NR2F6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NR2F6_HUMAN
• UniProt AC: P10588
• Protein Name: Nuclear receptor subfamily 2 group F member 6
• Gene Name: NR2F6
• Organism: Homo sapiens (Human).
• Sequence Length: 404
• Subcellular Localization: Nucleus .
• Protein Description: Transcription factor predominantly involved in transcriptional repression. Binds to promoter/enhancer response elements that contain the imperfect 5'-AGGTCA-3' direct or inverted repeats with various spacings which are also recognized by other nuclear hormone receptors. Involved in modulation of hormonal responses. Represses transcriptional activity of the lutropin-choriogonadotropic hormone receptor/LHCGR gene, the renin/REN gene and the oxytocin-neurophysin/OXT gene. Represses the triiodothyronine-dependent and -independent transcriptional activity of the thyroid hormone receptor gene in a cell type-specific manner. The corepressing function towards thyroid hormone receptor beta/THRB involves at least in part the inhibition of THRB binding to triiodothyronine response elements (TREs) by NR2F6. Inhibits NFATC transcription factor DNA binding and subsequently its transcriptional activity. Acts as transcriptional repressor of IL-17 expression in Th-17 differentiated CD4(+) T cells and may be involved in induction and/or maintenance of peripheral immunological tolerance and autoimmunity. Involved in development of forebrain circadian clock; is required early in the development of the locus coeruleus (LC)..
• Protein Sequence: MAMVTGGWGGPGGDTNGVDKAGGYPRAAEDDSASPPGAASDAEPGDEERPGLQVDCVVCGDKSSGKHYGVFTCEGCKSFFKRSIRRNLSYTCRSNRDCQIDQHHRNQCQYCRLKKCFRVGMRKEAVQRGRIPHSLPGAVAASSGSPPGSALAAVASGGDLFPGQPVSELIAQLLRAEPYPAAAGRFGAGGGAAGAVLGIDNVCELAARLLFSTVEWARHAPFFPELPVADQVALLRLSWSELFVLNAAQAALPLHTAPLLAAAGLHAAPMAAERAVAFMDQVRAFQEQVDKLGRLQVDSAEYGCLKAIALFTPDACGLSDPAHVESLQEKAQVALTEYVRAQYPSQPQRFGRLLLRLPALRAVPASLISQLFFMRLVGKTPIETLIRDMLLSGSTFNWPYGSGQ

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MAMVTGGWGGPG ---CCCCCCCCCCCC	19.52	23401153
15	Phosphorylation	WGGPGGDTNGVDKAG CCCCCCCCCCCCCCC	36.83	23401153
32	Phosphorylation	PRAAEDDSASPPGAA CCCCCCCCCCCCCCC	42.86	30278072
34	Phosphorylation	AAEDDSASPPGAASD CCCCCCCCCCCCCCC	35.26	23401153
40	Phosphorylation	ASPPGAASDAEPGDE CCCCCCCCCCCCCCC	36.50	23401153
83	Phosphorylation	CKSFFKRSIRRNLSY HHHHHHHHHHHHHCH	22.49	10713182
89	Phosphorylation	RSIRRNLSYTCRSNR HHHHHHHCHHCCCCC	23.19	27251275
110	Phosphorylation	HHRNQCQYCRLKKCF HHHHHHHHHHHHHHH	6.28	28152594
134	Phosphorylation	QRGRIPHSLPGAVAA HCCCCCCCCCCCHHH	30.79	27174698
142	Phosphorylation	LPGAVAASSGSPPGS CCCCHHHCCCCCCHH	26.04	20068231
143	Phosphorylation	PGAVAASSGSPPGSA CCCHHHCCCCCCHHH	38.27	20068231
145	Phosphorylation	AVAASSGSPPGSALA CHHHCCCCCCHHHHH	29.84	29496963
149	Phosphorylation	SSGSPPGSALAAVAS CCCCCCHHHHHHHHC	26.36	20068231
156	Phosphorylation	SALAAVASGGDLFPG HHHHHHHCCCCCCCC	36.39	27174698
167	Phosphorylation	LFPGQPVSELIAQLL CCCCCCHHHHHHHHH	33.11	20068231
291	Ubiquitination	AFQEQVDKLGRLQVD HHHHHHHHHCCCCCC	54.72	21906983
330	Ubiquitination	HVESLQEKAQVALTE HHHHHHHHHHHHHHH	31.03	-
336	Phosphorylation	EKAQVALTEYVRAQY HHHHHHHHHHHHHHC	18.61	20068231
338	Phosphorylation	AQVALTEYVRAQYPS HHHHHHHHHHHHCCC	7.04	20068231
343	Phosphorylation	TEYVRAQYPSQPQRF HHHHHHHCCCCCCHH	12.13	24043423
345	Phosphorylation	YVRAQYPSQPQRFGR HHHHHCCCCCCHHHH	49.94	24043423
379	Ubiquitination	FFMRLVGKTPIETLI HHHHHHCCCCHHHHH	43.58	21906983
380	Phosphorylation	FMRLVGKTPIETLIR HHHHHCCCCHHHHHH	24.46	-
384	Phosphorylation	VGKTPIETLIRDMLL HCCCCHHHHHHHHHH	28.36	-
392	Phosphorylation	LIRDMLLSGSTFNWP HHHHHHHHCCCCCCC	27.08	-

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
83	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
83	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
83	S	Phosphorylation	Kinase	PRKCQ	Q04759	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NR2F6_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of NR2F6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NCOA1_HUMAN	NCOA1	physical	10713182
GCR_HUMAN	NR3C1	physical	10713182
THB_HUMAN	THRB	physical	10713182
ESR1_HUMAN	ESR1	physical	10713182
COT2_HUMAN	NR2F2	physical	15604093
NP1L1_HUMAN	NAP1L1	physical	20195357
CBX1_HUMAN	CBX1	physical	20195357
BC11A_HUMAN	BCL11A	physical	23975195

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34 AND SER-40, AND MASSSPECTROMETRY.
PubMed: 19413330

"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-40, AND MASSSPECTROMETRY.
PubMed: 18669648

"The nuclear orphan receptor NR2F6 suppresses lymphocyte activationand T helper 17-dependent autoimmunity.";
Hermann-Kleiter N., Gruber T., Lutz-Nicoladoni C., Thuille N.,Fresser F., Labi V., Schiefermeier N., Warnecke M., Huber L.,Villunger A., Eichele G., Kaminski S., Baier G.;
Immunity 29:205-216(2008).
Cited for: FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-83.
PubMed: 18701084

"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, AND MASSSPECTROMETRY.
PubMed: 15302935