SNAI2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SNAI2_HUMAN
• UniProt AC: O43623
• Protein Name: Zinc finger protein SNAI2
• Gene Name: SNAI2
• Organism: Homo sapiens (Human).
• Sequence Length: 268
• Subcellular Localization: Nucleus . Cytoplasm. Observed in discrete foci in interphase nuclei. These nuclear foci do not overlap with the nucleoli, the SP100 and the HP1 heterochromatin or the coiled body, suggesting SNAI2 is associated with active transcription or active spl
• Protein Description: Transcriptional repressor that modulates both activator-dependent and basal transcription. Involved in the generation and migration of neural crest cells. Plays a role in mediating RAF1-induced transcriptional repression of the TJ protein, occludin (OCLN) and subsequent oncogenic transformation of epithelial cells (By similarity). Represses BRCA2 expression by binding to its E2-box-containing silencer and recruiting CTBP1 and HDAC1 in breast cells. In epidermal keratinocytes, binds to the E-box in ITGA3 promoter and represses its transcription. Involved in the regulation of ITGB1 and ITGB4 expression and cell adhesion and proliferation in epidermal keratinocytes. Binds to E-box2 domain of BSG and activates its expression during TGFB1-induced epithelial-mesenchymal transition (EMT) in hepatocytes. Represses E-Cadherin/CDH1 transcription via E-box elements. Involved in osteoblast maturation. Binds to RUNX2 and SOC9 promoters and may act as a positive and negative transcription regulator, respectively, in osteoblasts. Binds to CXCL12 promoter via E-box regions in mesenchymal stem cells and osteoblasts. Plays an essential role in TWIST1-induced EMT and its ability to promote invasion and metastasis..
• Protein Sequence: MPRSFLVKKHFNASKKPNYSELDTHTVIISPYLYESYSMPVIPQPEILSSGAYSPITVWTTAAPFHAQLPNGLSPLSGYSSSLGRVSPPPPSDTSSKDHSGSESPISDEEERLQSKLSDPHAIEAEKFQCNLCNKTYSTFSGLAKHKQLHCDAQSRKSFSCKYCDKEYVSLGALKMHIRTHTLPCVCKICGKAFSRPWLLQGHIRTHTGEKPFSCPHCNRAFADRSNLRAHLQTHSDVKKYQCKNCSKTFSRMSLLHKHEESGCCVAH

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Acetylation	MPRSFLVKKHFNASK CCCCHHHHHHCCCCC	42.55	118343407
54	Phosphorylation	ILSSGAYSPITVWTT HHCCCCCCCEEEEEC	14.86	-
87	Phosphorylation	SSSLGRVSPPPPSDT CCCCCCCCCCCCCCC	30.26	29255136
92	Phosphorylation	RVSPPPPSDTSSKDH CCCCCCCCCCCCCCC	60.33	23927012
94	Phosphorylation	SPPPPSDTSSKDHSG CCCCCCCCCCCCCCC	38.96	28060719
95	Phosphorylation	PPPPSDTSSKDHSGS CCCCCCCCCCCCCCC	40.14	26657352
96	Phosphorylation	PPPSDTSSKDHSGSE CCCCCCCCCCCCCCC	44.17	26657352
100	Phosphorylation	DTSSKDHSGSESPIS CCCCCCCCCCCCCCC	54.90	23090842
102	Phosphorylation	SSKDHSGSESPISDE CCCCCCCCCCCCCHH	37.61	23090842
104	Phosphorylation	KDHSGSESPISDEEE CCCCCCCCCCCHHHH	29.27	25850435
107	Phosphorylation	SGSESPISDEEERLQ CCCCCCCCHHHHHHH	42.21	29255136
115	Phosphorylation	DEEERLQSKLSDPHA HHHHHHHHHHCCHHH	39.91	23090842
116	Acetylation	EEERLQSKLSDPHAI HHHHHHHHHCCHHHH	38.76	118343403
136	Phosphorylation	QCNLCNKTYSTFSGL CCCCCCCCCCCCHHH	14.55	-
158	Phosphorylation	CDAQSRKSFSCKYCD CCCCCCCCCCCCCCC	22.68	-
166	Acetylation	FSCKYCDKEYVSLGA CCCCCCCHHEEECCE	47.59	118343409
168	Phosphorylation	CKYCDKEYVSLGALK CCCCCHHEEECCEEH	10.90	22210691
170	Phosphorylation	YCDKEYVSLGALKMH CCCHHEEECCEEHHH	21.86	22210691
175	Ubiquitination	YVSLGALKMHIRTHT EEECCEEHHHHHHCC	28.09	-
206	Phosphorylation	LLQGHIRTHTGEKPF HHCCEEECCCCCCCC	24.16	-
208	Phosphorylation	QGHIRTHTGEKPFSC CCEEECCCCCCCCCC	46.56	-
234	Phosphorylation	NLRAHLQTHSDVKKY HHHHHHHHHHHHHHH	29.70	29449344
236	Phosphorylation	RAHLQTHSDVKKYQC HHHHHHHHHHHHHCC	47.70	29449344
247	Phosphorylation	KYQCKNCSKTFSRMS HHCCCCCCHHHCHHH	44.09	-
251	Phosphorylation	KNCSKTFSRMSLLHK CCCCHHHCHHHHHHH	32.10	24719451
254	Phosphorylation	SKTFSRMSLLHKHEE CHHHCHHHHHHHHCC	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
54	S	Phosphorylation	Kinase	CDK2	P24941	PSP
87	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
92	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
96	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
100	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
104	S	Phosphorylation	Kinase	CDK2	P24941	PSP
104	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
104	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
158	S	Phosphorylation	Kinase	PAK4	O96013	PSP
251	S	Phosphorylation	Kinase	PAK1	Q13153	PSP
254	S	Phosphorylation	Kinase	PAK4	O96013	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	FBXL14	Q8N1E6	PMID:24658274
-	K	Ubiquitination	E3 ubiquitin ligase	FBXO45	P0C2W1	PMID:25460509

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SNAI2_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of SNAI2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HDAC2_HUMAN	HDAC2	physical	14673164
HDAC1_HUMAN	HDAC1	physical	14673164
SIN3A_MOUSE	Sin3a	physical	14673164
KDM1A_HUMAN	KDM1A	physical	23011797
HDAC1_HUMAN	HDAC1	physical	23011797
CHD4_HUMAN	CHD4	physical	23011797
A4_HUMAN	APP	physical	21832049
GSK3B_HUMAN	GSK3B	physical	23851495
P53_HUMAN	TP53	physical	23851495
ZO2_HUMAN	TJP2	physical	23851495
PSMD1_HUMAN	PSMD1	physical	23851495
PP2AB_HUMAN	PPP2CB	physical	23851495
PSMD3_HUMAN	PSMD3	physical	23851495
PSA3_HUMAN	PSMA3	physical	23851495
PP6R3_HUMAN	PPP6R3	physical	23851495
CHIP_HUMAN	STUB1	physical	23851495
2ABD_HUMAN	PPP2R2D	physical	23851495
PRS4_HUMAN	PSMC1	physical	23851495
MDM2_HUMAN	MDM2	physical	26992741
U17L2_HUMAN	USP17L2	physical	29088851
FBX31_HUMAN	FBXO31	physical	28500896

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 608890: Waardenburg syndrome 2D (WS2D)
• 172800: Piebald trait (PBT)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.