dbPTM

1433Z_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	1433Z_HUMAN
UniProt AC	P63104
Protein Name	14-3-3 protein zeta/delta
Gene Name	YWHAZ
Organism	Homo sapiens (Human).
Sequence Length	245
Subcellular Localization	Cytoplasm . Melanosome . Located to stage I to stage IV melanosomes.
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..
Protein Sequence	MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDTQGDEAEAGEGGEN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDKNELVQ -------CCHHHHHH	17.45	22814378
3	Methylation	-----MDKNELVQKA -----CCHHHHHHHH	51.53	19608861
3	Malonylation	-----MDKNELVQKA -----CCHHHHHHHH	51.53	26320211
3	Ubiquitination	-----MDKNELVQKA -----CCHHHHHHHH	51.53	19608861
3	Acetylation	-----MDKNELVQKA -----CCHHHHHHHH	51.53	19608861
9	Acetylation	DKNELVQKAKLAEQA CHHHHHHHHHHHHHH	39.75	25953088
9	Ubiquitination	DKNELVQKAKLAEQA CHHHHHHHHHHHHHH	39.75	21890473
9	Malonylation	DKNELVQKAKLAEQA CHHHHHHHHHHHHHH	39.75	26320211
11	Acetylation	NELVQKAKLAEQAER HHHHHHHHHHHHHHH	56.09	72611865
11	Ubiquitination	NELVQKAKLAEQAER HHHHHHHHHHHHHHH	56.09	21906983
19	Phosphorylation	LAEQAERYDDMAACM HHHHHHHHHHHHHHH	14.06	76971701
25	S-nitrosocysteine	RYDDMAACMKSVTEQ HHHHHHHHHHHHHHH	2.27	-
25	S-nitrosylation	RYDDMAACMKSVTEQ HHHHHHHHHHHHHHH	2.27	25040305
27	Ubiquitination	DDMAACMKSVTEQGA HHHHHHHHHHHHHHH	41.48	-
27	Acetylation	DDMAACMKSVTEQGA HHHHHHHHHHHHHHH	41.48	25953088
28	Phosphorylation	DMAACMKSVTEQGAE HHHHHHHHHHHHHHH	13.85	25849741
30	Phosphorylation	AACMKSVTEQGAELS HHHHHHHHHHHHHCC	29.67	23090842
37	Phosphorylation	TEQGAELSNEERNLL HHHHHHCCHHHHHHH	33.43	29978859
45	Phosphorylation	NEERNLLSVAYKNVV HHHHHHHHHHHHHHH	14.10	19664994
47	Ubiquitination	ERNLLSVAYKNVVGA HHHHHHHHHHHHHCC	13.25	21890473
48	Phosphorylation	RNLLSVAYKNVVGAR HHHHHHHHHHHHCCC	10.84	22617229
49	Malonylation	NLLSVAYKNVVGARR HHHHHHHHHHHCCCC	33.26	26320211
49	Methylation	NLLSVAYKNVVGARR HHHHHHHHHHHCCCC	33.26	19608861
49	Acetylation	NLLSVAYKNVVGARR HHHHHHHHHHHCCCC	33.26	19608861
49	Ubiquitination	NLLSVAYKNVVGARR HHHHHHHHHHHCCCC	33.26	21906983
57	Phosphorylation	NVVGARRSSWRVVSS HHHCCCCCCHHHHHH	28.79	23882029
58	Phosphorylation	VVGARRSSWRVVSSI HHCCCCCCHHHHHHH	19.65	15883165
63	Phosphorylation	RSSWRVVSSIEQKTE CCCHHHHHHHHHHCC	23.81	26657352
64	Phosphorylation	SSWRVVSSIEQKTEG CCHHHHHHHHHHCCH	20.66	29255136
68	Ubiquitination	VVSSIEQKTEGAEKK HHHHHHHHCCHHHHH	35.44	21906983
68	Malonylation	VVSSIEQKTEGAEKK HHHHHHHHCCHHHHH	35.44	26320211
68	Acetylation	VVSSIEQKTEGAEKK HHHHHHHHCCHHHHH	35.44	19608861
69	Phosphorylation	VSSIEQKTEGAEKKQ HHHHHHHCCHHHHHH	39.07	23312004
74	Acetylation	QKTEGAEKKQQMARE HHCCHHHHHHHHHHH	56.18	7851853
74	Ubiquitination	QKTEGAEKKQQMARE HHCCHHHHHHHHHHH	56.18	-
75	Acetylation	KTEGAEKKQQMAREY HCCHHHHHHHHHHHH	36.95	11924237
75	Ubiquitination	KTEGAEKKQQMAREY HCCHHHHHHHHHHHH	36.95	-
82	Phosphorylation	KQQMAREYREKIETE HHHHHHHHHHHHHHH	20.65	75027
85	Ubiquitination	MAREYREKIETELRD HHHHHHHHHHHHHHH	36.52	-
85	Acetylation	MAREYREKIETELRD HHHHHHHHHHHHHHH	36.52	23749302
85	Methylation	MAREYREKIETELRD HHHHHHHHHHHHHHH	36.52	-
88	Phosphorylation	EYREKIETELRDICN HHHHHHHHHHHHHHH	43.74	101661999
94	S-palmitoylation	ETELRDICNDVLSLL HHHHHHHHHHHHHHH	4.10	26865113
94	Glutathionylation	ETELRDICNDVLSLL HHHHHHHHHHHHHHH	4.10	22555962
94	S-nitrosylation	ETELRDICNDVLSLL HHHHHHHHHHHHHHH	4.10	19483679
94	S-nitrosocysteine	ETELRDICNDVLSLL HHHHHHHHHHHHHHH	4.10	-
99	Phosphorylation	DICNDVLSLLEKFLI HHHHHHHHHHHHHCC	30.65	28450419
103	Ubiquitination	DVLSLLEKFLIPNAS HHHHHHHHHCCCCHH	45.50	-
110	Phosphorylation	KFLIPNASQAESKVF HHCCCCHHHCCHHEE	36.24	29255136
114	Phosphorylation	PNASQAESKVFYLKM CCHHHCCHHEEEEEE	36.82	29255136
115	Succinylation	NASQAESKVFYLKMK CHHHCCHHEEEEEEC	28.06	23954790
115	Acetylation	NASQAESKVFYLKMK CHHHCCHHEEEEEEC	28.06	23954790
115	Ubiquitination	NASQAESKVFYLKMK CHHHCCHHEEEEEEC	28.06	21890473
120	Acetylation	ESKVFYLKMKGDYYR CHHEEEEEECCHHHH	27.47	19608861
120	Ubiquitination	ESKVFYLKMKGDYYR CHHEEEEEECCHHHH	27.47	21906983
122	Ubiquitination	KVFYLKMKGDYYRYL HEEEEEECCHHHHHH	47.22	21906983
125	Phosphorylation	YLKMKGDYYRYLAEV EEEECCHHHHHHHHH	9.86	28152594
126	Phosphorylation	LKMKGDYYRYLAEVA EEECCHHHHHHHHHH	9.49	28152594
128	Phosphorylation	MKGDYYRYLAEVAAG ECCHHHHHHHHHHCC	8.31	28102081
138	Acetylation	EVAAGDDKKGIVDQS HHHCCCCCCCCCCHH	58.60	23749302
138	Ubiquitination	EVAAGDDKKGIVDQS HHHCCCCCCCCCCHH	58.60	21906983
139	Acetylation	VAAGDDKKGIVDQSQ HHCCCCCCCCCCHHH	61.95	70527
139	Malonylation	VAAGDDKKGIVDQSQ HHCCCCCCCCCCHHH	61.95	26320211
139	Ubiquitination	VAAGDDKKGIVDQSQ HHCCCCCCCCCCHHH	61.95	21890473
145	Phosphorylation	KKGIVDQSQQAYQEA CCCCCCHHHHHHHHH	21.57	28152594
149	Phosphorylation	VDQSQQAYQEAFEIS CCHHHHHHHHHHHHH	11.53	20560217
156	Phosphorylation	YQEAFEISKKEMQPT HHHHHHHHHHHCCCC	30.40	28152594
157	Malonylation	QEAFEISKKEMQPTH HHHHHHHHHHCCCCC	59.42	26320211
157	Acetylation	QEAFEISKKEMQPTH HHHHHHHHHHCCCCC	59.42	25953088
157	Ubiquitination	QEAFEISKKEMQPTH HHHHHHHHHHCCCCC	59.42	-
158	Ubiquitination	EAFEISKKEMQPTHP HHHHHHHHHCCCCCC	52.18	21906983
160	Sulfoxidation	FEISKKEMQPTHPIR HHHHHHHCCCCCCCC	8.75	28183972
178	Phosphorylation	ALNFSVFYYEILNSP EEEHHHHHHHHHCCH	9.68	-
184	Phosphorylation	FYYEILNSPEKACSL HHHHHHCCHHHHHHH	30.87	20058876
184	O-linked_Glycosylation	FYYEILNSPEKACSL HHHHHHCCHHHHHHH	30.87	23301498
189	S-nitrosocysteine	LNSPEKACSLAKTAF HCCHHHHHHHHHHHH	5.19	-
189	S-nitrosylation	LNSPEKACSLAKTAF HCCHHHHHHHHHHHH	5.19	19483679
190	Phosphorylation	NSPEKACSLAKTAFD CCHHHHHHHHHHHHH	35.90	24719451
193	Ubiquitination	EKACSLAKTAFDEAI HHHHHHHHHHHHHHH	45.75	21906983
194	Phosphorylation	KACSLAKTAFDEAIA HHHHHHHHHHHHHHH	27.27	28464451
205	Phosphorylation	EAIAELDTLSEESYK HHHHHHHCCCHHHCC	44.82	29255136
207	Phosphorylation	IAELDTLSEESYKDS HHHHHCCCHHHCCCH	41.22	19664994
210	Phosphorylation	LDTLSEESYKDSTLI HHCCCHHHCCCHHHH	33.17	29255136
211	Phosphorylation	DTLSEESYKDSTLIM HCCCHHHCCCHHHHH	23.30	28176443
212	"N6,N6-dimethyllysine"	TLSEESYKDSTLIMQ CCCHHHCCCHHHHHH	55.25	-
212	Methylation	TLSEESYKDSTLIMQ CCCHHHCCCHHHHHH	55.25	-
214	Phosphorylation	SEESYKDSTLIMQLL CHHHCCCHHHHHHHH	22.44	28450419
215	Phosphorylation	EESYKDSTLIMQLLR HHHCCCHHHHHHHHH	30.36	29255136
226	Phosphorylation	QLLRDNLTLWTSDTQ HHHHHCCEEEECCCC	26.89	22167270
229	Phosphorylation	RDNLTLWTSDTQGDE HHCCEEEECCCCCCC	21.60	30266825
230	Phosphorylation	DNLTLWTSDTQGDEA HCCEEEECCCCCCCC	27.38	30266825
232	Phosphorylation	LTLWTSDTQGDEAEA CEEEECCCCCCCCCC	33.93	30266825

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
58	S	Phosphorylation	Kinase	AKT1	P31749	Uniprot
58	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
58	S	Phosphorylation	Kinase	MAPKAPK2	P49137	PSP
58	S	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
58	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
58	S	Phosphorylation	Kinase	PKA	-	Uniprot
58	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
58	S	Phosphorylation	Kinase	PKB_GROUP	-	PhosphoELM
184	S	Phosphorylation	Kinase	MK08	P45983	PhosphoELM
232	T	Phosphorylation	Kinase	BCR	P11274	PSP
232	T	Phosphorylation	Kinase	CSNK1A1	P48729	GPS
232	T	Phosphorylation	Kinase	CK1	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
58	S	Phosphorylation	11956222
Phosphorylated on Ser-58 by PKA and protein kinase C delta type catalytic subunit in a sphingosine-dependent fashion.
58	S	Phosphorylation	12865427
Phosphorylation on Ser-58 by PKA; disrupts homodimerization and heterodimerization with YHAE and TP53.
184	S	Phosphorylation	15071501
Phosphorylation on Ser-184 by MAPK8; promotes dissociation of BAX and translocation of BAX to mitochondria.
232	T	Phosphorylation	14613942
Phosphorylation on Thr-232; inhibits binding of RAF1.

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 1433Z_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MPIP1_HUMAN	CDC25A	physical	11912208
BCAR1_HUMAN	BCAR1	physical	10026197
KINH_HUMAN	KIF5B	physical	17353931
SMAG2_HUMAN	SAMD4B	physical	17353931
E41L3_HUMAN	EPB41L3	physical	17353931
UBP8_HUMAN	USP8	physical	17353931
DFFA_HUMAN	DFFA	physical	17353931
BRAF_HUMAN	BRAF	physical	17353931
KLC1_HUMAN	KLC1	physical	17353931
PAK4_HUMAN	PAK4	physical	17353931
ZO2_HUMAN	TJP2	physical	17353931
TRA2B_HUMAN	TRA2B	physical	17353931
NOLC1_HUMAN	NOLC1	physical	17353931
RAI14_HUMAN	RAI14	physical	17353931
RGPS2_HUMAN	RALGPS2	physical	17353931
EDC3_HUMAN	EDC3	physical	17353931
K0930_HUMAN	KIAA0930	physical	17353931
KLC4_HUMAN	KLC4	physical	17353931
NADK_HUMAN	NADK	physical	17353931
RL31_HUMAN	RPL31	physical	17353931
NCKP1_HUMAN	NCKAP1	physical	17353931
HNRPL_HUMAN	HNRNPL	physical	17353931
PABP4_HUMAN	PABPC4	physical	17353931
LARP1_HUMAN	LARP1	physical	17353931
SF3B1_HUMAN	SF3B1	physical	17353931
RAF1_HUMAN	RAF1	physical	9261098
KPCI_HUMAN	PRKCI	physical	12893243
KPCZ_HUMAN	PRKCZ	physical	12893243
KPCD1_HUMAN	PRKD1	physical	12893243
HDAC4_HUMAN	HDAC4	physical	11504882
REM1_HUMAN	REM1	physical	10441394
RAD_HUMAN	RRAD	physical	10441394
XRCC6_HUMAN	XRCC6	physical	16169070
CE126_HUMAN	KIAA1377	physical	16169070
TSC2_HUMAN	TSC2	physical	12176984
VIME_HUMAN	VIM	physical	10887173
1433Z_HUMAN	YWHAZ	physical	10887173
RAF1_HUMAN	RAF1	physical	10887173
SNAT_HUMAN	AANAT	physical	11336675
LIMK1_HUMAN	LIMK1	physical	12323073
FOXO3_HUMAN	FOXO3	physical	10102273
P53_HUMAN	TP53	physical	9620776
GP1BA_HUMAN	GP1BA	physical	8631758
IL9R_HUMAN	IL9R	physical	10642536
BAD_HUMAN	BAD	physical	11410287
I5P1_HUMAN	INPP5A	physical	9398266
RGS3_HUMAN	RGS3	physical	11985497
KPCE_HUMAN	PRKCE	physical	11950841
KPCA_HUMAN	PRKCA	physical	11950841
KPCD_HUMAN	PRKCD	physical	11950841
MPIP2_HUMAN	CDC25B	physical	10713667
TAU_HUMAN	MAPT	physical	10840038
GP1BB_HUMAN	GP1BB	physical	8034572
GP1BA_HUMAN	GP1BA	physical	10627461
GP1BB_HUMAN	GP1BB	physical	10627461
NFAC4_HUMAN	NFATC4	physical	10611249
RAF1_HUMAN	RAF1	physical	10611249
BAD_HUMAN	BAD	physical	20936779
E41L2_HUMAN	EPB41L2	physical	20936779
ZEP2_HUMAN	HIVEP2	physical	20936779
LCP2_HUMAN	LCP2	physical	20936779
LRMP_HUMAN	LRMP	physical	20936779
MYH9_HUMAN	MYH9	physical	20936779
SSFA2_HUMAN	SSFA2	physical	20936779
TNAP3_HUMAN	TNFAIP3	physical	20936779
TENS1_HUMAN	TNS1	physical	20936779
1433E_HUMAN	YWHAE	physical	20936779
1433Z_HUMAN	YWHAZ	physical	20936779
MADD_HUMAN	MADD	physical	20936779
EIF3A_HUMAN	EIF3A	physical	20936779
HDAC9_HUMAN	HDAC9	physical	20936779
RIPR2_HUMAN	FAM65B	physical	20936779
K0232_HUMAN	KIAA0232	physical	20936779
CAF1A_HUMAN	CHAF1A	physical	20936779
MPP9_HUMAN	MPHOSPH9	physical	20936779
CSN5_HUMAN	COPS5	physical	20936779
SYNPO_HUMAN	SYNPO	physical	20936779
RPGP2_HUMAN	RAP1GAP2	physical	20936779
NED4L_HUMAN	NEDD4L	physical	20936779
WWTR1_HUMAN	WWTR1	physical	20936779
FHOD1_HUMAN	FHOD1	physical	20936779
FA13B_HUMAN	FAM13B	physical	20936779
FA53C_HUMAN	FAM53C	physical	20936779
MSL2_HUMAN	MSL2	physical	20936779
RMD3_HUMAN	RMDN3	physical	20936779
ZN839_HUMAN	ZNF839	physical	20936779
CENPJ_HUMAN	CENPJ	physical	20936779
RASL3_HUMAN	RASAL3	physical	20936779
WNK1_HUMAN	WNK1	physical	20936779
WNK2_HUMAN	WNK2	physical	20936779
CGNL1_HUMAN	CGNL1	physical	20936779
SYNP2_HUMAN	SYNPO2	physical	20936779
SIMC1_HUMAN	SIMC1	physical	20936779
ING1_HUMAN	ING1	physical	16581770
SAMN1_HUMAN	SAMSN1	physical	20478393
EXO1_HUMAN	EXO1	physical	21533173
SIK3_HUMAN	SIK3	physical	16306228
SIK1_HUMAN	SIK1	physical	16306228
MARK3_HUMAN	MARK3	physical	16306228
BAD_HUMAN	BAD	physical	21076048
ATPA_HUMAN	ATP5A1	physical	15324660
BRAF_HUMAN	BRAF	physical	15324660
DFFA_HUMAN	DFFA	physical	15324660
ENOA_HUMAN	ENO1	physical	15324660
KINH_HUMAN	KIF5B	physical	15324660
TRA2B_HUMAN	TRA2B	physical	15324660
RO52_HUMAN	TRIM21	physical	15324660
UBC_HUMAN	UBC	physical	15324660
UBP8_HUMAN	USP8	physical	15324660
ZO2_HUMAN	TJP2	physical	15324660
PAK4_HUMAN	PAK4	physical	15324660
STK38_HUMAN	STK38	physical	15324660
TBA3C_HUMAN	TUBA3C	physical	15324660
E41L3_HUMAN	EPB41L3	physical	15324660
LARP1_HUMAN	LARP1	physical	15324660
SMAG2_HUMAN	SAMD4B	physical	15324660
RGPS2_HUMAN	RALGPS2	physical	15324660
KLC4_HUMAN	KLC4	physical	15324660
TBB5_HUMAN	TUBB	physical	15324660
PARD3_HUMAN	PARD3	physical	14676191
KPCI_HUMAN	PRKCI	physical	14676191
PAR6A_HUMAN	PARD6A	physical	14676191
MARK3_HUMAN	MARK3	physical	14676191
MARK2_HUMAN	MARK2	physical	14676191
DCAF7_HUMAN	DCAF7	physical	14676191
PNMA2_HUMAN	PNMA2	physical	14676191
KIF23_HUMAN	KIF23	physical	14676191
MARK1_HUMAN	MARK1	physical	14676191
CYFP1_HUMAN	CYFIP1	physical	14676191
PNMA1_HUMAN	PNMA1	physical	14676191
DOCK7_HUMAN	DOCK7	physical	14676191
TBG1_HUMAN	TUBG1	physical	14676191
CYFP2_HUMAN	CYFIP2	physical	14676191
RFWD2_HUMAN	RFWD2	physical	20843328
KAT8_HUMAN	KAT8	physical	19766566
1433E_HUMAN	YWHAE	physical	19766566
H31_HUMAN	HIST1H3A	physical	19766566
ELOA1_HUMAN	TCEB3	physical	19766566
BRD4_HUMAN	BRD4	physical	19766566
CDN1B_HUMAN	CDKN1B	physical	15057270
H31_HUMAN	HIST1H3A	physical	16246723
EXO1_HUMAN	EXO1	physical	22222486
RAF1_HUMAN	RAF1	physical	22222486
BAD_HUMAN	BAD	physical	11697890
RAF1_HUMAN	RAF1	physical	11697890
CBL_HUMAN	CBL	physical	11697890
CTNB1_HUMAN	CTNNB1	physical	22912335
PSA5_HUMAN	PSMA5	physical	9092538
MARK3_HUMAN	MARK3	physical	16968750
ZHX2_HUMAN	ZHX2	physical	16968750
SIK3_HUMAN	SIK3	physical	16968750
ERRFI_HUMAN	ERRFI1	physical	15778465
AJUBA_HUMAN	AJUBA	physical	15778465
RAF1_HUMAN	RAF1	physical	9632690
CBL_HUMAN	CBL	physical	9632690
MDM4_HUMAN	MDM4	physical	18356162
A4_HUMAN	APP	physical	21832049
KC1D_HUMAN	CSNK1D	physical	15003508
CTNB1_HUMAN	CTNNB1	physical	15492215
RAF1_HUMAN	RAF1	physical	15664191
ABL1_HUMAN	ABL1	physical	16888623
PHB_HUMAN	PHB	physical	19725029
ANM5_HUMAN	PRMT5	physical	23455924
RAF1_HUMAN	RAF1	physical	16093354
BAG3_HUMAN	BAG3	physical	23824909
M3K20_HUMAN	ZAK	physical	21988832
CD11B_HUMAN	CDK11B	physical	15883043
LRRK2_HUMAN	LRRK2	physical	20642453
MARK3_HUMAN	MARK3	physical	20642453
OLA1_HUMAN	OLA1	physical	22863883
MARE1_HUMAN	MAPRE1	physical	22863883
PAK2_HUMAN	PAK2	physical	22863883
PUR4_HUMAN	PFAS	physical	22863883
1433S_HUMAN	SFN	physical	22863883
RUXF_HUMAN	SNRPF	physical	22863883
VINC_HUMAN	VCL	physical	22863883
1433E_HUMAN	YWHAE	physical	22863883
1433G_HUMAN	YWHAG	physical	22863883
1433F_HUMAN	YWHAH	physical	22863883
1433T_HUMAN	YWHAQ	physical	22863883
ANCHR_HUMAN	ZFYVE19	physical	22863883
1433Z_HUMAN	YWHAZ	physical	20384366
DDIT4_HUMAN	DDIT4	physical	22001647
TSC2_HUMAN	TSC2	physical	22001647
TAU_HUMAN	MAPT	physical	19138662
DTL_HUMAN	DTL	physical	25154416
RIPR2_HUMAN	FAM65B	physical	24687993
TAU_HUMAN	MAPT	physical	19647741
1433Z_HUMAN	YWHAZ	physical	19647741
CTNB1_HUMAN	CTNNB1	physical	17287208
ROA1_HUMAN	HNRNPA1	physical	25324306
PGK1_HUMAN	PGK1	physical	26344197
1433B_HUMAN	YWHAB	physical	26344197
1433G_HUMAN	YWHAG	physical	26344197
YAP1_HUMAN	YAP1	physical	26578655
BRAF_HUMAN	BRAF	physical	26496610
CLK3_HUMAN	CLK3	physical	26496610
COPB_HUMAN	COPB1	physical	26496610
MARK3_HUMAN	MARK3	physical	26496610
PCNT_HUMAN	PCNT	physical	26496610
PRCC_HUMAN	PRCC	physical	26496610
PTPRA_HUMAN	PTPRA	physical	26496610
ASPP2_HUMAN	TP53BP2	physical	26496610
XPO1_HUMAN	XPO1	physical	26496610
1433B_HUMAN	YWHAB	physical	26496610
1433E_HUMAN	YWHAE	physical	26496610
1433G_HUMAN	YWHAG	physical	26496610
1433F_HUMAN	YWHAH	physical	26496610
SMC1A_HUMAN	SMC1A	physical	26496610
AP3B1_HUMAN	AP3B1	physical	26496610
PRP18_HUMAN	PRPF18	physical	26496610
IRS2_HUMAN	IRS2	physical	26496610
SNR40_HUMAN	SNRNP40	physical	26496610
CWC27_HUMAN	CWC27	physical	26496610
SRSF8_HUMAN	SRSF8	physical	26496610
1433T_HUMAN	YWHAQ	physical	26496610
DNJB4_HUMAN	DNAJB4	physical	26496610
B4GT7_HUMAN	B4GALT7	physical	26496610
RFIP2_HUMAN	RAB11FIP2	physical	26496610
UH1BL_HUMAN	UHRF1BP1L	physical	26496610
MYCB2_HUMAN	MYCBP2	physical	26496610
NBEL2_HUMAN	NBEAL2	physical	26496610
PHF3_HUMAN	PHF3	physical	26496610
NSL1_HUMAN	NSL1	physical	26496610
TIM13_HUMAN	TIMM13	physical	26496610
S61A1_HUMAN	SEC61A1	physical	26496610
CAB45_HUMAN	SDF4	physical	26496610
RBM27_HUMAN	RBM27	physical	26496610
BDP1_HUMAN	BDP1	physical	26496610
KLHL7_HUMAN	KLHL7	physical	26496610
RBM26_HUMAN	RBM26	physical	26496610
CSN7B_HUMAN	COPS7B	physical	26496610
PCGF5_HUMAN	PCGF5	physical	26496610
SPIR2_HUMAN	SPIRE2	physical	26496610
SPRY3_HUMAN	SPRYD3	physical	26496610
H6ST2_HUMAN	HS6ST2	physical	26496610
PR14L_HUMAN	PRR14L	physical	26496610
WDR62_HUMAN	WDR62	physical	26496610
CCD84_HUMAN	CCDC84	physical	26496610
LIPB1_HUMAN	PPFIBP1	physical	25770209
KIF11_HUMAN	KIF11	physical	25770209
TBCD4_HUMAN	TBC1D4	physical	25770209
BAD_HUMAN	BAD	physical	25770209
MAPK2_HUMAN	MAPKAPK2	physical	12861023
1433Z_HUMAN	YWHAZ	physical	12861023
RAF1_HUMAN	RAF1	physical	12861023
1433Z_HUMAN	YWHAZ	physical	22450747
CP131_HUMAN	CEP131	physical	26616734
PCM1_HUMAN	PCM1	physical	26616734
1433Z_HUMAN	YWHAZ	physical	16376338
1433E_HUMAN	YWHAE	physical	16376338
P53_HUMAN	TP53	physical	16376338

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 1433Z_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 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-3; LYS-49; LYS-68; LYS-115AND LYS-120, AND MASS SPECTROMETRY.	19608861 [Abstract]
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-207, AND MASSSPECTROMETRY.	19690332 [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 SER-210, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Protein kinase A phosphorylates and regulates dimerization of 14-3-3epsilon."; Gu Y.-M., Jin Y.-H., Choi J.-K., Baek K.-H., Yeo C.-Y., Lee K.-Y.; FEBS Lett. 580:305-310(2006). Cited for: PHOSPHORYLATION AT SER-58, DIMERIZATION, INTERACTION WITH TP53 ANDYWHAE, FUNCTION, AND MUTAGENESIS OF SER-58.	16376338 [Abstract]
"JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting ofc-Abl in the apoptotic response to DNA damage."; Yoshida K., Yamaguchi T., Natsume T., Kufe D., Miki Y.; Nat. Cell Biol. 7:278-285(2005). Cited for: INTERACTION WITH ABL1, MASS SPECTROMETRY, PHOSPHORYLATION AT SER-184,AND MUTAGENESIS OF SER-184.	15696159 [Abstract]
"Sphingosine activates protein kinase A type II by a novel cAMP-independent mechanism."; Ma Y., Pitson S., Hercus T., Murphy J., Lopez A., Woodcock J.; J. Biol. Chem. 280:26011-26017(2005). Cited for: PHOSPHORYLATION AT SER-58, AND MUTAGENESIS OF SER-58.	15883165 [Abstract]
"JNK promotes Bax translocation to mitochondria throughphosphorylation of 14-3-3 proteins."; Tsuruta F., Sunayama J., Mori Y., Hattori S., Shimizu S.,Tsujimoto Y., Yoshioka K., Masuyama N., Gotoh Y.; EMBO J. 23:1889-1899(2004). Cited for: PHOSPHORYLATION AT SER-184, INTERACTION WITH BAX, FUNCTION, ANDMUTAGENESIS OF SER-184.	15071501 [Abstract]
"The dimeric versus monomeric status of 14-3-3zeta is controlled byphosphorylation of Ser58 at the dimer interface."; Woodcock J.M., Murphy J., Stomski F.C., Berndt M.C., Lopez A.F.; J. Biol. Chem. 278:36323-36327(2003). Cited for: PHOSPHORYLATION AT SER-58, AND DIMERIZATION.	12865427 [Abstract]
"Identification of 14-3-3zeta as a protein kinase B/Akt substrate."; Powell D.W., Rane M.J., Chen Q., Singh S., McLeish K.R.; J. Biol. Chem. 277:21639-21642(2002). Cited for: PHOSPHORYLATION AT SER-58, AND INTERACTION WITH AKT1.	11956222 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-232, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-232, AND MASSSPECTROMETRY.	17081983 [Abstract]
"14-3-3 is phosphorylated by casein kinase I on residue 233.Phosphorylation at this site in vivo regulates Raf/14-3-3interaction."; Dubois T., Rommel C., Howell S., Steinhussen U., Soneji Y.,Morrice N., Moelling K., Aitken A.; J. Biol. Chem. 272:28882-28888(1997). Cited for: PHOSPHORYLATION AT THR-232, INTERACTION WITH RAF1, AND FUNCTION.	9360956 [Abstract]

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