dbPTM

NR2C2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NR2C2_HUMAN
UniProt AC	P49116
Protein Name	Nuclear receptor subfamily 2 group C member 2
Gene Name	NR2C2
Organism	Homo sapiens (Human).
Sequence Length	596
Subcellular Localization	Nucleus .
Protein Description	Orphan nuclear receptor that can act as a repressor or activator of transcription. An important repressor of nuclear receptor signaling pathways such as retinoic acid receptor, retinoid X, vitamin D3 receptor, thyroid hormone receptor and estrogen receptor pathways. May regulate gene expression during the late phase of spermatogenesis. Together with NR2C1, forms the core of the DRED (direct repeat erythroid-definitive) complex that represses embryonic and fetal globin transcription including that of GATA1. Binds to hormone response elements (HREs) consisting of two 5'-AGGTCA-3' half site direct repeat consensus sequences. Plays a fundamental role in early embryonic development and embryonic stem cells. Required for normal spermatogenesis and cerebellum development. Appears to be important for neurodevelopmentally regulated behavior (By similarity). Activates transcriptional activity of LHCG. Antagonist of PPARA-mediated transactivation..
Protein Sequence	MTSPSPRIQIISTDSAVASPQRIQIVTDQQTGQKIQIVTAVDASGSPKQQFILTSPDGAGTGKVILASPETSSAKQLIFTTSDNLVPGRIQIVTDSASVERLLGKTDVQRPQVVEYCVVCGDKASGRHYGAVSCEGCKGFFKRSVRKNLTYSCRSNQDCIINKHHRNRCQFCRLKKCLEMGMKMESVQSERKPFDVQREKPSNCAASTEKIYIRKDLRSPLIATPTFVADKDGARQTGLLDPGMLVNIQQPLIREDGTVLLATDSKAETSQGALGTLANVVTSLANLSESLNNGDTSEIQPEDQSASEITRAFDTLAKALNTTDSSSSPSLADGIDTSGGGSIHVISRDQSTPIIEVEGPLLSDTHVTFKLTMPSPMPEYLNVHYICESASRLLFLSMHWARSIPAFQALGQDCNTSLVRACWNELFTLGLAQCAQVMSLSTILAAIVNHLQNSIQEDKLSGDRIKQVMEHIWKLQEFCNSMAKLDIDGYEYAYLKAIVLFSPDHPGLTSTSQIEKFQEKAQMELQDYVQKTYSEDTYRLARILVRLPALRLMSSNITEELFFTGLIGNVSIDSIIPYILKMETAEYNGQITGASL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MTSPSPRIQ ------CCCCCCCEE	49.71	20860994
5	Phosphorylation	---MTSPSPRIQIIS ---CCCCCCCEEEEE	26.95	17081983
12	Phosphorylation	SPRIQIISTDSAVAS CCCEEEEECCCCCCC	27.99	23927012
13	Phosphorylation	PRIQIISTDSAVASP CCEEEEECCCCCCCC	24.46	23927012
13 (in isoform 2)	Phosphorylation	-	24.46	24719451
15 (in isoform 2)	Phosphorylation	-	25.40	27251275
15	Phosphorylation	IQIISTDSAVASPQR EEEEECCCCCCCCCE	25.40	23927012
19 (in isoform 2)	Phosphorylation	-	18.24	28985074
19	Phosphorylation	STDSAVASPQRIQIV ECCCCCCCCCEEEEE	18.24	29255136
27	Phosphorylation	PQRIQIVTDQQTGQK CCEEEEEECCCCCCE	29.71	20068231
37 (in isoform 2)	Phosphorylation	-	3.19	25627689
38 (in isoform 2)	Phosphorylation	-	1.29	25627689
39	Phosphorylation	GQKIQIVTAVDASGS CCEEEEEEEEECCCC	23.69	28464451
44	Phosphorylation	IVTAVDASGSPKQQF EEEEEECCCCCCEEE	35.03	30266825
46	Phosphorylation	TAVDASGSPKQQFIL EEEECCCCCCEEEEE	26.82	29255136
54	Phosphorylation	PKQQFILTSPDGAGT CCEEEEEECCCCCCC	33.14	30266825
55	Phosphorylation	KQQFILTSPDGAGTG CEEEEEECCCCCCCC	19.97	30266825
61	Phosphorylation	TSPDGAGTGKVILAS ECCCCCCCCEEEEEC	33.04	29255136
63	Ubiquitination	PDGAGTGKVILASPE CCCCCCCEEEEECCC	26.41	-
65 (in isoform 2)	Phosphorylation	-	2.79	24719451
68	Phosphorylation	TGKVILASPETSSAK CCEEEEECCCCCCCC	21.59	30266825
71	Phosphorylation	VILASPETSSAKQLI EEEECCCCCCCCEEE	31.22	30266825
72	O-linked_Glycosylation	ILASPETSSAKQLIF EEECCCCCCCCEEEE	27.00	31492838
72	Phosphorylation	ILASPETSSAKQLIF EEECCCCCCCCEEEE	27.00	30266825
73	Phosphorylation	LASPETSSAKQLIFT EECCCCCCCCEEEEE	47.08	30266825
73 (in isoform 2)	Phosphorylation	-	47.08	27251275
82 (in isoform 2)	Ubiquitination	-	22.80	-
87 (in isoform 2)	Phosphorylation	-	29.52	24719451
94	Phosphorylation	PGRIQIVTDSASVER CCCEEEEECCHHHHH	26.35	30266825
96	Phosphorylation	RIQIVTDSASVERLL CEEEEECCHHHHHHH	17.05	30266825
98	Phosphorylation	QIVTDSASVERLLGK EEEECCHHHHHHHCC	28.59	30266825
115 (in isoform 2)	Phosphorylation	-	34.07	24719451
116	Phosphorylation	QRPQVVEYCVVCGDK CCCEEEEEEEEECCC	4.48	-
117 (in isoform 2)	Phosphorylation	-	0.87	27251275
189	Phosphorylation	MKMESVQSERKPFDV CCHHHHHCCCCCCCC	36.89	28555341
192	Ubiquitination	ESVQSERKPFDVQRE HHHHCCCCCCCCCCC	46.08	-
192	Sumoylation	ESVQSERKPFDVQRE HHHHCCCCCCCCCCC	46.08	28112733
200	Acetylation	PFDVQREKPSNCAAS CCCCCCCCCCCCCCC	56.80	25953088
207	Phosphorylation	KPSNCAASTEKIYIR CCCCCCCCCCEEEEE	20.69	28348404
208	Phosphorylation	PSNCAASTEKIYIRK CCCCCCCCCEEEEEC	36.25	28985074
219	Phosphorylation	YIRKDLRSPLIATPT EEECCCCCCCEECCC	31.21	29255136
224	Phosphorylation	LRSPLIATPTFVADK CCCCCEECCCEEECC	18.83	25159151
226	Phosphorylation	SPLIATPTFVADKDG CCCEECCCEEECCCC	26.79	21712546
231	Ubiquitination	TPTFVADKDGARQTG CCCEEECCCCCCCCC	48.61	-
231	Acetylation	TPTFVADKDGARQTG CCCEEECCCCCCCCC	48.61	23954790
238 (in isoform 2)	Phosphorylation	-	18.86	24719451
243 (in isoform 2)	Phosphorylation	-	23.02	24719451
322	Phosphorylation	TLAKALNTTDSSSSP HHHHHHCCCCCCCCC	32.60	29978859
323	Phosphorylation	LAKALNTTDSSSSPS HHHHHCCCCCCCCCC	32.58	29978859
325	Phosphorylation	KALNTTDSSSSPSLA HHHCCCCCCCCCCCC	29.99	29978859
326	Phosphorylation	ALNTTDSSSSPSLAD HHCCCCCCCCCCCCC	37.33	29978859
327	Phosphorylation	LNTTDSSSSPSLADG HCCCCCCCCCCCCCC	50.66	25850435
328	Phosphorylation	NTTDSSSSPSLADGI CCCCCCCCCCCCCCE	22.06	23401153
330	Phosphorylation	TDSSSSPSLADGIDT CCCCCCCCCCCCEEC	37.83	28464451
337	Phosphorylation	SLADGIDTSGGGSIH CCCCCEECCCCCEEE	27.61	29978859
338	Phosphorylation	LADGIDTSGGGSIHV CCCCEECCCCCEEEE	31.52	29978859
342	Phosphorylation	IDTSGGGSIHVISRD EECCCCCEEEEEECC	16.88	29978859
346 (in isoform 2)	Phosphorylation	-	1.40	24719451
347 (in isoform 2)	Phosphorylation	-	28.81	27251275
347	Phosphorylation	GGSIHVISRDQSTPI CCEEEEEECCCCCCE	28.81	29978859
351	Phosphorylation	HVISRDQSTPIIEVE EEEECCCCCCEEEEE	40.20	29255136
352	Phosphorylation	VISRDQSTPIIEVEG EEECCCCCCEEEEEC	16.93	29255136
363	Phosphorylation	EVEGPLLSDTHVTFK EEECCCCCCCEEEEE	48.42	23403867
365	Phosphorylation	EGPLLSDTHVTFKLT ECCCCCCCEEEEEEE	18.18	23403867
368	Phosphorylation	LLSDTHVTFKLTMPS CCCCCEEEEEEECCC	13.88	23403867
370 (in isoform 2)	Phosphorylation	-	33.41	27251275
371 (in isoform 2)	Phosphorylation	-	4.30	24719451
516	Ubiquitination	TSTSQIEKFQEKAQM CCHHHHHHHHHHHHH	54.71	-
531	Ubiquitination	ELQDYVQKTYSEDTY HHHHHHHHHCCHHHH	39.11	-
550 (in isoform 2)	Ubiquitination	-	4.00	-
571	Phosphorylation	TGLIGNVSIDSIIPY CCCCCCEEHHHHHHH	25.36	-

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
19	S	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
19	S	Phosphorylation	Kinase	MAPK	-	Uniprot
55	S	Phosphorylation	Kinase	MAPK	-	Uniprot
68	S	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
68	S	Phosphorylation	Kinase	MAPK	-	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	TRAF6	Q9Y4K3	PMID:15492226

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
19	S	Phosphorylation	19690332
Phosphorylation on Ser-19 and Ser-68 is an important regulator of NR2C2-mediated transcriptional activity.
68	S	Phosphorylation	20068231
Phosphorylation on Ser-19 and Ser-68 is an important regulator of NR2C2-mediated 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 NR2C2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HDAC3_HUMAN	HDAC3	physical	12943985
HDAC4_HUMAN	HDAC4	physical	12943985
ESR1_HUMAN	ESR1	physical	11844790
ANDR_HUMAN	AR	physical	10611280
HNF4A_HUMAN	HNF4A	physical	12522137
RXRB_HUMAN	RXRB	physical	15604093
TAB1_HUMAN	TAB1	physical	22158122
PDLI7_HUMAN	PDLIM7	physical	16446357
TAB2_HUMAN	TAB2	physical	20064081
TRAF6_HUMAN	TRAF6	physical	20064081
JAZF1_HUMAN	JAZF1	physical	15302918
NR2C2_HUMAN	NR2C2	physical	15302918
KDM1A_HUMAN	KDM1A	physical	23455924
DDB1_HUMAN	DDB1	physical	24703702
DCAF1_HUMAN	VPRBP	physical	24703702
CUL4B_HUMAN	CUL4B	physical	24703702
S10A4_HUMAN	S100A4	physical	26496610
SMRC1_HUMAN	SMARCC1	physical	26496610
EED_HUMAN	EED	physical	26496610
RPP38_HUMAN	RPP38	physical	26496610
PATZ1_HUMAN	PATZ1	physical	26496610
TANC2_HUMAN	TANC2	physical	26496610
RBMX2_HUMAN	RBMX2	physical	26496610
PR40A_HUMAN	PRPF40A	physical	26496610
KLHL7_HUMAN	KLHL7	physical	26496610
UBB_HUMAN	UBB	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 NR2C2_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-19 AND SER-46, AND MASSSPECTROMETRY.	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 SER-219 AND THR-224, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND MASSSPECTROMETRY.	19007248 [Abstract]

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