SNAI2_HUMAN
ID SNAI2_HUMAN Reviewed; 268 AA.
AC O43623; B2R6P6; Q53FC1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Zinc finger protein SNAI2;
DE AltName: Full=Neural crest transcription factor Slug;
DE AltName: Full=Protein snail homolog 2;
GN Name=SNAI2; Synonyms=SLUG, SLUGH;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Melanocyte;
RX PubMed=10866665; DOI=10.1128/mcb.20.14.5087-5095.2000;
RA Hemavathy K., Guru S.C., Harris J., Chen J.D., Ip Y.T.;
RT "Human Slug is a repressor that localizes to sites of active
RT transcription.";
RL Mol. Cell. Biol. 20:5087-5095(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9721220; DOI=10.1006/geno.1998.5367;
RA Cohen M.E., Yin M., Paznekas W.A., Schertzer M., Wood S., Jabs E.W.;
RT "Human SLUG gene organization, expression, and chromosome map location on
RT 8q.";
RL Genomics 51:468-471(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-119.
RX PubMed=10479723; DOI=10.1016/s1383-5726(99)00002-3;
RA Stegmann K., Boecker J., Kosan C., Ermert A., Kunz J., Koch M.C.;
RT "Human transcription factor SLUG: mutation analysis in patients with neural
RT tube defects and identification of a missense mutation (D119E) in the Slug
RT subfamily-defining region.";
RL Mutat. Res. 406:63-69(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Dermoid cancer;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP FUNCTION.
RX PubMed=11912130;
RA Hajra K.M., Chen D.Y., Fearon E.R.;
RT "The SLUG zinc-finger protein represses E-cadherin in breast cancer.";
RL Cancer Res. 62:1613-1618(2002).
RN [9]
RP INVOLVEMENT IN WS2D.
RX PubMed=12444107; DOI=10.1093/hmg/11.25.3231;
RA Sanchez-Martin M., Rodriguez-Garcia A., Perez-Losada J., Sagrera A.,
RA Read A.P., Sanchez-Garcia I.;
RT "SLUG (SNAI2) deletions in patients with Waardenburg disease.";
RL Hum. Mol. Genet. 11:3231-3236(2002).
RN [10]
RP INVOLVEMENT IN PBT.
RX PubMed=12955764; DOI=10.1002/ajmg.a.20345;
RA Sanchez-Martin M., Perez-Losada J., Rodriguez-Garcia A.,
RA Gonzalez-Sanchez B., Korf B.R., Kuster W., Moss C., Spritz R.A.,
RA Sanchez-Garcia I.;
RT "Deletion of the SLUG (SNAI2) gene results in human piebaldism.";
RL Am. J. Med. Genet. A 122:125-132(2003).
RN [11]
RP FUNCTION.
RX PubMed=15734731; DOI=10.1074/jbc.m501375200;
RA Tripathi M.K., Misra S., Khedkar S.V., Hamilton N., Irvin-Wilson C.,
RA Sharan C., Sealy L., Chaudhuri G.;
RT "Regulation of BRCA2 gene expression by the SLUG repressor protein in human
RT breast cells.";
RL J. Biol. Chem. 280:17163-17171(2005).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16707493; DOI=10.1074/jbc.m509731200;
RA Turner F.E., Broad S., Khanim F.L., Jeanes A., Talma S., Hughes S.,
RA Tselepis C., Hotchin N.A.;
RT "Slug regulates integrin expression and cell proliferation in human
RT epidermal keratinocytes.";
RL J. Biol. Chem. 281:21321-21331(2006).
RN [13]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19756381; DOI=10.1007/s00018-009-0149-5;
RA Lambertini E., Lisignoli G., Torreggiani E., Manferdini C., Gabusi E.,
RA Franceschetti T., Penolazzi L., Gambari R., Facchini A., Piva R.;
RT "Slug gene expression supports human osteoblast maturation.";
RL Cell. Mol. Life Sci. 66:3641-3653(2009).
RN [14]
RP INTERACTION WITH KPNA2; KPNB1; TNPO1 AND IPO7, AND MUTAGENESIS OF LYS-166;
RP LYS-175; LYS-192; ARG-196; ARG-225 AND ARG-229.
RX PubMed=19386897; DOI=10.1242/jcs.041749;
RA Mingot J.M., Vega S., Maestro B., Sanz J.M., Nieto M.A.;
RT "Characterization of Snail nuclear import pathways as representatives of
RT C2H2 zinc finger transcription factors.";
RL J. Cell Sci. 122:1452-1460(2009).
RN [15]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=21182836; DOI=10.1016/j.yexcr.2010.12.011;
RA Piva R., Manferdini C., Lambertini E., Torreggiani E., Penolazzi L.,
RA Gambari R., Pastore A., Pelucchi S., Gabusi E., Piacentini A., Filardo G.,
RA Facchini A., Lisignoli G.;
RT "Slug contributes to the regulation of CXCL12 expression in human
RT osteoblasts.";
RL Exp. Cell Res. 317:1159-1168(2011).
RN [16]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION, AND MUTAGENESIS OF SER-87; SER-92;
RP SER-96; SER-100 AND SER-104.
RX PubMed=22727060; DOI=10.1111/j.1742-4658.2012.08674.x;
RA Kim J.Y., Kim Y.M., Yang C.H., Cho S.K., Lee J.W., Cho M.;
RT "Functional regulation of Slug/Snail2 is dependent on GSK-3beta-mediated
RT phosphorylation.";
RL FEBS J. 279:2929-2939(2012).
RN [17]
RP SUBCELLULAR LOCATION.
RX PubMed=25893292; DOI=10.1038/onc.2015.100;
RA Hwangbo C., Tae N., Lee S., Kim O., Park O.K., Kim J., Kwon S.H., Lee J.H.;
RT "Syntenin regulates TGF-beta1-induced Smad activation and the epithelial-
RT to-mesenchymal transition by inhibiting caveolin-mediated TGF-beta type I
RT receptor internalization.";
RL Oncogene 35:389-401(2016).
CC -!- FUNCTION: Transcriptional repressor that modulates both activator-
CC dependent and basal transcription. Involved in the generation and
CC migration of neural crest cells. Plays a role in mediating RAF1-induced
CC transcriptional repression of the TJ protein, occludin (OCLN) and
CC subsequent oncogenic transformation of epithelial cells (By
CC similarity). Represses BRCA2 expression by binding to its E2-box-
CC containing silencer and recruiting CTBP1 and HDAC1 in breast cells. In
CC epidermal keratinocytes, binds to the E-box in ITGA3 promoter and
CC represses its transcription. Involved in the regulation of ITGB1 and
CC ITGB4 expression and cell adhesion and proliferation in epidermal
CC keratinocytes. Binds to E-box2 domain of BSG and activates its
CC expression during TGFB1-induced epithelial-mesenchymal transition (EMT)
CC in hepatocytes. Represses E-Cadherin/CDH1 transcription via E-box
CC elements. Involved in osteoblast maturation. Binds to RUNX2 and SOC9
CC promoters and may act as a positive and negative transcription
CC regulator, respectively, in osteoblasts. Binds to CXCL12 promoter via
CC E-box regions in mesenchymal stem cells and osteoblasts. Plays an
CC essential role in TWIST1-induced EMT and its ability to promote
CC invasion and metastasis. {ECO:0000250, ECO:0000269|PubMed:10866665,
CC ECO:0000269|PubMed:11912130, ECO:0000269|PubMed:15734731,
CC ECO:0000269|PubMed:16707493, ECO:0000269|PubMed:19756381,
CC ECO:0000269|PubMed:21182836}.
CC -!- SUBUNIT: Interacts (via SNAG domain) with LIMD1 (via LIM domains), WTIP
CC (via LIM domains) and AJUBA (via LIM domains) (By similarity).
CC Interacts (via zinc fingers) with KPNA2, KPNB1, and TNPO1. May interact
CC (via zinc fingers) with IPO7. {ECO:0000250,
CC ECO:0000269|PubMed:19386897}.
CC -!- INTERACTION:
CC O43623; Q9NPB3: CABP2; NbExp=3; IntAct=EBI-9876238, EBI-12011224;
CC O43623; P68400: CSNK2A1; NbExp=3; IntAct=EBI-9876238, EBI-347804;
CC O43623; P21673: SAT1; NbExp=3; IntAct=EBI-9876238, EBI-711613;
CC O43623; P36406: TRIM23; NbExp=3; IntAct=EBI-9876238, EBI-740098;
CC O43623; P36508: ZNF76; NbExp=3; IntAct=EBI-9876238, EBI-7254550;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25893292}. Cytoplasm.
CC Note=Observed in discrete foci in interphase nuclei. These nuclear foci
CC do not overlap with the nucleoli, the SP100 and the HP1 heterochromatin
CC or the coiled body, suggesting SNAI2 is associated with active
CC transcription or active splicing regions.
CC -!- TISSUE SPECIFICITY: Expressed in most adult human tissues, including
CC spleen, thymus, prostate, testis, ovary, small intestine, colon, heart,
CC brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Not
CC detected in peripheral blood leukocyte. Expressed in the dermis and in
CC all layers of the epidermis, with high levels of expression in the
CC basal layers (at protein level). Expressed in osteoblasts (at protein
CC level). Expressed in mesenchymal stem cells (at protein level).
CC Expressed in breast tumor cells (at protein level).
CC {ECO:0000269|PubMed:10866665, ECO:0000269|PubMed:16707493,
CC ECO:0000269|PubMed:19756381, ECO:0000269|PubMed:21182836}.
CC -!- DOMAIN: Repression activity depends on the C-terminal DNA-binding zinc
CC fingers and on the N-terminal repression domain.
CC -!- PTM: GSK3B-mediated phosphorylation results in cytoplasmic localization
CC and degradation. {ECO:0000269|PubMed:22727060}.
CC -!- DISEASE: Waardenburg syndrome 2D (WS2D) [MIM:608890]: WS2 is a
CC genetically heterogeneous, autosomal dominant disorder characterized by
CC sensorineural deafness, pigmentary disturbances, and absence of
CC dystopia canthorum. The frequency of deafness is higher in WS2 than in
CC WS1. {ECO:0000269|PubMed:12444107}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Piebald trait (PBT) [MIM:172800]: Autosomal dominant genetic
CC developmental abnormality of pigmentation characterized by congenital
CC patches of white skin and hair that lack melanocytes.
CC {ECO:0000269|PubMed:12955764}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the snail C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SNAI2ID453.html";
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DR EMBL; AF042001; AAC34288.1; -; Genomic_DNA.
DR EMBL; AF084243; AAD55240.1; -; Genomic_DNA.
DR EMBL; AK312661; BAG35543.1; -; mRNA.
DR EMBL; AK223368; BAD97088.1; -; mRNA.
DR EMBL; CH471068; EAW86700.1; -; Genomic_DNA.
DR EMBL; BC014890; AAH14890.1; -; mRNA.
DR EMBL; BC015895; AAH15895.1; -; mRNA.
DR CCDS; CCDS6146.1; -.
DR RefSeq; NP_003059.1; NM_003068.4.
DR AlphaFoldDB; O43623; -.
DR SMR; O43623; -.
DR BioGRID; 112476; 42.
DR IntAct; O43623; 5.
DR STRING; 9606.ENSP00000380034; -.
DR iPTMnet; O43623; -.
DR PhosphoSitePlus; O43623; -.
DR BioMuta; SNAI2; -.
DR EPD; O43623; -.
DR MassIVE; O43623; -.
DR PaxDb; O43623; -.
DR PeptideAtlas; O43623; -.
DR PRIDE; O43623; -.
DR ProteomicsDB; 49085; -.
DR Antibodypedia; 3182; 1027 antibodies from 43 providers.
DR CPTC; O43623; 2 antibodies.
DR DNASU; 6591; -.
DR Ensembl; ENST00000020945.4; ENSP00000020945.1; ENSG00000019549.13.
DR GeneID; 6591; -.
DR KEGG; hsa:6591; -.
DR MANE-Select; ENST00000020945.4; ENSP00000020945.1; NM_003068.5; NP_003059.1.
DR UCSC; uc003xqp.5; human.
DR CTD; 6591; -.
DR DisGeNET; 6591; -.
DR GeneCards; SNAI2; -.
DR HGNC; HGNC:11094; SNAI2.
DR HPA; ENSG00000019549; Low tissue specificity.
DR MalaCards; SNAI2; -.
DR MIM; 172800; phenotype.
DR MIM; 602150; gene.
DR MIM; 608890; phenotype.
DR neXtProt; NX_O43623; -.
DR OpenTargets; ENSG00000019549; -.
DR Orphanet; 2884; Piebaldism.
DR Orphanet; 895; Waardenburg syndrome type 2.
DR PharmGKB; PA35945; -.
DR VEuPathDB; HostDB:ENSG00000019549; -.
DR eggNOG; KOG2462; Eukaryota.
DR GeneTree; ENSGT00940000154511; -.
DR HOGENOM; CLU_002678_42_3_1; -.
DR InParanoid; O43623; -.
DR OMA; VFFTPHI; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; O43623; -.
DR TreeFam; TF315515; -.
DR PathwayCommons; O43623; -.
DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
DR SignaLink; O43623; -.
DR SIGNOR; O43623; -.
DR BioGRID-ORCS; 6591; 27 hits in 1095 CRISPR screens.
DR GeneWiki; SNAI2; -.
DR GenomeRNAi; 6591; -.
DR Pharos; O43623; Tbio.
DR PRO; PR:O43623; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; O43623; protein.
DR Bgee; ENSG00000019549; Expressed in tibia and 173 other tissues.
DR ExpressionAtlas; O43623; baseline and differential.
DR Genevisible; O43623; HS.
DR GO; GO:0000785; C:chromatin; IDA:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR GO; GO:0070888; F:E-box binding; IDA:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0003180; P:aortic valve morphogenesis; TAS:BHF-UCL.
DR GO; GO:0060536; P:cartilage morphogenesis; IEA:Ensembl.
DR GO; GO:0003273; P:cell migration involved in endocardial cushion formation; ISS:BHF-UCL.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IDA:BHF-UCL.
DR GO; GO:0071479; P:cellular response to ionizing radiation; IEA:Ensembl.
DR GO; GO:0035921; P:desmosome disassembly; IMP:BHF-UCL.
DR GO; GO:0043542; P:endothelial cell migration; IEA:Ensembl.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IMP:BHF-UCL.
DR GO; GO:0003198; P:epithelial to mesenchymal transition involved in endocardial cushion formation; ISS:BHF-UCL.
DR GO; GO:0060429; P:epithelium development; ISS:BHF-UCL.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; IEA:Ensembl.
DR GO; GO:0033028; P:myeloid cell apoptotic process; IEA:Ensembl.
DR GO; GO:2000811; P:negative regulation of anoikis; IMP:BHF-UCL.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:BHF-UCL.
DR GO; GO:0006933; P:negative regulation of cell adhesion involved in substrate-bound cell migration; IEA:Ensembl.
DR GO; GO:0033629; P:negative regulation of cell adhesion mediated by integrin; IDA:BHF-UCL.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IMP:BHF-UCL.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IMP:BHF-UCL.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISS:BHF-UCL.
DR GO; GO:1902034; P:negative regulation of hematopoietic stem cell proliferation; IEA:Ensembl.
DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IMP:BHF-UCL.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IDA:BHF-UCL.
DR GO; GO:0033033; P:negative regulation of myeloid cell apoptotic process; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0010957; P:negative regulation of vitamin D biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0070563; P:negative regulation of vitamin D receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0014032; P:neural crest cell development; IMP:BHF-UCL.
DR GO; GO:0061314; P:Notch signaling involved in heart development; TAS:BHF-UCL.
DR GO; GO:0007219; P:Notch signaling pathway; IMP:BHF-UCL.
DR GO; GO:0001649; P:osteoblast differentiation; IEP:UniProtKB.
DR GO; GO:0043473; P:pigmentation; IMP:BHF-UCL.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:BHF-UCL.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IEA:Ensembl.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IEA:Ensembl.
DR GO; GO:2000810; P:regulation of bicellular tight junction assembly; IMP:BHF-UCL.
DR GO; GO:0060693; P:regulation of branching involved in salivary gland morphogenesis; IEA:Ensembl.
DR GO; GO:0032642; P:regulation of chemokine production; IMP:BHF-UCL.
DR GO; GO:0045667; P:regulation of osteoblast differentiation; IMP:BHF-UCL.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IMP:BHF-UCL.
DR GO; GO:0050872; P:white fat cell differentiation; IEA:Ensembl.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 5.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW Cytoplasm; Deafness; Developmental protein; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Waardenburg syndrome; Zinc; Zinc-finger.
FT CHAIN 1..268
FT /note="Zinc finger protein SNAI2"
FT /id="PRO_0000047032"
FT ZN_FING 128..150
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 159..181
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 185..207
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 213..235
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 241..264
FT /note="C2H2-type 5; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..20
FT /note="SNAG domain"
FT /evidence="ECO:0000250"
FT REGION 80..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 31
FT /note="P -> T (in dbSNP:rs11544360)"
FT /id="VAR_069163"
FT VARIANT 119
FT /note="D -> E (in a patient with neural tube defects;
FT dbSNP:rs748917911)"
FT /evidence="ECO:0000269|PubMed:10479723"
FT /id="VAR_009873"
FT VARIANT 234
FT /note="T -> I (in dbSNP:rs13280993)"
FT /id="VAR_069164"
FT MUTAGEN 87
FT /note="S->A: Increases protein stability. Does not affect
FT repressor activity on E-cadherin/CDH1 promoter."
FT /evidence="ECO:0000269|PubMed:22727060"
FT MUTAGEN 92
FT /note="S->A: Increases protein stability, nuclear
FT accumulation and repressor activity on E-cadherin/CDH1
FT promoter; when associated with A-96."
FT /evidence="ECO:0000269|PubMed:22727060"
FT MUTAGEN 96
FT /note="S->A: Increases protein stability, nuclear
FT accumulation and repressor activity on E-cadherin/CDH1
FT promoter; when associated with A-92."
FT /evidence="ECO:0000269|PubMed:22727060"
FT MUTAGEN 100
FT /note="S->A: Increases protein stability and half-life,
FT nuclear accumulation and repressor activity on E-
FT cadherin/CDH1 promoter; when associated with A-104."
FT /evidence="ECO:0000269|PubMed:22727060"
FT MUTAGEN 104
FT /note="S->A: Increases protein stability and half-life,
FT nuclear accumulation and repressor activity on E-
FT cadherin/CDH1 promoter; when associated with A-100."
FT /evidence="ECO:0000269|PubMed:22727060"
FT MUTAGEN 166
FT /note="K->E: Abolishes binding to KPNA2, KPNB1 and IPO7 and
FT impairs binding to TMPO1; when associated with E-175."
FT /evidence="ECO:0000269|PubMed:19386897"
FT MUTAGEN 175
FT /note="K->E: Abolishes binding to KPNA2, KPNB1 and IPO7 and
FT impairs binding to TMPO1; when associated with E-166."
FT /evidence="ECO:0000269|PubMed:19386897"
FT MUTAGEN 192
FT /note="K->E: Abolishes binding to KPNA2 and impairs binding
FT to KPNB1, IPO7 and TMPO1; when associated with E-196."
FT /evidence="ECO:0000269|PubMed:19386897"
FT MUTAGEN 196
FT /note="R->E: Abolishes binding to KPNA2 and impairs binding
FT to KPNB1, IPO7 and TMPO1; when associated with E-192."
FT /evidence="ECO:0000269|PubMed:19386897"
FT MUTAGEN 225
FT /note="R->E: Abolishes binding to KPNA2, KPNB1 and IPO7 and
FT impairs binding to TMPO1; when associated with E-229."
FT /evidence="ECO:0000269|PubMed:19386897"
FT MUTAGEN 229
FT /note="R->E: Abolishes binding to KPNA2, KPNB1 and IPO7 and
FT impairs binding to TMPO1; when associated with E-225."
FT /evidence="ECO:0000269|PubMed:19386897"
FT CONFLICT 126
FT /note="E -> K (in Ref. 5; BAD97088)"
FT /evidence="ECO:0000305"
SQ 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
