dbPTM

SNAI1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SNAI1_HUMAN
UniProt AC	O95863
Protein Name	Zinc finger protein SNAI1
Gene Name	SNAI1
Organism	Homo sapiens (Human).
Sequence Length	264
Subcellular Localization	Nucleus . Cytoplasm. Once phosphorylated (probably on Ser-107, Ser-111, Ser-115 and Ser-119) it is exported from the nucleus to the cytoplasm where subsequent phosphorylation of the destruction motif and ubiquitination involving BTRC occurs.
Protein Description	Involved in induction of the epithelial to mesenchymal transition (EMT), formation and maintenance of embryonic mesoderm, growth arrest, survival and cell migration. Binds to 3 E-boxes of the E-cadherin/CDH1 gene promoter and to the promoters of CLDN7 and KRT8 and, in association with histone demethylase KDM1A which it recruits to the promoters, causes a decrease in dimethylated H3K4 levels and represses transcription. During EMT, involved with LOXL2 in negatively regulating pericentromeric heterochromatin transcription (By similarity). SNAI1 recruits LOXL2 to pericentromeric regions to oxidize histone H3 and repress transcription which leads to release of heterochromatin component CBX5/HP1A, enabling chromatin reorganization and acquisition of mesenchymal traits (By similarity). Associates with EGR1 and SP1 to mediate tetradecanoyl phorbol acetate (TPA)-induced up-regulation of CDKN2B, possibly by binding to the CDKN2B promoter region 5'-TCACA-3. In addition, may also activate the CDKN2B promoter by itself..
Protein Sequence	MPRSFLVRKPSDPNRKPNYSELQDSNPEFTFQQPYDQAHLLAAIPPPEILNPTASLPMLIWDSVLAPQAQPIAWASLRLQESPRVAELTSLSDEDSGKGSQPPSPPSPAPSSFSSTSVSSLEAEAYAAFPGLGQVPKQLAQLSEAKDLQARKAFNCKYCNKEYLSLGALKMHIRSHTLPCVCGTCGKAFSRPWLLQGHVRTHTGEKPFSCPHCSRAFADRSNLRAHLQTHSDVKKYQCQACARTFSRMSLLHKHQESGCSGCPR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Phosphorylation	SFLVRKPSDPNRKPN CCCCCCCCCCCCCCC	69.59	22276203
82	Phosphorylation	ASLRLQESPRVAELT HHHHCCCCCCEEEHH	12.68	22817900
89	Phosphorylation	SPRVAELTSLSDEDS CCCEEEHHCCCCCCC	21.08	22199227
90	Phosphorylation	PRVAELTSLSDEDSG CCEEEHHCCCCCCCC	38.20	29255136
92	Phosphorylation	VAELTSLSDEDSGKG EEEHHCCCCCCCCCC	38.43	29255136
96	Phosphorylation	TSLSDEDSGKGSQPP HCCCCCCCCCCCCCC	40.12	15647282
98	Ubiquitination	LSDEDSGKGSQPPSP CCCCCCCCCCCCCCC	60.38	19955572
100	Phosphorylation	DEDSGKGSQPPSPPS CCCCCCCCCCCCCCC	42.89	20305697
104	Phosphorylation	GKGSQPPSPPSPAPS CCCCCCCCCCCCCCC	57.01	15647282
107	Phosphorylation	SQPPSPPSPAPSSFS CCCCCCCCCCCCCCC	36.76	15647282
111	Phosphorylation	SPPSPAPSSFSSTSV CCCCCCCCCCCCCCH	46.23	22817900
112	O-linked_Glycosylation	PPSPAPSSFSSTSVS CCCCCCCCCCCCCHH	28.26	20959806
112	Phosphorylation	PPSPAPSSFSSTSVS CCCCCCCCCCCCCHH	28.26	-
115	Phosphorylation	PAPSSFSSTSVSSLE CCCCCCCCCCHHHHH	23.77	22817900
119	Phosphorylation	SFSSTSVSSLEAEAY CCCCCCHHHHHHHHH	29.04	22817900
137	Ubiquitination	PGLGQVPKQLAQLSE CCCCHHHHHHHHHHH	60.12	19955572
146	Ubiquitination	LAQLSEAKDLQARKA HHHHHHHHHHHHHHH	55.72	19955572
165	Phosphorylation	YCNKEYLSLGALKMH CCCHHHCCCCHHHHH	24.69	28555341
175	Phosphorylation	ALKMHIRSHTLPCVC HHHHHHHHCCCCEEC	21.88	21712546
177	Phosphorylation	KMHIRSHTLPCVCGT HHHHHHCCCCEECCC	33.37	21712546
187	Acetylation	CVCGTCGKAFSRPWL EECCCCCCHHCCCCH	48.70	126719599
201	Phosphorylation	LLQGHVRTHTGEKPF HHCCEEEECCCCCCC	23.77	-
203	Phosphorylation	QGHVRTHTGEKPFSC CCEEEECCCCCCCCC	46.56	29214152
206	Ubiquitination	VRTHTGEKPFSCPHC EEECCCCCCCCCCCH	53.35	-
229	Phosphorylation	NLRAHLQTHSDVKKY HHHHHHHHHHHHHHH	29.70	29449344
231	Phosphorylation	RAHLQTHSDVKKYQC HHHHHHHHHHHHHHH	47.70	29449344
234	Ubiquitination	LQTHSDVKKYQCQAC HHHHHHHHHHHHHHH	51.24	-
235	Ubiquitination	QTHSDVKKYQCQACA HHHHHHHHHHHHHHH	40.16	-
246	Phosphorylation	QACARTFSRMSLLHK HHHHHHHHHHHHHHH	26.85	15647282
249	Phosphorylation	ARTFSRMSLLHKHQE HHHHHHHHHHHHHHH	27.03	-

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
11	S	Phosphorylation	Kinase	PKA	-	Uniprot
11	S	Phosphorylation	Kinase	PRKD1	Q15139	PSP
11	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
82	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
92	S	Phosphorylation	Kinase	CK2	-	Uniprot
92	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
92	S	Phosphorylation	Kinase	CK2B	P67870	PSP
96	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
100	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
104	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
104	S	Phosphorylation	Kinase	CSNK1E	P49674	GPS
104	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
104	S	Phosphorylation	Kinase	DYRK2	Q92630	PSP
107	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
107	S	Phosphorylation	Kinase	CSNK1E	P49674	GPS
107	S	Phosphorylation	Kinase	P38A	Q16539	PSP
111	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
115	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
119	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
203	T	Phosphorylation	Kinase	LATS2	Q9NRM7	Uniprot
246	S	Phosphorylation	Kinase	PAK1	Q13153	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	FBXL5	Q9UKA1	PMID:24157836
-	K	Ubiquitination	E3 ubiquitin ligase	FBXL14	Q8N1E6	PMID:24658274
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	MDM2	Q00987	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	FBXW7	Q969H0	PMID:30094882
-	K	Ubiquitination	E3 ubiquitin ligase	FBXO45	P0C2W1	PMID:25460509

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
11	S	Phosphorylation	15448698
Phosphorylation at Ser-11 and Ser-92 positively regulates its functions in induction of EMT and cell survival, respectively.
92	S	Phosphorylation	19923321
Phosphorylation at Ser-11 and Ser-92 positively regulates its functions in induction of EMT and cell survival, respectively.
96	S	Phosphorylation	15448698
Phosphorylation by CSNK1E, probably at Ser-104, provides the priming site for the subsequent phosphorylation by GSK3B, probably at Ser-100 and Ser-96.
98	K	ubiquitylation	16096638
Ubiquitinated on Lys-98, Lys-137 and Lys-146 by FBXL14 and BTRC leading to degradation.
100	S	Phosphorylation	15448698
Phosphorylation by CSNK1E, probably at Ser-104, provides the priming site for the subsequent phosphorylation by GSK3B, probably at Ser-100 and Ser-96.
104	S	Phosphorylation	15448698
Phosphorylation by CSNK1E, probably at Ser-104, provides the priming site for the subsequent phosphorylation by GSK3B, probably at Ser-100 and Ser-96.
112	S	Phosphorylation	20959806
O-GlcNAcylation at Ser-112 is enhanced in hyperglycaemic conditions, it opposes phosphorylation by GSK3B, and stabilizes the protein.
137	K	ubiquitylation	16096638
Ubiquitinated on Lys-98, Lys-137 and Lys-146 by FBXL14 and BTRC leading to degradation.
146	K	ubiquitylation	19955572
Ubiquitinated on Lys-98, Lys-137 and Lys-146 by FBXL14 and BTRC leading to degradation.

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 SNAI1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
QRIC2_HUMAN	QRICH2	physical	17353931
TTC25_HUMAN	TTC25	physical	17353931
CTDSL_HUMAN	CTDSPL	physical	19004823
CTDS2_HUMAN	CTDSP2	physical	19004823
CTDS1_HUMAN	CTDSP1	physical	19004823
GSK3B_HUMAN	GSK3B	physical	15647282
FBW1A_HUMAN	BTRC	physical	15647282
FBW1A_HUMAN	BTRC	physical	15448698
HDAC2_HUMAN	HDAC2	physical	14673164
HDAC1_HUMAN	HDAC1	physical	14673164
SIN3A_MOUSE	Sin3a	physical	14673164
AJUBA_HUMAN	AJUBA	physical	18347060
RCOR1_HUMAN	RCOR1	physical	20562920
KDM1A_HUMAN	KDM1A	physical	20562920
HDAC1_HUMAN	HDAC1	physical	20562920
EGR1_HUMAN	EGR1	physical	20121949
KDM1A_HUMAN	KDM1A	physical	20389281
H31_HUMAN	HIST1H3A	physical	20389281
FXL14_HUMAN	FBXL14	physical	19955572
FBW1A_HUMAN	BTRC	physical	19955572
NOTC1_HUMAN	NOTCH1	physical	22128911
MDM2_HUMAN	MDM2	physical	22128911
EZH2_HUMAN	EZH2	physical	21685935
HDAC1_HUMAN	HDAC1	physical	21685935
HDAC2_HUMAN	HDAC2	physical	21685935
HDAC3_HUMAN	HDAC3	physical	21685935
KDM1A_HUMAN	KDM1A	physical	23011797
HDAC1_HUMAN	HDAC1	physical	23011797
CHD4_HUMAN	CHD4	physical	23011797
P53_HUMAN	TP53	physical	20385133
MDM2_HUMAN	MDM2	physical	20385133
GSK3B_HUMAN	GSK3B	physical	19411070
FBW1A_HUMAN	BTRC	physical	19411070
FBXL5_HUMAN	FBXL5	physical	24157836
LATS2_HUMAN	LATS2	physical	24157836
RING1_HUMAN	RING1	physical	24903147
RING2_HUMAN	RNF2	physical	24903147
EZH2_HUMAN	EZH2	physical	24903147
TRIM1_HUMAN	MID2	physical	25416956
MTUS2_HUMAN	MTUS2	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
KR103_HUMAN	KRTAP10-3	physical	25416956
NT2NL_HUMAN	NOTCH2NL	physical	25416956
AKT1_HUMAN	AKT1	physical	22158034
AKT2_HUMAN	AKT2	physical	22158034
KDM1A_HUMAN	KDM1A	physical	26186194
GSE1_HUMAN	GSE1	physical	26186194
DPP9_HUMAN	DPP9	physical	26186194
RCOR1_HUMAN	RCOR1	physical	26186194
RCOR3_HUMAN	RCOR3	physical	26186194
SIR2_HUMAN	SIRT2	physical	26186194
HM20A_HUMAN	HMG20A	physical	26186194
HM20B_HUMAN	HMG20B	physical	26186194
EGR2_HUMAN	EGR2	physical	26186194
CBP_HUMAN	CREBBP	physical	25314079
EP300_HUMAN	EP300	physical	25314079
AJUBA_HUMAN	AJUBA	physical	25314079
HDAC1_HUMAN	HDAC1	physical	25314079
HDAC2_HUMAN	HDAC2	physical	25314079
TF65_HUMAN	RELA	physical	25314079
FBXL5_HUMAN	FBXL5	physical	25832584
U17L2_HUMAN	USP17L2	physical	28198361
U17L2_HUMAN	USP17L2	physical	28067227
ATM_HUMAN	ATM	physical	28067227
UBP10_HUMAN	USP10	physical	28067227
UBP7_HUMAN	USP7	physical	28067227
P53_HUMAN	TP53	physical	28067227
UBP11_HUMAN	USP11	physical	28067227
DNMT1_HUMAN	DNMT1	physical	28067227
CSK21_HUMAN	CSNK2A1	physical	28067227
EGR2_HUMAN	EGR2	physical	28514442
GSE1_HUMAN	GSE1	physical	28514442
HM20A_HUMAN	HMG20A	physical	28514442
SIR2_HUMAN	SIRT2	physical	28514442
RCOR3_HUMAN	RCOR3	physical	28514442
DPP9_HUMAN	DPP9	physical	28514442
RCOR1_HUMAN	RCOR1	physical	28514442
HM20B_HUMAN	HMG20B	physical	28514442
FBXL8_HUMAN	FBXL8	physical	28514442
HDAC1_HUMAN	HDAC1	physical	26794444
DNMT1_HUMAN	DNMT1	physical	26794444
GSK3B_HUMAN	GSK3B	physical	28892081
KPCD1_HUMAN	PRKD1	physical	28892081
HDAC1_MOUSE	Hdac1	physical	28892081
HDAC2_MOUSE	Hdac2	physical	28892081
SIN3A_MOUSE	Sin3a	physical	28892081
FBX31_HUMAN	FBXO31	physical	29117943

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 SNAI1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND MASSSPECTROMETRY.	15302935 [Abstract]

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