dbPTM

RXRA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RXRA_HUMAN
UniProt AC	P19793
Protein Name	Retinoic acid receptor RXR-alpha
Gene Name	RXRA
Organism	Homo sapiens (Human).
Sequence Length	462
Subcellular Localization	Nucleus .
Protein Description	Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. The high affinity ligand for RXRs is 9-cis retinoic acid. RXRA serves as a common heterodimeric partner for a number of nuclear receptors. In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone acetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation. The RXRA/PPARA heterodimer is required for PPARA transcriptional activity on fatty acid oxidation genes such as ACOX1 and the P450 system genes..
Protein Sequence	MDTKHFLPLDFSTQVNSSLTSPTGRGSMAAPSLHPSLGPGIGSPGQLHSPISTLSSPINGMGPPFSVISSPMGPHSMSVPTTPTLGFSTGSPQLSSPMNPVSSSEDIKPPLGLNGVLKVPAHPSGNMASFTKHICAICGDRSSGKHYGVYSCEGCKGFFKRTVRKDLTYTCRDNKDCLIDKRQRNRCQYCRYQKCLAMGMKREAVQEERQRGKDRNENEVESTSSANEDMPVERILEAELAVEPKTETYVEANMGLNPSSPNDPVTNICQAADKQLFTLVEWAKRIPHFSELPLDDQVILLRAGWNELLIASFSHRSIAVKDGILLATGLHVHRNSAHSAGVGAIFDRVLTELVSKMRDMQMDKTELGCLRAIVLFNPDSKGLSNPAEVEALREKVYASLEAYCKHKYPEQPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQMT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Sumoylation	----MDTKHFLPLDF ----CCCCCCCCCCC	28.26	28112733
12	Phosphorylation	HFLPLDFSTQVNSSL CCCCCCCCCCCCCCC	20.00	23090842
13	Phosphorylation	FLPLDFSTQVNSSLT CCCCCCCCCCCCCCC	36.21	23663014
17	Phosphorylation	DFSTQVNSSLTSPTG CCCCCCCCCCCCCCC	28.06	23663014
18	Phosphorylation	FSTQVNSSLTSPTGR CCCCCCCCCCCCCCC	30.39	23663014
20	Phosphorylation	TQVNSSLTSPTGRGS CCCCCCCCCCCCCCC	34.31	30266825
21	Phosphorylation	QVNSSLTSPTGRGSM CCCCCCCCCCCCCCC	26.26	30266825
23	Phosphorylation	NSSLTSPTGRGSMAA CCCCCCCCCCCCCCC	39.00	30266825
27	Phosphorylation	TSPTGRGSMAAPSLH CCCCCCCCCCCCCCC	12.14	11162439
32	Phosphorylation	RGSMAAPSLHPSLGP CCCCCCCCCCCCCCC	34.28	16184197
49	Phosphorylation	GSPGQLHSPISTLSS CCCCCCCCCCHHCCC	32.30	-
56	Phosphorylation	SPISTLSSPINGMGP CCCHHCCCCCCCCCC	32.67	-
66	Phosphorylation	NGMGPPFSVISSPMG CCCCCCCEEEECCCC	25.06	-
70	Phosphorylation	PPFSVISSPMGPHSM CCCEEEECCCCCCCC	14.05	-
78	Phosphorylation	PMGPHSMSVPTTPTL CCCCCCCCCCCCCCC	28.14	-
82	Phosphorylation	HSMSVPTTPTLGFST CCCCCCCCCCCCCCC	14.27	20432439
108	Sumoylation	VSSSEDIKPPLGLNG CCCCCCCCCCCCCCC	53.56	16912044
108	Sumoylation	VSSSEDIKPPLGLNG CCCCCCCCCCCCCCC	53.56	-
124	Phosphorylation	LKVPAHPSGNMASFT EEECCCCCCCHHHHH	32.69	28555341
129	Phosphorylation	HPSGNMASFTKHICA CCCCCHHHHHHEEEH	23.76	23917254
145	Acetylation	CGDRSSGKHYGVYSC CCCCCCCCEEEEEEC	35.28	17761950
147	Phosphorylation	DRSSGKHYGVYSCEG CCCCCCEEEEEECCC	16.27	-
150	Phosphorylation	SGKHYGVYSCEGCKG CCCEEEEEECCCCCC	11.84	28152594
151	Phosphorylation	GKHYGVYSCEGCKGF CCEEEEEECCCCCCH	11.86	28152594
222	Phosphorylation	RNENEVESTSSANED CCCCCCCCCCCCCCC	38.47	20873877
223	Phosphorylation	NENEVESTSSANEDM CCCCCCCCCCCCCCC	17.13	20873877
224	Phosphorylation	ENEVESTSSANEDMP CCCCCCCCCCCCCCC	36.41	20873877
225	Phosphorylation	NEVESTSSANEDMPV CCCCCCCCCCCCCCH	34.89	20873877
246	Phosphorylation	ELAVEPKTETYVEAN EEECCCCCCEEEEEC	44.25	29449344
248	Phosphorylation	AVEPKTETYVEANMG ECCCCCCEEEEECCC	37.79	29449344
249	Phosphorylation	VEPKTETYVEANMGL CCCCCCEEEEECCCC	7.05	20432439
259	Phosphorylation	ANMGLNPSSPNDPVT ECCCCCCCCCCCHHH	58.30	26657352
259	Ubiquitination	ANMGLNPSSPNDPVT ECCCCCCCCCCCHHH	58.30	-
260	Phosphorylation	NMGLNPSSPNDPVTN CCCCCCCCCCCHHHH	29.04	30278072
266	Phosphorylation	SSPNDPVTNICQAAD CCCCCHHHHHHHHHH	25.01	28450419
267	Ubiquitination	SPNDPVTNICQAADK CCCCHHHHHHHHHHH	33.02	-
320	Ubiquitination	FSHRSIAVKDGILLA CCCCCEEEECCEEEE	5.75	-
356	Ubiquitination	VLTELVSKMRDMQMD HHHHHHHHHHHCCCC	30.40	-
364	Ubiquitination	MRDMQMDKTELGCLR HHHCCCCHHHHHCEE	38.26	-
397	Phosphorylation	EALREKVYASLEAYC HHHHHHHHHHHHHHH	11.09	-
403	Phosphorylation	VYASLEAYCKHKYPE HHHHHHHHHHCCCCC	7.83	-
417	Ubiquitination	EQPGRFAKLLLRLPA CCCCHHHHHHHHHHH	36.63	-
417	Acetylation	EQPGRFAKLLLRLPA CCCCHHHHHHHHHHH	36.63	25953088

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
27	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
49	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
56	S	Phosphorylation	Kinase	MAPK8	P45983	Uniprot
56	S	Phosphorylation	Kinase	MAPK9	P45984	Uniprot
66	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
70	S	Phosphorylation	Kinase	MAPK8	P45983	Uniprot
70	S	Phosphorylation	Kinase	MAPK9	P45984	Uniprot
78	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
82	T	Phosphorylation	Kinase	MAPK_GROUP	-	PhosphoELM
82	T	Phosphorylation	Kinase	MAPK8	P45983	Uniprot
82	T	Phosphorylation	Kinase	MAPK9	P45984	Uniprot
82	T	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
249	Y	Phosphorylation	Kinase	MAP2K4	P45985	GPS
260	S	Phosphorylation	Kinase	MAPK_GROUP	-	PhosphoELM
260	S	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
260	S	Phosphorylation	Kinase	JNK2	P45984	PSP
260	S	Phosphorylation	Kinase	JNK1	P45983	PSP
260	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
260	S	Phosphorylation	Kinase	MAPK1	P28482	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
21	S	Phosphorylation	11162439
Constitutively phosphorylated on Ser-21 in the presence or absence of ligand (By similarity).
27	S	Phosphorylation	11162439
Phosphorylated on Ser-27, in vitro, by PKA.
56	S	Phosphorylation	11162439
Under stress conditions, hyperphosphorylated by activated JNK on Ser-56, Ser-70, Thr-82 and Ser-260 (By similarity).
70	S	Phosphorylation	11162439
Under stress conditions, hyperphosphorylated by activated JNK on Ser-56, Ser-70, Thr-82 and Ser-260 (By similarity).
82	T	Phosphorylation	11162439
Under stress conditions, hyperphosphorylated by activated JNK on Ser-56, Ser-70, Thr-82 and Ser-260 (By similarity).
260	S	Phosphorylation	11162439
Under stress conditions, hyperphosphorylated by activated JNK on Ser-56, Ser-70, Thr-82 and Ser-260 (By similarity).

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 RXRA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BRD8_HUMAN	BRD8	physical	10517671
CTNB1_HUMAN	CTNNB1	physical	12771132
RNF8_HUMAN	RNF8	physical	14981089
NR4A1_HUMAN	NR4A1	physical	14980220
HDAC3_HUMAN	HDAC3	physical	12943985
HDAC4_HUMAN	HDAC4	physical	12943985
RARA_HUMAN	RARA	physical	12052862
MYOD1_HUMAN	MYOD1	physical	9692544
TADA3_HUMAN	TADA3	physical	12235159
NR1H4_HUMAN	NR1H4	physical	7760852
NR1H2_HUMAN	NR1H2	physical	7760852
NCOA6_HUMAN	NCOA6	physical	11773444
NR2F6_HUMAN	NR2F6	physical	10318855
NR1H3_HUMAN	NR1H3	physical	8621574
PARP1_RAT	Parp1	physical	10082530
PRGC1_HUMAN	PPARGC1A	physical	11714715
NRIP1_HUMAN	NRIP1	physical	8887632
SP1_HUMAN	SP1	physical	10361124
PPARG_HUMAN	PPARG	physical	7838715
CENPR_HUMAN	ITGB3BP	physical	10490654
NPAS2_HUMAN	NPAS2	physical	11439184
CLOCK_HUMAN	CLOCK	physical	11439184
BMAL1_HUMAN	ARNTL	physical	11439184
NR1I3_HUMAN	NR1I3	physical	8114692
TIF1A_HUMAN	TRIM24	physical	11851396
NCOA2_HUMAN	NCOA2	physical	11851396
NCOA3_HUMAN	NCOA3	physical	11851396
VDR_HUMAN	VDR	physical	9632709
NCOA2_MOUSE	Ncoa2	physical	11514567
SNW1_HUMAN	SNW1	physical	11514567
NCOA2_HUMAN	NCOA2	physical	11514567
THB_HUMAN	THRB	physical	9171239
NCOA1_HUMAN	NCOA1	physical	9171239
IBP3_HUMAN	IGFBP3	physical	10874028
THB_HUMAN	THRB	physical	19211732
VDR_HUMAN	VDR	physical	16357103
NCOA3_HUMAN	NCOA3	physical	15863722
MED1_HUMAN	MED1	physical	15863722
RPB1_HUMAN	POLR2A	physical	15863722
SMCA4_HUMAN	SMARCA4	physical	15774904
NCOA2_HUMAN	NCOA2	physical	15657427
VDR_HUMAN	VDR	physical	15647825
VDR_HUMAN	VDR	physical	11149488
VDR_HUMAN	VDR	physical	11075811
NCOA1_HUMAN	NCOA1	physical	11027271
NCOA3_HUMAN	NCOA3	physical	11027271
GRIP1_HUMAN	GRIP1	physical	11027271
MED1_HUMAN	MED1	physical	11027271
NCOA1_HUMAN	NCOA1	physical	10935544
VDR_HUMAN	VDR	physical	10733574
VDR_HUMAN	VDR	physical	10037600
VDR_HUMAN	VDR	physical	14726489
CTCF_HUMAN	CTCF	physical	20404925
VDR_HUMAN	VDR	physical	20564192
KIF1A_HUMAN	KIF1A	physical	15604093
PRS8_HUMAN	PSMC5	physical	8598193
TIF1A_HUMAN	TRIM24	physical	8598193
NCOA3_HUMAN	NCOA3	physical	9346901
TRI32_HUMAN	TRIM32	physical	21984809
NR4A1_HUMAN	NR4A1	physical	17761950
EP300_HUMAN	EP300	physical	17761950
NR4A1_HUMAN	NR4A1	genetic	17761950
VDR_HUMAN	VDR	physical	11124027
NCOR1_HUMAN	NCOR1	physical	11124027
NCOA1_HUMAN	NCOA1	physical	11124027
BHE40_HUMAN	BHLHE40	physical	19786558
BHE41_HUMAN	BHLHE41	physical	19786558
ARI5A_HUMAN	ARID5A	physical	15941852
PRS8_HUMAN	PSMC5	physical	8603043
NCOA2_HUMAN	NCOA2	physical	9430642
VDR_HUMAN	VDR	physical	12847098
CHD9_HUMAN	CHD9	physical	16554032
STAT1_HUMAN	STAT1	physical	21988832
VDR_HUMAN	VDR	physical	21988832
NCOA4_HUMAN	NCOA4	physical	10347167
LX15B_HUMAN	ALOX15B	physical	15698583
NCOA1_HUMAN	NCOA1	physical	23975195
PPARA_HUMAN	PPARA	physical	23711995
PPARG_HUMAN	PPARG	physical	23711995
NCOR1_HUMAN	NCOR1	physical	11903058
RARA_HUMAN	RARA	physical	21478865
VDR_HUMAN	VDR	physical	21478865
PPARG_HUMAN	PPARG	physical	14587029
PPARG_HUMAN	PPARG	physical	17312272
PPARG_HUMAN	PPARG	physical	18217139
RXRA_HUMAN	RXRA	physical	25795708
NCOA1_HUMAN	NCOA1	physical	10454579
TRIP4_HUMAN	TRIP4	physical	10454579
RARA_HUMAN	RARA	physical	7705655
NCOA1_HUMAN	NCOA1	physical	11438648
MED1_HUMAN	MED1	physical	11438648
GRIP1_MOUSE	Grip1	physical	11438648
SRF_HUMAN	SRF	physical	11641790
RXRA_HUMAN	RXRA	physical	9121466
NCOA1_HUMAN	NCOA1	physical	9121466
RARA_HUMAN	RARA	physical	25241761
CTNB1_HUMAN	CTNNB1	physical	25241761
TF65_HUMAN	RELA	physical	25241761
ZBT16_HUMAN	ZBTB16	physical	25241761
KLF5_HUMAN	KLF5	physical	16224062
RARA_HUMAN	RARA	physical	16224062
TRAF2_HUMAN	TRAF2	physical	25795708
TF65_HUMAN	RELA	physical	16608838
P85A_HUMAN	PIK3R1	physical	20541701
NR1I2_HUMAN	NR1I2	physical	22976785
VDR_HUMAN	VDR	physical	26329759

Drug and Disease Associations

Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
DB00459	Acitretin
DB00210	Adapalene
DB00523	Alitretinoin
DB00307	Bexarotene
DB00749	Etodolac

Regulatory Network of RXRA_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Serine 27, a human retinoid X receptor alpha residue, phosphorylatedby protein kinase A is essential for cyclicAMP-mediated downregulationof RXRalpha function."; Harish S., Ashok M.S., Khanam T., Rangarajan P.N.; Biochem. Biophys. Res. Commun. 279:853-857(2000). Cited for: PHOSPHORYLATION AT SER-27, FUNCTION, AND MUTAGENESIS OF SER-27.	11162439 [Abstract]
Sumoylation
Reference	PubMed
"Negative modulation of RXRalpha transcriptional activity by smallubiquitin-related modifier (SUMO) modification and its reversal bySUMO-specific protease SUSP1."; Choi S.J., Chung S.S., Rho E.J., Lee H.W., Lee M.H., Choi H.S.,Seol J.H., Baek S.H., Bang O.S., Chung C.H.; J. Biol. Chem. 281:30669-30677(2006). Cited for: SUMOYLATION AT LYS-108, AND INTERACTION WITH SENP6.	16912044 [Abstract]

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