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O43623 (SNAI2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Zinc finger protein SNAI2
Alternative name(s):
Neural crest transcription factor Slug
Protein snail homolog 2
Gene names
Name:SNAI2
Synonyms:SLUG, SLUGH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length268 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.8 Ref.11 Ref.12 Ref.13 Ref.15

Subunit structure

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. Ref.14

Subcellular location

Nucleus. 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. Ref.1 Ref.12 Ref.16

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). Ref.1 Ref.12 Ref.13 Ref.15

Domain

Repression activity depends on the C-terminal DNA-binding zinc fingers and on the N-terminal repression domain.

Post-translational modification

GSK3B-mediated phosphorylation results in cytoplasmic localization and degradation.

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9

Piebald trait (PBT) [MIM:172800]: Autosomal dominant genetic developmental abnormality of pigmentation characterized by congenital patches of white skin and hair that lack melanocytes.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10

Sequence similarities

Belongs to the snail C2H2-type zinc-finger protein family.

Contains 5 C2H2-type zinc fingers.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   DiseaseDeafness
Waardenburg syndrome
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionDevelopmental protein
Repressor
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNotch signaling pathway

Inferred from mutant phenotype PubMed 18663143. Source: BHF-UCL

canonical Wnt signaling pathway

Inferred from mutant phenotype PubMed 20128911. Source: UniProtKB

cartilage morphogenesis

Inferred from electronic annotation. Source: Ensembl

cell migration involved in endocardial cushion formation

Inferred from sequence or structural similarity. Source: BHF-UCL

cellular response to epidermal growth factor stimulus

Inferred from direct assay PubMed 18716062. Source: BHF-UCL

cellular response to fibroblast growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to ionizing radiation

Inferred from electronic annotation. Source: Ensembl

desmosome disassembly

Inferred from mutant phenotype PubMed 9182671. Source: BHF-UCL

embryo development

Inferred from electronic annotation. Source: Ensembl

epithelial to mesenchymal transition

Inferred from mutant phenotype PubMed 17984306PubMed 9182671. Source: BHF-UCL

epithelial to mesenchymal transition involved in endocardial cushion formation

Inferred from sequence or structural similarity. Source: BHF-UCL

epithelium development

Inferred from sequence or structural similarity PubMed 18716062. Source: BHF-UCL

negative regulation of DNA damage response, signal transduction by p53 class mediator

Inferred from mutant phenotype PubMed 15314165. Source: BHF-UCL

negative regulation of anoikis

Inferred from mutant phenotype PubMed 17984306. Source: BHF-UCL

negative regulation of canonical Wnt signaling pathway

Inferred from direct assay PubMed 19502595. Source: BHF-UCL

negative regulation of catenin import into nucleus

Inferred from direct assay PubMed 19502595. Source: BHF-UCL

negative regulation of cell adhesion involved in substrate-bound cell migration

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell adhesion mediated by integrin

Inferred by curator Ref.12. Source: BHF-UCL

negative regulation of cell-cell adhesion by negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 15737616Ref.12PubMed 17984306. Source: BHF-UCL

negative regulation of chondrocyte differentiation

Inferred from mutant phenotype Ref.13. Source: BHF-UCL

negative regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from sequence or structural similarity PubMed 10518215. Source: BHF-UCL

negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from mutant phenotype PubMed 15314165. Source: BHF-UCL

negative regulation of keratinocyte proliferation

Inferred from direct assay Ref.12. Source: BHF-UCL

negative regulation of stem cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.1Ref.8. Source: BHF-UCL

negative regulation of vitamin D biosynthetic process

Inferred from direct assay PubMed 18485278PubMed 19502595. Source: BHF-UCL

negative regulation of vitamin D receptor signaling pathway

Inferred from direct assay PubMed 19502595. Source: BHF-UCL

neural crest cell development

Inferred from mutant phenotype Ref.9. Source: BHF-UCL

osteoblast differentiation

Inferred from expression pattern PubMed 20128911. Source: UniProtKB

palate development

Inferred from electronic annotation. Source: Ensembl

pigmentation

Inferred from mutant phenotype Ref.9. Source: BHF-UCL

positive regulation of cell migration

Inferred from mutant phenotype PubMed 15314165. Source: BHF-UCL

positive regulation of fat cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of histone acetylation

Inferred from electronic annotation. Source: Ensembl

regulation of branching involved in salivary gland morphogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of chemokine production

Inferred from mutant phenotype Ref.15. Source: BHF-UCL

regulation of osteoblast differentiation

Inferred from mutant phenotype Ref.13Ref.15. Source: BHF-UCL

regulation of tight junction assembly

Inferred from mutant phenotype PubMed 15314165. Source: BHF-UCL

sensory perception of sound

Inferred from mutant phenotype Ref.9. Source: BHF-UCL

white fat cell differentiation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear chromatin

Inferred from direct assay Ref.13. Source: BHF-UCL

nucleus

Inferred from direct assay Ref.1. Source: BHF-UCL

   Molecular_functionRNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription

Inferred from direct assay Ref.1Ref.8Ref.12PubMed 18663143. Source: BHF-UCL

RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

chromatin binding

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

sequence-specific DNA binding

Inferred from direct assay PubMed 10518215Ref.1. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 268268Zinc finger protein SNAI2
PRO_0000047032

Regions

Zinc finger128 – 15023C2H2-type 1
Zinc finger159 – 18123C2H2-type 2
Zinc finger185 – 20723C2H2-type 3
Zinc finger213 – 23523C2H2-type 4
Zinc finger241 – 26424C2H2-type 5; atypical
Region1 – 2020SNAG domain By similarity

Natural variations

Natural variant311P → T.
Corresponds to variant rs11544360 [ dbSNP | Ensembl ].
VAR_069163
Natural variant1191D → E in a patient with neural tube defects. Ref.3
VAR_009873
Natural variant2341T → I.
Corresponds to variant rs13280993 [ dbSNP | Ensembl ].
VAR_069164

Experimental info

Mutagenesis871S → A: Increases protein stability. Does not affect repressor activity on E-cadherin/CDH1 promoter. Ref.16
Mutagenesis921S → A: Increases protein stability, nuclear accumulation and repressor activity on E-cadherin/CDH1 promoter; when associated with A-96. Ref.16
Mutagenesis961S → A: Increases protein stability, nuclear accumulation and repressor activity on E-cadherin/CDH1 promoter; when associated with A-92. Ref.16
Mutagenesis1001S → A: Increases protein stability and half-life, nuclear accumulation and repressor activity on E-cadherin/CDH1 promoter; when associated with A-104. Ref.16
Mutagenesis1041S → A: Increases protein stability and half-life, nuclear accumulation and repressor activity on E-cadherin/CDH1 promoter; when associated with A-100. Ref.16
Mutagenesis1661K → E: Abolishes binding to KPNA2, KPNB1 and IPO7 and impairs binding to TMPO1; when associated with E-175. Ref.14
Mutagenesis1751K → E: Abolishes binding to KPNA2, KPNB1 and IPO7 and impairs binding to TMPO1; when associated with E-166. Ref.14
Mutagenesis1921K → E: Abolishes binding to KPNA2 and impairs binding to KPNB1, IPO7 and TMPO1; when associated with E-196. Ref.14
Mutagenesis1961R → E: Abolishes binding to KPNA2 and impairs binding to KPNB1, IPO7 and TMPO1; when associated with E-192. Ref.14
Mutagenesis2251R → E: Abolishes binding to KPNA2, KPNB1 and IPO7 and impairs binding to TMPO1; when associated with E-229. Ref.14
Mutagenesis2291R → E: Abolishes binding to KPNA2, KPNB1 and IPO7 and impairs binding to TMPO1; when associated with E-225. Ref.14
Sequence conflict1261E → K in BAD97088. Ref.5

Sequences

Sequence LengthMass (Da)Tools
O43623 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 63F068C8E6B275D4

FASTA26829,986
        10         20         30         40         50         60 
MPRSFLVKKH FNASKKPNYS ELDTHTVIIS PYLYESYSMP VIPQPEILSS GAYSPITVWT 

        70         80         90        100        110        120 
TAAPFHAQLP NGLSPLSGYS SSLGRVSPPP PSDTSSKDHS GSESPISDEE ERLQSKLSDP 

       130        140        150        160        170        180 
HAIEAEKFQC NLCNKTYSTF SGLAKHKQLH CDAQSRKSFS CKYCDKEYVS LGALKMHIRT 

       190        200        210        220        230        240 
HTLPCVCKIC GKAFSRPWLL QGHIRTHTGE KPFSCPHCNR AFADRSNLRA HLQTHSDVKK 

       250        260 
YQCKNCSKTF SRMSLLHKHE ESGCCVAH 

« Hide

References

« Hide 'large scale' references
[1]"Human Slug is a repressor that localizes to sites of active transcription."
Hemavathy K., Guru S.C., Harris J., Chen J.D., Ip Y.T.
Mol. Cell. Biol. 20:5087-5095(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Melanocyte.
[2]"Human SLUG gene organization, expression, and chromosome map location on 8q."
Cohen M.E., Yin M., Paznekas W.A., Schertzer M., Wood S., Jabs E.W.
Genomics 51:468-471(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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."
Stegmann K., Boecker J., Kosan C., Ermert A., Kunz J., Koch M.C.
Mutat. Res. 406:63-69(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLU-119.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Dermoid cancer.
[6]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Uterus.
[8]"The SLUG zinc-finger protein represses E-cadherin in breast cancer."
Hajra K.M., Chen D.Y., Fearon E.R.
Cancer Res. 62:1613-1618(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"SLUG (SNAI2) deletions in patients with Waardenburg disease."
Sanchez-Martin M., Rodriguez-Garcia A., Perez-Losada J., Sagrera A., Read A.P., Sanchez-Garcia I.
Hum. Mol. Genet. 11:3231-3236(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN WS2D.
[10]"Deletion of the SLUG (SNAI2) gene results in human piebaldism."
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.
Am. J. Med. Genet. A 122:125-132(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN PBT.
[11]"Regulation of BRCA2 gene expression by the SLUG repressor protein in human breast cells."
Tripathi M.K., Misra S., Khedkar S.V., Hamilton N., Irvin-Wilson C., Sharan C., Sealy L., Chaudhuri G.
J. Biol. Chem. 280:17163-17171(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Slug regulates integrin expression and cell proliferation in human epidermal keratinocytes."
Turner F.E., Broad S., Khanim F.L., Jeanes A., Talma S., Hughes S., Tselepis C., Hotchin N.A.
J. Biol. Chem. 281:21321-21331(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[13]"Slug gene expression supports human osteoblast maturation."
Lambertini E., Lisignoli G., Torreggiani E., Manferdini C., Gabusi E., Franceschetti T., Penolazzi L., Gambari R., Facchini A., Piva R.
Cell. Mol. Life Sci. 66:3641-3653(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[14]"Characterization of Snail nuclear import pathways as representatives of C2H2 zinc finger transcription factors."
Mingot J.M., Vega S., Maestro B., Sanz J.M., Nieto M.A.
J. Cell Sci. 122:1452-1460(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KPNA2; KPNB1; TNPO1 AND IPO7, MUTAGENESIS OF LYS-166; LYS-175; LYS-192; ARG-196; ARG-225 AND ARG-229.
[15]"Slug contributes to the regulation of CXCL12 expression in human osteoblasts."
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.
Exp. Cell Res. 317:1159-1168(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[16]"Functional regulation of Slug/Snail2 is dependent on GSK-3beta-mediated phosphorylation."
Kim J.Y., Kim Y.M., Yang C.H., Cho S.K., Lee J.W., Cho M.
FEBS J. 279:2929-2939(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF SER-87; SER-92; SER-96; SER-100 AND SER-104.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF042001 Genomic DNA. Translation: AAC34288.1.
AF084243 Genomic DNA. Translation: AAD55240.1.
AK312661 mRNA. Translation: BAG35543.1.
AK223368 mRNA. Translation: BAD97088.1.
CH471068 Genomic DNA. Translation: EAW86700.1.
BC014890 mRNA. Translation: AAH14890.1.
BC015895 mRNA. Translation: AAH15895.1.
CCDSCCDS6146.1.
RefSeqNP_003059.1. NM_003068.4.
UniGeneHs.360174.

3D structure databases

ProteinModelPortalO43623.
SMRO43623. Positions 128-264.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112476. 7 interactions.
STRING9606.ENSP00000020945.

PTM databases

PhosphoSiteO43623.

Proteomic databases

PaxDbO43623.
PRIDEO43623.

Protocols and materials databases

DNASU6591.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000020945; ENSP00000020945; ENSG00000019549.
ENST00000396822; ENSP00000380034; ENSG00000019549.
GeneID6591.
KEGGhsa:6591.
UCSCuc003xqp.3. human.

Organism-specific databases

CTD6591.
GeneCardsGC08M049830.
HGNCHGNC:11094. SNAI2.
HPACAB011671.
MIM172800. phenotype.
602150. gene.
608890. phenotype.
neXtProtNX_O43623.
Orphanet2884. Piebaldism.
895. Waardenburg syndrome type 2.
PharmGKBPA35945.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5048.
HOGENOMHOG000261665.
HOVERGENHBG007477.
InParanoidO43623.
KOK05706.
OMAEDEQMLP.
OrthoDBEOG7P2XSG.
PhylomeDBO43623.
TreeFamTF315515.

Gene expression databases

BgeeO43623.
CleanExHS_SNAI2.
GenevestigatorO43623.

Family and domain databases

Gene3D3.30.160.60. 4 hits.
InterProIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamPF00096. zf-C2H2. 1 hit.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 5 hits.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 4 hits.
PS50157. ZINC_FINGER_C2H2_2. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiSNAI2.
GenomeRNAi6591.
NextBio25641.
PROO43623.
SOURCESearch...

Entry information

Entry nameSNAI2_HUMAN
AccessionPrimary (citable) accession number: O43623
Secondary accession number(s): B2R6P6, Q53FC1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: June 1, 1998
Last modified: July 9, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM