SNAI1

Functionⁱ

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.By similarity6 Publications

Caution

The interaction with mouse KPNA2 may prevent SNAI1 nuclear import.1 Publication

Regions

Feature key	Position(s)	DescriptionActions	Length
Zinc fingerⁱ	154 – 176	C2H2-type 1PROSITE-ProRule annotationAdd BLAST	23
Zinc fingerⁱ	178 – 202	C2H2-type 2PROSITE-ProRule annotationAdd BLAST	25
Zinc fingerⁱ	208 – 230	C2H2-type 3PROSITE-ProRule annotationAdd BLAST	23
Zinc fingerⁱ	236 – 259	C2H2-type 4; atypicalPROSITE-ProRule annotationAdd BLAST	24

GO - Molecular functionⁱ

DNA-binding transcription factor activity, RNA polymerase II-specific Source: NTNU_SB
DNA-binding transcription repressor activity, RNA polymerase II-specific
Source: BHF-UCL
Inferred from direct assayⁱ
- 11912130
E-box binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 11912130
kinase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 15448698
metal ion binding Source: UniProtKB-KW
proximal promoter DNA-binding transcription repressor activity, RNA polymerase II-specific Source: Ensembl
RNA polymerase II regulatory region sequence-specific DNA binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 11912130

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

aortic valve morphogenesis
Source: BHF-UCL
Traceable author statementⁱ
- 20951801
cartilage morphogenesis Source: Ensembl
cell migration Source: Ensembl
epithelial to mesenchymal transition
Source: UniProtKB
Inferred from direct assayⁱ
- 16096638
epithelial to mesenchymal transition involved in endocardial cushion formation
Source: BHF-UCL
Traceable author statementⁱ
- 20951801
hair follicle morphogenesis Source: Ensembl
heterochromatin organization Source: UniProtKB
left/right pattern formation Source: Ensembl
mesoderm formation Source: UniProtKB
negative regulation of cell differentiation involved in embryonic placenta development Source: Ensembl
negative regulation of DNA damage response, signal transduction by p53 class mediator
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 15314165
negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 15314165
negative regulation of transcription by RNA polymerase II
Source: BHF-UCL
Inferred from direct assayⁱ
- 11912130
negative regulation of vitamin D biosynthetic process
Source: BHF-UCL
Inferred from direct assayⁱ
- 19502595
Notch signaling involved in heart development Source: BHF-UCL
osteoblast differentiation
Source: UniProtKB
Inferred from expression patternⁱ
- 20128911
positive regulation of cell migration
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 20018240
positive regulation of epithelial to mesenchymal transition
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 20018240
- 23288509
positive regulation of transcription, DNA-templated
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 20018240
regulation of bicellular tight junction assembly
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 15314165
roof of mouth development Source: Ensembl
trophoblast giant cell differentiation Source: Ensembl

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Developmental protein, DNA-binding
Ligand	Metal-binding, Zinc

Enzyme and pathway databases

Reactomeⁱ	R-HSA-8943724 Regulation of PTEN gene transcription
SIGNORⁱ	O95863

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Zinc finger protein SNAI1 Alternative name(s): Protein snail homolog 1 Short name: Protein sna
Gene namesⁱ	Name:SNAI1 Synonyms:SNAH
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 20

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000124216.3
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:11128 SNAI1
MIMⁱ	604238 gene
neXtProtⁱ	NX_O95863

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	2	P → A: Abolishes repressor activity on E-cadherin/CDH1 promoter and binding to KDM1A. 1 Publication	1
Mutagenesisⁱ	9	K → R: Does not affect E-cadherin/CDH1 repression; when associated with R-16. 1 Publication	1
Mutagenesisⁱ	11	S → A: Abolishes PKA phosphorylation. Strongly decreases repressor activity on E-cadherin/CDH1 and CLDN1 promoters. Increases protein stability. Affects function in EMT. 1 Publication	1
Mutagenesisⁱ	16	K → R: Does not affect E-cadherin repression; when associated with R-9. 1 Publication	1
Mutagenesisⁱ	92	S → A: Abolishes CK2 phosphorylation. Strongly decreases repressor activity on E-cadherin/CDH1 and CLDN1 promoters. Increases protein stability. Affects function in cell survival. Abolishes phosphorylation in the serine-rich region; when associated with A-104 and A-107. 1 Publication	1
Mutagenesisⁱ	92	S → E: Does not affect repressor activity on E-cadherin/CDH1 promoter. 1 Publication	1
Mutagenesisⁱ	96	S → A: Abolishes recognition and ubiquitination by BTRC which increases steady state level and half-life. Preferentially localizes to the nucleus. Induces a more aggressive tissue invasion program. Lower sensitivity to BTRC-triggered degradation, impairs phosphorylation by GSK3B and does not affect NOTCH1-induced degradation; when associated with A-100. Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-100; A-107; A-111; A-115 and A-119. 4 Publications	1
Mutagenesisⁱ	98	K → R: No change. Complete loss of sensitivity to FBXL14- and BTRC-triggered degradation and loss of ability to repress E-cadherin/CDH1; when associated with R-137 and R-146. 2 Publications	1
Mutagenesisⁱ	100	S → A: Lower sensitivity to BTRC-triggered degradation and impaired phosphorylation by GSK3B; when associated with A-96. Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-96; A-107; A-111; A-115 and A-119. Does not affect NOTCH1-induced degradation; when associated with A-96. Abolishes phosphorylation at S-96. 3 Publications	1
Mutagenesisⁱ	104	S → A: Increases protein stability, does not affect repressor activity on E-cadherin/CDH1 promoter, preferentially localizes to the nucleus, induces a more aggressive tissue invasion program and impairs phosphorylation by GSK3B, binding to BTRC and ubiquitination; when associated with A-107. Impairs phosphorylation in the serine-rich domain/region; when associated with A-92 and A-107. Abolishes phosphorylation at S-96. 3 Publications	1
Mutagenesisⁱ	107	S → A: Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-111; A-115 and A-119. Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-96; A-100; A-111; A-115 and A-119. Increases protein stability, does not affect repressor activity on E-cadherin promoter, preferentially localizes to the nucleus, induces a more aggressive tissue invasion program and impairs phosphorylation by GSK3B, binding to BTRC and ubiquitination; when associated with A-104. Impairs phosphorylation in the serine-rich region; when associated with A-92 and A-104. Abolishes phosphorylation at S-96. 4 Publications	1
Mutagenesisⁱ	107	S → E: Predominantly localized to the cytoplasm; when associated with E-111; E-115 and E-119. 4 Publications	1
Mutagenesisⁱ	111	S → A: Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-107; A-115 and A-119. Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-96; A-100; A-107; A-115 and A-119. 1 Publication	1
Mutagenesisⁱ	111	S → E: Predominantly localized to the cytoplasm; when associated with E-107; E-115 and E-119. 1 Publication	1
Mutagenesisⁱ	115	S → A: Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-107; A-111 and A-119. Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-96; A-100; A-107; A-111 and A-119. 1 Publication	1
Mutagenesisⁱ	115	S → E: Predominantly localized to the cytoplasm; when associated with E-107; E-111 and E-119. 1 Publication	1
Mutagenesisⁱ	119	S → A: Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-107; A-111 and A-119. Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-96; A-100; A-107; A-111 and A-115. 1 Publication	1
Mutagenesisⁱ	119	S → E: Predominantly localized to the cytoplasm; when associated with E-107; E-111 and E-115. 1 Publication	1
Mutagenesisⁱ	137	K → R: Lower sensitivity to FBXL14-triggered degradation. Lower sensitivity to FBXL14-triggered degradation; when associated with R-146. Complete loss of sensitivity to FBXL14- and BTRC-triggered degradation and loss of ability to repress E-cadherin; when associated with R-98 and R-146. 2 Publications	1
Mutagenesisⁱ	146	K → R: Lower sensitivity to FBXL14-triggered degradation. Lower sensitivity to FBXL14-triggered degradation; when associated with R-137. Complete loss of sensitivity to FBXL14- and BTRC-triggered degradation; when associated with R-98 and R-137. 1 Publication	1
Mutagenesisⁱ	151 – 152	RK → EE: Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. 1 Publication	2
Mutagenesisⁱ	156	C → A: Abolishes binding to KPNB1, KPNA2, IPO7 and TNPO1 and nuclear localization. 1 Publication	1
Mutagenesisⁱ	161	K → E: Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. No change in subcellular localization. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1 and abolishes nuclear localization, DNA binding and repressor activity on E-cadherin/CDH1 promoter; when associated with E-170. Abolishes binding to KPNB1, KPNA2, IPO7 and TNPO1 and nuclear localization; when associated with E-187 and/or E-220. 1 Publication	1
Mutagenesisⁱ	170	K → E: Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. No change in subcellular localization. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1 and abolishes nuclear localization, DNA binding and repressor activity on E-cadherin/CDH1 promoter; when associated with E-161. 1 Publication	1
Mutagenesisⁱ	182	C → A: Impairs binding to KPNB1, IPO7 and TNPO1 and abolishes binding to KPNA2. Localizes to cytoplasm and nucleus. 1 Publication	1
Mutagenesisⁱ	187	K → E: Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1 and abolishes nuclear localization, DNA binding and repressor activity on E-cadherin/CDH1 promoter; when associated with E-191. Abolishes binding to KPNB1, KPNA2, IPO7 and TNPO1 and nuclear localization; when associated with E-161 and/or E-220. 1 Publication	1
Mutagenesisⁱ	191	R → E: Mildly reduces binding to KPNB1 and nuclear import. Strongly reduces binding to KPNB1 and nuclear import; when associated with A-193. Loss of binding to KPNB1 and nuclear import; when associated with A-193 and A-196. 1 Publication	1
Mutagenesisⁱ	191	R → E: Mildly reduces binding to KPNB1. Does not affect binding to KPNA2, IPO7 or TNPO1. 1 Publication	1
Mutagenesisⁱ	193	W → A: Mildly reduces binding to KPNB1 and nuclear import. Strongly reduces binding to KPNB1 and nuclear import; when associated with E-191. Loss of binding to KPNB1 and nuclear import; when associated with E-191 and A-196. 1 Publication	1
Mutagenesisⁱ	196	Q → A: Loss of binding to KPNB1 and nuclear import; when associated with E-191 and A-193. 1 Publication	1
Mutagenesisⁱ	203	T → A: Abolishes LATS2 phosphorylation. Does not affect binding to LATS2. Reduces protein stability. Equally distributed between nucleus and cytoplasm. Increases capacity to associate with nuclear pore importins. Unable to accumulate in the nucleus. Does not abrogate function. 1 Publication	1
Mutagenesisⁱ	203	T → E: Exclusively localizes to the cytoplasm. Reduces capacity to associate with nuclear pore importins. Unable to enter the nucleus. Does not abrogate function. 1 Publication	1
Mutagenesisⁱ	210	C → A: Impairs binding to KPNB1, IPO7 and TNPO1 and abolishes binding to KPNA2. Localizes to cytoplasm and nucleus. 1 Publication	1
Mutagenesisⁱ	215	R → E: Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1. No change in subcellular localization. 1 Publication	1
Mutagenesisⁱ	220	R → E: Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. No change in subcellular localization. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1; when associated with E-222 and E-224. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1 and abolishes nuclear localization, DNA binding and repressor activity on E-cadherin/CDH1 promoter; when associated with E-224. Abolishes binding to KPNB1, KPNA2, IPO7 and TNPO1 and nuclear localization; when associated with E-161 and/or E-187. 1 Publication	1
Mutagenesisⁱ	222	N → E: Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. No change in subcellular localization. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1; when associated with E-220 and E-224. 1 Publication	1
Mutagenesisⁱ	224	R → E: Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. No change in subcellular localization. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1; when associated with E-220 and E-222. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1 and abolishes nuclear localization, DNA binding and repressor activity on E-cadherin/CDH1 promoter; when associated with E-220. 1 Publication	1
Mutagenesisⁱ	224	R → E: Mildly reduces binding to KPNB1 and nuclear import. Strongly reduces binding to KPNB1 and nuclear import; when associated with A-228. 1 Publication	1
Mutagenesisⁱ	228	Q → A: Very minor effect on binding to KPNB1 and nuclear import. Strongly reduces binding to KPNB1 and nuclear import; when associated with E-224. 1 Publication	1
Mutagenesisⁱ	232 – 235	DVKK → KVEE: Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. 1 Publication	4
Mutagenesisⁱ	238	C → A: Impairs binding to KPNB1 and IPO7 and abolishes binding to KPNA2 and TNPO1 and nuclear localization. 1 Publication	1
Mutagenesisⁱ	239	Q → E: Does not affect binding to KPNB1, KPNA2, IPO7, TNPO1 or DNA. 1 Publication	1
Mutagenesisⁱ	246	S → A: Decreases repression activity on E-cadherin/CDH1, occludin and aromatase promoters. Preferentially localizes to the cytoplasm. Abolishes phosphorylation by PAK1. 1 Publication	1
Mutagenesisⁱ	247	R → E: Mildly reduces binding to KPNB1 and nuclear import. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	6615
Open Targets More...OpenTargetsⁱ	ENSG00000124216
PharmGKBⁱ	PA35977

Polymorphism and mutation databases

BioMutaⁱ	SNAI1

BioMutaⁱ

SNAI1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000047029	1 – 264	Zinc finger protein SNAI1Add BLAST		264

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	11	Phosphoserine; by PKA1 Publication	1
Modified residueⁱ	82	Phosphoserine1 Publication	1
Modified residueⁱ	92	Phosphoserine; by CK21 Publication	1
Modified residueⁱ	96	Phosphoserine1 Publication1 Publication	1
Cross-linkⁱ	98	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residueⁱ	100	Phosphoserine1 Publication	1
Modified residueⁱ	104	Phosphoserine1 Publication2 Publications	1
Modified residueⁱ	107	Phosphoserine1 Publication2 Publications	1
Modified residueⁱ	111	Phosphoserine1 Publication	1
Glycosylationⁱ	112	O-linked (GlcNAc) serine1 Publication	1
Modified residueⁱ	115	Phosphoserine1 Publication	1
Modified residueⁱ	119	Phosphoserine1 Publication	1
Cross-linkⁱ	137	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-linkⁱ	146	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residueⁱ	203	Phosphothreonine; by LATS21 Publication	1
Modified residueⁱ	246	Phosphoserine; by PAK11 Publication	1

Post-translational modificationⁱ

Phosphorylated by GSK3B. Once phosphorylated, it becomes a target for BTRC ubiquitination. Phosphorylation by CSNK1E, probably at Ser-104, provides the priming site for the subsequent phosphorylation by GSK3B, probably at Ser-100 and Ser-96. Phosphorylation by PAK1 may modulate its transcriptional activity by promoting increased accumulation in the nucleus. Phosphorylation at Ser-11 and Ser-92 positively regulates its functions in induction of EMT and cell survival, respectively. Phosphorylation by LATS2, upon mitotic stress, oncogenic stress or Hippo pathway activation, occurs in the nucleus and promotes nuclear retention and stabilization of total cellular protein level.1 Publication3 Publications

Ubiquitinated on Lys-98, Lys-137 and Lys-146 by FBXL14 and BTRC leading to degradation. BTRC-triggered ubiquitination requires previous GSK3B-mediated SNAI1 phosphorylation. Ubiquitination induced upon interaction with NOTCH1 or TP53/p53 is mediated by MDM2.

O-GlcNAcylation at Ser-112 is enhanced in hyperglycaemic conditions, it opposes phosphorylation by GSK3B, and stabilizes the protein.

ADP-ribosylation by PARP1 increases protein half-life and may be involved in TGFB-induced SNAI1 up-regulation.

Keywords - PTMⁱ

ADP-ribosylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	O95863
PaxDbⁱ	O95863
PeptideAtlas More...PeptideAtlasⁱ	O95863
PRIDEⁱ	O95863
ProteomicsDBⁱ	51096

PTM databases

iPTMnetⁱ	O95863
PhosphoSitePlusⁱ	O95863
SwissPalmⁱ	O95863

Expressionⁱ

Tissue specificityⁱ

Expressed in a variety of tissues with the highest expression in kidney. Expressed in mesenchymal and epithelial cell lines.1 Publication

Inductionⁱ

Induced by TPA maximally by 2.5-fold at 4 hours, in HepG2 cells (at protein level).1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000124216 Expressed in 120 organ(s), highest expression level in left coronary artery
CleanExⁱ	HS_SNAI1
Genevisibleⁱ	O95863 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB005883 CAB078687 HPA056831 HPA069985

HPAⁱ

CAB005883
CAB078687
HPA056831
HPA069985

Interactionⁱ

Subunit structureⁱ

Interacts with FBXL14 and GSK3B. Interacts with BTRC; interaction occurs when it is phosphorylated on the destruction motif. Interacts (via SNAG domain) with WTIP (via LIM domains) (By similarity). Interacts (via SNAG domain) with LIMD1 (via LIM domains), and AJUBA (via LIM domains). Interacts with LOXL2 and LOXL3. Interacts (via N-terminal region) with CSNK2A1. Interacts with EGR1 upon TPA induction. Interacts (via N-terminal region) with LATS2; the interaction is dependent on LATS2 kinase activity but independent of SNAI1 Thr-203 phosphorylation. Interacts (via zinc fingers) with KPNB1 and TNPO1; the interactions mediate nuclear import. Interacts (via zinc fingers) with KPNA1; the interaction disrupts the transport complex with KPNB1 and prevents nuclear import increasing SNAI1 degradation in the cytoplasm. Interacts (via zinc fingers) with KPNA2; the interaction, in combination with KPNB1, mediates nuclear import. Interacts with KPNA4; this interaction mediates nuclear import. May interact (via zinc fingers) with IPO7. Interacts (via zinc fingers) with PARP1; the interaction requires SNAI1 to be poly-ADP-ribosylated and non-phosphorylated (active) by GSK3B. Interacts (via SNAG domain) with KDM1A; the interaction is necessary for the down-regulation of dimethylated H3K4 mark and promoter activity of E-cadherin/CDH1, CDN7 and KRT8. Interacts with TP53/p53 and (via zinc fingers) with NOTCH1 (via intracellular domain); the interactions induce SNAI1 degradation via MDM2-mediated ubiquitination and inhibit SNAI1-induced cell invasion. Interacts with MDM2; the interaction promotes SNAI1 ubiquitination. Interacts (via zinc fingers) with CSNK1E. Interacts with PAK1.By similarity16 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
ACTN2	P35609	5	EBI-1045459,EBI-77797
AJUBA	Q96IF1	3	EBI-1045459,EBI-949782
BTRC	Q9Y297	2	EBI-1045459,EBI-307461
CREBBP	Q92793	9	EBI-1045459,EBI-81215
Crebbp	P45481	7	EBI-1045459,EBI-296306	From Mus musculus.
EP300	Q09472	3	EBI-1045459,EBI-447295
FBXL14	Q8N1E6	2	EBI-1045459,EBI-6425532
FBXO11	Q86XK2	6	EBI-1045459,EBI-1047804
GSK3B	P49841	5	EBI-1045459,EBI-373586
HDAC1	Q13547	3	EBI-1045459,EBI-301834
HDAC2	Q92769	2	EBI-1045459,EBI-301821
KDM1A	O60341	32	EBI-1045459,EBI-710124
KRT31	Q15323	3	EBI-1045459,EBI-948001
KRT40	Q6A162	3	EBI-1045459,EBI-10171697
Mapk1	P63085	3	EBI-1045459,EBI-397697	From Mus musculus.
MID2	Q9UJV3-2	3	EBI-1045459,EBI-10172526
MTUS2	Q5JR59	3	EBI-1045459,EBI-742948
NOTCH2NL	Q7Z3S9	3	EBI-1045459,EBI-945833
PARP1	P09874	10	EBI-1045459,EBI-355676
RELA	Q04206	5	EBI-1045459,EBI-73886
SOCS3	O14543	3	EBI-1045459,EBI-714146
SPSB1	Q96BD6	3	EBI-1045459,EBI-2659201
TP53	P04637	2	EBI-1045459,EBI-366083
TRIM23	P36406	5	EBI-1045459,EBI-740098
TRIM5	Q9C035	3	EBI-1045459,EBI-924214

GO - Molecular functionⁱ

kinase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 15448698

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	112499, 71 interactors
Database of interacting proteins More...DIPⁱ	DIP-50870N
IntActⁱ	O95863, 55 interactors
Molecular INTeraction database More...MINTⁱ	O95863
STRINGⁱ	9606.ENSP00000244050

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	3 – 5	Combined sources	3
Turnⁱ	157 – 159	Combined sources	3
Beta strandⁱ	163 – 165	Combined sources	3
Helixⁱ	166 – 173	Combined sources	8
Helixⁱ	174 – 176	Combined sources	3
Beta strandⁱ	183 – 185	Combined sources	3
Beta strandⁱ	188 – 191	Combined sources	4
Helixⁱ	192 – 200	Combined sources	9
Turnⁱ	211 – 213	Combined sources	3
Beta strandⁱ	216 – 219	Combined sources	4
Helixⁱ	220 – 227	Combined sources	8
Turnⁱ	239 – 241	Combined sources	3
Beta strandⁱ	244 – 247	Combined sources	4
Helixⁱ	248 – 256	Combined sources	9

Show more details

3D structure databases

ProteinModelPortalⁱ	O95863
SMRⁱ	O95863
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

O95863

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	1 – 20	SNAG domainBy similarityAdd BLAST	20
Regionⁱ	10 – 40	LATS2 bindingAdd BLAST	31
Regionⁱ	120 – 151	Required for FBXL14-triggered degradationAdd BLAST	32
Regionⁱ	151 – 264	Required for nuclear localization and interaction with KPNB1, NOTCH1 and PARP12 PublicationsAdd BLAST	114

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	95 – 100	Destruction motif		6

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	90 – 120	Ser-richAdd BLAST		31

Sequence similaritiesⁱ

Belongs to the snail C2H2-type zinc-finger protein family.Curated

Zinc finger

Feature key	Position(s)	DescriptionActions	Length
Zinc fingerⁱ	154 – 176	C2H2-type 1PROSITE-ProRule annotationAdd BLAST	23
Zinc fingerⁱ	178 – 202	C2H2-type 2PROSITE-ProRule annotationAdd BLAST	25
Zinc fingerⁱ	208 – 230	C2H2-type 3PROSITE-ProRule annotationAdd BLAST	23
Zinc fingerⁱ	236 – 259	C2H2-type 4; atypicalPROSITE-ProRule annotationAdd BLAST	24

Keywords - Domainⁱ

Repeat, Zinc-finger

Phylogenomic databases

eggNOGⁱ	KOG2462 Eukaryota ENOG41106JS LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000011027
HOGENOMⁱ	HOG000261665
HOVERGENⁱ	HBG007477
InParanoidⁱ	O95863
KEGG Orthology (KO) More...KOⁱ	K05707
OMAⁱ	PRRKPNY
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0Q0V
PhylomeDBⁱ	O95863
TreeFamⁱ	TF315515

Family and domain databases

InterProⁱ	View protein in InterPro IPR036236 Znf_C2H2_sf IPR013087 Znf_C2H2_type
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00096 zf-C2H2, 2 hits
SMARTⁱ	View protein in SMART SM00355 ZnF_C2H2, 4 hits
SUPFAMⁱ	SSF57667 SSF57667, 3 hits
PROSITEⁱ	View protein in PROSITE PS00028 ZINC_FINGER_C2H2_1, 3 hits PS50157 ZINC_FINGER_C2H2_2, 4 hits

Sequenceⁱ

Sequence statusⁱ: Complete.

O95863-1 [UniParc]FASTA Add to basket

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        10         20         30         40         50
MPRSFLVRKP SDPNRKPNYS ELQDSNPEFT FQQPYDQAHL LAAIPPPEIL 
        60         70         80         90        100
NPTASLPMLI WDSVLAPQAQ PIAWASLRLQ ESPRVAELTS LSDEDSGKGS 
       110        120        130        140        150
QPPSPPSPAP SSFSSTSVSS LEAEAYAAFP GLGQVPKQLA QLSEAKDLQA 
       160        170        180        190        200
RKAFNCKYCN KEYLSLGALK MHIRSHTLPC VCGTCGKAFS RPWLLQGHVR 
       210        220        230        240        250
THTGEKPFSC PHCSRAFADR SNLRAHLQTH SDVKKYQCQA CARTFSRMSL 
       260 
LHKHQESGCS GCPR

Length:264

Mass (Da):29,083

Last modified:December 1, 2000 - v2

Checksum:ⁱ70E298C9BB154115

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	46	P → L in BAG36039 (PubMed:14702039).Curated		1
Sequence conflictⁱ	154	F → S in AAF32527 (PubMed:10655587).Curated		1

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_069162	66	A → V. Corresponds to variant dbSNP:rs34261470Ensembl.		1
Natural variantⁱVAR_019969	118	V → A1 PublicationCorresponds to variant dbSNP:rs4647958Ensembl.		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF125377 mRNA Translation: AAD17332.1 AJ245657, AJ245658, AJ245659 Genomic DNA Translation: CAB52414.1 AF155233 Genomic DNA Translation: AAD52986.1 AF177731 Genomic DNA Translation: AAD52996.1 AK313228 mRNA Translation: BAG36039.1 AL121712 Genomic DNA No translation available. BC012910 mRNA Translation: AAH12910.1 AF131208 mRNA Translation: AAF32527.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS13423.1
NCBI Reference Sequences More...RefSeqⁱ	NP_005976.2, NM_005985.3
UniGeneⁱ	Hs.48029

Genome annotation databases

Ensemblⁱ	ENST00000244050; ENSP00000244050; ENSG00000124216
GeneIDⁱ	6615
KEGGⁱ	hsa:6615
UCSC genome browser More...UCSCⁱ	uc002xuz.4 human

Keywords - Coding sequence diversityⁱ

Polymorphism

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
O95863	Snail family transcriptional repressor 1		SAIBB		265	UniRef90_O95863
SNAI1 isoform 1		PANTR		264
Uncharacterized protein		PANPA		264
Uncharacterized protein		PROCO		264
Protein snail-like protein 1		MACMU		264
+23

Protein	Similar proteins		Species	Score	Length	Source
O95863	Snail family transcriptional repressor 1		SAIBB		265	UniRef50_O95863
Uncharacterized protein		COLAP		264
Uncharacterized protein		Cebus capucinus imitator		264
Snail family transcriptional repressor 1		CALJA		264
SNAI1 isoform 1		PANTR		264
+195

Cross-referencesⁱ

Web resourcesⁱ

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF125377 mRNA Translation: AAD17332.1 AJ245657, AJ245658, AJ245659 Genomic DNA Translation: CAB52414.1 AF155233 Genomic DNA Translation: AAD52986.1 AF177731 Genomic DNA Translation: AAD52996.1 AK313228 mRNA Translation: BAG36039.1 AL121712 Genomic DNA No translation available. BC012910 mRNA Translation: AAH12910.1 AF131208 mRNA Translation: AAF32527.1
CCDSⁱ	CCDS13423.1
RefSeqⁱ	NP_005976.2, NM_005985.3
UniGeneⁱ	Hs.48029

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	2Y48	X-ray	3.00	C	2-21	[»]
	3W5K	X-ray	2.60	B	1-264	[»]
	4QLI	X-ray	1.45	B	175-180	[»]
ProteinModelPortalⁱ	O95863
SMRⁱ	O95863
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	112499, 71 interactors
DIPⁱ	DIP-50870N
IntActⁱ	O95863, 55 interactors
MINTⁱ	O95863
STRINGⁱ	9606.ENSP00000244050

PTM databases

iPTMnetⁱ	O95863
PhosphoSitePlusⁱ	O95863
SwissPalmⁱ	O95863

Polymorphism and mutation databases

BioMutaⁱ	SNAI1

BioMutaⁱ

SNAI1

Proteomic databases

EPDⁱ	O95863
PaxDbⁱ	O95863
PeptideAtlasⁱ	O95863
PRIDEⁱ	O95863
ProteomicsDBⁱ	51096

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	6615
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000244050; ENSP00000244050; ENSG00000124216
GeneIDⁱ	6615
KEGGⁱ	hsa:6615
UCSCⁱ	uc002xuz.4 human

Organism-specific databases

CTDⁱ	6615
DisGeNETⁱ	6615
EuPathDBⁱ	HostDB:ENSG00000124216.3
GeneCardsⁱ	SNAI1
HGNCⁱ	HGNC:11128 SNAI1
HPAⁱ	CAB005883 CAB078687 HPA056831 HPA069985
MIMⁱ	604238 gene
neXtProtⁱ	NX_O95863
OpenTargetsⁱ	ENSG00000124216
PharmGKBⁱ	PA35977
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG2462 Eukaryota ENOG41106JS LUCA
GeneTreeⁱ	ENSGT00390000011027
HOGENOMⁱ	HOG000261665
HOVERGENⁱ	HBG007477
InParanoidⁱ	O95863
KOⁱ	K05707
OMAⁱ	PRRKPNY
OrthoDBⁱ	EOG091G0Q0V
PhylomeDBⁱ	O95863
TreeFamⁱ	TF315515

Enzyme and pathway databases

Reactomeⁱ	R-HSA-8943724 Regulation of PTEN gene transcription
SIGNORⁱ	O95863

Miscellaneous databases

EvolutionaryTraceⁱ	O95863
GeneWikiⁱ	SNAI1
GenomeRNAiⁱ	6615
Protein Ontology More...PROⁱ	PR:O95863
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000124216 Expressed in 120 organ(s), highest expression level in left coronary artery
CleanExⁱ	HS_SNAI1
Genevisibleⁱ	O95863 HS

Family and domain databases

InterProⁱ	View protein in InterPro IPR036236 Znf_C2H2_sf IPR013087 Znf_C2H2_type
Pfamⁱ	View protein in Pfam PF00096 zf-C2H2, 2 hits
SMARTⁱ	View protein in SMART SM00355 ZnF_C2H2, 4 hits
SUPFAMⁱ	SSF57667 SSF57667, 3 hits
PROSITEⁱ	View protein in PROSITE PS00028 ZINC_FINGER_C2H2_1, 3 hits PS50157 ZINC_FINGER_C2H2_2, 4 hits
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	SNAI1_HUMAN
Accessionⁱ	O95863Primary (citable) accession number: O95863 Secondary accession number(s): B2R842 , Q9P113, Q9UBP7, Q9UHH7
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
	Last sequence update:	December 1, 2000
	Last modified:	November 7, 2018
	This is version 189 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
Human chromosome 20
Human chromosome 20: entries, gene names and cross-references to MIM
PDB cross-references
Index of Protein Data Bank (PDB) cross-references

UniProtKB

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UniProtKB - O95863 (SNAI1_HUMAN)

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Zinc finger protein SNAI1

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Caution

Regions

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GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

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Cytosol

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Motif

Compositional bias

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Zinc finger

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ