNTTVFVSQSDAFEG CCCEEEECCHHHCCC	16.71	22817900
597	Phosphorylation	GFVQDSQYSGIGSMQ CCCCCCCCCCCCCCC	16.90	22817900

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
267	S	Phosphorylation	Kinase	PKA	-	Uniprot
516	S	Phosphorylation	Kinase	CHUK	O15111	GPS
516	S	Phosphorylation	Kinase	IKBKB	O14920	GPS
526	S	Phosphorylation	Kinase	CHUK	O15111	GPS
526	S	Phosphorylation	Kinase	IKBKB	O14920	GPS
557	S	Phosphorylation	Kinase	CHUK	O15111	GPS
557	S	Phosphorylation	Kinase	IKBKB	O14920	GPS

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PP4C_HUMAN	PPP4C	physical	9837938
M3K8_HUMAN	MAP3K8	physical	14743216
PAPOA_HUMAN	PAPOLA	physical	14743216
TF65_HUMAN	RELA	physical	14743216
TNIP2_HUMAN	TNIP2	physical	14743216
IKBE_HUMAN	NFKBIE	physical	8415639
TF65_HUMAN	RELA	physical	8139561
MTPN_HUMAN	MTPN	physical	11971907
TF65_HUMAN	RELA	physical	11967310
IKBE_HUMAN	NFKBIE	physical	10706725
IKBA_HUMAN	NFKBIA	physical	10706725
IKBB_HUMAN	NFKBIB	physical	10706725
CDK2_HUMAN	CDK2	physical	9731206
CBP_HUMAN	CREBBP	physical	19948376
EP300_HUMAN	EP300	physical	19948376
SOCS3_HUMAN	SOCS3	physical	21451109
IKBA_HUMAN	NFKBIA	physical	8887627
IKBB_HUMAN	NFKBIB	physical	8887627
TM165_HUMAN	TMEM165	physical	21988832
ANDR_HUMAN	AR	physical	17011549
TF65_HUMAN	RELA	physical	25416956
SAT1_HUMAN	SAT1	physical	25416956
ATX1_HUMAN	ATXN1	physical	25416956
SDCB1_HUMAN	SDCBP	physical	25416956
S6A12_HUMAN	SLC6A12	physical	25416956
RECK_HUMAN	RECK	physical	25416956
NCK2_HUMAN	NCK2	physical	25416956
HAT1_HUMAN	HAT1	physical	25416956
CGBP1_HUMAN	CGGBP1	physical	25416956
STK16_HUMAN	STK16	physical	25416956
EIF3A_HUMAN	EIF3A	physical	25416956
EIF3D_HUMAN	EIF3D	physical	25416956
IF4E2_HUMAN	EIF4E2	physical	25416956
RBM39_HUMAN	RBM39	physical	25416956
K0100_HUMAN	KIAA0100	physical	25416956
EPMIP_HUMAN	EPM2AIP1	physical	25416956
ACOT8_HUMAN	ACOT8	physical	25416956
CAF1A_HUMAN	CHAF1A	physical	25416956
TSSC4_HUMAN	TSSC4	physical	25416956
ARI2_HUMAN	ARIH2	physical	25416956
MD2L2_HUMAN	MAD2L2	physical	25416956
GA45G_HUMAN	GADD45G	physical	25416956
MO4L1_HUMAN	MORF4L1	physical	25416956
EXOS8_HUMAN	EXOSC8	physical	25416956
R3HD2_HUMAN	R3HDM2	physical	25416956
SC31A_HUMAN	SEC31A	physical	25416956
SZT2_HUMAN	SZT2	physical	25416956
TNS2_HUMAN	TENC1	physical	25416956
DAAM2_HUMAN	DAAM2	physical	25416956
EMAL2_HUMAN	EML2	physical	25416956
RPA1_HUMAN	POLR1A	physical	25416956
NDUF3_HUMAN	NDUFAF3	physical	25416956
NECP1_HUMAN	NECAP1	physical	25416956
I36RA_HUMAN	IL36RN	physical	25416956
OSTF1_HUMAN	OSTF1	physical	25416956
HSPB7_HUMAN	HSPB7	physical	25416956
RSP14_HUMAN	RSPH14	physical	25416956
CPSF1_HUMAN	CPSF1	physical	25416956
NDK7_HUMAN	NME7	physical	25416956
OSGI1_HUMAN	OSGIN1	physical	25416956
A1CF_HUMAN	A1CF	physical	25416956
NGN3_HUMAN	NEUROG3	physical	25416956
EXOS1_HUMAN	EXOSC1	physical	25416956
MEMO1_HUMAN	MEMO1	physical	25416956
CHCH2_HUMAN	CHCHD2	physical	25416956
DC1L1_HUMAN	DYNC1LI1	physical	25416956
POP5_HUMAN	POP5	physical	25416956
CINP_HUMAN	CINP	physical	25416956
HDAC7_HUMAN	HDAC7	physical	25416956
OAZ3_HUMAN	OAZ3	physical	25416956
TPC2L_HUMAN	TRAPPC2L	physical	25416956
UBS3A_HUMAN	UBASH3A	physical	25416956
OTUD4_HUMAN	OTUD4	physical	25416956
TTC19_HUMAN	TTC19	physical	25416956
S41A3_HUMAN	SLC41A3	physical	25416956
CA109_HUMAN	C1orf109	physical	25416956
TXN4B_HUMAN	TXNL4B	physical	25416956
MGN2_HUMAN	MAGOHB	physical	25416956
NAGK_HUMAN	NAGK	physical	25416956
ASAP3_HUMAN	ASAP3	physical	25416956
NXT2_HUMAN	NXT2	physical	25416956
CABP5_HUMAN	CABP5	physical	25416956
IF5A2_HUMAN	EIF5A2	physical	25416956
PPL13_HUMAN	LGALS14	physical	25416956
PLCD_HUMAN	AGPAT4	physical	25416956
M3KCL_HUMAN	MAP3K7CL	physical	25416956
EXOS5_HUMAN	EXOSC5	physical	25416956
PRD10_HUMAN	PRDM10	physical	25416956
CNBP1_HUMAN	CTNNBIP1	physical	25416956
COKA1_HUMAN	COL20A1	physical	25416956
RN213_HUMAN	RNF213	physical	25416956
LSM2_HUMAN	LSM2	physical	25416956
NGB_HUMAN	NGB	physical	25416956
DMRT3_HUMAN	DMRT3	physical	25416956
TMM8A_HUMAN	TMEM8A	physical	25416956
PARVG_HUMAN	PARVG	physical	25416956
UBE2Z_HUMAN	UBE2Z	physical	25416956
OTUB2_HUMAN	OTUB2	physical	25416956
FND11_HUMAN	C20orf195	physical	25416956
ATG9A_HUMAN	ATG9A	physical	25416956
CCNJL_HUMAN	CCNJL	physical	25416956
SNR25_HUMAN	SNRNP25	physical	25416956
NOL9_HUMAN	NOL9	physical	25416956
FAD1_HUMAN	FLAD1	physical	25416956
TSSK3_HUMAN	TSSK3	physical	25416956
RASF5_HUMAN	RASSF5	physical	25416956
CK068_HUMAN	C11orf68	physical	25416956
PKHN1_HUMAN	PLEKHN1	physical	25416956
MIEN1_HUMAN	MIEN1	physical	25416956
VPS25_HUMAN	VPS25	physical	25416956
CEP19_HUMAN	CEP19	physical	25416956
KRA94_HUMAN	KRTAP9-4	physical	25416956
BMF_HUMAN	BMF	physical	25416956
S39AD_HUMAN	SLC39A13	physical	25416956
ATPF2_HUMAN	ATPAF2	physical	25416956
ZN765_HUMAN	ZNF765	physical	25416956
RIPP1_HUMAN	RIPPLY1	physical	25416956
EGLN3_HUMAN	EGLN3	physical	25416956
EFHC1_HUMAN	EFHC1	physical	25416956
KLH32_HUMAN	KLHL32	physical	25416956
CIB3_HUMAN	CIB3	physical	25416956
PIHD2_HUMAN	PIH1D2	physical	25416956
RM10_HUMAN	MRPL10	physical	25416956
NR2CA_HUMAN	NR2C2AP	physical	25416956
KLH40_HUMAN	KLHL40	physical	25416956
GLCTK_HUMAN	GLYCTK	physical	25416956
ZN572_HUMAN	ZNF572	physical	25416956
ZN417_HUMAN	ZNF417	physical	25416956
TSTD2_HUMAN	TSTD2	physical	25416956
PATE1_HUMAN	PATE1	physical	25416956
ZN550_HUMAN	ZNF550	physical	25416956
ZN564_HUMAN	ZNF564	physical	25416956
FUT11_HUMAN	FUT11	physical	25416956
TT21A_HUMAN	TTC21A	physical	25416956
CENPX_HUMAN	STRA13	physical	25416956
CI072_HUMAN	C9orf72	physical	25416956
CPNE2_HUMAN	CPNE2	physical	25416956
NEIL2_HUMAN	NEIL2	physical	25416956
ZDH24_HUMAN	ZDHHC24	physical	25416956
NUD14_HUMAN	NUDT14	physical	25416956
S14L4_HUMAN	SEC14L4	physical	25416956
BARH2_HUMAN	BARHL2	physical	25416956
RAB41_HUMAN	RAB41	physical	25416956
TRI74_HUMAN	TRIM74	physical	25416956
OCC1_HUMAN	C12orf75	physical	25416956
EP300_HUMAN	EP300	physical	24529102
IKBE_HUMAN	NFKBIE	physical	26186194
NFKB2_HUMAN	NFKB2	physical	26186194
NFKB1_HUMAN	NFKB1	physical	26186194
TF65_HUMAN	RELA	physical	26186194
RELB_HUMAN	RELB	physical	26186194
TSR3_HUMAN	TSR3	physical	26186194
TNIP2_HUMAN	TNIP2	physical	26186194
BIRC3_HUMAN	BIRC3	physical	25565375
NFKB2_HUMAN	NFKB2	physical	28514442
IKBE_HUMAN	NFKBIE	physical	28514442
TF65_HUMAN	RELA	physical	28514442
NFKB1_HUMAN	NFKB1	physical	28514442
TNIP2_HUMAN	TNIP2	physical	28514442
TSR3_HUMAN	TSR3	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 REL_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Tumor necrosis factor-alpha activation of NF-kappa B requires thephosphorylation of Ser-471 in the transactivation domain of c-Rel."; Martin A.G., Fresno M.; J. Biol. Chem. 275:24383-24391(2000). Cited for: PHOSPHORYLATION AT SER-503.	10823840 [Abstract]