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O95863 (SNAI1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Zinc finger protein SNAI1
Alternative name(s):
Protein snail homolog 1
Short name=Protein sna
Gene names
Name:SNAI1
Synonyms:SNAH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length264 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. 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. Ref.7 Ref.10 Ref.12 Ref.16 Ref.21 Ref.26

Subunit structure

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. Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24

Subcellular location

Nucleus. Cytoplasm. Note: 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. Ref.8 Ref.9 Ref.11 Ref.18 Ref.22 Ref.24 Ref.26

Tissue specificity

Expressed in a variety of tissues with the highest expression in kidney. Expressed in mesenchymal and epithelial cell lines. Ref.7

Induction

Induced by TPA maximally by 2.5-fold at 4 hours, in HepG2 cells (at protein level). Ref.16

Post-translational modification

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. Ref.8 Ref.9 Ref.12 Ref.19 Ref.20 Ref.26

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. Ref.8 Ref.17 Ref.18 Ref.22

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.

Sequence similarities

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

Contains 4 C2H2-type zinc fingers.

Caution

The interaction with mouse KPNA2 may prevent SNAI1 nuclear import (Ref.23).

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionDevelopmental protein
   PTMADP-ribosylation
Glycoprotein
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNotch signaling involved in heart development

Inferred from sequence or structural similarity. Source: BHF-UCL

cartilage morphogenesis

Inferred from electronic annotation. Source: Ensembl

cell migration

Inferred from electronic annotation. Source: Ensembl

epithelial to mesenchymal transition

Inferred from direct assay Ref.10. Source: UniProtKB

hair follicle morphogenesis

Inferred from electronic annotation. Source: Ensembl

left/right pattern formation

Inferred from electronic annotation. Source: Ensembl

mesoderm formation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of DNA damage response, signal transduction by p53 class mediator

Inferred from mutant phenotype PubMed 15314165. Source: BHF-UCL

negative regulation of cell differentiation involved in embryonic placenta development

Inferred from electronic annotation. Source: Ensembl

negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from mutant phenotype PubMed 15314165. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of vitamin D biosynthetic process

Inferred from direct assay PubMed 19502595. Source: BHF-UCL

osteoblast differentiation

Inferred from expression pattern PubMed 20128911. Source: UniProtKB

palate development

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration

Inferred from mutant phenotype PubMed 20018240. Source: UniProtKB

positive regulation of epithelial to mesenchymal transition

Inferred from mutant phenotype PubMed 20018240. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 20018240. Source: UniProtKB

regulation of tight junction assembly

Inferred from mutant phenotype PubMed 15314165. Source: BHF-UCL

trophoblast giant cell differentiation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay Ref.8Ref.18. Source: UniProtKB

nucleus

Inferred from direct assay Ref.8Ref.18. Source: UniProtKB

   Molecular_functionRNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription

Inferred from direct assay PubMed 11912130. Source: BHF-UCL

kinase binding

Inferred from physical interaction Ref.8. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 264264Zinc finger protein SNAI1
PRO_0000047029

Regions

Zinc finger154 – 17623C2H2-type 1
Zinc finger178 – 20225C2H2-type 2
Zinc finger208 – 23023C2H2-type 3
Zinc finger236 – 25924C2H2-type 4; atypical
Region1 – 2020SNAG domain By similarity
Region10 – 4031LATS2 binding
Region120 – 15132Required for FBXL14-triggered degradation
Region151 – 264114Required for nuclear localization and interaction with KPNB1, NOTCH1 and PARP1
Motif95 – 1006Destruction motif
Compositional bias90 – 12031Ser-rich

Amino acid modifications

Modified residue111Phosphoserine; by PKA Ref.19
Modified residue821Phosphoserine Ref.19
Modified residue921Phosphoserine; by CK2 Ref.19
Modified residue961Phosphoserine Ref.20
Modified residue1001Phosphoserine Probable
Modified residue1041Phosphoserine Ref.12 Ref.19
Modified residue1071Phosphoserine Ref.12 Ref.19
Modified residue1111Phosphoserine Probable
Modified residue1151Phosphoserine Probable
Modified residue1191Phosphoserine Probable
Modified residue2031Phosphothreonine; by LATS2 Ref.26
Modified residue2461Phosphoserine; by PAK1 Ref.9
Glycosylation1121O-linked (GlcNAc) Ref.15
Cross-link98Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link146Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Natural variations

Natural variant661A → V.
Corresponds to variant rs34261470 [ dbSNP | Ensembl ].
VAR_069162
Natural variant1181V → A. Ref.1
Corresponds to variant rs4647958 [ dbSNP | Ensembl ].
VAR_019969

Experimental info

Mutagenesis21P → A: Abolishes repressor activity on E-cadherin/CDH1 promoter and binding to KDM1A. Ref.21
Mutagenesis91K → R: Does not affect E-cadherin/CDH1 repression; when associated with R-16. Ref.10
Mutagenesis111S → A: Abolishes PKA phosphorylation. Strongly decreases repressor activity on E-cadherin/CDH1 and CLDN1 promoters. Increases protein stability. Affects function in EMT. Ref.19
Mutagenesis161K → R: Does not affect E-cadherin repression; when associated with R-9. Ref.10
Mutagenesis921S → 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. Ref.19
Mutagenesis921S → E: Does not affect repressor activity on E-cadherin/CDH1 promoter. Ref.19
Mutagenesis961S → 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. Ref.8 Ref.12 Ref.20 Ref.22
Mutagenesis981K → 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. Ref.10 Ref.18
Mutagenesis1001S → 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. Ref.8 Ref.20 Ref.22
Mutagenesis1041S → 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. Ref.12 Ref.19 Ref.20
Mutagenesis1071S → 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. Ref.8 Ref.12 Ref.19 Ref.20
Mutagenesis1071S → E: Predominantly localized to the cytoplasm; when associated with E-111; E-115 and E-119. Ref.8 Ref.12 Ref.19 Ref.20
Mutagenesis1111S → 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. Ref.8
Mutagenesis1111S → E: Predominantly localized to the cytoplasm; when associated with E-107; E-115 and E-119. Ref.8
Mutagenesis1151S → 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. Ref.8
Mutagenesis1151S → E: Predominantly localized to the cytoplasm; when associated with E-107; E-111 and E-119. Ref.8
Mutagenesis1191S → 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. Ref.8
Mutagenesis1191S → E: Predominantly localized to the cytoplasm; when associated with E-107; E-111 and E-115. Ref.8
Mutagenesis1371K → R: Lower sensitivity to FBXL14-triggered degradation. Lower sensitivity to FBXL14-triggered degradation; when associated to 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. Ref.10 Ref.18
Mutagenesis1461K → 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. Ref.18
Mutagenesis151 – 1522RK → EE: Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1.
Mutagenesis1561C → A: Abolishes binding to KPNB1, KPNA2, IPO7 and TNPO1 and nuclear localization. Ref.14
Mutagenesis1611K → 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. Ref.14
Mutagenesis1701K → 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. Ref.14
Mutagenesis1821C → A: Impairs binding to KPNB1, IPO7 and TNPO1 and abolishes binding to KPNA2. Localizes to cytoplasm and nucleus. Ref.14
Mutagenesis1871K → 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. Ref.14
Mutagenesis1911R → E: Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. Ref.14
Mutagenesis2031T → 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. Ref.26
Mutagenesis2031T → E: Exclusively localizes to the cytoplasm. Reduces capacity to associate with nuclear pore importins. Unable to enter the nucleus. Does not abrogate function. Ref.26
Mutagenesis2101C → A: Impairs binding to KPNB1, IPO7 and TNPO1 and abolishes binding to KPNA2. Localizes to cytoplasm and nucleus. Ref.14
Mutagenesis2151R → E: Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1. No change in subcellular localization. Ref.14
Mutagenesis2201R → 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. Ref.14
Mutagenesis2221N → 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. Ref.14
Mutagenesis2241R → 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. Ref.14
Mutagenesis232 – 2354DVKK → KVEE: Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. Ref.14
Mutagenesis2381C → A: Impairs binding to KPNB1 and IPO7 and abolishes binding to KPNA2 and TNPO1 and nuclear localization. Ref.14
Mutagenesis2391Q → E: Does not affect binding to KPNB1, KPNA2, IPO7, TNPO1 or DNA. Ref.14
Mutagenesis2461S → A: Decreases repression activity on E-cadherin/CDH1, occludin and aromatase promoters. Preferentially localizes to the cytoplasm. Abolishes phosphorylation by PAK1. Ref.9
Sequence conflict461P → L in BAG36039. Ref.4
Sequence conflict1541F → S in AAF32527. Ref.7

Secondary structure

... 264
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O95863 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 70E298C9BB154115

FASTA26429,083
        10         20         30         40         50         60 
MPRSFLVRKP SDPNRKPNYS ELQDSNPEFT FQQPYDQAHL LAAIPPPEIL NPTASLPMLI 

        70         80         90        100        110        120 
WDSVLAPQAQ PIAWASLRLQ ESPRVAELTS LSDEDSGKGS QPPSPPSPAP SSFSSTSVSS 

       130        140        150        160        170        180 
LEAEAYAAFP GLGQVPKQLA QLSEAKDLQA RKAFNCKYCN KEYLSLGALK MHIRSHTLPC 

       190        200        210        220        230        240 
VCGTCGKAFS RPWLLQGHVR THTGEKPFSC PHCSRAFADR SNLRAHLQTH SDVKKYQCQA 

       250        260 
CARTFSRMSL LHKHQESGCS GCPR 

« Hide

References

« Hide 'large scale' references
[1]"Down-regulation of promoter 1.3 activity of the human aromatase gene in breast tissue by zinc-finger protein, snail (SnaH)."
Okubo T., Truong T.K., Yu B., Itoh T., Zhao J., Grube B., Zhou D., Chen S.
Cancer Res. 61:1338-1346(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-118.
Tissue: Mammary gland.
[2]"Characterisation of the human snail (SNAI1) gene and exclusion as a major disease gene in craniosynostosis."
Twigg S.R., Wilkie A.O.M.
Hum. Genet. 105:320-326(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Genomic organization, expression, and chromosome location of the human SNAIL gene (SNAI1) and a related processed pseudogene (SNAI1P)."
Paznekas W.A., Okajima K., Schertzer M., Wood S., Jabs E.W.
Genomics 62:42-49(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Teratocarcinoma.
[5]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[7]"The transcription factor Snail is a repressor of E-cadherin gene expression in epithelial tumour cells."
Batlle E., Sancho E., Franci C., Dominguez D., Monfar M., Baulida J., Garcia de Herreros A.
Nat. Cell Biol. 2:84-89(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-172, FUNCTION, TISSUE SPECIFICITY.
[8]"Dual regulation of Snail by GSK-3beta-mediated phosphorylation in control of epithelial-mesenchymal transition."
Zhou B.P., Deng J., Xia W., Xu J., Li Y.M., Gunduz M., Hung M.C.
Nat. Cell Biol. 6:931-940(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GSK3B AND BTRC, PHOSPHORYLATION BY GSK3B, UBIQUITINATION BY BTRC, MUTAGENESIS OF SER-96; SER-100; SER-107; SER-111; SER-115 AND SER-119, SUBCELLULAR LOCATION.
[9]"Pak1 phosphorylation of snail, a master regulator of epithelial-to-mesenchyme transition, modulates snail's subcellular localization and functions."
Yang Z., Rayala S., Nguyen D., Vadlamudi R.K., Chen S., Kumar R.
Cancer Res. 65:3179-3184(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-246 BY PAK1, MUTAGENESIS OF SER-246.
[10]"A molecular role for lysyl oxidase-like 2 enzyme in snail regulation and tumor progression."
Peinado H., Del Carmen Iglesias-de la Cruz M., Olmeda D., Csiszar K., Fong K.S., Vega S., Nieto M.A., Cano A., Portillo F.
EMBO J. 24:3446-3458(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH LOXL2 AND LOXL3, MUTAGENESIS OF LYS-9; LYS-16; LYS-98 AND LYS-137.
[11]"Zinc finger domain of Snail functions as a nuclear localization signal for importin beta-mediated nuclear import pathway."
Yamasaki H., Sekimoto T., Ohkubo T., Douchi T., Nagata Y., Ozawa M., Yoneda Y.
Genes Cells 10:455-464(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH KPNB1.
[12]"Wnt-dependent regulation of the E-cadherin repressor snail."
Yook J.I., Li X.Y., Ota I., Fearon E.R., Weiss S.J.
J. Biol. Chem. 280:11740-11748(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GSK3B AND BTRC, PHOSPHORYLATION AT SER-104 AND SER-107, MUTAGENESIS OF SER-96; SER-104 AND SER-107.
[13]"Ajuba LIM proteins are snail/slug corepressors required for neural crest development in Xenopus."
Langer E.M., Feng Y., Zhaoyuan H., Rauscher F.J. III, Kroll K.L., Longmore G.D.
Dev. Cell 14:424-436(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LIMD1 AND AJUBA.
[14]"Characterization of Snail nuclear import pathways as representatives of C2H2 zinc finger transcription factors."
Mingot J.M., Vega S., Maestro B., Sanz J.M., Nieto M.A.
J. Cell Sci. 122:1452-1460(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KPNA2; KPNB1; TNPO1 AND IPO7, MUTAGENESIS OF 151-ARG-LYS-152; CYS-156; LYS-161; LYS-170; CYS-182; LYS-187; ARG-191; CYS-210; ARG-215; ARG-220; ASN-222; ARG-224; 232-ASP--LYS-235; CYS-238 AND GLN-239.
[15]"Snail1 is stabilized by O-GlcNAc modification in hyperglycaemic condition."
Park S.Y., Kim H.S., Kim N.H., Ji S., Cha S.Y., Kang J.G., Ota I., Shimada K., Konishi N., Nam H.W., Hong S.W., Yang W.H., Roth J., Yook J.I., Cho J.W.
EMBO J. 29:3787-3796(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT SER-112.
[16]"Snail associates with EGR-1 and SP-1 to upregulate transcriptional activation of p15INK4b."
Hu C.T., Chang T.Y., Cheng C.C., Liu C.S., Wu J.R., Li M.C., Wu W.S.
FEBS J. 277:1202-1218(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EGR1, INDUCTION.
[17]"p53 inhibits tumor cell invasion via the degradation of snail protein in hepatocellular carcinoma."
Lim S.O., Kim H., Jung G.
FEBS Lett. 584:2231-2236(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TP53 AND MDM2, UBIQUITINATION BY MDM2.
[18]"The hypoxia-controlled FBXL14 ubiquitin ligase targets SNAIL1 for proteasome degradation."
Vinas-Castells R., Beltran M., Valls G., Gomez I., Garcia J.M., Montserrat-Sentis B., Baulida J., Bonilla F., de Herreros A.G., Diaz V.M.
J. Biol. Chem. 285:3794-3805(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION BY FBXL14 AND BTRC, INTERACTION WITH FBXL14, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-98; LYS-137 AND LYS-146.
[19]"Phosphorylation of serine 11 and serine 92 as new positive regulators of human Snail1 function: potential involvement of casein kinase-2 and the cAMP-activated kinase protein kinase A."
MacPherson M.R., Molina P., Souchelnytskyi S., Wernstedt C., Martin-Perez J., Portillo F., Cano A.
Mol. Biol. Cell 21:244-253(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CSNK2A1, PHOSPHORYLATION AT SER-11; SER-82; SER-92; SER-104 AND SER-107, MUTAGENESIS OF SER-11; SER-92; SER-104 AND SER-107.
[20]"Role of CK1 in GSK3beta-mediated phosphorylation and degradation of snail."
Xu Y., Lee S.H., Kim H.S., Kim N.H., Piao S., Park S.H., Jung Y.S., Yook J.I., Park B.J., Ha N.C.
Oncogene 29:3124-3133(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CSNK1E, PHOSPHORYLATION BY CSNK1E AND GSK3B, PHOSPHORYLATION AT SER-96, MUTAGENESIS OF SER-96; SER-100; SER-104 AND SER-107.
[21]"Requirement of the histone demethylase LSD1 in Snai1-mediated transcriptional repression during epithelial-mesenchymal transition."
Lin T., Ponn A., Hu X., Law B.K., Lu J.
Oncogene 29:4896-4904(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH KDM1A, MUTAGENESIS OF PRO-2.
[22]"Notch1 binds and induces degradation of Snail in hepatocellular carcinoma."
Lim S.O., Kim H.S., Quan X., Ahn S.M., Kim H., Hsieh D., Seong J.K., Jung G.
BMC Biol. 9:83-83(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH NOTCH1 AND MDM2, SUBCELLULAR LOCATION, UBIQUITINATION BY MDM2, MUTAGENESIS OF SER-96 AND SER-100.
[23]"Importin alpha protein acts as a negative regulator for Snail protein nuclear import."
Sekimoto T., Miyamoto Y., Arai S., Yoneda Y.
J. Biol. Chem. 286:15126-15131(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KPNB1; KPNA1; KPNA4 AND KPNA2.
[24]"Poly(ADP-ribose)-dependent regulation of Snail1 protein stability."
Rodriguez M.I., Gonzalez-Flores A., Dantzer F., Collard J., de Herreros A.G., Oliver F.J.
Oncogene 30:4365-4372(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PARP1, SUBCELLULAR LOCATION, ADP-RIBOSYLATION BY PARP1.
[25]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"Lats2 kinase potentiates Snail1 activity by promoting nuclear retention upon phosphorylation."
Zhang K., Rodriguez-Aznar E., Yabuta N., Owen R.J., Mingot J.M., Nojima H., Nieto M.A., Longmore G.D.
EMBO J. 31:29-43(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-203 BY LATS2, MUTAGENESIS OF THR-203.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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. Translation: CAC07340.1.
BC012910 mRNA. Translation: AAH12910.1.
AF131208 mRNA. Translation: AAF32527.1.
RefSeqNP_005976.2. NM_005985.3.
UniGeneHs.48029.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y48X-ray3.00C2-21[»]
3W5KX-ray2.60B1-264[»]
ProteinModelPortalO95863.
SMRO95863. Positions 125-259.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112499. 28 interactions.
DIPDIP-50870N.
IntActO95863. 16 interactions.
MINTMINT-7384880.
STRING9606.ENSP00000244050.

PTM databases

PhosphoSiteO95863.

Proteomic databases

PaxDbO95863.
PRIDEO95863.

Protocols and materials databases

DNASU6615.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000244050; ENSP00000244050; ENSG00000124216.
GeneID6615.
KEGGhsa:6615.
UCSCuc002xuz.3. human.

Organism-specific databases

CTD6615.
GeneCardsGC20P048599.
HGNCHGNC:11128. SNAI1.
HPACAB005883.
MIM604238. gene.
neXtProtNX_O95863.
PharmGKBPA35977.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5048.
HOGENOMHOG000261665.
HOVERGENHBG007477.
InParanoidO95863.
KOK05707.
OMAPYDQAHL.
OrthoDBEOG7P2XSG.
PhylomeDBO95863.
TreeFamTF315515.

Gene expression databases

BgeeO95863.
CleanExHS_SNAI1.
GenevestigatorO95863.

Family and domain databases

Gene3D3.30.160.60. 3 hits.
InterProIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamPF00096. zf-C2H2. 1 hit.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 4 hits.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO95863.
GeneWikiSNAI1.
GenomeRNAi6615.
NextBio25757.
PROO95863.
SOURCESearch...

Entry information

Entry nameSNAI1_HUMAN
AccessionPrimary (citable) accession number: O95863
Secondary accession number(s): B2R842 expand/collapse secondary AC list , Q9P113, Q9UBP7, Q9UHH7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: December 1, 2000
Last modified: April 16, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM