dbPTM

1433B_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	1433B_MOUSE
UniProt AC	Q9CQV8
Protein Name	14-3-3 protein beta/alpha
Gene Name	Ywhab
Organism	Mus musculus (Mouse).
Sequence Length	246
Subcellular Localization	Cytoplasm . Melanosome .
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. Negative regulator of osteogenesis. Blocks the nuclear translocation of the phosphorylated form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on cyclin D1 expression resulting in blockage of neuronal apoptosis elicited by SRPK2. Negative regulator of signaling cascades that mediate activation of MAP kinases via AKAP13..
Protein Sequence	MTMDKSELVQKAKLAEQAERYDDMAAAMKAVTEQGHELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTERNEKKQQMGKEYREKIEAELQDICNDVLELLDKYLILNATQAESKVFYLKMKGDYFRYLSEVASGENKQTTVSNSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLNEESYKDSTLIMQLLRDNLTLWTSENQGDEGDAGEGEN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MTMDKSEL -------CCCCHHHH	6.72	-
1 (in isoform 2)	Acetylation	-	6.72	-
2	Acetylation	------MTMDKSELV ------CCCCHHHHH	33.79	-
2	Phosphorylation	------MTMDKSELV ------CCCCHHHHH	33.79	25266776
5	Acetylation	---MTMDKSELVQKA ---CCCCHHHHHHHH	34.70	22826441
6	Phosphorylation	--MTMDKSELVQKAK --CCCCHHHHHHHHH	31.72	20415495
9 (in isoform 2)	Ubiquitination	-	4.88	-
11	Ubiquitination	DKSELVQKAKLAEQA CHHHHHHHHHHHHHH	39.75	22790023
11 (in isoform 2)	Ubiquitination	-	39.75	22790023
13 (in isoform 2)	Ubiquitination	-	56.09	22790023
13	Acetylation	SELVQKAKLAEQAER HHHHHHHHHHHHHHH	56.09	23806337
13	Ubiquitination	SELVQKAKLAEQAER HHHHHHHHHHHHHHH	56.09	22790023
21	Phosphorylation	LAEQAERYDDMAAAM HHHHHHHHHHHHHHH	14.06	26239621
29	Ubiquitination	DDMAAAMKAVTEQGH HHHHHHHHHHHHHCH	34.67	-
47	Phosphorylation	NEERNLLSVAYKNVV HHHHHHHHHHHHHHH	14.10	26824392
50	Phosphorylation	RNLLSVAYKNVVGAR HHHHHHHHHHHHCCC	10.84	24865951
51	Ubiquitination	NLLSVAYKNVVGARR HHHHHHHHHHHCCCH	33.26	-
51	Acetylation	NLLSVAYKNVVGARR HHHHHHHHHHHCCCH	33.26	130487
59	Phosphorylation	NVVGARRSSWRVISS HHHCCCHHHHHHHHH	28.79	23375375
60	Phosphorylation	VVGARRSSWRVISSI HHCCCHHHHHHHHHH	19.65	7785491
65	Phosphorylation	RSSWRVISSIEQKTE HHHHHHHHHHHHHHH	23.54	20415495
66	Phosphorylation	SSWRVISSIEQKTER HHHHHHHHHHHHHHH	21.01	25521595
70	Acetylation	VISSIEQKTERNEKK HHHHHHHHHHHHHHH	39.29	22826441
70	Malonylation	VISSIEQKTERNEKK HHHHHHHHHHHHHHH	39.29	26320211
70	Ubiquitination	VISSIEQKTERNEKK HHHHHHHHHHHHHHH	39.29	-
84	Nitration	KQQMGKEYREKIEAE HHHHHHHHHHHHHHH	27.79	16800626
84	Nitration	KQQMGKEYREKIEAE HHHHHHHHHHHHHHH	27.79	16800626
84	Nitrated tyrosine	KQQMGKEYREKIEAE HHHHHHHHHHHHHHH	27.79	-
106	Nitration	VLELLDKYLILNATQ HHHHHHHHHHHCCCC	9.91	16800626
106	Nitration	VLELLDKYLILNATQ HHHHHHHHHHHCCCC	9.91	16800626
106	Nitrated tyrosine	VLELLDKYLILNATQ HHHHHHHHHHHCCCC	9.91	-
106	Phosphorylation	VLELLDKYLILNATQ HHHHHHHHHHHCCCC	9.91	25777480
112	Phosphorylation	KYLILNATQAESKVF HHHHHCCCCCCCCEE	27.52	25777480
116	Phosphorylation	LNATQAESKVFYLKM HCCCCCCCCEEEEEE	36.82	22817900
117	Acetylation	NATQAESKVFYLKMK CCCCCCCCEEEEEEC	28.06	-
120	Phosphorylation	QAESKVFYLKMKGDY CCCCCEEEEEECCHH	14.38	25777480
122	Acetylation	ESKVFYLKMKGDYFR CCCEEEEEECCHHHH	27.47	7298885
122	Ubiquitination	ESKVFYLKMKGDYFR CCCEEEEEECCHHHH	27.47	-
124	Ubiquitination	KVFYLKMKGDYFRYL CEEEEEECCHHHHHH	47.22	-
130	Phosphorylation	MKGDYFRYLSEVASG ECCHHHHHHHHHHCC	12.51	7178859
136	Phosphorylation	RYLSEVASGENKQTT HHHHHHHCCCCCCCC	52.38	25521595
140	Ubiquitination	EVASGENKQTTVSNS HHHCCCCCCCCCCCH	44.73	-
159	Acetylation	QEAFEISKKEMQPTH HHHHHHHHHHCCCCC	59.42	-
159	Ubiquitination	QEAFEISKKEMQPTH HHHHHHHHHHCCCCC	59.42	-
160	Ubiquitination	EAFEISKKEMQPTHP HHHHHHHHHCCCCCC	52.18	-
181	Phosphorylation	LNFSVFYYEILNSPE EEHHHHHHHHHCCHH	5.75	14630809
186	Phosphorylation	FYYEILNSPEKACSL HHHHHHCCHHHHHHH	30.87	21082442
191	Glutathionylation	LNSPEKACSLAKTAF HCCHHHHHHHHHHHH	5.19	24333276
192	Phosphorylation	NSPEKACSLAKTAFD CCHHHHHHHHHHHHH	35.90	29899451
195	Ubiquitination	EKACSLAKTAFDEAI HHHHHHHHHHHHHHH	45.75	-
196	Phosphorylation	KACSLAKTAFDEAIA HHHHHHHHHHHHHHH	27.27	21183079
212	Phosphorylation	LDTLNEESYKDSTLI HHCCCHHHCCCHHHH	31.16	25195567
213	Nitration	DTLNEESYKDSTLIM HCCCHHHCCCHHHHH	23.30	-
216	Phosphorylation	NEESYKDSTLIMQLL CHHHCCCHHHHHHHH	22.44	28066266
217	Phosphorylation	EESYKDSTLIMQLLR HHHCCCHHHHHHHHH	30.36	28066266
231	Phosphorylation	RDNLTLWTSENQGDE HHCCEEEECCCCCCC	29.31	29899451
232	Phosphorylation	DNLTLWTSENQGDEG HCCEEEECCCCCCCC	23.98	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
60	S	Phosphorylation	Kinase	PRKCD	P09215	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
60	S	Phosphorylation		9705322
Phosphorylated on Ser-60 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 1433B_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RIN1_MOUSE	Rin1	physical	9144171
1433E_MOUSE	Ywhae	physical	18687683
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 1433B_MOUSE

Related Literatures of Post-Translational Modification

Nitration
Reference	PubMed
"Endogenously nitrated proteins in mouse brain: links toneurodegenerative disease."; Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,Squier T.C., Bigelow D.J.; Biochemistry 45:8009-8022(2006). Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-84 AND TYR-106, AND MASSSPECTROMETRY.	16800626 [Abstract]

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