dbPTM

NR2C1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NR2C1_HUMAN
UniProt AC	P13056
Protein Name	Nuclear receptor subfamily 2 group C member 1
Gene Name	NR2C1
Organism	Homo sapiens (Human).
Sequence Length	603
Subcellular Localization	Nucleus . Nucleus, PML body. Recruited by HDAC3, after all-trans retinoic acid stimulated MAPK1-mediated Thr-223 phosphorylation, to PML bodies for subsequent sumoylation..
Protein Description	Orphan nuclear receptor. Binds the IR7 element in the promoter of its own gene in an autoregulatory negative feedback mechanism. Primarily repressor of a broad range of genes. Binds to hormone response elements (HREs) consisting of two 5'-AGGTCA-3' half site direct repeat consensus sequences. Together with NR2C2, forms the core of the DRED (direct repeat erythroid-definitive) complex that represses embryonic and fetal globin transcription. Also activator of OCT4 gene expression. May be involved in stem cell proliferation and differentiation. Mediator of retinoic acid-regulated preadipocyte proliferation..
Protein Sequence	MATIEEIAHQIIEQQMGEIVTEQQTGQKIQIVTALDHNTQGKQFILTNHDGSTPSKVILARQDSTPGKVFLTTPDAAGVNQLFFTTPDLSAQHLQLLTDNSPDQGPNKVFDLCVVCGDKASGRHYGAVTCEGCKGFFKRSIRKNLVYSCRGSKDCIINKHHRNRCQYCRLQRCIAFGMKQDSVQCERKPIEVSREKSSNCAASTEKIYIRKDLRSPLTATPTFVTDSESTRSTGLLDSGMFMNIHPSGVKTESAVLMTSDKAESCQGDLSTLANVVTSLANLGKTKDLSQNSNEMSMIESLSNDDTSLCEFQEMQTNGDVSRAFDTLAKALNPGESTACQSSVAGMEGSVHLITGDSSINYTEKEGPLLSDSHVAFRLTMPSPMPEYLNVHYIGESASRLLFLSMHWALSIPSFQALGQENSISLVKAYWNELFTLGLAQCWQVMNVATILATFVNCLHNSLQQDKMSTERRKLLMEHIFKLQEFCNSMVKLCIDGYEYAYLKAIVLFSPDHPSLENMEQIEKFQEKAYVEFQDYITKTYPDDTYRLSRLLLRLPALRLMNATITEELFFKGLIGNIRIDSVIPHILKMEPADYNSQIIGHSI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
21	Phosphorylation	QQMGEIVTEQQTGQK HHHHHHEECCHHCCE	33.46	23879269
42	Ubiquitination	LDHNTQGKQFILTNH EECCCCCCEEEEECC	32.02	-
47	Phosphorylation	QGKQFILTNHDGSTP CCCEEEEECCCCCCC	26.20	25159151
52	Phosphorylation	ILTNHDGSTPSKVIL EEECCCCCCCCEEEE	43.11	25159151
53	Phosphorylation	LTNHDGSTPSKVILA EECCCCCCCCEEEEE	36.79	25159151
55	Phosphorylation	NHDGSTPSKVILARQ CCCCCCCCEEEEEEC	39.38	29396449
56	Acetylation	HDGSTPSKVILARQD CCCCCCCEEEEEECC	34.20	26051181
56	Ubiquitination	HDGSTPSKVILARQD CCCCCCCEEEEEECC	34.20	-
64	Phosphorylation	VILARQDSTPGKVFL EEEEECCCCCCEEEE	28.32	17001009
65	Phosphorylation	ILARQDSTPGKVFLT EEEECCCCCCEEEEE	44.33	28985074
72	Phosphorylation	TPGKVFLTTPDAAGV CCCEEEEECCCCCCC	25.48	27251275
73	Phosphorylation	PGKVFLTTPDAAGVN CCEEEEECCCCCCCC	22.71	27251275
90	Phosphorylation	FFTTPDLSAQHLQLL EEECCCCCHHHHHHH	33.01	22199227
98	Phosphorylation	AQHLQLLTDNSPDQG HHHHHHHCCCCCCCC	41.55	22199227
101	Phosphorylation	LQLLTDNSPDQGPNK HHHHCCCCCCCCCCC	32.44	22199227
119	Ubiquitination	LCVVCGDKASGRHYG EEEEECCCCCCCCCE	29.72	-
148	O-linked_Glycosylation	IRKNLVYSCRGSKDC HHCCCCEECCCCCCE	7.00	30379171
152	Phosphorylation	LVYSCRGSKDCIINK CCEECCCCCCEEECH	13.13	24719451
188	Ubiquitination	DSVQCERKPIEVSRE CCEECCCCCEEECHH	28.22	-
196	Acetylation	PIEVSREKSSNCAAS CEEECHHHCCCCCCC	59.06	30590901
197	Phosphorylation	IEVSREKSSNCAAST EEECHHHCCCCCCCC	23.25	-
204	Phosphorylation	SSNCAASTEKIYIRK CCCCCCCCCEEEEEC	36.25	28985074
208	Phosphorylation	AASTEKIYIRKDLRS CCCCCEEEEECCCCC	13.02	22817900
215	Phosphorylation	YIRKDLRSPLTATPT EEECCCCCCCCCCCE	31.40	29255136
218	Phosphorylation	KDLRSPLTATPTFVT CCCCCCCCCCCEEEC	31.69	29255136
220	Phosphorylation	LRSPLTATPTFVTDS CCCCCCCCCEEECCC	20.02	29255136
222	Phosphorylation	SPLTATPTFVTDSES CCCCCCCEEECCCCC	26.78	29255136
225	Phosphorylation	TATPTFVTDSESTRS CCCCEEECCCCCCCC	29.62	22199227
227	Phosphorylation	TPTFVTDSESTRSTG CCEEECCCCCCCCCC	24.87	26074081
229	Phosphorylation	TFVTDSESTRSTGLL EEECCCCCCCCCCCC	32.83	26074081
230	Phosphorylation	FVTDSESTRSTGLLD EECCCCCCCCCCCCC	25.29	26074081
233	Phosphorylation	DSESTRSTGLLDSGM CCCCCCCCCCCCCCC	28.67	22210691
238	Phosphorylation	RSTGLLDSGMFMNIH CCCCCCCCCCEEEEC	31.93	22210691
247	Phosphorylation	MFMNIHPSGVKTESA CEEEECCCCCCCCEE	41.90	22210691
250	Sumoylation	NIHPSGVKTESAVLM EECCCCCCCCEEEEE	50.53	28112733
251	Phosphorylation	IHPSGVKTESAVLMT ECCCCCCCCEEEEEE	32.53	20068231
392	Phosphorylation	PEYLNVHYIGESASR CCCCCEEEECCHHHH	13.31	-
424	Phosphorylation	LGQENSISLVKAYWN HCCCCCHHHHHHHHH	27.25	24719451
523	Ubiquitination	ENMEQIEKFQEKAYV CCHHHHHHHHHHHHH	54.71	-
529	Phosphorylation	EKFQEKAYVEFQDYI HHHHHHHHHHHHHHH	16.16	26074081
538	Ubiquitination	EFQDYITKTYPDDTY HHHHHHHHHCCCCHH	36.18	-
581	Phosphorylation	IGNIRIDSVIPHILK HCCEEECCHHHHHHC	21.41	-
581	O-linked_Glycosylation	IGNIRIDSVIPHILK HCCEEECCHHHHHHC	21.41	30379171
588	Sumoylation	SVIPHILKMEPADYN CHHHHHHCCCCCCCC	40.38	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
222	T	Phosphorylation	Kinase	MAPK1	P28482	Uniprot
581	S	Phosphorylation	Kinase	PKC	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
222	T	Phosphorylation	-
Phosphorylation on Thr-222, stimulated by all-trans retinoic acid (atRA) mediates PML location and sumoylation in proliferating cells which then modulates its association with effector molecules, KAT2B and NRIP1.
222	T	Sumoylation	-
Phosphorylation on Thr-222, stimulated by all-trans retinoic acid (atRA) mediates PML location and sumoylation in proliferating cells which then modulates its association with effector molecules, KAT2B and NRIP1.
581	S	Phosphorylation	-
Phosphorylation on Ser-581 by PKC is important for protein stability and function as activator of RARB (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 NR2C1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ANDR_HUMAN	AR	physical	12949936
HDAC3_HUMAN	HDAC3	physical	14521922
HDAC3_HUMAN	HDAC3	physical	12943985
HDAC4_HUMAN	HDAC4	physical	12943985
HDAC3_HUMAN	HDAC3	physical	11463856
HDAC4_HUMAN	HDAC4	physical	11463856
ESR1_HUMAN	ESR1	physical	12093804
HDAC3_HUMAN	HDAC3	physical	19204783
PML_HUMAN	PML	physical	19204783
PML_HUMAN	PML	physical	21360626
NR2C2_HUMAN	NR2C2	physical	21670149
DNMT1_HUMAN	DNMT1	physical	21670149
CHD4_HUMAN	CHD4	physical	21670149
HDAC1_HUMAN	HDAC1	physical	21670149
HDAC2_HUMAN	HDAC2	physical	21670149
RBBP4_HUMAN	RBBP4	physical	21670149
RBBP7_HUMAN	RBBP7	physical	21670149
MTA1_HUMAN	MTA1	physical	21670149
MTA2_HUMAN	MTA2	physical	21670149
TIF1B_HUMAN	TRIM28	physical	21670149
KDM1A_HUMAN	KDM1A	physical	21670149
NONO_HUMAN	NONO	physical	21670149
SFPQ_HUMAN	SFPQ	physical	21670149
PSPC1_HUMAN	PSPC1	physical	21670149
SIN3A_HUMAN	SIN3A	physical	21670149
HCFC1_HUMAN	HCFC1	physical	21670149
RBM39_HUMAN	RBM39	physical	21670149
SMCA4_HUMAN	SMARCA4	physical	21670149
RCOR1_HUMAN	RCOR1	physical	21670149
MBD3_HUMAN	MBD3	physical	21670149
DPOD3_HUMAN	POLD3	physical	21670149
HDAC3_HUMAN	HDAC3	physical	21670149

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 NR2C1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-215 AND THR-220, ANDMASS SPECTROMETRY.	18669648 [Abstract]

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