dbPTM

1433F_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	1433F_HUMAN
UniProt AC	Q04917
Protein Name	14-3-3 protein eta
Gene Name	YWHAH
Organism	Homo sapiens (Human).
Sequence Length	246
Subcellular Localization
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. Negatively regulates the kinase activity of PDPK1..
Protein Sequence	MGDREQLLQRARLAEQAERYDDMASAMKAVTELNEPLSNEDRNLLSVAYKNVVGARRSSWRVISSIEQKTMADGNEKKLEKVKAYREKIEKELETVCNDVLSLLDKFLIKNCNDFQYESKVFYLKMKGDYYRYLAEVASGEKKNSVVEASEAAYKEAFEISKEQMQPTHPIRLGLALNFSVFYYEIQNAPEQACLLAKQAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDEEAGEGN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MGDREQLLQ ------CCHHHHHHH	42.56	-
20	Phosphorylation	LAEQAERYDDMASAM HHHHHHHHHHHHHHH	14.06	20068231
25	Phosphorylation	ERYDDMASAMKAVTE HHHHHHHHHHHHHHH	23.43	20068231
38	Phosphorylation	TELNEPLSNEDRNLL HHHCCCCCHHHCCHH	49.22	46155625
42	Methylation	EPLSNEDRNLLSVAY CCCCHHHCCHHHHHH	29.53	-
46	Phosphorylation	NEDRNLLSVAYKNVV HHHCCHHHHHHHHHH	14.10	19664994
49	Phosphorylation	RNLLSVAYKNVVGAR CCHHHHHHHHHHCCC	10.84	22617229
50	Acetylation	NLLSVAYKNVVGARR CHHHHHHHHHHCCCC	33.26	129327
50	Ubiquitination	NLLSVAYKNVVGARR CHHHHHHHHHHCCCC	33.26	21906983
50	Methylation	NLLSVAYKNVVGARR CHHHHHHHHHHCCCC	33.26	-
58	Phosphorylation	NVVGARRSSWRVISS HHHCCCCCCCHHHHH	28.79	23882029
59	Phosphorylation	VVGARRSSWRVISSI HHCCCCCCCHHHHHH	19.65	7785495
64	Phosphorylation	RSSWRVISSIEQKTM CCCCHHHHHHHHHHC	23.54	27273156
65	Phosphorylation	SSWRVISSIEQKTMA CCCHHHHHHHHHHCC	21.01	23911959
69	Malonylation	VISSIEQKTMADGNE HHHHHHHHHCCCCCH	27.72	26320211
69	Ubiquitination	VISSIEQKTMADGNE HHHHHHHHHCCCCCH	27.72	21890473
69	Acetylation	VISSIEQKTMADGNE HHHHHHHHHCCCCCH	27.72	23954790
69	Succinylation	VISSIEQKTMADGNE HHHHHHHHHCCCCCH	27.72	23954790
77	Ubiquitination	TMADGNEKKLEKVKA HCCCCCHHHHHHHHH	67.66	21906983
91	Ubiquitination	AYREKIEKELETVCN HHHHHHHHHHHHHHH	71.69	-
106	Ubiquitination	DVLSLLDKFLIKNCN HHHHHHHHHHHHCCC	41.88	-
110	Acetylation	LLDKFLIKNCNDFQY HHHHHHHHCCCCCCE	58.56	26051181
110	Ubiquitination	LLDKFLIKNCNDFQY HHHHHHHHCCCCCCE	58.56	21890473
117	Phosphorylation	KNCNDFQYESKVFYL HCCCCCCEEECEEEE	23.36	28152594
119	Phosphorylation	CNDFQYESKVFYLKM CCCCCEEECEEEEEE	29.23	28152594
120	Ubiquitination	NDFQYESKVFYLKMK CCCCEEECEEEEEEC	25.15	-
120	Acetylation	NDFQYESKVFYLKMK CCCCEEECEEEEEEC	25.15	26051181
123	Phosphorylation	QYESKVFYLKMKGDY CEEECEEEEEECCHH	14.38	7101457
125	Acetylation	ESKVFYLKMKGDYYR EECEEEEEECCHHHH	27.47	7298949
125	Ubiquitination	ESKVFYLKMKGDYYR EECEEEEEECCHHHH	27.47	21906983
127	Ubiquitination	KVFYLKMKGDYYRYL CEEEEEECCHHHHHH	47.22	21906983
130	Phosphorylation	YLKMKGDYYRYLAEV EEEECCHHHHHHHHH	9.86	28152594
131	Phosphorylation	LKMKGDYYRYLAEVA EEECCHHHHHHHHHH	9.49	28152594
133	Phosphorylation	MKGDYYRYLAEVASG ECCHHHHHHHHHHCC	8.31	28152594
139	Phosphorylation	RYLAEVASGEKKNSV HHHHHHHCCCCCCCH	53.30	110748691
142	Ubiquitination	AEVASGEKKNSVVEA HHHHCCCCCCCHHHH	61.86	21906983
142	Acetylation	AEVASGEKKNSVVEA HHHHCCCCCCCHHHH	61.86	25953088
143	Ubiquitination	EVASGEKKNSVVEAS HHHCCCCCCCHHHHH	50.59	-
145	Phosphorylation	ASGEKKNSVVEASEA HCCCCCCCHHHHHHH	36.10	20873877
154	Phosphorylation	VEASEAAYKEAFEIS HHHHHHHHHHHHHCC	19.19	110748699
155	Ubiquitination	EASEAAYKEAFEISK HHHHHHHHHHHHCCH	37.53	-
162	Ubiquitination	KEAFEISKEQMQPTH HHHHHCCHHHCCCCC	58.59	21890473
165	Sulfoxidation	FEISKEQMQPTHPIR HHCCHHHCCCCCCCC	5.59	30846556
168	Phosphorylation	SKEQMQPTHPIRLGL CHHHCCCCCCCCHHH	24.32	20068231
210	Phosphorylation	DAIAELDTLNEDSYK HHHHHHHCCCCCCCC	44.07	110747425
215	Phosphorylation	LDTLNEDSYKDSTLI HHCCCCCCCCCHHHH	28.09	20068231
216	Phosphorylation	DTLNEDSYKDSTLIM HCCCCCCCCCHHHHH	31.01	119397
219	Phosphorylation	NEDSYKDSTLIMQLL CCCCCCCHHHHHHHH	22.44	25850435
220	Phosphorylation	EDSYKDSTLIMQLLR CCCCCCHHHHHHHHH	30.36	19664994
223	Sulfoxidation	YKDSTLIMQLLRDNL CCCHHHHHHHHHHCC	2.30	30846556
234	Phosphorylation	RDNLTLWTSDQQDEE HHCCEEEECCHHCHH	26.07	24275569
235	Phosphorylation	DNLTLWTSDQQDEEA HCCEEEECCHHCHHC	23.11	27251275

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
59	S	Phosphorylation	Kinase	PDK3	Q15120	GPS
59	S	Phosphorylation	Kinase	PDKC	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
59	S	Phosphorylation		-
Phosphorylated on Ser-59 by protein kinase C delta type catalytic subunit in a sphingosine-dependent fashion.

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 1433F_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RIMS1_HUMAN	RIMS1	physical	12871946
RIMS2_HUMAN	RIMS2	physical	12871946
RP3A_HUMAN	RPH3A	physical	12871946
REM1_HUMAN	REM1	physical	10441394
TTP_HUMAN	ZFP36	physical	11886850
TLX2_HUMAN	TLX2	physical	9738002
KLC3_HUMAN	KLC3	physical	11969417
ARAF_HUMAN	ARAF	physical	11969417
RUXE_HUMAN	SNRPE	physical	11969417
RAF1_HUMAN	RAF1	physical	11969417
IRS1_HUMAN	IRS1	physical	11969417
PK3CA_HUMAN	PIK3CA	physical	11969417
MPIP3_HUMAN	CDC25C	physical	11969417
KINH_HUMAN	KIF5B	physical	11969417
PDPK1_HUMAN	PDPK1	physical	12177059
MPIP2_HUMAN	CDC25B	physical	10713667
E41L3_HUMAN	EPB41L3	physical	11996670
MDM4_HUMAN	MDM4	physical	16511560
ING1_HUMAN	ING1	physical	16581770
SAMN1_HUMAN	SAMSN1	physical	20478393
MARK4_HUMAN	MARK4	physical	14676191
KPCI_HUMAN	PRKCI	physical	14676191
DCAF7_HUMAN	DCAF7	physical	14676191
MARK2_HUMAN	MARK2	physical	14676191
MARK3_HUMAN	MARK3	physical	14676191
ARHG2_HUMAN	ARHGEF2	physical	14676191
RASF8_HUMAN	RASSF8	physical	14676191
DOCK7_HUMAN	DOCK7	physical	14676191
KIF23_HUMAN	KIF23	physical	14676191
PAR6B_HUMAN	PARD6B	physical	14676191
PARD3_HUMAN	PARD3	physical	14676191
CYFP1_HUMAN	CYFIP1	physical	14676191
PAR6G_HUMAN	PARD6G	physical	14676191
PAR6A_HUMAN	PARD6A	physical	14676191
MARK1_HUMAN	MARK1	physical	14676191
CYFP2_HUMAN	CYFIP2	physical	14676191
TBG1_HUMAN	TUBG1	physical	14676191
GRDN_HUMAN	CCDC88A	physical	14676191
EXO1_HUMAN	EXO1	physical	22222486
BAD_HUMAN	BAD	physical	11697890
RAF1_HUMAN	RAF1	physical	11697890
CBL_HUMAN	CBL	physical	11697890
PRKN_HUMAN	PARK2	physical	16096643
SNCAP_HUMAN	SNCAIP	physical	16096643
MEX3B_HUMAN	MEX3B	physical	18779327
MEX3D_HUMAN	MEX3D	physical	18779327
MEX3C_HUMAN	MEX3C	physical	18779327
1433F_HUMAN	YWHAH	physical	18779327
ABL1_HUMAN	ABL1	physical	16888623
RAF1_HUMAN	RAF1	physical	16093354
LRRK2_HUMAN	LRRK2	physical	20642453
MARK3_HUMAN	MARK3	physical	20642453
HNRPK_HUMAN	HNRNPK	physical	22863883
LIS1_HUMAN	PAFAH1B1	physical	22863883
PAK2_HUMAN	PAK2	physical	22863883
PP1A_HUMAN	PPP1CA	physical	22863883
UBFD1_HUMAN	UBFD1	physical	22863883
DTL_HUMAN	DTL	physical	25154416
1433B_HUMAN	YWHAB	physical	26344197
1433G_HUMAN	YWHAG	physical	26344197
1433Z_HUMAN	YWHAZ	physical	26344197
ABCA2_HUMAN	ABCA2	physical	26496610
ARAF_HUMAN	ARAF	physical	26496610
CLK3_HUMAN	CLK3	physical	26496610
NHS_HUMAN	NHS	physical	26496610
LGMN_HUMAN	LGMN	physical	26496610
RAF1_HUMAN	RAF1	physical	26496610
ASPP2_HUMAN	TP53BP2	physical	26496610
1433B_HUMAN	YWHAB	physical	26496610
1433E_HUMAN	YWHAE	physical	26496610
1433G_HUMAN	YWHAG	physical	26496610
1433Z_HUMAN	YWHAZ	physical	26496610
RAE1L_HUMAN	RAE1	physical	26496610
IRS2_HUMAN	IRS2	physical	26496610
HOME3_HUMAN	HOMER3	physical	26496610
FXR2_HUMAN	FXR2	physical	26496610
CAPON_HUMAN	NOS1AP	physical	26496610
HDAC4_HUMAN	HDAC4	physical	26496610
RUSC2_HUMAN	RUSC2	physical	26496610
DCR1A_HUMAN	DCLRE1A	physical	26496610
SRSF8_HUMAN	SRSF8	physical	26496610
1433T_HUMAN	YWHAQ	physical	26496610
RASF8_HUMAN	RASSF8	physical	26496610
MYCB2_HUMAN	MYCBP2	physical	26496610
KIF1B_HUMAN	KIF1B	physical	26496610
SRRM2_HUMAN	SRRM2	physical	26496610
TFB1M_HUMAN	TFB1M	physical	26496610
HDAC7_HUMAN	HDAC7	physical	26496610
PTOV1_HUMAN	PTOV1	physical	26496610
PARD3_HUMAN	PARD3	physical	26496610
PEO1_HUMAN	C10orf2	physical	26496610
ZC3HE_HUMAN	ZC3H14	physical	26496610
ERMP1_HUMAN	ERMP1	physical	26496610
F192A_HUMAN	FAM192A	physical	26496610
REEP4_HUMAN	REEP4	physical	26496610
EPIPL_HUMAN	EPPK1	physical	26496610
SPRY3_HUMAN	SPRYD3	physical	26496610
OSBL5_HUMAN	OSBPL5	physical	26496610
FBSP1_HUMAN	FBXO45	physical	26496610
OARD1_HUMAN	OARD1	physical	26496610
EMAL3_HUMAN	EML3	physical	26496610
WDR62_HUMAN	WDR62	physical	26496610
FRYL_HUMAN	FRYL	physical	26496610
NSUN4_HUMAN	NSUN4	physical	26496610
FA83G_HUMAN	FAM83G	physical	26496610
NF1_HUMAN	NF1	physical	14741381

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 1433F_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-25, AND MASSSPECTROMETRY.	19690332 [Abstract]

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