SNAI1_MOUSE - dbPTM
SNAI1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNAI1_MOUSE
UniProt AC Q02085
Protein Name Zinc finger protein SNAI1
Gene Name Snai1
Organism Mus musculus (Mouse).
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 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. [PubMed: 24239292 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]
Protein Sequence MPRSFLVRKPSDPRRKPNYSELQDACVEFTFQQPYDQAHLLAAIPPPEVLNPAASLPTLIWDSLLVPQVRPVAWATLPLRESPKAVELTSLSDEDSGKSSQPPSPPSPAPSSFSSTSASSLEAEAFIAFPGLGQLPKQLARLSVAKDPQSRKIFNCKYCNKEYLSLGALKMHIRSHTLPCVCTTCGKAFSRPWLLQGHVRTHTGEKPFSCSHCNRAFADRSNLRAHLQTHSDVKRYQCQACARTFSRMSLLHKHQESGCSGGPR
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 Orthologous
Protein Cluster
11PhosphorylationSFLVRKPSDPRRKPN
CCCCCCCCCCCCCCC
64.38-
82PhosphorylationATLPLRESPKAVELT
EECCCCCCCCEEEEE
25.85-
89PhosphorylationSPKAVELTSLSDEDS
CCCEEEEEECCCCCC
17.7025619855
90PhosphorylationPKAVELTSLSDEDSG
CCEEEEEECCCCCCC
38.2025619855
92PhosphorylationAVELTSLSDEDSGKS
EEEEEECCCCCCCCC
38.4325619855
96PhosphorylationTSLSDEDSGKSSQPP
EECCCCCCCCCCCCC
46.1812832491
100PhosphorylationDEDSGKSSQPPSPPS
CCCCCCCCCCCCCCC
50.6312832491
104PhosphorylationGKSSQPPSPPSPAPS
CCCCCCCCCCCCCCC
57.01-
107PhosphorylationSQPPSPPSPAPSSFS
CCCCCCCCCCCCCCC
36.7612832491
111PhosphorylationSPPSPAPSSFSSTSA
CCCCCCCCCCCCCCC
46.2312832491
112O-linked_GlycosylationPPSPAPSSFSSTSAS
CCCCCCCCCCCCCCC
28.26-
115PhosphorylationPAPSSFSSTSASSLE
CCCCCCCCCCCCHHC
25.1112832491
119PhosphorylationSFSSTSASSLEAEAF
CCCCCCCCHHCEEEE
34.9112832491
143PhosphorylationPKQLARLSVAKDPQS
HHHHHHHHCCCCCCC
17.9324719451
203PhosphorylationQGHVRTHTGEKPFSC
CCCEEECCCCCCCCC
46.56-
231PhosphorylationRAHLQTHSDVKRYQC
HHHHHHHHHHHHHHH
47.7027149854
246PhosphorylationQACARTFSRMSLLHK
HHHHHHHHHHHHHHH
26.85-

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
-KUbiquitinationE3 ubiquitin ligaseBtrcQ3ULA2
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
11SPhosphorylation

-
96SPhosphorylation

-
98Kubiquitylation

-
100SPhosphorylation

-
104SPhosphorylation

-
104SPhosphorylation

-
112SPhosphorylation

-
137Kubiquitylation

-
146Kubiquitylation

-

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FXL14_HUMANFBXL14physical
19955572
TNAP3_MOUSETnfaip3physical
28892081
GSK3B_MOUSEGsk3bphysical
28892081

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SNAI1_MOUSE

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Related Literatures of Post-Translational Modification

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