dbPTM

1433F_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	1433F_MOUSE
UniProt AC	P68510
Protein Name	14-3-3 protein eta
Gene Name	Ywhah
Organism	Mus musculus (Mouse).
Sequence Length	246
Subcellular Localization	Cytoplasm.
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 (By similarity)..
Protein Sequence	MGDREQLLQRARLAEQAERYDDMASAMKAVTELNEPLSNEDRNLLSVAYKNVVGARRSSWRVISSIEQKTMADGNEKKLEKVKAYREKIEKELETVCNDVLALLDKFLIKNCNDFQYESKVFYLKMKGDYYRYLAEVASGEKKNSVVEASEAAYKEAFEISKEHMQPTHPIRLGLALNFSVFYYEIQNAPEQACLLAKQAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDEEAGEGN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MGDREQLLQ ------CCHHHHHHH	42.56	-
25	Phosphorylation	ERYDDMASAMKAVTE HHHHHHHHHHHHHHH	23.43	25338131
38	Phosphorylation	TELNEPLSNEDRNLL HHHCCCCCHHHCCHH	49.22	46155627
46	Phosphorylation	NEDRNLLSVAYKNVV HHHCCHHHHHHHHHH	14.10	26824392
49	Phosphorylation	RNLLSVAYKNVVGAR CCHHHHHHHHHHCCC	10.84	24865983
50	Acetylation	NLLSVAYKNVVGARR CHHHHHHHHHHCCCC	33.26	129329
50	Ubiquitination	NLLSVAYKNVVGARR CHHHHHHHHHHCCCC	33.26	22790023
58	Phosphorylation	NVVGARRSSWRVISS HHHCCCCCCCHHHHH	28.79	23375375
59	Phosphorylation	VVGARRSSWRVISSI HHCCCCCCCHHHHHH	19.65	7785491
64	Phosphorylation	RSSWRVISSIEQKTM CCCCHHHHHHHHHHC	23.54	20415495
65	Phosphorylation	SSWRVISSIEQKTMA CCCHHHHHHHHHHCC	21.01	25521595
69	Acetylation	VISSIEQKTMADGNE HHHHHHHHHCCCCCH	27.72	23236377
69	Ubiquitination	VISSIEQKTMADGNE HHHHHHHHHCCCCCH	27.72	22790023
77	Ubiquitination	TMADGNEKKLEKVKA HCCCCCHHHHHHHHH	67.66	22790023
77	Acetylation	TMADGNEKKLEKVKA HCCCCCHHHHHHHHH	67.66	19859541
97	Glutathionylation	EKELETVCNDVLALL HHHHHHHHHHHHHHH	4.74	24333276
110	Ubiquitination	LLDKFLIKNCNDFQY HHHHHHHHCCCCCCE	58.56	22790023
110	Acetylation	LLDKFLIKNCNDFQY HHHHHHHHCCCCCCE	58.56	22826441
112	S-nitrosocysteine	DKFLIKNCNDFQYES HHHHHHCCCCCCEEE	4.37	-
112	S-nitrosylation	DKFLIKNCNDFQYES HHHHHHCCCCCCEEE	4.37	19101475
117	Phosphorylation	KNCNDFQYESKVFYL HCCCCCCEEECEEEE	23.36	22817900
120	Ubiquitination	NDFQYESKVFYLKMK CCCCEEECEEEEEEC	25.15	22790023
120	Acetylation	NDFQYESKVFYLKMK CCCCEEECEEEEEEC	25.15	23236377
125	Ubiquitination	ESKVFYLKMKGDYYR EECEEEEEECCHHHH	27.47	22790023
125	Acetylation	ESKVFYLKMKGDYYR EECEEEEEECCHHHH	27.47	7298953
127	Ubiquitination	KVFYLKMKGDYYRYL CEEEEEECCHHHHHH	47.22	27667366
131	Phosphorylation	LKMKGDYYRYLAEVA EEECCHHHHHHHHHH	9.49	2021627
133	Phosphorylation	MKGDYYRYLAEVASG ECCHHHHHHHHHHCC	8.31	28464351
142	Ubiquitination	AEVASGEKKNSVVEA HHHHCCCCCCCHHHH	61.86	22790023
143	Ubiquitination	EVASGEKKNSVVEAS HHHCCCCCCCHHHHH	50.59	22790023
145	Phosphorylation	ASGEKKNSVVEASEA HCCCCCCCHHHHHHH	36.10	29899451
215	Phosphorylation	LDTLNEDSYKDSTLI HHCCCCCCCCCHHHH	28.09	25195567
219	Phosphorylation	NEDSYKDSTLIMQLL CCCCCCCHHHHHHHH	22.44	28066266
220	Phosphorylation	EDSYKDSTLIMQLLR CCCCCCHHHHHHHHH	30.36	28066266
235	Phosphorylation	DNLTLWTSDQQDEEA HCCEEEECCHHCHHC	23.11	19854140

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	PRKACA	P00517	GPS
59	S	Phosphorylation	Kinase	PRKCD	P09215	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
59	S	Phosphorylation		9705322
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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LRRK2_MOUSE	Lrrk2	physical	21390248
MARK2_MOUSE	Mark2	physical	16959763
MARK3_MOUSE	Mark3	physical	16959763
MARK4_MOUSE	Mark4	physical	16959763
TAU_MOUSE	Mapt	physical	19014373

Drug and Disease Associations

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

Regulatory Network of 1433F_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-117, AND MASSSPECTROMETRY.	18034455 [Abstract]

show