dbPTM

NFAC2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NFAC2_MOUSE
UniProt AC	Q60591
Protein Name	Nuclear factor of activated T-cells, cytoplasmic 2
Gene Name	Nfatc2
Organism	Mus musculus (Mouse).
Sequence Length	927
Subcellular Localization	Cytoplasm . Nucleus . Cytoplasmic for the phosphorylated form and nuclear after activation that is controlled by calcineurin-mediated dephosphorylation. Rapid nuclear exit of NFATC is thought to be one mechanism by which cells distinguish between sus
Protein Description	Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2, IL-3, IL-4, TNF-alpha or GM-CSF. Promotes invasive migration through the activation of GPC6 expression and WNT5A signaling pathway..
Protein Sequence	MDVPEPQPDPDGGDGPGHEPGGSPQDELDFSILFDYDYLNPIEEEPIAHKAISSPSGLAYPDDVLDYGLKPCNPLASLSGEPPGRFGEPDSIGFQNFLSPVKPAGASGPSPRIEITPSHELMQAGGALRGRDAGLSPEQPALALAGVAASPRFTLPVPGYEGYREPLCLSPASSGSSASFISDTFSPYTSPCVSPNNAGPDDLCPQFQNIPAHYSPRTSPIMSPRTSLAEDSCLGRHSPVPRPASRSSSPGAKRRHSCAEALVAPLPAASPQRSRSPSPQPSPHVALQDDSIPAGYPPTAGSAVLMDALNTLATDSPCGIPSKIWKTSPDPTPVSTAPSKAGLARHIYPTVEFLGPCEQEERRNSAPESILLVPPTWPKQLVPAIPICSIPVTASLPPLEWPLSNQSGSYELRIEVQPKPHHRAHYETEGSRGAVKAPTGGHPVVQLHGYMENKPLGLQIFIGTADERILKPHAFYQVHRITGKTVTTTSYEKIVGNTKVLEIPLEPKNNMRATIDCAGILKLRNADIELRKGETDIGRKNTRVRLVFRVHVPEPSGRIVSLQAASNPIECSQRSAHELPMVERQDMDSCLVYGGQQMILTGQNFTAESKVVFMEKTTDGQQIWEMEATVDKDKSQPNMLFVEIPEYRNKHIRVPVKVNFYVINGKRKRSQPQHFTYHPVPAIKTEPSDEYEPSLICSPAHGGLGSQPYYPQHPMLAESPSCLVATMAPCQQFRSGLSSPDARYQQQSPAAALYQRSKSLSPGLLGYQQPSLLAAPLGLADAHRSVLVHAGSQGQGQGSTLPHTSSASQQASPVIHYSPTNQQLRGGGHQEFQHIMYCENFGPSSARPGPPPINQGQRLSPGAYPTVIQQQTAPSQRAAKNGPSDQKEALPTGVTVKQEQNLDQTYLDDVNEIIRKEFSGPPSRNQT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
23	Phosphorylation	PGHEPGGSPQDELDF CCCCCCCCCCHHCCE	25.88	-
53	Phosphorylation	PIAHKAISSPSGLAY CCCCCCCCCCCCCCC	40.85	25266776
54	Phosphorylation	IAHKAISSPSGLAYP CCCCCCCCCCCCCCC	19.57	25266776
56	Phosphorylation	HKAISSPSGLAYPDD CCCCCCCCCCCCCHH	48.68	25266776
60	Phosphorylation	SSPSGLAYPDDVLDY CCCCCCCCCHHHHCC	16.55	30635358
67	Phosphorylation	YPDDVLDYGLKPCNP CCHHHHCCCCCCCCC	21.87	30635358
72	Glutathionylation	LDYGLKPCNPLASLS HCCCCCCCCCCHHHC	8.61	24333276
79	Phosphorylation	CNPLASLSGEPPGRF CCCCHHHCCCCCCCC	38.32	-
91	Phosphorylation	GRFGEPDSIGFQNFL CCCCCCCCCCCCCCC	35.01	30635358
99	Phosphorylation	IGFQNFLSPVKPAGA CCCCCCCCCCCCCCC	24.41	22942356
107	Phosphorylation	PVKPAGASGPSPRIE CCCCCCCCCCCCCEE	50.77	27180971
110	Phosphorylation	PAGASGPSPRIEITP CCCCCCCCCCEEECC	30.27	25159016
116	Phosphorylation	PSPRIEITPSHELMQ CCCCEEECCHHHHHH	13.12	16534747
136	Phosphorylation	RGRDAGLSPEQPALA CCCCCCCCCCCCHHH	26.02	27087446
150	Phosphorylation	ALAGVAASPRFTLPV HHHHHCCCCCEECCC	13.58	27087446
170	Phosphorylation	YREPLCLSPASSGSS CCCCCCCCCCCCCCC	19.88	19395856
173	Phosphorylation	PLCLSPASSGSSASF CCCCCCCCCCCCCCH	38.32	22817900
174	Phosphorylation	LCLSPASSGSSASFI CCCCCCCCCCCCCHH	44.81	22817900
176	Phosphorylation	LSPASSGSSASFISD CCCCCCCCCCCHHCC	25.36	22817900
177	Phosphorylation	SPASSGSSASFISDT CCCCCCCCCCHHCCC	31.30	22817900
179	Phosphorylation	ASSGSSASFISDTFS CCCCCCCCHHCCCCC	25.68	22817900
182	Phosphorylation	GSSASFISDTFSPYT CCCCCHHCCCCCCCC	28.70	22817900
215	Phosphorylation	QNIPAHYSPRTSPIM CCCCCCCCCCCCCCC	9.68	22817900
218	Phosphorylation	PAHYSPRTSPIMSPR CCCCCCCCCCCCCCC	42.09	21082442
219	Phosphorylation	AHYSPRTSPIMSPRT CCCCCCCCCCCCCCC	17.44	15743762
223	Phosphorylation	PRTSPIMSPRTSLAE CCCCCCCCCCCCCCC	16.37	15743762
226	Phosphorylation	SPIMSPRTSLAEDSC CCCCCCCCCCCCCCC	31.32	29176673
227	Phosphorylation	PIMSPRTSLAEDSCL CCCCCCCCCCCCCCC	27.19	29472430
232	Phosphorylation	RTSLAEDSCLGRHSP CCCCCCCCCCCCCCC	11.62	25266776
238	Phosphorylation	DSCLGRHSPVPRPAS CCCCCCCCCCCCCCC	26.65	27742792
245	Phosphorylation	SPVPRPASRSSSPGA CCCCCCCCCCCCCCH	35.06	11030334
247	Phosphorylation	VPRPASRSSSPGAKR CCCCCCCCCCCCHHH	32.45	25266776
248	Phosphorylation	PRPASRSSSPGAKRR CCCCCCCCCCCHHHC	39.17	25266776
249	Phosphorylation	RPASRSSSPGAKRRH CCCCCCCCCCHHHCC	28.71	25266776
257	Phosphorylation	PGAKRRHSCAEALVA CCHHHCCCHHHHHHC	17.14	30387612
270	Phosphorylation	VAPLPAASPQRSRSP HCCCCCCCCCCCCCC	24.54	27742792
276	Phosphorylation	ASPQRSRSPSPQPSP CCCCCCCCCCCCCCC	30.86	22817900
278	Phosphorylation	PQRSRSPSPQPSPHV CCCCCCCCCCCCCCE	37.10	22817900
282	Phosphorylation	RSPSPQPSPHVALQD CCCCCCCCCCEECCC	23.53	11030334
327	Phosphorylation	IPSKIWKTSPDPTPV CCHHHCCCCCCCCCC	30.41	22942356
328	Phosphorylation	PSKIWKTSPDPTPVS CHHHCCCCCCCCCCC	24.47	22942356
332	Phosphorylation	WKTSPDPTPVSTAPS CCCCCCCCCCCCCCC	43.64	16534747
335	Phosphorylation	SPDPTPVSTAPSKAG CCCCCCCCCCCCCCC	21.76	28833060
336	Phosphorylation	PDPTPVSTAPSKAGL CCCCCCCCCCCCCCH	42.70	25367039
348	Phosphorylation	AGLARHIYPTVEFLG CCHHHHHCCCCCEEC	6.16	25367039
365	Phosphorylation	EQEERRNSAPESILL CHHHHHCCCCCCEEE	43.31	22942356
369	Phosphorylation	RRNSAPESILLVPPT HHCCCCCCEEECCCC	19.92	28833060
532	Acetylation	NADIELRKGETDIGR CCCEEECCCCCCCCC	73.96	23576753
617	Phosphorylation	KVVFMEKTTDGQQIW EEEEEEECCCCCEEE	19.47	22817900
618	Phosphorylation	VVFMEKTTDGQQIWE EEEEEECCCCCEEEE	49.56	22817900
684	Sumoylation	YHPVPAIKTEPSDEY ECCCCCCCCCCCCCC	49.28	-
684	Sumoylation	YHPVPAIKTEPSDEY ECCCCCCCCCCCCCC	49.28	-
738	Phosphorylation	QQFRSGLSSPDARYQ HHHHHCCCCCCHHHH	43.26	27566939
739	Phosphorylation	QFRSGLSSPDARYQQ HHHHCCCCCCHHHHH	31.66	25266776
744	Phosphorylation	LSSPDARYQQQSPAA CCCCCHHHHHHCHHH	16.64	28285833
748	Phosphorylation	DARYQQQSPAAALYQ CHHHHHHCHHHHHHH	16.51	26745281
757	Phosphorylation	AAALYQRSKSLSPGL HHHHHHHHHCCCCCC	15.86	25266776
759	Phosphorylation	ALYQRSKSLSPGLLG HHHHHHHCCCCCCCC	35.01	26239621
761	Phosphorylation	YQRSKSLSPGLLGYQ HHHHHCCCCCCCCCC	24.82	26824392
767	Phosphorylation	LSPGLLGYQQPSLLA CCCCCCCCCCHHHHH	12.16	26239621
771	Phosphorylation	LLGYQQPSLLAAPLG CCCCCCHHHHHCCCC	31.51	26239621
812	Phosphorylation	SSASQQASPVIHYSP CCCCCCCCCEEEECC	18.50	30387612
817	Phosphorylation	QASPVIHYSPTNQQL CCCCEEEECCCCCCC	12.76	30387612
818	Phosphorylation	ASPVIHYSPTNQQLR CCCEEEECCCCCCCC	15.87	30387612
820	Phosphorylation	PVIHYSPTNQQLRGG CEEEECCCCCCCCCC	39.45	30387612
838	Glutathionylation	EFQHIMYCENFGPSS HHEEEEEECCCCCCC	1.58	24333276
860	Phosphorylation	INQGQRLSPGAYPTV CCCCCCCCCCCCCCH	24.39	27087446
864	Phosphorylation	QRLSPGAYPTVIQQQ CCCCCCCCCCHHEEC	12.83	28833060
866	Phosphorylation	LSPGAYPTVIQQQTA CCCCCCCCHHEECCC	19.98	28833060
897	Sumoylation	LPTGVTVKQEQNLDQ CCCCCCEEEECCCCC	38.46	-
897	Sumoylation	LPTGVTVKQEQNLDQ CCCCCCEEEECCCCC	38.46	-
905	Phosphorylation	QEQNLDQTYLDDVNE EECCCCCCHHHHHHH	26.22	25266776

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
79	S	Phosphorylation	Kinase	MAPK14	P47811	GPS
110	S	Phosphorylation	Kinase	MAPK8	P45983	GPS
110	S	Phosphorylation	Kinase	JNK-SUBFAMILY	-	GPS
116	T	Phosphorylation	Kinase	MAPK8	P45983	GPS
116	T	Phosphorylation	Kinase	JNK-SUBFAMILY	-	GPS
170	S	Phosphorylation	Kinase	MAPK8	P45983	GPS
170	S	Phosphorylation	Kinase	JNK-SUBFAMILY	-	GPS
215	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
219	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
219	S	Phosphorylation	Kinase	MAPK8	P45983	GPS
219	S	Phosphorylation	Kinase	JNK-SUBFAMILY	-	GPS
223	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
223	S	Phosphorylation	Kinase	MAPK8	P45983	GPS
223	S	Phosphorylation	Kinase	JNK-SUBFAMILY	-	GPS
332	T	Phosphorylation	Kinase	MAPK8	P45983	GPS
332	T	Phosphorylation	Kinase	JNK-SUBFAMILY	-	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
53	S	Phosphorylation	11030334
Simultaneously, one site among Ser-53; Ser-54 and Ser-56 is phosphorylated; which is required for full transcriptional activity.
54	S	Phosphorylation	11030334
Simultaneously, one site among Ser-53; Ser-54 and Ser-56 is phosphorylated; which is required for full transcriptional activity.
56	S	Phosphorylation	11030334
Simultaneously, one site among Ser-53; Ser-54 and Ser-56 is phosphorylated; which is required for full transcriptional activity.
245	S	Phosphorylation	11030334
Upon cell stimulation, all these sites except Ser-245 are dephosphorylated by calcineurin.

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 NFAC2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
VRK2_HUMAN	VRK2	physical	23105117

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of NFAC2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, AND MASSSPECTROMETRY.	19367708 [Abstract]
"Concerted dephosphorylation of the transcription factor NFAT1 inducesa conformational switch that regulates transcriptional activity."; Okamura H., Aramburu J., Garcia-Rodriguez C., Viola J.P.B.,Raghavan A., Tahiliani M., Zhang X., Qin J., Hogan P.G., Rao A.; Mol. Cell 6:539-550(2000). Cited for: PHOSPHORYLATION AT SER-99; SER-136; SER-170; SER-173; SER-174;SER-176; SER-177; SER-179; SER-182; SER-215; SER-219; SER-223;SER-238; SER-245; SER-270; SER-276; SER-278; SER-282; SER-328 ANDSER-365, SUBCELLULAR LOCATION, INTERACTION WITH XPO1, MUTAGENESIS OFARG-164, AND MASS SPECTROMETRY.	11030334 [Abstract]

show

show

show

show