dbPTM

1433E_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	1433E_HUMAN
UniProt AC	P62258
Protein Name	14-3-3 protein epsilon
Gene Name	YWHAE
Organism	Homo sapiens (Human).
Sequence Length	255
Subcellular Localization	Nucleus . Cytoplasm . Melanosome . Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Protein Description	Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). Positively regulates phosphorylated protein HSF1 nuclear export to the cytoplasm. [PubMed: 12917326]
Protein Sequence	MDDREDLVYQAKLAEQAERYDEMVESMKKVAGMDVELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEENKGGEDKLKMIREYRQMVETELKLICCDILDVLDKHLIPAANTGESKVFYYKMKGDYHRYLAEFATGNDRKEAAENSLVAYKAASDIAMTELPPTHPIRLGLALNFSVFYYEILNSPDRACRLAKAAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDMQGDGEEQNKEALQDVEDENQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDDREDLV -------CCHHHHHH	12.49	19413330
1	Sulfoxidation	-------MDDREDLV -------CCHHHHHH	12.49	28465586
4	Methylation	----MDDREDLVYQA ----CCHHHHHHHHH	34.76	-
9	Phosphorylation	DDREDLVYQAKLAEQ CHHHHHHHHHHHHHH	15.28	27155012
12	Acetylation	EDLVYQAKLAEQAER HHHHHHHHHHHHHHH	32.48	23749302
12	Ubiquitination	EDLVYQAKLAEQAER HHHHHHHHHHHHHHH	32.48	21890473
12	Ubiquitination	EDLVYQAKLAEQAER HHHHHHHHHHHHHHH	32.48	21890473
23	Sulfoxidation	QAERYDEMVESMKKV HHHHHHHHHHHHHHH	3.56	30846556
26	Phosphorylation	RYDEMVESMKKVAGM HHHHHHHHHHHHCCC	25.21	30622161
27	Sulfoxidation	YDEMVESMKKVAGMD HHHHHHHHHHHCCCC	2.85	30846556
28	Succinylation	DEMVESMKKVAGMDV HHHHHHHHHHCCCCE	54.07	23954790
28	Acetylation	DEMVESMKKVAGMDV HHHHHHHHHHCCCCE	54.07	25953088
28	Ubiquitination	DEMVESMKKVAGMDV HHHHHHHHHHCCCCE	54.07	-
29	Ubiquitination	EMVESMKKVAGMDVE HHHHHHHHHCCCCEE	28.77	21906983
33	Sulfoxidation	SMKKVAGMDVELTVE HHHHHCCCCEEEEHH	3.63	21406390
38	Phosphorylation	AGMDVELTVEERNLL CCCCEEEEHHHHHHH	16.62	19060867
46	Phosphorylation	VEERNLLSVAYKNVI HHHHHHHHHHHHHHH	14.10	19664994
49	Phosphorylation	RNLLSVAYKNVIGAR HHHHHHHHHHHHHHH	10.84	22617229
50	Ubiquitination	NLLSVAYKNVIGARR HHHHHHHHHHHHHHH	34.69	21890473
50	Succinylation	NLLSVAYKNVIGARR HHHHHHHHHHHHHHH	34.69	23954790
50	Sumoylation	NLLSVAYKNVIGARR HHHHHHHHHHHHHHH	34.69	28112733
50	2-Hydroxyisobutyrylation	NLLSVAYKNVIGARR HHHHHHHHHHHHHHH	34.69	-
50	Ubiquitination	NLLSVAYKNVIGARR HHHHHHHHHHHHHHH	34.69	21890473
50	Acetylation	NLLSVAYKNVIGARR HHHHHHHHHHHHHHH	34.69	19608861
59	Phosphorylation	VIGARRASWRIISSI HHHHHHHHHHHHHHH	18.31	23882029
64	Phosphorylation	RASWRIISSIEQKEE HHHHHHHHHHHHHHH	23.92	20068231
65	Phosphorylation	ASWRIISSIEQKEEN HHHHHHHHHHHHHHC	21.53	20068231
69	Ubiquitination	IISSIEQKEENKGGE HHHHHHHHHHCCCCH	54.96	6983
69	Acetylation	IISSIEQKEENKGGE HHHHHHHHHHCCCCH	54.96	19608861
73	Ubiquitination	IEQKEENKGGEDKLK HHHHHHCCCCHHHHH	72.13	21906983
78	Acetylation	ENKGGEDKLKMIREY HCCCCHHHHHHHHHH	45.78	23749302
80	Ubiquitination	KGGEDKLKMIREYRQ CCCHHHHHHHHHHHH	37.71	-
85	Phosphorylation	KLKMIREYRQMVETE HHHHHHHHHHHHHHH	9.04	28634298
88	Sulfoxidation	MIREYRQMVETELKL HHHHHHHHHHHHHHH	1.86	21406390
91	Phosphorylation	EYRQMVETELKLICC HHHHHHHHHHHHHHH	34.90	20363803
97	Glutathionylation	ETELKLICCDILDVL HHHHHHHHHHHHHHH	2.18	22555962
97	S-nitrosylation	ETELKLICCDILDVL HHHHHHHHHHHHHHH	2.18	22178444
97	S-palmitoylation	ETELKLICCDILDVL HHHHHHHHHHHHHHH	2.18	29575903
97	S-nitrosocysteine	ETELKLICCDILDVL HHHHHHHHHHHHHHH	2.18	-
98	Glutathionylation	TELKLICCDILDVLD HHHHHHHHHHHHHHH	2.64	22555962
98	S-nitrosylation	TELKLICCDILDVLD HHHHHHHHHHHHHHH	2.64	22178444
98	S-palmitoylation	TELKLICCDILDVLD HHHHHHHHHHHHHHH	2.64	29575903
98	S-nitrosocysteine	TELKLICCDILDVLD HHHHHHHHHHHHHHH	2.64	-
106	2-Hydroxyisobutyrylation	DILDVLDKHLIPAAN HHHHHHHHHCCCCCC	35.83	-
106	Ubiquitination	DILDVLDKHLIPAAN HHHHHHHHHCCCCCC	35.83	21906983
106	Ubiquitination	DILDVLDKHLIPAAN HHHHHHHHHCCCCCC	35.83	21890473
106	Acetylation	DILDVLDKHLIPAAN HHHHHHHHHCCCCCC	35.83	21466224
114	Phosphorylation	HLIPAANTGESKVFY HCCCCCCCCCCEEEE	37.28	23911959
117	Phosphorylation	PAANTGESKVFYYKM CCCCCCCCEEEEEEE	35.15	108826409
118	Ubiquitination	AANTGESKVFYYKMK CCCCCCCEEEEEEEC	31.87	21890473
118	2-Hydroxyisobutyrylation	AANTGESKVFYYKMK CCCCCCCEEEEEEEC	31.87	-
118	Succinylation	AANTGESKVFYYKMK CCCCCCCEEEEEEEC	31.87	23954790
118	Acetylation	AANTGESKVFYYKMK CCCCCCCEEEEEEEC	31.87	19608861
118	Ubiquitination	AANTGESKVFYYKMK CCCCCCCEEEEEEEC	31.87	21890473
122	Phosphorylation	GESKVFYYKMKGDYH CCCEEEEEEECCCHH	7.98	24719451
123	Acetylation	ESKVFYYKMKGDYHR CCEEEEEEECCCHHH	23.82	19608861
123	2-Hydroxyisobutyrylation	ESKVFYYKMKGDYHR CCEEEEEEECCCHHH	23.82	-
123	Ubiquitination	ESKVFYYKMKGDYHR CCEEEEEEECCCHHH	23.82	21890473
123	Ubiquitination	ESKVFYYKMKGDYHR CCEEEEEEECCCHHH	23.82	21890473
123	Succinylation	ESKVFYYKMKGDYHR CCEEEEEEECCCHHH	23.82	23954790
125	Ubiquitination	KVFYYKMKGDYHRYL EEEEEEECCCHHHHH	44.47	21906983
125	2-Hydroxyisobutyrylation	KVFYYKMKGDYHRYL EEEEEEECCCHHHHH	44.47	-
130	Methylation	KMKGDYHRYLAEFAT EECCCHHHHHHHHHC	23.18	-
131	Phosphorylation	MKGDYHRYLAEFATG ECCCHHHHHHHHHCC	9.28	24927040
137	Phosphorylation	RYLAEFATGNDRKEA HHHHHHHCCCCHHHH	41.67	26437602
142	Malonylation	FATGNDRKEAAENSL HHCCCCHHHHHHHHH	55.35	26320211
142	Ubiquitination	FATGNDRKEAAENSL HHCCCCHHHHHHHHH	55.35	21890473
142	2-Hydroxyisobutyrylation	FATGNDRKEAAENSL HHCCCCHHHHHHHHH	55.35	-
142	Acetylation	FATGNDRKEAAENSL HHCCCCHHHHHHHHH	55.35	23954790
142	Ubiquitination	FATGNDRKEAAENSL HHCCCCHHHHHHHHH	55.35	21890473
148	Phosphorylation	RKEAAENSLVAYKAA HHHHHHHHHHHHHHH	18.74	21712546
153	Acetylation	ENSLVAYKAASDIAM HHHHHHHHHHCHHCC	27.95	25953088
153	Ubiquitination	ENSLVAYKAASDIAM HHHHHHHHHHCHHCC	27.95	21906983
153	Methylation	ENSLVAYKAASDIAM HHHHHHHHHHCHHCC	27.95	-
160	Sulfoxidation	KAASDIAMTELPPTH HHHCHHCCCCCCCCC	2.82	21406390
181	Phosphorylation	ALNFSVFYYEILNSP EEEEEHHHHHHHCCH	9.68	30459007
187	Phosphorylation	FYYEILNSPDRACRL HHHHHHCCHHHHHHH	25.40	22817901
196	Ubiquitination	DRACRLAKAAFDDAI HHHHHHHHHHHHHHH	44.85	21890473
196	2-Hydroxyisobutyrylation	DRACRLAKAAFDDAI HHHHHHHHHHHHHHH	44.85	-
196	Ubiquitination	DRACRLAKAAFDDAI HHHHHHHHHHHHHHH	44.85	21890473
196	Acetylation	DRACRLAKAAFDDAI HHHHHHHHHHHHHHH	44.85	26822725
208	Phosphorylation	DAIAELDTLSEESYK HHHHHHHCCCHHHCC	44.82	29255136
210	Phosphorylation	IAELDTLSEESYKDS HHHHHCCCHHHCCCH	41.22	19664994
213	Phosphorylation	LDTLSEESYKDSTLI HHCCCHHHCCCHHHH	33.17	29255136
214	Phosphorylation	DTLSEESYKDSTLIM HCCCHHHCCCHHHHH	23.30	28176443
215	Methylation	TLSEESYKDSTLIMQ CCCHHHCCCHHHHHH	55.25	23644510
217	Phosphorylation	SEESYKDSTLIMQLL CHHHCCCHHHHHHHH	22.44	22617229
218	Phosphorylation	EESYKDSTLIMQLLR HHHCCCHHHHHHHHH	30.36	29255136
221	Sulfoxidation	YKDSTLIMQLLRDNL CCCHHHHHHHHHCCC	2.30	30846556
229	Phosphorylation	QLLRDNLTLWTSDMQ HHHHCCCEEEECCCC	26.89	21815630
232	Phosphorylation	RDNLTLWTSDMQGDG HCCCEEEECCCCCCC	20.26	25159151
233	Phosphorylation	DNLTLWTSDMQGDGE CCCEEEECCCCCCCH	21.36	25159151
235	Sulfoxidation	LTLWTSDMQGDGEEQ CEEEECCCCCCCHHH	4.87	28465586
244	Acetylation	GDGEEQNKEALQDVE CCCHHHHHHHHHHCH	44.02	26051181
244	Ubiquitination	GDGEEQNKEALQDVE CCCHHHHHHHHHHCH	44.02	21906983

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
208	T	Phosphorylation	Kinase	PLK2	Q9NYY3	PSP
208	T	Phosphorylation	Kinase	PLK3	Q9H4B4	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of 1433E_HUMAN !!

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 1433E_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IGF1R_HUMAN	IGF1R	physical	9111084
GRIN2_HUMAN	GPRIN2	physical	16189514
SRBS2_HUMAN	SORBS2	physical	16189514
GRAP2_HUMAN	GRAP2	physical	16189514
HDAC4_HUMAN	HDAC4	physical	11504882
REM1_HUMAN	REM1	physical	10441394
MPIP3_HUMAN	CDC25C	physical	10330186
M3K3_HUMAN	MAP3K3	physical	9452471
M3K1_HUMAN	MAP3K1	physical	9452471
M3K2_HUMAN	MAP3K2	physical	9452471
IRS1_HUMAN	IRS1	physical	9111084
BEX3_HUMAN	NGFRAP1	physical	11278287
KCNH2_HUMAN	KCNH2	physical	11953308
MPIP2_HUMAN	CDC25B	physical	10713667
TOP2A_HUMAN	TOP2A	physical	10788521
TGFB1_HUMAN	TGFB1	physical	11172812
MDM4_HUMAN	MDM4	physical	16511560
MDM4_HUMAN	MDM4	physical	16227609
BAD_HUMAN	BAD	physical	20936779
ZEP2_HUMAN	HIVEP2	physical	20936779
LRMP_HUMAN	LRMP	physical	20936779
COX2_HUMAN	COX2	physical	20936779
MYH10_HUMAN	MYH10	physical	20936779
LIPP_HUMAN	PNLIP	physical	20936779
SSFA2_HUMAN	SSFA2	physical	20936779
1433B_HUMAN	YWHAB	physical	20936779
1433F_HUMAN	YWHAH	physical	20936779
HDAC9_HUMAN	HDAC9	physical	20936779
HDAC4_HUMAN	HDAC4	physical	20936779
K0232_HUMAN	KIAA0232	physical	20936779
TLK1_HUMAN	TLK1	physical	20936779
CAF1A_HUMAN	CHAF1A	physical	20936779
CAP2_HUMAN	CAP2	physical	20936779
1433T_HUMAN	YWHAQ	physical	20936779
RPGP2_HUMAN	RAP1GAP2	physical	20936779
SH3B4_HUMAN	SH3BP4	physical	20936779
WWTR1_HUMAN	WWTR1	physical	20936779
FA13B_HUMAN	FAM13B	physical	20936779
MSL2_HUMAN	MSL2	physical	20936779
ZN839_HUMAN	ZNF839	physical	20936779
RASL3_HUMAN	RASAL3	physical	20936779
WNK1_HUMAN	WNK1	physical	20936779
ENKD1_HUMAN	ENKD1	physical	20936779
CGNL1_HUMAN	CGNL1	physical	20936779
CEP95_HUMAN	CEP95	physical	20936779
ING1_HUMAN	ING1	physical	16581770
SAMN1_HUMAN	SAMSN1	physical	20478393
HDAC7_HUMAN	HDAC7	physical	17369396
EXO1_HUMAN	EXO1	physical	21533173
KAT8_HUMAN	KAT8	physical	19766566
1433Z_HUMAN	YWHAZ	physical	19766566
H31_HUMAN	HIST1H3A	physical	19766566
ELOA1_HUMAN	TCEB3	physical	19766566
BRD4_HUMAN	BRD4	physical	19766566
FBX4_HUMAN	FBXO4	physical	21242966
CDN1B_HUMAN	CDKN1B	physical	15057270
EXO1_HUMAN	EXO1	physical	22222486
BAD_HUMAN	BAD	physical	11697890
RAF1_HUMAN	RAF1	physical	11697890
CBL_HUMAN	CBL	physical	11697890
MDM4_HUMAN	MDM4	physical	18356162
1433Z_HUMAN	YWHAZ	physical	22939629
ACTA_HUMAN	ACTA2	physical	22939629
CBX3_HUMAN	CBX3	physical	22939629
HS90B_HUMAN	HSP90AB1	physical	20462248
NPM_HUMAN	NPM1	physical	20462248
ATPB_HUMAN	ATP5B	physical	20462248
ATPA_HUMAN	ATP5A1	physical	20462248
STML2_HUMAN	STOML2	physical	20462248
ICLN_HUMAN	CLNS1A	physical	20462248
IPO8_HUMAN	IPO8	physical	20462248
IMB1_HUMAN	KPNB1	physical	20462248
RLA0_HUMAN	RPLP0	physical	20462248
RL6_HUMAN	RPL6	physical	20462248
RL4_HUMAN	RPL4	physical	20462248
RS3_HUMAN	RPS3	physical	20462248
RS8_HUMAN	RPS8	physical	20462248
DNJA1_HUMAN	DNAJA1	physical	20462248
IF4B_HUMAN	EIF4B	physical	20462248
EIF3E_HUMAN	EIF3E	physical	20462248
EF1G_HUMAN	EEF1G	physical	20462248
EF1A2_HUMAN	EEF1A2	physical	20462248
ROA2_HUMAN	HNRNPA2B1	physical	20462248
ILF2_HUMAN	ILF2	physical	20462248
RUVB2_HUMAN	RUVBL2	physical	20462248
RCN2_HUMAN	RCN2	physical	20462248
TBB5_HUMAN	TUBB	physical	20462248
TBB4B_HUMAN	TUBB4B	physical	20462248
TBB2B_HUMAN	TUBB2B	physical	20462248
KPRA_HUMAN	PRPSAP1	physical	20462248
TBA3E_HUMAN	TUBA3E	physical	20462248
DDX21_HUMAN	DDX21	physical	20462248
ADH1B_HUMAN	ADH1B	physical	20462248
ADH4_HUMAN	ADH4	physical	20462248
SPYA_HUMAN	AGXT	physical	20462248
ROA3_HUMAN	HNRNPA3	physical	20462248
HNRPC_HUMAN	HNRNPC	physical	20462248
RBY1A_HUMAN	RBMY1A1	physical	20462248
SF3B1_HUMAN	SF3B1	physical	20462248
PCBP1_HUMAN	PCBP1	physical	20462248
RBM10_HUMAN	RBM10	physical	20462248
M3K7_HUMAN	MAP3K7	physical	20462248
TBK1_HUMAN	TBK1	physical	20462248
PPM1B_HUMAN	PPM1B	physical	20462248
SPIN1_HUMAN	SPIN1	physical	20462248
CDC37_HUMAN	CDC37	physical	20462248
PHB_HUMAN	PHB	physical	20462248
KPRB_HUMAN	PRPSAP2	physical	20462248
PRPS1_HUMAN	PRPS1	physical	20462248
QPCTL_HUMAN	QPCTL	physical	20462248
LAP2A_HUMAN	TMPO	physical	20462248
LAP2B_HUMAN	TMPO	physical	20462248
CK084_HUMAN	C11orf84	physical	20462248
HDX_HUMAN	HDX	physical	20462248
CFA43_HUMAN	CFAP43	physical	20462248
PARD3_HUMAN	PARD3	physical	17979178
KINH_HUMAN	KIF5B	physical	17979178
1433Z_HUMAN	YWHAZ	physical	17979178
KLC2_HUMAN	KLC2	physical	17979178
LMO7_HUMAN	LMO7	physical	17979178
1433T_HUMAN	YWHAQ	physical	17979178
1433G_HUMAN	YWHAG	physical	17979178
1433B_HUMAN	YWHAB	physical	17979178
TBCD4_HUMAN	TBC1D4	physical	17979178
KLC3_HUMAN	KLC3	physical	17979178
KLC4_HUMAN	KLC4	physical	17979178
1433F_HUMAN	YWHAH	physical	17979178
KLC1_HUMAN	KLC1	physical	17979178
CLAP2_HUMAN	CLASP2	physical	17979178
LIMA1_HUMAN	LIMA1	physical	17979178
MARK2_HUMAN	MARK2	physical	17979178
TSC2_HUMAN	TSC2	physical	17979178
CLAP1_HUMAN	CLASP1	physical	17979178
HSP7C_HUMAN	HSPA8	physical	17979178
MARK3_HUMAN	MARK3	physical	17979178
PAK4_HUMAN	PAK4	physical	17979178
RFIP2_HUMAN	RAB11FIP2	physical	17979178
MAST3_HUMAN	MAST3	physical	17979178
TBCD1_HUMAN	TBC1D1	physical	17979178
KIF1C_HUMAN	KIF1C	physical	17979178
OSBL3_HUMAN	OSBPL3	physical	17979178
TIAM1_HUMAN	TIAM1	physical	17979178
ABLM1_HUMAN	ABLIM1	physical	17979178
RAF1_HUMAN	RAF1	physical	17979178
LARP1_HUMAN	LARP1	physical	17979178
BRAF_HUMAN	BRAF	physical	17979178
BAIP2_HUMAN	BAIAP2	physical	17979178
IRS2_HUMAN	IRS2	physical	17979178
SHRM2_HUMAN	SHROOM2	physical	17979178
LSR_HUMAN	LSR	physical	17979178
KIF1B_HUMAN	KIF1B	physical	17979178
PTN14_HUMAN	PTPN14	physical	17979178
ARAF_HUMAN	ARAF	physical	17979178
RFIP1_HUMAN	RAB11FIP1	physical	17979178
AFAD_HUMAN	MLLT4	physical	17979178
MAST2_HUMAN	MAST2	physical	17979178
F262_HUMAN	PFKFB2	physical	17979178
CDK18_HUMAN	CDK18	physical	17979178
PKP2_HUMAN	PKP2	physical	17979178
BAD_HUMAN	BAD	physical	17979178
M3K2_HUMAN	MAP3K2	physical	17979178
MYCPP_HUMAN	DENND4A	physical	17979178
ASPP2_HUMAN	TP53BP2	physical	17979178
HDAC7_HUMAN	HDAC7	physical	17979178
HDAC4_HUMAN	HDAC4	physical	17979178
CING_HUMAN	CGN	physical	17979178
TISD_HUMAN	ZFP36L2	physical	17979178
FOXO3_HUMAN	FOXO3	physical	17979178
TBA1A_HUMAN	TUBA1A	physical	17979178
KSR1_HUMAN	KSR1	physical	17979178
RABE1_HUMAN	RABEP1	physical	17979178
IF4E2_HUMAN	EIF4E2	physical	17979178
KC1A_HUMAN	CSNK1A1	physical	17979178
PDZ11_HUMAN	PDZD11	physical	17979178
KPCI_HUMAN	PRKCI	physical	17979178
DCAF7_HUMAN	DCAF7	physical	17979178
NADK_HUMAN	NADK	physical	17979178
UBP8_HUMAN	USP8	physical	17979178
C1QBP_HUMAN	C1QBP	physical	17979178
TSC1_HUMAN	TSC1	physical	17979178
REEP1_HUMAN	REEP1	physical	17979178
KIF23_HUMAN	KIF23	physical	17979178
ADT3_HUMAN	SLC25A6	physical	17979178
SRGP2_HUMAN	SRGAP2	physical	17979178
FA53C_HUMAN	FAM53C	physical	17979178
TRIPB_HUMAN	TRIP11	physical	17979178
BCAR1_HUMAN	BCAR1	physical	17979178
CRTC1_HUMAN	CRTC1	physical	17979178
RASF8_HUMAN	RASSF8	physical	17979178
CP250_HUMAN	CEP250	physical	17979178
VAMP8_HUMAN	VAMP8	physical	17979178
IL7RA_HUMAN	IL7R	physical	23151878
ABL1_HUMAN	ABL1	physical	16888623
RAF1_HUMAN	RAF1	physical	16093354
1433G_HUMAN	YWHAG	physical	21988832
1433Z_HUMAN	YWHAZ	physical	21988832
1433T_HUMAN	YWHAQ	physical	21988832
CD11B_HUMAN	CDK11B	physical	15883043
RAF1_HUMAN	RAF1	physical	19608861
KIF1C_HUMAN	KIF1C	physical	19608861
SRSF1_HUMAN	SRSF1	physical	19608861
UBP8_HUMAN	USP8	physical	19608861
HDAC4_HUMAN	HDAC4	physical	19608861
SRSF6_HUMAN	SRSF6	physical	19608861
SRRM2_HUMAN	SRRM2	physical	19608861
LARP1_HUMAN	LARP1	physical	19608861
SRSF4_HUMAN	SRSF4	physical	19608861
NOLC1_HUMAN	NOLC1	physical	19608861
TRA2B_HUMAN	TRA2B	physical	19608861
ARAF_HUMAN	ARAF	physical	19608861
PKHO2_HUMAN	PLEKHO2	physical	19608861
HMHA1_HUMAN	HMHA1	physical	19608861
SRSF7_HUMAN	SRSF7	physical	19608861
NCBP1_HUMAN	NCBP1	physical	19608861
DOK3_HUMAN	DOK3	physical	19608861
VASP_HUMAN	VASP	physical	19608861
C1QBP_HUMAN	C1QBP	physical	19608861
K0930_HUMAN	KIAA0930	physical	19608861
GAB2_HUMAN	GAB2	physical	19608861
RUBIC_HUMAN	KIAA0226	physical	19608861
TBCD1_HUMAN	TBC1D1	physical	19608861
PI3R4_HUMAN	PIK3R4	physical	19608861
PRAG1_HUMAN	SGK223	physical	19608861
ZN363_HUMAN	RCHY1	physical	19608861
TSC1_HUMAN	TSC1	physical	19608861
TSC2_HUMAN	TSC2	physical	19608861
MYCPP_HUMAN	DENND4A	physical	19608861
UVRAG_HUMAN	UVRAG	physical	19608861
SRSF2_HUMAN	SRSF2	physical	19608861
LRRK2_HUMAN	LRRK2	physical	20642453
MARK3_HUMAN	MARK3	physical	20642453
PA1B2_HUMAN	PAFAH1B2	physical	22863883
IPP2_HUMAN	PPP1R2	physical	22863883
PLPHP_HUMAN	PROSC	physical	22863883
GDS1_HUMAN	RAP1GDS1	physical	22863883
TMOD3_HUMAN	TMOD3	physical	22863883
TFIP8_HUMAN	TNFAIP8	physical	22863883
TBB2A_HUMAN	TUBB2A	physical	22863883
UBXN1_HUMAN	UBXN1	physical	22863883
VINC_HUMAN	VCL	physical	22863883
XPO1_HUMAN	XPO1	physical	22863883
1433F_HUMAN	YWHAH	physical	22863883
GRB10_HUMAN	GRB10	physical	15722337
DTL_HUMAN	DTL	physical	25154416
SRBS2_HUMAN	SORBS2	physical	25416956
FA53C_HUMAN	FAM53C	physical	25416956
MDM4_MOUSE	Mdm4	physical	19573810
ROA1_HUMAN	HNRNPA1	physical	25324306
THIC_HUMAN	ACAT2	physical	26344197
PUR9_HUMAN	ATIC	physical	26344197
CALR_HUMAN	CALR	physical	26344197
CENPE_HUMAN	CENPE	physical	26344197
MACF1_HUMAN	MACF1	physical	26344197
MK14_HUMAN	MAPK14	physical	26344197
MCFD2_HUMAN	MCFD2	physical	26344197
RPB4_HUMAN	POLR2D	physical	26344197
PSB2_HUMAN	PSMB2	physical	26344197
GLYM_HUMAN	SHMT2	physical	26344197
SMD1_HUMAN	SNRPD1	physical	26344197
1433B_HUMAN	YWHAB	physical	26344197
1433G_HUMAN	YWHAG	physical	26344197
1433F_HUMAN	YWHAH	physical	26344197
1433Z_HUMAN	YWHAZ	physical	26344197
ZPR1_HUMAN	ZPR1	physical	26344197
UBP8_HUMAN	USP8	physical	25675982
UBP8_HUMAN	USP8	physical	25485838
PRDX6_HUMAN	PRDX6	physical	21346153
SNF8_HUMAN	SNF8	physical	16260042
ANKZ1_HUMAN	ANKZF1	physical	16260042
SMAGP_HUMAN	SMAGP	physical	16260042
TEANC_HUMAN	TCEANC	physical	16260042
LCP2_HUMAN	LCP2	physical	16260042
MAP2_HUMAN	METAP2	physical	16260042
MAGB4_HUMAN	MAGEB4	physical	16260042
CHSTB_HUMAN	CHST11	physical	16260042
NIPA_HUMAN	ZC3HC1	physical	16260042
MCM10_HUMAN	MCM10	physical	16260042
DDX54_HUMAN	DDX54	physical	16260042
HNRPC_HUMAN	HNRNPC	physical	16260042
CH059_HUMAN	C8orf59	physical	16260042
NAF1_HUMAN	NAF1	physical	16260042
FGF12_HUMAN	FGF12	physical	16260042
GSTM3_HUMAN	GSTM3	physical	16260042
STAC_HUMAN	STAC	physical	16260042
PIMRE_HUMAN	FAM64A	physical	16260042
VATO_HUMAN	ATP6V0B	physical	16260042
CP131_HUMAN	CEP131	physical	26616734
PCM1_HUMAN	PCM1	physical	26616734
CBY1_HUMAN	CBY1	physical	27173435
CE170_HUMAN	CEP170	physical	27173435

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 1433E_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-38 AND SER-210, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-50; LYS-69; LYS-118 ANDLYS-123, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND MASSSPECTROMETRY.	19369195 [Abstract]
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-38 AND SER-210, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND MASSSPECTROMETRY.	18318008 [Abstract]