dbPTM

NFAC2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NFAC2_HUMAN
UniProt AC	Q13469
Protein Name	Nuclear factor of activated T-cells, cytoplasmic 2
Gene Name	NFATC2
Organism	Homo sapiens (Human).
Sequence Length	925
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 susta
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	MNAPERQPQPDGGDAPGHEPGGSPQDELDFSILFDYEYLNPNEEEPNAHKVASPPSGPAYPDDVLDYGLKPYSPLASLSGEPPGRFGEPDRVGPQKFLSAAKPAGASGLSPRIEITPSHELIQAVGPLRMRDAGLLVEQPPLAGVAASPRFTLPVPGFEGYREPLCLSPASSGSSASFISDTFSPYTSPCVSPNNGGPDDLCPQFQNIPAHYSPRTSPIMSPRTSLAEDSCLGRHSPVPRPASRSSSPGAKRRHSCAEALVALPPGASPQRSRSPSPQPSSHVAPQDHGSPAGYPPVAGSAVIMDALNSLATDSPCGIPPKMWKTSPDPSPVSAAPSKAGLPRHIYPAVEFLGPCEQGERRNSAPESILLVPPTWPKPLVPAIPICSIPVTASLPPLEWPLSSQSGSYELRIEVQPKPHHRAHYETEGSRGAVKAPTGGHPVVQLHGYMENKPLGLQIFIGTADERILKPHAFYQVHRITGKTVTTTSYEKIVGNTKVLEIPLEPKNNMRATIDCAGILKLRNADIELRKGETDIGRKNTRVRLVFRVHIPESSGRIVSLQTASNPIECSQRSAHELPMVERQDTDSCLVYGGQQMILTGQNFTSESKVVFTEKTTDGQQIWEMEATVDKDKSQPNMLFVEIPEYRNKHIRTPVKVNFYVINGKRKRSQPQHFTYHPVPAIKTEPTDEYDPTLICSPTHGGLGSQPYYPQHPMVAESPSCLVATMAPCQQFRTGLSSPDARYQQQNPAAVLYQRSKSLSPSLLGYQQPALMAAPLSLADAHRSVLVHAGSQGQSSALLHPSPTNQQASPVIHYSPTNQQLRCGSHQEFQHIMYCENFAPGTTRPGPPPVSQGQRLSPGSYPTVIQQQNATSQRAAKNGPPVSDQKEVLPAGVTIKQEQNLDQTYLDDVNEIIRKEFSGPPARNQT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
20	Phosphorylation	GDAPGHEPGGSPQDE CCCCCCCCCCCCCCC	46.93	27251275
20 (in isoform 3)	Phosphorylation	-	46.93	29507054
20 (in isoform 4)	Phosphorylation	-	46.93	29507054
23	Phosphorylation	PGHEPGGSPQDELDF CCCCCCCCCCCCCCE	25.88	28192239
31	Phosphorylation	PQDELDFSILFDYEY CCCCCCEEEEEEECC	20.32	26074081
33 (in isoform 3)	Phosphorylation	-	2.30	29507054
33 (in isoform 4)	Phosphorylation	-	2.30	29507054
36	Phosphorylation	DFSILFDYEYLNPNE CEEEEEEECCCCCCC	10.11	26074081
38	Phosphorylation	SILFDYEYLNPNEEE EEEEEECCCCCCCCC	12.92	26074081
53	Phosphorylation	PNAHKVASPPSGPAY CCCCCCCCCCCCCCC	40.09	28674151
56	Phosphorylation	HKVASPPSGPAYPDD CCCCCCCCCCCCCCC	61.87	28450419
60	Phosphorylation	SPPSGPAYPDDVLDY CCCCCCCCCCCCCCC	15.44	28450419
67	Phosphorylation	YPDDVLDYGLKPYSP CCCCCCCCCCCCCCC	21.87	26657352
70	Ubiquitination	DVLDYGLKPYSPLAS CCCCCCCCCCCCHHH	37.23	-
72	Phosphorylation	LDYGLKPYSPLASLS CCCCCCCCCCHHHHC	22.72	26657352
73	Phosphorylation	DYGLKPYSPLASLSG CCCCCCCCCHHHHCC	23.20	21712546
77	Phosphorylation	KPYSPLASLSGEPPG CCCCCHHHHCCCCCC	30.65	28450419
79	Phosphorylation	YSPLASLSGEPPGRF CCCHHHHCCCCCCCC	38.32	28450419
96	Ubiquitination	PDRVGPQKFLSAAKP CCCCCHHHHHHHCCC	51.94	-
99	Dephosphorylation	VGPQKFLSAAKPAGA CCHHHHHHHCCCCCC	29.34	11030334
99	Phosphorylation	VGPQKFLSAAKPAGA CCHHHHHHHCCCCCC	29.34	29978859
102	Ubiquitination	QKFLSAAKPAGASGL HHHHHHCCCCCCCCC	34.81	-
107	Phosphorylation	AAKPAGASGLSPRIE HCCCCCCCCCCCCEE	39.07	29255136
110	Phosphorylation	PAGASGLSPRIEITP CCCCCCCCCCEEECC	18.69	29255136
116	Dephosphorylation	LSPRIEITPSHELIQ CCCCEEECCCHHHHH	13.12	9660947
116	Phosphorylation	LSPRIEITPSHELIQ CCCCEEECCCHHHHH	13.12	28450419
118	Phosphorylation	PRIEITPSHELIQAV CCEEECCCHHHHHHH	22.42	23186163
148	Phosphorylation	PLAGVAASPRFTLPV CCCCCCCCCCEECCC	13.58	23401153
150	Methylation	AGVAASPRFTLPVPG CCCCCCCCEECCCCC	34.39	81462421
168	Phosphorylation	YREPLCLSPASSGSS CCCCCEECCCCCCCC	19.88	11030334
171	Phosphorylation	PLCLSPASSGSSASF CCEECCCCCCCCCCH	38.32	11030334
172	Phosphorylation	LCLSPASSGSSASFI CEECCCCCCCCCCHH	44.81	11030334
174	Phosphorylation	LSPASSGSSASFISD ECCCCCCCCCCHHCC	25.36	11030334
175	Phosphorylation	SPASSGSSASFISDT CCCCCCCCCCHHCCC	31.30	11030334
177	Phosphorylation	ASSGSSASFISDTFS CCCCCCCCHHCCCCC	25.68	11030334
180	Phosphorylation	GSSASFISDTFSPYT CCCCCHHCCCCCCCC	28.70	11030334
212	Phosphorylation	FQNIPAHYSPRTSPI HCCCCCCCCCCCCCC	23.60	26074081
213	Dephosphorylation	QNIPAHYSPRTSPIM CCCCCCCCCCCCCCC	9.68	11030334
213	Phosphorylation	QNIPAHYSPRTSPIM CCCCCCCCCCCCCCC	9.68	26074081
216	Phosphorylation	PAHYSPRTSPIMSPR CCCCCCCCCCCCCCC	42.09	30278072
217	Dephosphorylation	AHYSPRTSPIMSPRT CCCCCCCCCCCCCCC	17.44	11030334
217	Phosphorylation	AHYSPRTSPIMSPRT CCCCCCCCCCCCCCC	17.44	23401153
221	Dephosphorylation	PRTSPIMSPRTSLAE CCCCCCCCCCCCCCC	16.37	11030334
221	Phosphorylation	PRTSPIMSPRTSLAE CCCCCCCCCCCCCCC	16.37	23401153
224	O-linked_Glycosylation	SPIMSPRTSLAEDSC CCCCCCCCCCCCCCC	31.32	29351928
224	Phosphorylation	SPIMSPRTSLAEDSC CCCCCCCCCCCCCCC	31.32	30108239
225	O-linked_Glycosylation	PIMSPRTSLAEDSCL CCCCCCCCCCCCCCC	27.19	29351928
225	Phosphorylation	PIMSPRTSLAEDSCL CCCCCCCCCCCCCCC	27.19	23401153
230	Phosphorylation	RTSLAEDSCLGRHSP CCCCCCCCCCCCCCC	11.62	23401153
236	Dephosphorylation	DSCLGRHSPVPRPAS CCCCCCCCCCCCCCC	26.65	11030334
236	Phosphorylation	DSCLGRHSPVPRPAS CCCCCCCCCCCCCCC	26.65	23401153
243	Phosphorylation	SPVPRPASRSSSPGA CCCCCCCCCCCCCCH	35.06	23401153
245	Phosphorylation	VPRPASRSSSPGAKR CCCCCCCCCCCCHHH	32.45	30576142
246	Phosphorylation	PRPASRSSSPGAKRR CCCCCCCCCCCHHHC	39.17	30576142
247	Phosphorylation	RPASRSSSPGAKRRH CCCCCCCCCCHHHCC	28.71	22210691
255	Phosphorylation	PGAKRRHSCAEALVA CCHHHCCCHHHHHHH	17.14	23401153
268	Dephosphorylation	VALPPGASPQRSRSP HHCCCCCCCCCCCCC	27.72	11030334
268	Phosphorylation	VALPPGASPQRSRSP HHCCCCCCCCCCCCC	27.72	29255136
272	Phosphorylation	PGASPQRSRSPSPQP CCCCCCCCCCCCCCC	31.68	27080861
274	Dephosphorylation	ASPQRSRSPSPQPSS CCCCCCCCCCCCCCC	30.86	11030334
274	Phosphorylation	ASPQRSRSPSPQPSS CCCCCCCCCCCCCCC	30.86	11030334
276	Dephosphorylation	PQRSRSPSPQPSSHV CCCCCCCCCCCCCCC	37.10	11030334
276	Phosphorylation	PQRSRSPSPQPSSHV CCCCCCCCCCCCCCC	37.10	11030334
280	Dephosphorylation	RSPSPQPSSHVAPQD CCCCCCCCCCCCCCC	28.03	11030334
280	Phosphorylation	RSPSPQPSSHVAPQD CCCCCCCCCCCCCCC	28.03	11030334
281	Phosphorylation	SPSPQPSSHVAPQDH CCCCCCCCCCCCCCC	28.76	27080861
290	Phosphorylation	VAPQDHGSPAGYPPV CCCCCCCCCCCCCCC	14.25	26074081
294	Phosphorylation	DHGSPAGYPPVAGSA CCCCCCCCCCCCCHH	13.38	26074081
314	O-linked_Glycosylation	LNSLATDSPCGIPPK HHHHHCCCCCCCCHH	20.10	29351928
325	Phosphorylation	IPPKMWKTSPDPSPV CCHHHCCCCCCCCCC	29.94	23401153
326	Dephosphorylation	PPKMWKTSPDPSPVS CHHHCCCCCCCCCCC	24.47	11030334
326	Phosphorylation	PPKMWKTSPDPSPVS CHHHCCCCCCCCCCC	24.47	29255136
330	Phosphorylation	WKTSPDPSPVSAAPS CCCCCCCCCCCCCCC	45.36	22617229
333	O-linked_Glycosylation	SPDPSPVSAAPSKAG CCCCCCCCCCCCCCC	23.30	29351928
333	Phosphorylation	SPDPSPVSAAPSKAG CCCCCCCCCCCCCCC	23.30	22617229
337	Phosphorylation	SPVSAAPSKAGLPRH CCCCCCCCCCCCCCC	30.34	21712546
338	Ubiquitination	PVSAAPSKAGLPRHI CCCCCCCCCCCCCCC	45.47	-
346	Phosphorylation	AGLPRHIYPAVEFLG CCCCCCCCEECHHCC	4.49	22817900
363	Dephosphorylation	EQGERRNSAPESILL CCCCCCCCCCCCEEE	43.31	11030334
363	Phosphorylation	EQGERRNSAPESILL CCCCCCCCCCCCEEE	43.31	22617229
367	Phosphorylation	RRNSAPESILLVPPT CCCCCCCCEEECCCC	19.92	22617229
374	Phosphorylation	SILLVPPTWPKPLVP CEEECCCCCCCCCCC	48.61	20068231
429	Phosphorylation	AHYETEGSRGAVKAP CEEECCCCCCCEECC	22.70	23403867
482	Ubiquitination	QVHRITGKTVTTTSY EEEEECCCEEECCEE	31.04	-
483	Phosphorylation	VHRITGKTVTTTSYE EEEECCCEEECCEEE	25.16	20068231
485	Phosphorylation	RITGKTVTTTSYEKI EECCCEEECCEEEEE	29.59	20068231
486	Phosphorylation	ITGKTVTTTSYEKIV ECCCEEECCEEEEEE	14.92	20068231
487	Phosphorylation	TGKTVTTTSYEKIVG CCCEEECCEEEEEEC	21.68	20068231
488	Phosphorylation	GKTVTTTSYEKIVGN CCEEECCEEEEEECC	29.24	20068231
489	Phosphorylation	KTVTTTSYEKIVGNT CEEECCEEEEEECCC	21.10	20068231
491	Ubiquitination	VTTTSYEKIVGNTKV EECCEEEEEECCCEE	34.16	-
497	Ubiquitination	EKIVGNTKVLEIPLE EEEECCCEEEEEECC	49.15	-
520	Ubiquitination	IDCAGILKLRNADIE EEHHHHHHHHCCCEE	43.40	-
530	Ubiquitination	NADIELRKGETDIGR CCCEEECCCCCCCCC	73.96	-
570	Phosphorylation	ASNPIECSQRSAHEL CCCCCCCHHCCCCCC	18.81	28857561
585	Phosphorylation	PMVERQDTDSCLVYG CCEECCCCCCEEEEC	22.82	22817900
599	Phosphorylation	GGQQMILTGQNFTSE CCEEEEEECCCCCCC	26.29	22817900
605	Phosphorylation	LTGQNFTSESKVVFT EECCCCCCCCEEEEE	35.42	22817900
633	O-linked_Glycosylation	ATVDKDKSQPNMLFV EEECCCCCCCCEEEE	62.09	29351928
633	Phosphorylation	ATVDKDKSQPNMLFV EEECCCCCCCCEEEE	62.09	27135362
652	Phosphorylation	YRNKHIRTPVKVNFY HCCCCCCCCCEEEEE	31.65	24719451
674	Phosphorylation	RSQPQHFTYHPVPAI CCCCCCCEECCCCCC	20.85	26074081
675	Phosphorylation	SQPQHFTYHPVPAIK CCCCCCEECCCCCCC	11.81	26074081
683	Phosphorylation	HPVPAIKTEPTDEYD CCCCCCCCCCCCCCC	40.87	26074081
686	Phosphorylation	PAIKTEPTDEYDPTL CCCCCCCCCCCCCCE	34.92	26074081
689	Phosphorylation	KTEPTDEYDPTLICS CCCCCCCCCCCEEEC	29.99	26074081
692	Phosphorylation	PTDEYDPTLICSPTH CCCCCCCCEEECCCC	26.34	26074081
696	Phosphorylation	YDPTLICSPTHGGLG CCCCEEECCCCCCCC	26.32	26074081
698	Phosphorylation	PTLICSPTHGGLGSQ CCEEECCCCCCCCCC	19.50	26074081
704	Phosphorylation	PTHGGLGSQPYYPQH CCCCCCCCCCCCCCC	32.78	26074081
707	Phosphorylation	GGLGSQPYYPQHPMV CCCCCCCCCCCCCCC	21.82	26074081
708	Phosphorylation	GLGSQPYYPQHPMVA CCCCCCCCCCCCCCC	11.78	26074081
717	Phosphorylation	QHPMVAESPSCLVAT CCCCCCCCCCEEEEE	16.63	26074081
719	Phosphorylation	PMVAESPSCLVATMA CCCCCCCCEEEEEEC	29.39	26074081
724	Phosphorylation	SPSCLVATMAPCQQF CCCEEEEEECCHHHH	13.34	26074081
733	O-linked_Glycosylation	APCQQFRTGLSSPDA CCHHHHHCCCCCCCH	43.70	29351928
733	Phosphorylation	APCQQFRTGLSSPDA CCHHHHHCCCCCCCH	43.70	26074081
736	Phosphorylation	QQFRTGLSSPDARYQ HHHHCCCCCCCHHHH	40.96	25849741
737	Phosphorylation	QFRTGLSSPDARYQQ HHHCCCCCCCHHHHH	31.66	25849741
752	Phosphorylation	QNPAAVLYQRSKSLS HCHHHHHHHCCCCCC	8.69	29978859
755	Phosphorylation	AAVLYQRSKSLSPSL HHHHHHCCCCCCHHH	15.86	22617229
757	Phosphorylation	VLYQRSKSLSPSLLG HHHHCCCCCCHHHHC	35.01	29255136
759	Phosphorylation	YQRSKSLSPSLLGYQ HHCCCCCCHHHHCCC	21.38	29255136
761	Phosphorylation	RSKSLSPSLLGYQQP CCCCCCHHHHCCCCC	32.61	29255136
765	Phosphorylation	LSPSLLGYQQPALMA CCHHHHCCCCCHHHH	12.16	28102081
776	Phosphorylation	ALMAAPLSLADAHRS HHHHCCCCHHHHCHH	22.06	26074081
783	Phosphorylation	SLADAHRSVLVHAGS CHHHHCHHEEEECCC	15.22	23312004
790	Phosphorylation	SVLVHAGSQGQSSAL HEEEECCCCCCCCCC	31.74	25850435
794	Phosphorylation	HAGSQGQSSALLHPS ECCCCCCCCCCCCCC	25.14	25850435
795	Phosphorylation	AGSQGQSSALLHPSP CCCCCCCCCCCCCCC	18.30	25850435
801	Phosphorylation	SSALLHPSPTNQQAS CCCCCCCCCCCCCCC	33.34	30576142
803	Phosphorylation	ALLHPSPTNQQASPV CCCCCCCCCCCCCCE	50.42	28464451
808	Phosphorylation	SPTNQQASPVIHYSP CCCCCCCCCEEEECC	18.50	28464451
813	Phosphorylation	QASPVIHYSPTNQQL CCCCEEEECCCCCEE	12.76	28796482
814	Phosphorylation	ASPVIHYSPTNQQLR CCCEEEECCCCCEEC	15.87	23898821
816	Phosphorylation	PVIHYSPTNQQLRCG CEEEECCCCCEECCC	39.45	28796482
824	Phosphorylation	NQQLRCGSHQEFQHI CCEECCCCCHHHHEE	26.14	28348404
850	O-linked_Glycosylation	RPGPPPVSQGQRLSP CCCCCCCCCCCCCCC	34.07	29351928
856	Phosphorylation	VSQGQRLSPGSYPTV CCCCCCCCCCCCCCH	29.42	23401153
859	Phosphorylation	GQRLSPGSYPTVIQQ CCCCCCCCCCCHHEE	31.18	23401153
860	Phosphorylation	QRLSPGSYPTVIQQQ CCCCCCCCCCHHEEC	14.61	30278072
862	Phosphorylation	LSPGSYPTVIQQQNA CCCCCCCCHHEECCH	23.23	30278072
870	Phosphorylation	VIQQQNATSQRAAKN HHEECCHHHHHHHHH	32.70	23403867
871	Phosphorylation	IQQQNATSQRAAKNG HEECCHHHHHHHHHC	18.43	23403867
882	Phosphorylation	AKNGPPVSDQKEVLP HHHCCCCCCCCCEEC	39.85	20068231
885	Ubiquitination	GPPVSDQKEVLPAGV CCCCCCCCCEECCCC	55.57	-
893	Phosphorylation	EVLPAGVTIKQEQNL CEECCCCEEEEECCC	22.87	-
895	Sumoylation	LPAGVTIKQEQNLDQ ECCCCEEEEECCCCC	38.12	-
903	Phosphorylation	QEQNLDQTYLDDVNE EECCCCCCHHHHHHH	26.22	28796482
904	Phosphorylation	EQNLDQTYLDDVNEI ECCCCCCHHHHHHHH	11.51	28796482

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
-	K	Ubiquitination	E3 ubiquitin ligase	MDM2	Q00987	PMID:16338656

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
53	S	Phosphorylation	-
Simultaneously, Ser-53 or Ser-56 is phosphorylated; which is required for full transcriptional activity.
56	S	Phosphorylation	-
Simultaneously, Ser-53 or Ser-56 is phosphorylated; which is required for full transcriptional activity.
243	S	Phosphorylation	-
Upon cell stimulation, all these sites except Ser-243 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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NFAC2_HUMAN	NFATC2	physical	12949493
EP300_HUMAN	EP300	physical	9625762
MED31_HUMAN	MED31	physical	16169070
VIME_HUMAN	VIM	physical	16169070
KPCZ_HUMAN	PRKCZ	physical	12021260
IRF4_HUMAN	IRF4	physical	11956291
SUV91_HUMAN	SUV39H1	physical	22079596
TBA1A_HUMAN	TUBA1A	physical	21278340
IMB1_HUMAN	KPNB1	physical	21278340
TAF9_HUMAN	TAF9	physical	10821850
I2BP2_HUMAN	IRF2BP2	physical	21576369
NFAC2_HUMAN	NFATC2	physical	19060202
JUN_HUMAN	JUN	physical	20557936
LRRK2_HUMAN	LRRK2	physical	21983832
IQGA1_HUMAN	IQGAP1	physical	21983832
XPO2_HUMAN	CSE1L	physical	21983832
TNPO1_HUMAN	TNPO1	physical	21983832
2AAA_HUMAN	PPP2R1A	physical	21983832
UBP22_HUMAN	USP22	physical	24561192
IKZF1_HUMAN	IKZF1	physical	27637333
JUN_HUMAN	JUN	physical	27637333
RPTOR_HUMAN	RPTOR	physical	27637333
CREB1_HUMAN	CREB1	physical	27637333
EP300_HUMAN	EP300	physical	27637333
FOS_HUMAN	FOS	physical	27637333
CHK1_HUMAN	CHEK1	physical	27637333
SCAI_HUMAN	SCAI	physical	27637333
IKZF2_HUMAN	IKZF2	physical	27637333
GSK3B_HUMAN	GSK3B	physical	27637333
RUNX1_HUMAN	RUNX1	physical	27637333
SATB1_HUMAN	SATB1	physical	27637333
WDR48_HUMAN	WDR48	physical	27637333
ZN384_HUMAN	ZNF384	physical	27637333
ATF7_HUMAN	ATF7	physical	27637333
ZN131_HUMAN	ZNF131	physical	27637333
MAFK_HUMAN	MAFK	physical	27637333
XRCC5_HUMAN	XRCC5	physical	27637333
PRKDC_HUMAN	PRKDC	physical	27637333
KC1D_HUMAN	CSNK1D	physical	27637333
JUNB_HUMAN	JUNB	physical	27637333
NFYC_HUMAN	NFYC	physical	27637333
PLK1_HUMAN	PLK1	physical	27637333
DNLI3_HUMAN	LIG3	physical	27637333
XRCC1_HUMAN	XRCC1	physical	27637333
HLTF_HUMAN	HLTF	physical	27637333
BTAF1_HUMAN	BTAF1	physical	27637333
1433B_HUMAN	YWHAB	physical	27637333
CAF1B_HUMAN	CHAF1B	physical	27637333
LEF1_HUMAN	LEF1	physical	27637333
I2BP1_HUMAN	IRF2BP1	physical	27637333
JUND_HUMAN	JUND	physical	27637333
TFAM_HUMAN	TFAM	physical	27637333
MAFG_HUMAN	MAFG	physical	27637333
SSBP_HUMAN	SSBP1	physical	27637333
RANB9_HUMAN	RANBP9	physical	27637333
CHAP1_HUMAN	CHAMP1	physical	27637333
RFA1_HUMAN	RPA1	physical	27637333
WDR26_HUMAN	WDR26	physical	27637333
I2BP2_HUMAN	IRF2BP2	physical	27637333
ZN148_HUMAN	ZNF148	physical	27637333
FOXK1_HUMAN	FOXK1	physical	27637333
ZN217_HUMAN	ZNF217	physical	27637333
DEK_HUMAN	DEK	physical	27637333
RFA3_HUMAN	RPA3	physical	27637333
DPOG1_HUMAN	POLG	physical	27637333
CYBP_HUMAN	CACYBP	physical	27637333
RFA2_HUMAN	RPA2	physical	27637333
NFYB_HUMAN	NFYB	physical	27637333
PARP1_HUMAN	PARP1	physical	27637333
ETV6_HUMAN	ETV6	physical	27637333
XRCC6_HUMAN	XRCC6	physical	27637333
KIF4A_HUMAN	KIF4A	physical	27637333
RFC4_HUMAN	RFC4	physical	27637333
RFC3_HUMAN	RFC3	physical	27637333
EGR1_HUMAN	EGR1	physical	27637333
PYR1_HUMAN	CAD	physical	27637333
RFC5_HUMAN	RFC5	physical	27637333
CTBP1_HUMAN	CTBP1	physical	27637333
RFC2_HUMAN	RFC2	physical	27637333
BC11B_HUMAN	BCL11B	physical	27637333
1433G_HUMAN	YWHAG	physical	27637333
KIF2C_HUMAN	KIF2C	physical	27637333
MCE1_HUMAN	RNGTT	physical	27637333
PRD15_HUMAN	PRDM15	physical	27637333
P5CS_HUMAN	ALDH18A1	physical	27637333
MTDC_HUMAN	MTHFD2	physical	27637333
1433E_HUMAN	YWHAE	physical	27637333
RM39_HUMAN	MRPL39	physical	27637333
EFTU_HUMAN	TUFM	physical	27637333
IF16_HUMAN	IFI16	physical	27637333
TP53B_HUMAN	TP53BP1	physical	27637333
ERAL1_HUMAN	ERAL1	physical	27637333
SSRP1_HUMAN	SSRP1	physical	27637333
TRRAP_HUMAN	TRRAP	physical	27637333
1433T_HUMAN	YWHAQ	physical	27637333
HIRA_HUMAN	HIRA	physical	27637333
ERCC3_HUMAN	ERCC3	physical	27637333
UBE2S_HUMAN	UBE2S	physical	27637333
SPT6H_HUMAN	SUPT6H	physical	27637333
ARI1A_HUMAN	ARID1A	physical	27637333
GRP75_HUMAN	HSPA9	physical	27637333
POGZ_HUMAN	POGZ	physical	27637333
UHRF1_HUMAN	UHRF1	physical	27637333
SUCB1_HUMAN	SUCLA2	physical	27637333
GRP78_HUMAN	HSPA5	physical	27637333
REQU_HUMAN	DPF2	physical	27637333
1433Z_HUMAN	YWHAZ	physical	27637333
P66A_HUMAN	GATAD2A	physical	27637333
LRC47_HUMAN	LRRC47	physical	27637333
ZMYM2_HUMAN	ZMYM2	physical	27637333
DNJA1_HUMAN	DNAJA1	physical	27637333
IDH3A_HUMAN	IDH3A	physical	27637333
SDHA_HUMAN	SDHA	physical	27637333
CBX5_HUMAN	CBX5	physical	27637333
CABIN_HUMAN	CABIN1	physical	27637333
VAPA_HUMAN	VAPA	physical	27637333
CBX3_HUMAN	CBX3	physical	27637333
MRE11_HUMAN	MRE11A	physical	27637333
SMCA5_HUMAN	SMARCA5	physical	27637333
EF2_HUMAN	EEF2	physical	27637333
RB_HUMAN	RB1	physical	27637333
MCRS1_HUMAN	MCRS1	physical	27637333
EMD_HUMAN	EMD	physical	27637333
T2H2L_HUMAN	GTF2H2C	physical	27637333
TF2H2_HUMAN	GTF2H2	physical	27637333
SPT5H_HUMAN	SUPT5H	physical	27637333
RCOR1_HUMAN	RCOR1	physical	27637333
VAPB_HUMAN	VAPB	physical	27637333
RM17_HUMAN	MRPL17	physical	27637333
QCR2_HUMAN	UQCRC2	physical	27637333
HTF4_HUMAN	TCF12	physical	27637333
BEND3_HUMAN	BEND3	physical	27637333
SMCA4_HUMAN	SMARCA4	physical	27637333
KDM1A_HUMAN	KDM1A	physical	27637333
SMRD2_HUMAN	SMARCD2	physical	27637333
AIFM1_HUMAN	AIFM1	physical	27637333
MCM2_HUMAN	MCM2	physical	27637333
H2AY_HUMAN	H2AFY	physical	27637333
HSP7C_HUMAN	HSPA8	physical	27637333
PDIP2_HUMAN	POLDIP2	physical	27637333
RAD50_HUMAN	RAD50	physical	27637333
SMRC1_HUMAN	SMARCC1	physical	27637333
RPAC1_HUMAN	POLR1C	physical	27637333
TIM50_HUMAN	TIMM50	physical	27637333
MTA2_HUMAN	MTA2	physical	27637333
ECHA_HUMAN	HADHA	physical	27637333
TLK2_HUMAN	TLK2	physical	27637333
TLK1_HUMAN	TLK1	physical	27637333
RBBP4_HUMAN	RBBP4	physical	27637333
P66B_HUMAN	GATAD2B	physical	27637333
RBP2_HUMAN	RANBP2	physical	27637333
CEBPE_HUMAN	CEBPE	physical	27637333
ADNP_HUMAN	ADNP	physical	27637333
SMCE1_HUMAN	SMARCE1	physical	27637333
CN37_HUMAN	CNP	physical	27637333
CBX1_HUMAN	CBX1	physical	27637333
SMRC2_HUMAN	SMARCC2	physical	27637333
ZNF24_HUMAN	ZNF24	physical	27637333
CHD4_HUMAN	CHD4	physical	27637333
SMRD1_HUMAN	SMARCD1	physical	27637333
MBD3_HUMAN	MBD3	physical	27637333
NUDC_HUMAN	NUDC	physical	27637333
ACL6A_HUMAN	ACTL6A	physical	27637333
MTA1_HUMAN	MTA1	physical	27637333
IDH3B_HUMAN	IDH3B	physical	27637333
CSTF1_HUMAN	CSTF1	physical	27637333
RL23_HUMAN	RPL23	physical	27637333
PP1A_HUMAN	PPP1CA	physical	27637333
HS105_HUMAN	HSPH1	physical	27637333
MPPB_HUMAN	PMPCB	physical	27637333
TF3C5_HUMAN	GTF3C5	physical	27637333
TCPA_HUMAN	TCP1	physical	27637333
TF3C4_HUMAN	GTF3C4	physical	27637333
DCAF7_HUMAN	DCAF7	physical	27637333
HDAC1_HUMAN	HDAC1	physical	27637333

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 NFAC2_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-330; SER-755; SER-759;SER-856 AND SER-859, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-585; THR-599 ANDSER-605, AND MASS SPECTROMETRY.	17287340 [Abstract]
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry."; Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.; Anal. Chem. 76:2763-2772(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326 AND SER-330, ANDMASS SPECTROMETRY.	15144186 [Abstract]

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