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Protein

Zinc finger protein SNAI1

Gene

SNAI1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. 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.6 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri154 – 176C2H2-type 1PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri178 – 202C2H2-type 2PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri208 – 230C2H2-type 3PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri236 – 259C2H2-type 4; atypicalPROSITE-ProRule annotationAdd BLAST24

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000124216-MONOMER.
SIGNORiO95863.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:11128. SNAI1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2P → A: Abolishes repressor activity on E-cadherin/CDH1 promoter and binding to KDM1A. 1 Publication1
Mutagenesisi9K → R: Does not affect E-cadherin/CDH1 repression; when associated with R-16. 1 Publication1
Mutagenesisi11S → A: Abolishes PKA phosphorylation. Strongly decreases repressor activity on E-cadherin/CDH1 and CLDN1 promoters. Increases protein stability. Affects function in EMT. 1 Publication1
Mutagenesisi16K → R: Does not affect E-cadherin repression; when associated with R-9. 1 Publication1
Mutagenesisi92S → 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 Publication1
Mutagenesisi92S → E: Does not affect repressor activity on E-cadherin/CDH1 promoter. 1 Publication1
Mutagenesisi96S → 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 Publications1
Mutagenesisi98K → 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 Publications1
Mutagenesisi100S → 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 Publications1
Mutagenesisi104S → 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 Publications1
Mutagenesisi107S → 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 Publications1
Mutagenesisi107S → E: Predominantly localized to the cytoplasm; when associated with E-111; E-115 and E-119. 4 Publications1
Mutagenesisi111S → 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 Publication1
Mutagenesisi111S → E: Predominantly localized to the cytoplasm; when associated with E-107; E-115 and E-119. 1 Publication1
Mutagenesisi115S → 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 Publication1
Mutagenesisi115S → E: Predominantly localized to the cytoplasm; when associated with E-107; E-111 and E-119. 1 Publication1
Mutagenesisi119S → 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 Publication1
Mutagenesisi119S → E: Predominantly localized to the cytoplasm; when associated with E-107; E-111 and E-115. 1 Publication1
Mutagenesisi137K → 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 Publications1
Mutagenesisi146K → 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 Publication1
Mutagenesisi151 – 152RK → EE: Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. 1 Publication2
Mutagenesisi156C → A: Abolishes binding to KPNB1, KPNA2, IPO7 and TNPO1 and nuclear localization. 1 Publication1
Mutagenesisi161K → 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 Publication1
Mutagenesisi170K → 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 Publication1
Mutagenesisi182C → A: Impairs binding to KPNB1, IPO7 and TNPO1 and abolishes binding to KPNA2. Localizes to cytoplasm and nucleus. 1 Publication1
Mutagenesisi187K → 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 Publication1
Mutagenesisi191R → 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 Publication1
Mutagenesisi191R → E: Mildly reduces binding to KPNB1. Does not affect binding to KPNA2, IPO7 or TNPO1. 1 Publication1
Mutagenesisi193W → 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 Publication1
Mutagenesisi196Q → A: Loss of binding to KPNB1 and nuclear import; when associated with E-191 and A-193. 1 Publication1
Mutagenesisi203T → 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 Publication1
Mutagenesisi203T → E: Exclusively localizes to the cytoplasm. Reduces capacity to associate with nuclear pore importins. Unable to enter the nucleus. Does not abrogate function. 1 Publication1
Mutagenesisi210C → A: Impairs binding to KPNB1, IPO7 and TNPO1 and abolishes binding to KPNA2. Localizes to cytoplasm and nucleus. 1 Publication1
Mutagenesisi215R → E: Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1. No change in subcellular localization. 1 Publication1
Mutagenesisi220R → 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 Publication1
Mutagenesisi222N → 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 Publication1
Mutagenesisi224R → 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 Publication1
Mutagenesisi224R → E: Mildly reduces binding to KPNB1 and nuclear import. Strongly reduces binding to KPNB1 and nuclear import; when associated with A-228. 1 Publication1
Mutagenesisi228Q → 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 Publication1
Mutagenesisi232 – 235DVKK → KVEE: Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. 1 Publication4
Mutagenesisi238C → A: Impairs binding to KPNB1 and IPO7 and abolishes binding to KPNA2 and TNPO1 and nuclear localization. 1 Publication1
Mutagenesisi239Q → E: Does not affect binding to KPNB1, KPNA2, IPO7, TNPO1 or DNA. 1 Publication1
Mutagenesisi246S → A: Decreases repression activity on E-cadherin/CDH1, occludin and aromatase promoters. Preferentially localizes to the cytoplasm. Abolishes phosphorylation by PAK1. 1 Publication1
Mutagenesisi247R → E: Mildly reduces binding to KPNB1 and nuclear import. 1 Publication1

Organism-specific databases

DisGeNETi6615.
OpenTargetsiENSG00000124216.
PharmGKBiPA35977.

Polymorphism and mutation databases

BioMutaiSNAI1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000470291 – 264Zinc finger protein SNAI1Add BLAST264

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei11Phosphoserine; by PKA1 Publication1
Modified residuei82Phosphoserine1 Publication1
Modified residuei92Phosphoserine; by CK21 Publication1
Modified residuei96Phosphoserine1 Publication1
Cross-linki98Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei100PhosphoserineCurated1
Modified residuei104Phosphoserine2 Publications1
Modified residuei107Phosphoserine2 Publications1
Modified residuei111PhosphoserineCurated1
Glycosylationi112O-linked (GlcNAc)1 Publication1
Modified residuei115PhosphoserineCurated1
Modified residuei119PhosphoserineCurated1
Cross-linki137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-linki146Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei203Phosphothreonine; by LATS21 Publication1
Modified residuei246Phosphoserine; by PAK11 Publication1

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.3 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

EPDiO95863.
PaxDbiO95863.
PeptideAtlasiO95863.
PRIDEiO95863.

PTM databases

iPTMnetiO95863.
PhosphoSitePlusiO95863.

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

BgeeiENSG00000124216.
CleanExiHS_SNAI1.
GenevisibleiO95863. HS.

Organism-specific databases

HPAiCAB005883.

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

WithEntry#Exp.IntActNotes
ACTN2P356095EBI-1045459,EBI-77797
AJUBAQ96IF13EBI-1045459,EBI-949782
BTRCQ9Y2972EBI-1045459,EBI-307461
CREBBPQ927939EBI-1045459,EBI-81215
CrebbpP454817EBI-1045459,EBI-296306From a different organism.
EP300Q094723EBI-1045459,EBI-447295
FBXL14Q8N1E62EBI-1045459,EBI-6425532
FBXO11Q86XK26EBI-1045459,EBI-1047804
GSK3BP498415EBI-1045459,EBI-373586
HDAC1Q135473EBI-1045459,EBI-301834
HDAC2Q927692EBI-1045459,EBI-301821
KDM1AO6034132EBI-1045459,EBI-710124
KRT31Q153233EBI-1045459,EBI-948001
KRT40Q6A1623EBI-1045459,EBI-10171697
MID2Q9UJV3-23EBI-1045459,EBI-10172526
MTUS2Q5JR593EBI-1045459,EBI-742948
NOTCH2NLQ7Z3S93EBI-1045459,EBI-945833
PARP1P0987410EBI-1045459,EBI-355676
RELAQ042065EBI-1045459,EBI-73886
SOCS3O145433EBI-1045459,EBI-714146
SPSB1Q96BD63EBI-1045459,EBI-2659201
TP53P046372EBI-1045459,EBI-366083
TRIM23P364063EBI-1045459,EBI-740098
TRIM5Q9C0353EBI-1045459,EBI-924214

GO - Molecular functioni

  • kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112499. 58 interactors.
DIPiDIP-50870N.
IntActiO95863. 50 interactors.
MINTiMINT-7384880.
STRINGi9606.ENSP00000244050.

Structurei

Secondary structure

1264
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 5Combined sources3
Turni157 – 159Combined sources3
Beta strandi163 – 165Combined sources3
Helixi166 – 173Combined sources8
Helixi174 – 176Combined sources3
Beta strandi183 – 185Combined sources3
Beta strandi188 – 191Combined sources4
Helixi192 – 200Combined sources9
Turni211 – 213Combined sources3
Beta strandi216 – 219Combined sources4
Helixi220 – 227Combined sources8
Turni239 – 241Combined sources3
Beta strandi244 – 247Combined sources4
Helixi248 – 256Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Y48X-ray3.00C2-21[»]
3W5KX-ray2.60B1-264[»]
4QLIX-ray1.45B175-180[»]
ProteinModelPortaliO95863.
SMRiO95863.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO95863.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 20SNAG domainBy similarityAdd BLAST20
Regioni10 – 40LATS2 bindingAdd BLAST31
Regioni120 – 151Required for FBXL14-triggered degradationAdd BLAST32
Regioni151 – 264Required for nuclear localization and interaction with KPNB1, NOTCH1 and PARP12 PublicationsAdd BLAST114

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi95 – 100Destruction motif6

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi90 – 120Ser-richAdd BLAST31

Sequence similaritiesi

Contains 4 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri154 – 176C2H2-type 1PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri178 – 202C2H2-type 2PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri208 – 230C2H2-type 3PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri236 – 259C2H2-type 4; atypicalPROSITE-ProRule annotationAdd BLAST24

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG2462. Eukaryota.
ENOG41106JS. LUCA.
GeneTreeiENSGT00390000011027.
HOGENOMiHOG000261665.
HOVERGENiHBG007477.
InParanoidiO95863.
KOiK05707.
OMAiQPIGWAS.
OrthoDBiEOG091G0Q0V.
PhylomeDBiO95863.
TreeFamiTF315515.

Family and domain databases

Gene3Di3.30.160.60. 4 hits.
InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF00096. zf-C2H2. 1 hit.
PF13912. zf-C2H2_6. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 4 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O95863-1 [UniParc]FASTAAdd to basket

« Hide

        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 keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti46P → L in BAG36039 (PubMed:14702039).Curated1
Sequence conflicti154F → S in AAF32527 (PubMed:10655587).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06916266A → V.Corresponds to variant rs34261470dbSNPEnsembl.1
Natural variantiVAR_019969118V → A.1 PublicationCorresponds to variant rs4647958dbSNPEnsembl.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. Translation: CAC07340.1.
BC012910 mRNA. Translation: AAH12910.1.
AF131208 mRNA. Translation: AAF32527.1.
CCDSiCCDS13423.1.
RefSeqiNP_005976.2. NM_005985.3.
UniGeneiHs.48029.

Genome annotation databases

EnsembliENST00000244050; ENSP00000244050; ENSG00000124216.
GeneIDi6615.
KEGGihsa:6615.
UCSCiuc002xuz.4. human.

Keywords - Coding sequence diversityi

Polymorphism

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. Translation: CAC07340.1.
BC012910 mRNA. Translation: AAH12910.1.
AF131208 mRNA. Translation: AAF32527.1.
CCDSiCCDS13423.1.
RefSeqiNP_005976.2. NM_005985.3.
UniGeneiHs.48029.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Y48X-ray3.00C2-21[»]
3W5KX-ray2.60B1-264[»]
4QLIX-ray1.45B175-180[»]
ProteinModelPortaliO95863.
SMRiO95863.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112499. 58 interactors.
DIPiDIP-50870N.
IntActiO95863. 50 interactors.
MINTiMINT-7384880.
STRINGi9606.ENSP00000244050.

PTM databases

iPTMnetiO95863.
PhosphoSitePlusiO95863.

Polymorphism and mutation databases

BioMutaiSNAI1.

Proteomic databases

EPDiO95863.
PaxDbiO95863.
PeptideAtlasiO95863.
PRIDEiO95863.

Protocols and materials databases

DNASUi6615.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000244050; ENSP00000244050; ENSG00000124216.
GeneIDi6615.
KEGGihsa:6615.
UCSCiuc002xuz.4. human.

Organism-specific databases

CTDi6615.
DisGeNETi6615.
GeneCardsiSNAI1.
HGNCiHGNC:11128. SNAI1.
HPAiCAB005883.
MIMi604238. gene.
neXtProtiNX_O95863.
OpenTargetsiENSG00000124216.
PharmGKBiPA35977.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2462. Eukaryota.
ENOG41106JS. LUCA.
GeneTreeiENSGT00390000011027.
HOGENOMiHOG000261665.
HOVERGENiHBG007477.
InParanoidiO95863.
KOiK05707.
OMAiQPIGWAS.
OrthoDBiEOG091G0Q0V.
PhylomeDBiO95863.
TreeFamiTF315515.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000124216-MONOMER.
SIGNORiO95863.

Miscellaneous databases

EvolutionaryTraceiO95863.
GeneWikiiSNAI1.
GenomeRNAii6615.
PROiO95863.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000124216.
CleanExiHS_SNAI1.
GenevisibleiO95863. HS.

Family and domain databases

Gene3Di3.30.160.60. 4 hits.
InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF00096. zf-C2H2. 1 hit.
PF13912. zf-C2H2_6. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 4 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSNAI1_HUMAN
AccessioniPrimary (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 30, 2016
This is version 170 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Caution

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.