dbPTM

1433G_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	1433G_MOUSE
UniProt AC	P61982
Protein Name	14-3-3 protein gamma
Gene Name	Ywhag
Organism	Mus musculus (Mouse).
Sequence Length	247
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..
Protein Sequence	MVDREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTSADGNEKKIEMVRAYREKIEKELEAVCQDVLSLLDNYLIKNCSETQYESKVFYLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQPTHPIRLGLALNYSVFYYEIQNAPEQACHLAKTAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDDDGGEGNN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MVDREQLV -------CCCHHHHH	6.80	-
2	Acetylation	------MVDREQLVQ ------CCCHHHHHH	10.78	-
10	Malonylation	DREQLVQKARLAEQA CHHHHHHHHHHHHHH	28.17	26320211
10	Ubiquitination	DREQLVQKARLAEQA CHHHHHHHHHHHHHH	28.17	-
10	Acetylation	DREQLVQKARLAEQA CHHHHHHHHHHHHHH	28.17	23236377
20	Phosphorylation	LAEQAERYDDMAAAM HHHHHHHHHHHHHHH	14.06	26239621
28	Ubiquitination	DDMAAAMKNVTELNE HHHHHHHHCHHHHCC	43.47	-
38	Phosphorylation	TELNEPLSNEERNLL HHHCCCCCHHHHHHH	53.57	55443149
46	Phosphorylation	NEERNLLSVAYKNVV HHHHHHHHHHHHHHH	14.10	26824392
49	Phosphorylation	RNLLSVAYKNVVGAR HHHHHHHHHHHHCCC	10.84	24865951
50	Acetylation	NLLSVAYKNVVGARR HHHHHHHHHHHCCCC	33.26	23806337
50	Ubiquitination	NLLSVAYKNVVGARR HHHHHHHHHHHCCCC	33.26	-
58	Phosphorylation	NVVGARRSSWRVISS HHHCCCCCCCEEECC	28.79	23375375
59	Phosphorylation	VVGARRSSWRVISSI HHCCCCCCCEEECCC	19.65	7785491
64	Phosphorylation	RSSWRVISSIEQKTS CCCCEEECCCCHHCC	23.54	25619855
65	Phosphorylation	SSWRVISSIEQKTSA CCCEEECCCCHHCCC	21.01	25521595
69	Malonylation	VISSIEQKTSADGNE EECCCCHHCCCCCCH	31.49	26320211
69	Acetylation	VISSIEQKTSADGNE EECCCCHHCCCCCCH	31.49	23954790
69	Ubiquitination	VISSIEQKTSADGNE EECCCCHHCCCCCCH	31.49	-
70	Phosphorylation	ISSIEQKTSADGNEK ECCCCHHCCCCCCHH	28.92	26824392
71	Phosphorylation	SSIEQKTSADGNEKK CCCCHHCCCCCCHHH	31.25	25521595
77	Ubiquitination	TSADGNEKKIEMVRA CCCCCCHHHHHHHHH	64.15	-
78	Acetylation	SADGNEKKIEMVRAY CCCCCHHHHHHHHHH	37.41	30985401
88	Acetylation	MVRAYREKIEKELEA HHHHHHHHHHHHHHH	47.36	6569269
91	Acetylation	AYREKIEKELEAVCQ HHHHHHHHHHHHHHH	71.69	6568591
97	Glutathionylation	EKELEAVCQDVLSLL HHHHHHHHHHHHHHH	3.54	24333276
102	Phosphorylation	AVCQDVLSLLDNYLI HHHHHHHHHHHHHHH	27.08	22210690
112	S-nitrosylation	DNYLIKNCSETQYES HHHHHHCCCCCCCCC	3.10	21278135
112	S-nitrosocysteine	DNYLIKNCSETQYES HHHHHHCCCCCCCCC	3.10	-
113	Phosphorylation	NYLIKNCSETQYESK HHHHHCCCCCCCCCE	53.74	22817900
115	Phosphorylation	LIKNCSETQYESKVF HHHCCCCCCCCCEEE	21.84	28464351
117	Phosphorylation	KNCSETQYESKVFYL HCCCCCCCCCEEEEE	29.59	22817900
119	Phosphorylation	CSETQYESKVFYLKM CCCCCCCCEEEEEEE	29.23	18837663
120	Ubiquitination	SETQYESKVFYLKMK CCCCCCCEEEEEEEC	25.15	-
120	Acetylation	SETQYESKVFYLKMK CCCCCCCEEEEEEEC	25.15	22826441
125	Acetylation	ESKVFYLKMKGDYYR CCEEEEEEECCHHHH	27.47	7298931
125	Ubiquitination	ESKVFYLKMKGDYYR CCEEEEEEECCHHHH	27.47	-
127	Ubiquitination	KVFYLKMKGDYYRYL EEEEEEECCHHHHHH	47.22	-
130	Phosphorylation	YLKMKGDYYRYLAEV EEEECCHHHHHHHHH	9.86	29899451
131	Phosphorylation	LKMKGDYYRYLAEVA EEECCHHHHHHHHHH	9.49	29899451
133	Phosphorylation	MKGDYYRYLAEVATG ECCHHHHHHHHHHCC	8.31	31437461
139	Phosphorylation	RYLAEVATGEKRATV HHHHHHHCCCCEEEE	51.56	20469934
142	Ubiquitination	AEVATGEKRATVVES HHHHCCCCEEEEEEC	48.99	-
142	Acetylation	AEVATGEKRATVVES HHHHCCCCEEEEEEC	48.99	7669919
145	Phosphorylation	ATGEKRATVVESSEK HCCCCEEEEEECCHH	29.17	20469934
149	Phosphorylation	KRATVVESSEKAYSE CEEEEEECCHHHHHH	31.99	20469934
150	Phosphorylation	RATVVESSEKAYSEA EEEEEECCHHHHHHH	29.61	20469934
152	Ubiquitination	TVVESSEKAYSEAHE EEEECCHHHHHHHHH	55.35	-
155	Phosphorylation	ESSEKAYSEAHEISK ECCHHHHHHHHHHCH	32.92	28464351
162	Ubiquitination	SEAHEISKEHMQPTH HHHHHHCHHHCCCCC	58.25	-
162	Acetylation	SEAHEISKEHMQPTH HHHHHHCHHHCCCCC	58.25	23341599
194	S-nitrosylation	QNAPEQACHLAKTAF CCCHHHHHHHHHHHH	2.43	21278135
194	S-palmitoylation	QNAPEQACHLAKTAF CCCHHHHHHHHHHHH	2.43	28680068
194	Glutathionylation	QNAPEQACHLAKTAF CCCHHHHHHHHHHHH	2.43	24333276
194	S-nitrosocysteine	QNAPEQACHLAKTAF CCCHHHHHHHHHHHH	2.43	-
199	Phosphorylation	QACHLAKTAFDDAIA HHHHHHHHHHHHHHH	27.27	23984901
215	Phosphorylation	LDTLNEDSYKDSTLI HHCCCCCCCCCHHHH	28.09	25195567
216	Phosphorylation	DTLNEDSYKDSTLIM HCCCCCCCCCHHHHH	31.01	25619855
219	Phosphorylation	NEDSYKDSTLIMQLL CCCCCCCHHHHHHHH	22.44	28066266
220	Phosphorylation	EDSYKDSTLIMQLLR CCCCCCHHHHHHHHH	30.36	28066266
231	Phosphorylation	QLLRDNLTLWTSDQQ HHHHCCCEEEECCCC	26.89	23737553
234	Phosphorylation	RDNLTLWTSDQQDDD HCCCEEEECCCCCCC	26.07	23737553
235	Phosphorylation	DNLTLWTSDQQDDDG CCCEEEECCCCCCCC	23.11	25521595

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
235	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS

Functions of PTM Sites

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

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 1433G_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LRRK2_MOUSE	Lrrk2	physical	21390248
MARK3_MOUSE	Mark3	physical	16959763
MARK2_MOUSE	Mark2	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 1433G_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]