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Zinc finger protein SNAI2 (Neural crest transcription factor Slug) (Protein snail homolog 2)

 SNAI2_HUMAN             Reviewed;         268 AA.
O43623; B2R6P6; Q53FC1;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
12-SEP-2018, entry version 184.
RecName: Full=Zinc finger protein SNAI2;
AltName: Full=Neural crest transcription factor Slug;
AltName: Full=Protein snail homolog 2;
Name=SNAI2; Synonyms=SLUG, SLUGH;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Melanocyte;
PubMed=10866665; DOI=10.1128/MCB.20.14.5087-5095.2000;
Hemavathy K., Guru S.C., Harris J., Chen J.D., Ip Y.T.;
"Human Slug is a repressor that localizes to sites of active
transcription.";
Mol. Cell. Biol. 20:5087-5095(2000).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9721220; DOI=10.1006/geno.1998.5367;
Cohen M.E., Yin M., Paznekas W.A., Schertzer M., Wood S., Jabs E.W.;
"Human SLUG gene organization, expression, and chromosome map location
on 8q.";
Genomics 51:468-471(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-119.
PubMed=10479723; DOI=10.1016/S1383-5726(99)00002-3;
Stegmann K., Boecker J., Kosan C., Ermert A., Kunz J., Koch M.C.;
"Human transcription factor SLUG: mutation analysis in patients with
neural tube defects and identification of a missense mutation (D119E)
in the Slug subfamily-defining region.";
Mutat. Res. 406:63-69(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
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.,
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Dermoid cancer;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
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).
[8]
FUNCTION.
PubMed=11912130;
Hajra K.M., Chen D.Y., Fearon E.R.;
"The SLUG zinc-finger protein represses E-cadherin in breast cancer.";
Cancer Res. 62:1613-1618(2002).
[9]
INVOLVEMENT IN WS2D.
PubMed=12444107; DOI=10.1093/hmg/11.25.3231;
Sanchez-Martin M., Rodriguez-Garcia A., Perez-Losada J., Sagrera A.,
Read A.P., Sanchez-Garcia I.;
"SLUG (SNAI2) deletions in patients with Waardenburg disease.";
Hum. Mol. Genet. 11:3231-3236(2002).
[10]
INVOLVEMENT IN PBT.
PubMed=12955764; DOI=10.1002/ajmg.a.20345;
Sanchez-Martin M., Perez-Losada J., Rodriguez-Garcia A.,
Gonzalez-Sanchez B., Korf B.R., Kuster W., Moss C., Spritz R.A.,
Sanchez-Garcia I.;
"Deletion of the SLUG (SNAI2) gene results in human piebaldism.";
Am. J. Med. Genet. A 122:125-132(2003).
[11]
FUNCTION.
PubMed=15734731; DOI=10.1074/jbc.M501375200;
Tripathi M.K., Misra S., Khedkar S.V., Hamilton N., Irvin-Wilson C.,
Sharan C., Sealy L., Chaudhuri G.;
"Regulation of BRCA2 gene expression by the SLUG repressor protein in
human breast cells.";
J. Biol. Chem. 280:17163-17171(2005).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=16707493; DOI=10.1074/jbc.M509731200;
Turner F.E., Broad S., Khanim F.L., Jeanes A., Talma S., Hughes S.,
Tselepis C., Hotchin N.A.;
"Slug regulates integrin expression and cell proliferation in human
epidermal keratinocytes.";
J. Biol. Chem. 281:21321-21331(2006).
[13]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=19756381; DOI=10.1007/s00018-009-0149-5;
Lambertini E., Lisignoli G., Torreggiani E., Manferdini C., Gabusi E.,
Franceschetti T., Penolazzi L., Gambari R., Facchini A., Piva R.;
"Slug gene expression supports human osteoblast maturation.";
Cell. Mol. Life Sci. 66:3641-3653(2009).
[14]
INTERACTION WITH KPNA2; KPNB1; TNPO1 AND IPO7, AND MUTAGENESIS OF
LYS-166; LYS-175; LYS-192; ARG-196; ARG-225 AND ARG-229.
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).
[15]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=21182836; DOI=10.1016/j.yexcr.2010.12.011;
Piva R., Manferdini C., Lambertini E., Torreggiani E., Penolazzi L.,
Gambari R., Pastore A., Pelucchi S., Gabusi E., Piacentini A.,
Filardo G., Facchini A., Lisignoli G.;
"Slug contributes to the regulation of CXCL12 expression in human
osteoblasts.";
Exp. Cell Res. 317:1159-1168(2011).
[16]
SUBCELLULAR LOCATION, PHOSPHORYLATION, AND MUTAGENESIS OF SER-87;
SER-92; SER-96; SER-100 AND SER-104.
PubMed=22727060; DOI=10.1111/j.1742-4658.2012.08674.x;
Kim J.Y., Kim Y.M., Yang C.H., Cho S.K., Lee J.W., Cho M.;
"Functional regulation of Slug/Snail2 is dependent on GSK-3beta-
mediated phosphorylation.";
FEBS J. 279:2929-2939(2012).
[17]
SUBCELLULAR LOCATION.
PubMed=25893292; DOI=10.1038/onc.2015.100;
Hwangbo C., Tae N., Lee S., Kim O., Park O.K., Kim J., Kwon S.H.,
Lee J.H.;
"Syntenin regulates TGF-beta1-induced Smad activation and the
epithelial-to-mesenchymal transition by inhibiting caveolin-mediated
TGF-beta type I receptor internalization.";
Oncogene 35:389-401(2016).
-!- FUNCTION: Transcriptional repressor that modulates both activator-
dependent and basal transcription. Involved in the generation and
migration of neural crest cells. Plays a role in mediating RAF1-
induced transcriptional repression of the TJ protein, occludin
(OCLN) and subsequent oncogenic transformation of epithelial cells
(By similarity). Represses BRCA2 expression by binding to its E2-
box-containing silencer and recruiting CTBP1 and HDAC1 in breast
cells. In epidermal keratinocytes, binds to the E-box in ITGA3
promoter and represses its transcription. Involved in the
regulation of ITGB1 and ITGB4 expression and cell adhesion and
proliferation in epidermal keratinocytes. Binds to E-box2 domain
of BSG and activates its expression during TGFB1-induced
epithelial-mesenchymal transition (EMT) in hepatocytes. Represses
E-Cadherin/CDH1 transcription via E-box elements. Involved in
osteoblast maturation. Binds to RUNX2 and SOC9 promoters and may
act as a positive and negative transcription regulator,
respectively, in osteoblasts. Binds to CXCL12 promoter via E-box
regions in mesenchymal stem cells and osteoblasts. Plays an
essential role in TWIST1-induced EMT and its ability to promote
invasion and metastasis. {ECO:0000250,
ECO:0000269|PubMed:10866665, ECO:0000269|PubMed:11912130,
ECO:0000269|PubMed:15734731, ECO:0000269|PubMed:16707493,
ECO:0000269|PubMed:19756381, ECO:0000269|PubMed:21182836}.
-!- SUBUNIT: Interacts (via SNAG domain) with LIMD1 (via LIM domains),
WTIP (via LIM domains) and AJUBA (via LIM domains) (By
similarity). Interacts (via zinc fingers) with KPNA2, KPNB1, and
TNPO1. May interact (via zinc fingers) with IPO7. {ECO:0000250,
ECO:0000269|PubMed:19386897}.
-!- INTERACTION:
P68400:CSNK2A1; NbExp=4; IntAct=EBI-9876238, EBI-347804;
P21673:SAT1; NbExp=3; IntAct=EBI-9876238, EBI-711613;
P36406:TRIM23; NbExp=3; IntAct=EBI-9876238, EBI-740098;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25893292}.
Cytoplasm. Note=Observed in discrete foci in interphase nuclei.
These nuclear foci do not overlap with the nucleoli, the SP100 and
the HP1 heterochromatin or the coiled body, suggesting SNAI2 is
associated with active transcription or active splicing regions.
-!- TISSUE SPECIFICITY: Expressed in most adult human tissues,
including spleen, thymus, prostate, testis, ovary, small
intestine, colon, heart, brain, placenta, lung, liver, skeletal
muscle, kidney and pancreas. Not detected in peripheral blood
leukocyte. Expressed in the dermis and in all layers of the
epidermis, with high levels of expression in the basal layers (at
protein level). Expressed in osteoblasts (at protein level).
Expressed in mesenchymal stem cells (at protein level). Expressed
in breast tumor cells (at protein level).
{ECO:0000269|PubMed:10866665, ECO:0000269|PubMed:16707493,
ECO:0000269|PubMed:19756381, ECO:0000269|PubMed:21182836}.
-!- DOMAIN: Repression activity depends on the C-terminal DNA-binding
zinc fingers and on the N-terminal repression domain.
-!- PTM: GSK3B-mediated phosphorylation results in cytoplasmic
localization and degradation. {ECO:0000269|PubMed:22727060}.
-!- DISEASE: Waardenburg syndrome 2D (WS2D) [MIM:608890]: WS2 is a
genetically heterogeneous, autosomal dominant disorder
characterized by sensorineural deafness, pigmentary disturbances,
and absence of dystopia canthorum. The frequency of deafness is
higher in WS2 than in WS1. {ECO:0000269|PubMed:12444107}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Piebald trait (PBT) [MIM:172800]: Autosomal dominant
genetic developmental abnormality of pigmentation characterized by
congenital patches of white skin and hair that lack melanocytes.
{ECO:0000269|PubMed:12955764}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the snail C2H2-type zinc-finger protein
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/SNAI2ID453.html";
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EMBL; AF042001; AAC34288.1; -; Genomic_DNA.
EMBL; AF084243; AAD55240.1; -; Genomic_DNA.
EMBL; AK312661; BAG35543.1; -; mRNA.
EMBL; AK223368; BAD97088.1; -; mRNA.
EMBL; CH471068; EAW86700.1; -; Genomic_DNA.
EMBL; BC014890; AAH14890.1; -; mRNA.
EMBL; BC015895; AAH15895.1; -; mRNA.
CCDS; CCDS6146.1; -.
RefSeq; NP_003059.1; NM_003068.4.
UniGene; Hs.360174; -.
ProteinModelPortal; O43623; -.
SMR; O43623; -.
BioGrid; 112476; 23.
IntAct; O43623; 5.
STRING; 9606.ENSP00000020945; -.
iPTMnet; O43623; -.
PhosphoSitePlus; O43623; -.
BioMuta; SNAI2; -.
EPD; O43623; -.
PaxDb; O43623; -.
PeptideAtlas; O43623; -.
PRIDE; O43623; -.
ProteomicsDB; 49085; -.
DNASU; 6591; -.
Ensembl; ENST00000020945; ENSP00000020945; ENSG00000019549.
Ensembl; ENST00000642303; ENSP00000494171; ENSG00000019549.
GeneID; 6591; -.
KEGG; hsa:6591; -.
UCSC; uc003xqp.5; human.
CTD; 6591; -.
DisGeNET; 6591; -.
EuPathDB; HostDB:ENSG00000019549.8; -.
GeneCards; SNAI2; -.
HGNC; HGNC:11094; SNAI2.
HPA; CAB011671; -.
MalaCards; SNAI2; -.
MIM; 172800; phenotype.
MIM; 602150; gene.
MIM; 608890; phenotype.
neXtProt; NX_O43623; -.
OpenTargets; ENSG00000019549; -.
Orphanet; 2884; Piebaldism.
Orphanet; 895; Waardenburg syndrome type 2.
PharmGKB; PA35945; -.
eggNOG; KOG2462; Eukaryota.
eggNOG; ENOG41106JS; LUCA.
GeneTree; ENSGT00390000011027; -.
HOGENOM; HOG000261665; -.
HOVERGEN; HBG007477; -.
InParanoid; O43623; -.
KO; K05706; -.
OMA; VIPQPEV; -.
OrthoDB; EOG091G0Q0V; -.
PhylomeDB; O43623; -.
TreeFam; TF315515; -.
Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
SIGNOR; O43623; -.
GeneWiki; SNAI2; -.
GenomeRNAi; 6591; -.
PRO; PR:O43623; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000019549; Expressed in 205 organ(s), highest expression level in tibia.
CleanEx; HS_SNAI2; -.
ExpressionAtlas; O43623; baseline and differential.
Genevisible; O43623; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:UniProtKB.
GO; GO:0003273; P:cell migration involved in endocardial cushion formation; ISS:BHF-UCL.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IDA:BHF-UCL.
GO; GO:0035921; P:desmosome disassembly; IMP:BHF-UCL.
GO; GO:0001837; P:epithelial to mesenchymal transition; IMP:BHF-UCL.
GO; GO:0003198; P:epithelial to mesenchymal transition involved in endocardial cushion formation; ISS:BHF-UCL.
GO; GO:0060429; P:epithelium development; ISS:BHF-UCL.
GO; GO:2000811; P:negative regulation of anoikis; IMP:BHF-UCL.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:BHF-UCL.
GO; GO:0033629; P:negative regulation of cell adhesion mediated by integrin; IC:BHF-UCL.
GO; GO:1900387; P:negative regulation of cell-cell adhesion by negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IMP:BHF-UCL.
GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IMP:BHF-UCL.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISS:BHF-UCL.
GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IMP:BHF-UCL.
GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IDA:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0010957; P:negative regulation of vitamin D biosynthetic process; IDA:BHF-UCL.
GO; GO:0070563; P:negative regulation of vitamin D receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0014032; P:neural crest cell development; IMP:BHF-UCL.
GO; GO:0007219; P:Notch signaling pathway; IMP:BHF-UCL.
GO; GO:0001649; P:osteoblast differentiation; IEP:UniProtKB.
GO; GO:0043473; P:pigmentation; IMP:BHF-UCL.
GO; GO:0030335; P:positive regulation of cell migration; IMP:BHF-UCL.
GO; GO:2000810; P:regulation of bicellular tight junction assembly; IMP:BHF-UCL.
GO; GO:0032642; P:regulation of chemokine production; IMP:BHF-UCL.
GO; GO:0045667; P:regulation of osteoblast differentiation; IMP:BHF-UCL.
GO; GO:0007605; P:sensory perception of sound; IMP:BHF-UCL.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
SMART; SM00355; ZnF_C2H2; 5.
SUPFAM; SSF57667; SSF57667; 4.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Deafness; Developmental protein;
DNA-binding; Metal-binding; Nucleus; Polymorphism; Reference proteome;
Repeat; Repressor; Transcription; Transcription regulation;
Waardenburg syndrome; Zinc; Zinc-finger.
CHAIN 1 268 Zinc finger protein SNAI2.
/FTId=PRO_0000047032.
ZN_FING 128 150 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 159 181 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 185 207 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 213 235 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 241 264 C2H2-type 5; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
REGION 1 20 SNAG domain. {ECO:0000250}.
VARIANT 31 31 P -> T (in dbSNP:rs11544360).
/FTId=VAR_069163.
VARIANT 119 119 D -> E (in a patient with neural tube
defects; dbSNP:rs748917911).
{ECO:0000269|PubMed:10479723}.
/FTId=VAR_009873.
VARIANT 234 234 T -> I (in dbSNP:rs13280993).
/FTId=VAR_069164.
MUTAGEN 87 87 S->A: Increases protein stability. Does
not affect repressor activity on E-
cadherin/CDH1 promoter.
{ECO:0000269|PubMed:22727060}.
MUTAGEN 92 92 S->A: Increases protein stability,
nuclear accumulation and repressor
activity on E-cadherin/CDH1 promoter;
when associated with A-96.
{ECO:0000269|PubMed:22727060}.
MUTAGEN 96 96 S->A: Increases protein stability,
nuclear accumulation and repressor
activity on E-cadherin/CDH1 promoter;
when associated with A-92.
{ECO:0000269|PubMed:22727060}.
MUTAGEN 100 100 S->A: Increases protein stability and
half-life, nuclear accumulation and
repressor activity on E-cadherin/CDH1
promoter; when associated with A-104.
{ECO:0000269|PubMed:22727060}.
MUTAGEN 104 104 S->A: Increases protein stability and
half-life, nuclear accumulation and
repressor activity on E-cadherin/CDH1
promoter; when associated with A-100.
{ECO:0000269|PubMed:22727060}.
MUTAGEN 166 166 K->E: Abolishes binding to KPNA2, KPNB1
and IPO7 and impairs binding to TMPO1;
when associated with E-175.
{ECO:0000269|PubMed:19386897}.
MUTAGEN 175 175 K->E: Abolishes binding to KPNA2, KPNB1
and IPO7 and impairs binding to TMPO1;
when associated with E-166.
{ECO:0000269|PubMed:19386897}.
MUTAGEN 192 192 K->E: Abolishes binding to KPNA2 and
impairs binding to KPNB1, IPO7 and TMPO1;
when associated with E-196.
{ECO:0000269|PubMed:19386897}.
MUTAGEN 196 196 R->E: Abolishes binding to KPNA2 and
impairs binding to KPNB1, IPO7 and TMPO1;
when associated with E-192.
{ECO:0000269|PubMed:19386897}.
MUTAGEN 225 225 R->E: Abolishes binding to KPNA2, KPNB1
and IPO7 and impairs binding to TMPO1;
when associated with E-229.
{ECO:0000269|PubMed:19386897}.
MUTAGEN 229 229 R->E: Abolishes binding to KPNA2, KPNB1
and IPO7 and impairs binding to TMPO1;
when associated with E-225.
{ECO:0000269|PubMed:19386897}.
CONFLICT 126 126 E -> K (in Ref. 5; BAD97088).
{ECO:0000305}.
SEQUENCE 268 AA; 29986 MW; 63F068C8E6B275D4 CRC64;
MPRSFLVKKH FNASKKPNYS ELDTHTVIIS PYLYESYSMP VIPQPEILSS GAYSPITVWT
TAAPFHAQLP NGLSPLSGYS SSLGRVSPPP PSDTSSKDHS GSESPISDEE ERLQSKLSDP
HAIEAEKFQC NLCNKTYSTF SGLAKHKQLH CDAQSRKSFS CKYCDKEYVS LGALKMHIRT
HTLPCVCKIC GKAFSRPWLL QGHIRTHTGE KPFSCPHCNR AFADRSNLRA HLQTHSDVKK
YQCKNCSKTF SRMSLLHKHE ESGCCVAH


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EIAAB38930 Bos taurus,Bovine,Neural crest transcription factor Slug,Protein snail homolog 2,SLUG,SNAI2,Zinc finger protein SNAI2
EIAAB38933 Neural crest transcription factor Slug,Protein snail homolog 2,Rat,Rattus norvegicus,Slug,Slugh,Snai2,Zinc finger protein SNAI2
EIAAB38932 Mouse,Mus musculus,Neural crest transcription factor Slug,Protein snail homolog 2,Slug,Slugh,Snai2,Zinc finger protein SNAI2
EIAAB38931 Homo sapiens,Human,Neural crest transcription factor Slug,Protein snail homolog 2,SLUG,SLUGH,SNAI2,Zinc finger protein SNAI2
18-783-75568 RABBIT ANTI SLUG - SNAI2; Neural crest transcription factor Slug; Snail homolog 2 Polyclonal 0.1 mg
EIAAB26165 Kiaa1106,Mouse,Mus musculus,Myelin transcription factor 1-like protein,MyT1L,Myt1l,MyT1-L,Neural zinc finger factor 1,Nzf1,NZF-1,Png1,Postmitotic neural gene 1 protein,Zinc finger protein Png-1
EIAAB38935 Mouse,Mus musculus,Protein snail homolog 3,Smuc,Snai3,Snail-related gene from muscle cells,Zfp293,Zinc finger protein 293,Zinc finger protein SNAI3
27-822 SNAI2 is a member of the Snail family of C2H2-type zinc finger transcription factors. The protein acts as a transcriptional repressor that binds to E-box motifs and is also likely to repress E-cadheri 0.05 mg
EIAAB47355 Homo sapiens,Human,Neurotrophin receptor-interacting factor homolog,SP2114,Zf2,Zinc finger protein 274,Zinc finger protein HFB101,Zinc finger protein with KRAB and SCAN domains 19,Zinc finger protein
18-003-42276 Zinc finger and BTB domain-containing protein 7B - Zinc finger protein 67 homolog; Zfp-67; Zinc finger protein Th-POK; T-helper-inducing POZ_Krueppel-like factor; Krueppel-related zinc finger protein 0.1 mg Protein A
EIAAB38934 Homo sapiens,Human,Protein snail homolog 3,SNAI3,Zinc finger protein 293,Zinc finger protein SNAI3,ZNF293
EIAAB47194 Homo sapiens,Human,Zf47,ZFP47,Zfp-47,Zinc finger and SCAN domain-containing protein 13,Zinc finger protein 306,Zinc finger protein 309,Zinc finger protein 47 homolog,Zinc finger protein with KRAB and
EIAAB47047 Homo sapiens,Human,hZF5,ZBTB14,ZF5,ZFP161,Zfp-161,Zfp-5,Zinc finger and BTB domain-containing protein 14,Zinc finger protein 161 homolog,Zinc finger protein 478,Zinc finger protein 5 homolog,ZNF478
EIAAB47268 Beta enolase repressor factor 1,G-rich box-binding protein,Mouse,Mus musculus,Transcription factor BFCOL1,Transcription factor ZBP-89,Zbp89,Zfp148,Zinc finger DNA-binding protein 89,Zinc finger protei
EIAAB40110 C2-HC type zinc finger protein r-MyT3,Neural zinc finger factor 3,Nzf3,NZF-3,Rat,Rattus norvegicus,St18,Suppression of tumorigenicity 18 protein
EIAAB29957 BTB_POZ domain zinc finger transcription factor,Homo sapiens,Human,PATZ,PATZ1,POZ-, AT hook-, and zinc finger-containing protein 1,Protein kinase A RI subunit alpha-associated protein,RIAZ,ZBTB19,Zinc
EIAAB47193 Mouse,Mus musculus,SCAN-KRAB-zinc finger protein,Skz1,Zf47,Zfp306,Zfp307,Zfp47,Zfp-47,Zinc finger protein 306,Zinc finger protein 307,Zinc finger protein 47 homolog,Zinc finger protein with KRAB and S
18-003-42356 Zinc finger protein SNAI1 - Protein snail homolog; Protein sna Polyclonal 0.05 mg Aff Pur
EIAAB47360 GC-box-binding zinc finger protein 1,GZP1,Homo sapiens,Human,Transcription factor ZBP-99,ZBP99,Zinc finger DNA-binding protein 99,Zinc finger protein 281,ZNF281
EIAAB47907 GIOT2,GIOT-2,Gonadotropin-inducible ovary transcription repressor 2,Homo sapiens,Human,KOX7,Zinc finger protein 44,Zinc finger protein 55,Zinc finger protein 58,Zinc finger protein KOX7,ZNF44,ZNF55,ZN
28-572 Early Growth Response Protein 1 (EGR1, Krox-24 protein, nerve growth factor-induced protein A, Transcription factor ETR103, Zinc finger protein 225) belongs to the EGR family of C2H2-type zinc-finger 0.1 mg
27-526 Early Growth Response Protein 1 (EGR1, Krox-24 protein, nerve growth factor-induced protein A, Transcription factor ETR103, Zinc finger protein 225) belongs to the EGR family of C2H2-type zinc-finger 0.05 mg
EIAAB26167 Myelin transcription factor 1-like protein,MyT1L,Myt1l,MyT1-L,Neural zinc finger factor 1,Nzf1,NZF-1,Rat,Rattus norvegicus
EIAAB47325 Homo sapiens,Human,ZFP93,Zfp-93,Zinc finger protein 235,Zinc finger protein 270,Zinc finger protein 93 homolog,Zinc finger protein HZF6,ZNF235,ZNF270
EIAAB37218 Homo sapiens,HSal1,Human,SAL1,Sal-1,SALL1,Sal-like protein 1,Spalt-like transcription factor 1,Zinc finger protein 794,Zinc finger protein SALL1,Zinc finger protein Spalt-1,ZNF794


 

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