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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.
13-FEB-2019, entry version 189.
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; 24.
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; -.
H-InvDB; HIX0007497; -.
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; ENSGT00940000154511; -.
HOGENOM; HOG000261665; -.
HOVERGEN; HBG007477; -.
InParanoid; O43623; -.
KO; K05706; -.
OMA; YSPITMW; -.
OrthoDB; 1101977at2759; -.
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.
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:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0003677; F:DNA binding; IBA:GO_Central.
GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:BHF-UCL.
GO; GO:0070888; F:E-box binding; IDA:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0003180; P:aortic valve morphogenesis; TAS:BHF-UCL.
GO; GO:0060536; P:cartilage morphogenesis; IEA:Ensembl.
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:0071479; P:cellular response to ionizing radiation; IEA:Ensembl.
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:0006933; P:negative regulation of cell adhesion involved in substrate-bound cell migration; IEA:Ensembl.
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:2000647; P:negative regulation of stem cell proliferation; IEA:Ensembl.
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:0045600; P:positive regulation of fat cell differentiation; IEA:Ensembl.
GO; GO:0035066; P:positive regulation of histone acetylation; IEA:Ensembl.
GO; GO:2000810; P:regulation of bicellular tight junction assembly; IMP:BHF-UCL.
GO; GO:0060693; P:regulation of branching involved in salivary gland morphogenesis; IEA:Ensembl.
GO; GO:0032642; P:regulation of chemokine production; IMP:BHF-UCL.
GO; GO:0045667; P:regulation of osteoblast differentiation; IMP:BHF-UCL.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
GO; GO:0007605; P:sensory perception of sound; IMP:BHF-UCL.
GO; GO:0050872; P:white fat cell differentiation; IEA:Ensembl.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
Pfam; PF00096; zf-C2H2; 5.
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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Pathways :
WP2199: Seed Development
WP2064: Neural Crest Differentiation
WP2074: Neural Crest Differentiation
WP211: BMP signaling pathway
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair

Related Genes :
[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)
[Snai2 Slug Slugh] Zinc finger protein SNAI2 (Neural crest transcription factor Slug) (Protein snail homolog 2)
[SOX9] Transcription factor SOX-9
[Ajuba Jub] LIM domain-containing protein ajuba
[Wtip] Wilms tumor protein 1-interacting protein (WT1-interacting protein)
[Limd1] LIM domain-containing protein 1
[AJUBA JUB] LIM domain-containing protein ajuba
[LIMD1] LIM domain-containing protein 1
[Snai1 Sna] Zinc finger protein SNAI1 (Protein snail homolog 1) (Protein sna)
[SNAI1 SNAH] Zinc finger protein SNAI1 (Protein snail homolog 1) (Protein sna)
[KPNB1 NTF97] Importin subunit beta-1 (Importin-90) (Karyopherin subunit beta-1) (Nuclear factor p97) (Pore targeting complex 97 kDa subunit) (PTAC97)
[KPNA2 RCH1 SRP1] Importin subunit alpha-1 (Karyopherin subunit alpha-2) (RAG cohort protein 1) (SRP1-alpha)
[RAF1 RAF] RAF proto-oncogene serine/threonine-protein kinase (EC 2.7.11.1) (Proto-oncogene c-RAF) (cRaf) (Raf-1)
[Ajuba Jub] LIM domain-containing protein ajuba
[Raf1 Craf] RAF proto-oncogene serine/threonine-protein kinase (EC 2.7.11.1) (Proto-oncogene c-RAF) (cRaf) (Raf-1)
[WTIP] Wilms tumor protein 1-interacting protein (WT1-interacting protein)
[Raf1 Raf] RAF proto-oncogene serine/threonine-protein kinase (EC 2.7.11.1) (Proto-oncogene c-RAF) (cRaf) (Raf-1)
[RAF1] RAF proto-oncogene serine/threonine-protein kinase (EC 2.7.11.1) (Proto-oncogene c-RAF) (cRaf) (Raf-1)
[RAF1] RAF proto-oncogene serine/threonine-protein kinase (EC 2.7.11.1) (Proto-oncogene c-RAF) (cRaf) (Raf-1)
[KMT2A ALL1 CXXC7 HRX HTRX MLL MLL1 TRX1] Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.43) (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)]
[Limd1] LIM domain-containing protein 1
[LIMD1] LIM domain-containing protein 1
[Kpna2 Rch1] Importin subunit alpha-1 (Importin alpha P1) (Karyopherin subunit alpha-2) (Pendulin) (Pore targeting complex 58 kDa subunit) (PTAC58) (RAG cohort protein 1) (SRP1-alpha)
[CSNK2A1 CK2A1] Casein kinase II subunit alpha (CK II alpha) (EC 2.7.11.1)
[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)
[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)
[Kpnb1 Impnb] Importin subunit beta-1 (Karyopherin subunit beta-1) (Nuclear factor p97) (Pore targeting complex 97 kDa subunit) (PTAC97) (SCG)
[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)

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