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Zinc finger protein SNAI1 (Protein snail homolog 1) (Protein sna)

 SNAI1_MOUSE             Reviewed;         264 AA.
Q02085;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
17-JUN-2020, entry version 168.
RecName: Full=Zinc finger protein SNAI1;
AltName: Full=Protein snail homolog 1;
Short=Protein sna;
Name=Snai1; Synonyms=Sna;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Embryo;
PubMed=1295727;
Smith D.E., del Amo F.F., Gridley T.;
"Isolation of Sna, a mouse gene homologous to the Drosophila genes snail
and escargot: its expression pattern suggests multiple roles during
postimplantation development.";
Development 116:1033-1039(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1483390;
Nieto A.M., Bennett M.F., Sargent M.G., Wilkinson D.G.;
"Cloning and developmental expression of Sna, a murine homologue of the
Drosophila snail gene.";
Development 116:227-237(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II; TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
STRAIN=129/Sv;
PubMed=9271672; DOI=10.1007/s003359900537;
Jiang R., Copeland N.G., Gilbert D.J., Jenkins N.A., Gridley T.;
"Genomic organization and chromosomal localization of the mouse snail (Sna)
gene.";
Mamm. Genome 8:686-688(1997).
[5]
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=10655586; DOI=10.1038/35000025;
Cano A., Perez-Moreno M.A., Rodrigo I., Locascio A., Blanco M.J.,
del Barrio M.G., Portillo F., Nieto M.A.;
"The transcription factor snail controls epithelial-mesenchymal transitions
by repressing E-cadherin expression.";
Nat. Cell Biol. 2:76-83(2000).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=11689706; DOI=10.1128/mcb.21.23.8184-8188.2001;
Carver E.A., Jiang R., Lan Y., Oram K.F., Gridley T.;
"The mouse snail gene encodes a key regulator of the epithelial-mesenchymal
transition.";
Mol. Cell. Biol. 21:8184-8188(2001).
[7]
SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=12832491; DOI=10.1128/mcb.23.14.5078-5089.2003;
Dominguez D., Montserrat-Sentis B., Virgos-Soler A., Guaita S., Grueso J.,
Porta M., Puig I., Baulida J., Franci C., Garcia de Herreros A.;
"Phosphorylation regulates the subcellular location and activity of the
snail transcriptional repressor.";
Mol. Cell. Biol. 23:5078-5089(2003).
[8]
INTERACTION WITH LIMD1; WTIP AND AJUBA.
PubMed=18331720; DOI=10.1016/j.devcel.2008.01.005;
Langer E.M., Feng Y., Zhaoyuan H., Rauscher F.J. III, Kroll K.L.,
Longmore G.D.;
"Ajuba LIM proteins are snail/slug corepressors required for neural crest
development in Xenopus.";
Dev. Cell 14:424-436(2008).
[9]
INTERACTION WITH KPNA2.
PubMed=19386897; DOI=10.1242/jcs.041749;
Mingot J.M., Vega S., Maestro B., Sanz J.M., Nieto M.A.;
"Characterization of Snail nuclear import pathways as representatives of
C2H2 zinc finger transcription factors.";
J. Cell Sci. 122:1452-1460(2009).
[10]
UBIQUITINATION BY FBXL14.
PubMed=19955572; DOI=10.1074/jbc.m109.065995;
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.;
"The hypoxia-controlled FBXL14 ubiquitin ligase targets SNAIL1 for
proteasome degradation.";
J. Biol. Chem. 285:3794-3805(2010).
[11]
INTERACTION WITH CSNK2A1.
PubMed=19923321; DOI=10.1091/mbc.e09-06-0504;
MacPherson M.R., Molina P., Souchelnytskyi S., Wernstedt C.,
Martin-Perez J., Portillo F., Cano A.;
"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.";
Mol. Biol. Cell 21:244-253(2010).
[12]
INTERACTION WITH PARP1.
PubMed=21577210; DOI=10.1038/onc.2011.153;
Rodriguez M.I., Gonzalez-Flores A., Dantzer F., Collard J.,
de Herreros A.G., Oliver F.J.;
"Poly(ADP-ribose)-dependent regulation of Snail1 protein stability.";
Oncogene 30:4365-4372(2011).
[13]
FUNCTION.
PubMed=24239292; DOI=10.1016/j.molcel.2013.10.015;
Millanes-Romero A., Herranz N., Perrera V., Iturbide A.,
Loubat-Casanovas J., Gil J., Jenuwein T., Garcia de Herreros A., Peiro S.;
"Regulation of heterochromatin transcription by Snail1/LOXL2 during
epithelial-to-mesenchymal transition.";
Mol. Cell 52:746-757(2013).
-!- 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 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. 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. The N-terminal SNAG domain competes with
histone H3 for the same binding site on the histone demethylase complex
formed by KDM1A and RCOR1, and thereby inhibits demethylation of
histone H3 at 'Lys-4' (in vitro) (By similarity). During EMT, involved
with LOXL2 in negatively regulating pericentromeric heterochromatin
transcription (PubMed:24239292). SNAI1 recruits LOXL2 to
pericentromeric regions to oxidize histone H3 and repress transcription
which leads to release of heterochromatin component CBX5/HP1A, enabling
chromatin reorganization and acquisition of mesenchymal traits
(PubMed:24239292). Associates with EGR1 and SP1 to mediate 12-O-
tetradecanoylphorbol-13-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.
{ECO:0000250|UniProtKB:O95863, ECO:0000269|PubMed:10655586,
ECO:0000269|PubMed:11689706, ECO:0000269|PubMed:24239292}.
-!- SUBUNIT: Interacts with LOXL2 and LOXL3 (By similarity). Interacts with
FBXL14 and GSK3B. Interacts with BTRC; interaction occurs when it is
phosphorylated on the destruction motif. Interacts (via SNAG domain)
with LIMD1 (via LIM domains), WTIP (via LIM domains) and AJUBA (via LIM
domains). 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. {ECO:0000250|UniProtKB:O95863, ECO:0000269|PubMed:18331720,
ECO:0000269|PubMed:19386897, ECO:0000269|PubMed:19923321,
ECO:0000269|PubMed:21577210}.
-!- INTERACTION:
Q02085; P09874: PARP1; Xeno; NbExp=3; IntAct=EBI-6049807, EBI-355676;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12832491}. Cytoplasm
{ECO:0000269|PubMed:12832491}. 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.
{ECO:0000250|UniProtKB:O95863}.
-!- TISSUE SPECIFICITY: While expression is completely absent from non-
invasive cell lines, it is high in invasive and metastatic cell types.
-!- DEVELOPMENTAL STAGE: Postimplantation. Expression is observed in
undifferentiated mesoderm and in tissues undergoing EMTs, namely the
precursors of the neural crest cells and the primitive streak.
{ECO:0000269|PubMed:10655586}.
-!- PTM: 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-104
positively regulates its function in induction of EMT and/or 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. {ECO:0000250|UniProtKB:O95863}.
-!- PTM: 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 p53 is mediated by MDM2 (By similarity).
{ECO:0000250}.
-!- PTM: O-GlcNAcylation at Ser-112 is enhanced in hyperglycaemic
conditions, it opposes phosphorylation by GSK3B, and stabilizes the
protein. {ECO:0000250}.
-!- PTM: ADP-ribosylation by PARP1 increases protein half-life and may be
involved in TGFB-induced SNAI1 up-regulation. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Embryos die early in gestation, exhibiting
defects in gastrulation and mesoderm formation. Recessive lethal
mutation. {ECO:0000269|PubMed:11689706}.
-!- SIMILARITY: Belongs to the snail C2H2-type zinc-finger protein family.
{ECO:0000305}.
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EMBL; M95604; AAA03481.1; -; mRNA.
EMBL; X67253; CAA47675.1; -; mRNA.
EMBL; BC034857; AAH34857.1; -; mRNA.
EMBL; U95961; AAB58054.1; -; Genomic_DNA.
CCDS; CCDS17102.1; -.
PIR; A49149; A49149.
RefSeq; NP_035557.1; NM_011427.3.
SMR; Q02085; -.
BioGRID; 203361; 8.
IntAct; Q02085; 1.
STRING; 10090.ENSMUSP00000050581; -.
iPTMnet; Q02085; -.
PhosphoSitePlus; Q02085; -.
jPOST; Q02085; -.
PaxDb; Q02085; -.
PRIDE; Q02085; -.
Antibodypedia; 3135; 839 antibodies.
Ensembl; ENSMUST00000052631; ENSMUSP00000050581; ENSMUSG00000042821.
GeneID; 20613; -.
KEGG; mmu:20613; -.
UCSC; uc008nzy.1; mouse.
CTD; 6615; -.
MGI; MGI:98330; Snai1.
eggNOG; KOG2462; Eukaryota.
eggNOG; ENOG41106JS; LUCA.
GeneTree; ENSGT00940000154681; -.
HOGENOM; CLU_002678_42_3_1; -.
InParanoid; Q02085; -.
KO; K05707; -.
OMA; EGYVAFP; -.
OrthoDB; 1318335at2759; -.
PhylomeDB; Q02085; -.
TreeFam; TF315515; -.
BioGRID-ORCS; 20613; 6 hits in 14 CRISPR screens.
ChiTaRS; Snai1; mouse.
PRO; PR:Q02085; -.
Proteomes; UP000000589; Chromosome 2.
RNAct; Q02085; protein.
Bgee; ENSMUSG00000042821; Expressed in ectoplacental cone and 207 other tissues.
ExpressionAtlas; Q02085; baseline and differential.
Genevisible; Q02085; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005721; C:pericentric heterochromatin; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IBA:GO_Central.
GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
GO; GO:0070888; F:E-box binding; ISO:MGI.
GO; GO:0019900; F:kinase binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0060536; P:cartilage morphogenesis; IGI:MGI.
GO; GO:0016477; P:cell migration; IGI:MGI.
GO; GO:0001837; P:epithelial to mesenchymal transition; IDA:UniProtKB.
GO; GO:0003198; P:epithelial to mesenchymal transition involved in endocardial cushion formation; IGI:BHF-UCL.
GO; GO:0031069; P:hair follicle morphogenesis; IDA:MGI.
GO; GO:0070828; P:heterochromatin organization; IMP:UniProtKB.
GO; GO:0060972; P:left/right pattern formation; IMP:MGI.
GO; GO:0007498; P:mesoderm development; IMP:MGI.
GO; GO:0001707; P:mesoderm formation; IMP:UniProtKB.
GO; GO:0060806; P:negative regulation of cell differentiation involved in embryonic placenta development; IDA:MGI.
GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; ISO:MGI.
GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0010957; P:negative regulation of vitamin D biosynthetic process; ISO:MGI.
GO; GO:0061314; P:Notch signaling involved in heart development; IGI:BHF-UCL.
GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
GO; GO:0030335; P:positive regulation of cell migration; IMP:BHF-UCL.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:2000810; P:regulation of bicellular tight junction assembly; ISO:MGI.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IGI:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
GO; GO:0060021; P:roof of mouth development; IGI:MGI.
GO; GO:0060707; P:trophoblast giant cell differentiation; IDA:MGI.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
Pfam; PF00096; zf-C2H2; 2.
SMART; SM00355; ZnF_C2H2; 4.
SUPFAM; SSF57667; SSF57667; 3.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
1: Evidence at protein level;
ADP-ribosylation; Cytoplasm; Developmental protein; DNA-binding;
Glycoprotein; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1..264
/note="Zinc finger protein SNAI1"
/id="PRO_0000047030"
ZN_FING 156..176
/note="C2H2-type 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
ZN_FING 180..202
/note="C2H2-type 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
ZN_FING 210..230
/note="C2H2-type 3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
ZN_FING 236..259
/note="C2H2-type 4; atypical"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
REGION 1..20
/note="SNAG domain"
/evidence="ECO:0000305"
REGION 2..7
/note="Required and sufficient for interaction with KDM1A"
/evidence="ECO:0000250|UniProtKB:O95863"
REGION 10..40
/note="LATS2 binding"
/evidence="ECO:0000250"
REGION 120..151
/note="Required for FBXL14-triggered degradation"
/evidence="ECO:0000250"
REGION 151..264
/note="Required for nuclear localization and interaction
with KPNB1, NOTCH1 and PARP1"
/evidence="ECO:0000250"
MOTIF 95..100
/note="Destruction motif"
COMPBIAS 90..120
/note="Ser-rich"
MOD_RES 11
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O95863"
MOD_RES 82
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O95863"
MOD_RES 92
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O95863"
MOD_RES 96
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O95863"
MOD_RES 100
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O95863"
MOD_RES 104
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O95863"
MOD_RES 107
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O95863"
MOD_RES 111
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O95863"
MOD_RES 115
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O95863"
MOD_RES 119
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O95863"
MOD_RES 203
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:O95863"
MOD_RES 246
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O95863"
CARBOHYD 112
/note="O-linked (GlcNAc) serine"
/evidence="ECO:0000250"
CROSSLNK 98
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:O95863"
CROSSLNK 137
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:O95863"
CROSSLNK 146
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:O95863"
CONFLICT 219
/note="D -> V (in Ref. 2; CAA47675)"
/evidence="ECO:0000305"
SEQUENCE 264 AA; 29190 MW; 52E2061224A18DEB CRC64;
MPRSFLVRKP SDPRRKPNYS ELQDACVEFT FQQPYDQAHL LAAIPPPEVL NPAASLPTLI
WDSLLVPQVR PVAWATLPLR ESPKAVELTS LSDEDSGKSS QPPSPPSPAP SSFSSTSASS
LEAEAFIAFP GLGQLPKQLA RLSVAKDPQS RKIFNCKYCN KEYLSLGALK MHIRSHTLPC
VCTTCGKAFS RPWLLQGHVR THTGEKPFSC SHCNRAFADR SNLRAHLQTH SDVKRYQCQA
CARTFSRMSL LHKHQESGCS GGPR


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EIAAB47395 C2H2-like zinc finger protein rearranged in thyroid adenomas,Homo sapiens,Human,RITA,Zinc finger protein 331,Zinc finger protein 361,Zinc finger protein 463,ZNF331,ZNF361,ZNF463
EIAAB47878 HDSG1,Heart development-specific gene 1 protein,Homo sapiens,Human,KOX11,Zinc finger protein 18,Zinc finger protein 535,Zinc finger protein KOX11,Zinc finger protein with KRAB and SCAN domains 6,ZKSCA
EIAAB14743 Fez family zinc finger protein 2,FEZF2,FEZL,FKSG36,Forebrain embryonic zinc finger-like protein 2,Homo sapiens,Human,Zinc finger protein 312,Zinc finger protein Fez-like,ZNF312
EIAAB47275 Homo sapiens,Human,Zinc finger protein 167,Zinc finger protein 448,Zinc finger protein 64,Zinc finger protein with KRAB and SCAN domains 7,ZKSCAN7,ZNF167,ZNF448,ZNF64
CSB-EL021867MO Mouse Zinc finger protein SNAI1(SNAI1) ELISA kit SpeciesMouse 96T
ARP33314_P050 Anti-Zinc finger protein SNAI1 (SNAI1) Species_Reactivity: Human
ARP33314_P100 Anti-Zinc finger protein SNAI1 (SNAI1) Species_Reactivity: Human
CSB-EL021867HU Human Zinc finger protein SNAI1(SNAI1) ELISA kit SpeciesHuman 96T
Pathways :
WP2199: Seed Development
WP1659: Glycine, serine and threonine metabolism
WP232: G Protein Signaling Pathways
WP1049: G Protein Signaling Pathways
WP1713: Two-component system
WP1438: Influenza A virus infection
WP1892: Protein folding
WP1665: Limonene and pinene degradation
WP1675: Nitrogen metabolism
WP346: Protein Modifications
WP1531: Vitamin D synthesis
WP2032: TSH signaling pathway
WP1616: ABC transporters
WP210: Cytoplasmic Ribosomal Proteins
WP1685: Peptidoglycan biosynthesis
WP73: G Protein Signaling Pathways
WP1692: Protein export
WP931: G Protein Signaling Pathways
WP1644: DNA replication
WP2203: TSLP Signaling Pathway
WP1657: Glycerolipid metabolism
WP2292: Chemokine signaling pathway
WP1700: Selenoamino acid metabolism
WP1371: G Protein Signaling Pathways
WP1888: Post-translational protein modification

Related Genes :
[Snai1 Sna] Zinc finger protein SNAI1 (Protein snail homolog 1) (Protein sna)
[SNAI1 SNAH] Zinc finger protein SNAI1 (Protein snail homolog 1) (Protein sna)
[EGR1 KROX24 ZNF225] Early growth response protein 1 (EGR-1) (AT225) (Nerve growth factor-induced protein A) (NGFI-A) (Transcription factor ETR103) (Transcription factor Zif268) (Zinc finger protein 225) (Zinc finger protein Krox-24)
[SNAI2 SLUG SLUGH] Zinc finger protein SNAI2 (Neural crest transcription factor Slug) (Protein snail homolog 2)
[Snai2 Slug Slugh] Zinc finger protein SNAI2 (Neural crest transcription factor Slug) (Protein snail homolog 2)
[Snai2 Slug Slugh] Zinc finger protein SNAI2 (Neural crest transcription factor Slug) (Protein snail homolog 2)
[SNAI2 SLUG] Zinc finger protein SNAI2 (Neural crest transcription factor Slug) (Protein snail homolog 2)
[NOTCH1 TAN1] Neurogenic locus notch homolog protein 1 (Notch 1) (hN1) (Translocation-associated notch protein TAN-1) [Cleaved into: Notch 1 extracellular truncation (NEXT); Notch 1 intracellular domain (NICD)]
[LOXL2] Lysyl oxidase homolog 2 (EC 1.4.3.13) (Lysyl oxidase-like protein 2) (Lysyl oxidase-related protein 2) (Lysyl oxidase-related protein WS9-14)
[Egr1 Egr-1 Krox-24] Early growth response protein 1 (EGR-1) (Nerve growth factor-induced protein A) (NGFI-A) (Transcription factor Zif268) (Zinc finger protein Krox-24)
[Egr1] Early growth response protein 1 (EGR-1) (Nerve growth factor-induced protein A) (NGFI-A) (Transcription factor Zif268) (Zinc finger protein Krox-24)
[Glis2 Gli5 Nkl] Zinc finger protein GLIS2 (GLI-similar 2) (Neuronal Krueppel-like protein) (Zinc finger protein GLI5)
[Notch1 Motch] Neurogenic locus notch homolog protein 1 (Notch 1) (Motch A) (mT14) (p300) [Cleaved into: Notch 1 extracellular truncation (NEXT); Notch 1 intracellular domain (NICD)]
[KMT2A ALL1 CXXC7 HRX HTRX MLL MLL1 TRX1] Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.354) (ALL-1) (CXXC-type zinc finger protein 7) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Trithorax-like protein) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]
[MID2 FXY2 RNF60 TRIM1] Probable E3 ubiquitin-protein ligase MID2 (EC 2.3.2.27) (Midin-2) (Midline defect 2) (Midline-2) (RING finger protein 60) (RING-type E3 ubiquitin transferase MID2) (Tripartite motif-containing protein 1)
[LATS2 KPM] Serine/threonine-protein kinase LATS2 (EC 2.7.11.1) (Kinase phosphorylated during mitosis protein) (Large tumor suppressor homolog 2) (Serine/threonine-protein kinase kpm) (Warts-like kinase)
[GLIS2 NKL] Zinc finger protein GLIS2 (GLI-similar 2) (Neuronal Krueppel-like protein)
[Notch1] Neurogenic locus notch homolog protein 1 (Notch 1) [Cleaved into: Notch 1 extracellular truncation (NEXT); Notch 1 intracellular domain (NICD)]
[NOTCH1] Neurogenic locus notch homolog protein 1 (Notch 1) [Cleaved into: Notch 1 extracellular truncation (NEXT); Notch 1 intracellular domain (NICD)]
[ZNF274 ZKSCAN19 SP2114] Neurotrophin receptor-interacting factor homolog (Zinc finger protein 274) (Zinc finger protein HFB101) (Zinc finger protein with KRAB and SCAN domains 19) (Zinc finger protein zfp2) (Zf2)
[KPNA1 RCH2] Importin subunit alpha-5 (Karyopherin subunit alpha-1) (Nucleoprotein interactor 1) (NPI-1) (RAG cohort protein 2) (SRP1-beta) [Cleaved into: Importin subunit alpha-5, N-terminally processed]
[Loxl2] Lysyl oxidase homolog 2 (EC 1.4.3.13) (Lysyl oxidase-like protein 2)
[Lats2] Serine/threonine-protein kinase LATS2 (EC 2.7.11.1) (Kinase phosphorylated during mitosis protein) (Large tumor suppressor homolog 2) (Serine/threonine-protein kinase kpm)
[Loxl2] Lysyl oxidase homolog 2 (EC 1.4.3.13) (Lysyl oxidase-like protein 2)
[LOXL2] Lysyl oxidase homolog 2 (EC 1.4.3.13) (Lysyl oxidase-like protein 2)
[LOXL2] Lysyl oxidase homolog 2 (EC 1.4.3.13) (Lysyl oxidase-like protein 2)
[DBF4 ASK DBF4A ZDBF1] Protein DBF4 homolog A (Activator of S phase kinase) (Chiffon homolog A) (DBF4-type zinc finger-containing protein 1)
[LOXL2] Lysyl oxidase homolog 2 (EC 1.4.3.13) (Lysyl oxidase-like protein 2)
[Hivep3 KBP1 Kiaa1555 Krc Rc shn3 Zas3] Transcription factor HIVEP3 (Human immunodeficiency virus type I enhancer-binding protein 3 homolog) (KB-binding and recognition component) (Kappa-B and V(D)J recombination signal sequences-binding protein) (Kappa-binding protein 1) (KBP-1) (Recombinant component) (Schnurri-3) (Zinc finger protein ZAS3)
[BCL11A CTIP1 EVI9 KIAA1809 ZNF856] B-cell lymphoma/leukemia 11A (BCL-11A) (B-cell CLL/lymphoma 11A) (COUP-TF-interacting protein 1) (Ecotropic viral integration site 9 protein homolog) (EVI-9) (Zinc finger protein 856)

Bibliography :
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