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O95863

- SNAI1_HUMAN

UniProt

O95863 - SNAI1_HUMAN

Protein

Zinc finger protein SNAI1

Gene

SNAI1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 2 (01 Dec 2000)
      Previous versions | rss
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    Functioni

    Involved in induction of the epithelial to mesenchymal transition (EMT), formation and maintenance of embryonic mesoderm, growth arrest, survival and cell migration. Binds to 3 E-boxes of the E-cadherin/CDH1 gene promoter and to the promoters of CLDN7 and KRT8 and, in association with histone demethylase KDM1A which it recruits to the promoters, causes a decrease in dimethylated H3K4 levels and represses transcription. Associates with EGR1 and SP1 to mediate tetradecanoyl phorbol acetate (TPA)-induced up-regulation of CDKN2B, possibly by binding to the CDKN2B promoter region 5'-TCACA-3. In addition, may also activate the CDKN2B promoter by itself.6 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri154 – 17623C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri178 – 20225C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri208 – 23023C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri236 – 25924C2H2-type 4; atypicalPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. kinase binding Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: BHF-UCL
    5. sequence-specific DNA binding Source: Ensembl

    GO - Biological processi

    1. cartilage morphogenesis Source: Ensembl
    2. cell migration Source: Ensembl
    3. epithelial to mesenchymal transition Source: UniProtKB
    4. hair follicle morphogenesis Source: Ensembl
    5. left/right pattern formation Source: Ensembl
    6. mesoderm formation Source: UniProtKB
    7. negative regulation of cell differentiation involved in embryonic placenta development Source: Ensembl
    8. negative regulation of DNA damage response, signal transduction by p53 class mediator Source: BHF-UCL
    9. negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage Source: BHF-UCL
    10. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    11. negative regulation of vitamin D biosynthetic process Source: BHF-UCL
    12. Notch signaling involved in heart development Source: BHF-UCL
    13. osteoblast differentiation Source: UniProtKB
    14. palate development Source: Ensembl
    15. positive regulation of cell migration Source: UniProtKB
    16. positive regulation of epithelial to mesenchymal transition Source: UniProtKB
    17. positive regulation of transcription, DNA-templated Source: UniProtKB
    18. regulation of tight junction assembly Source: BHF-UCL
    19. trophoblast giant cell differentiation Source: Ensembl

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Zinc finger protein SNAI1
    Alternative name(s):
    Protein snail homolog 1
    Short name:
    Protein sna
    Gene namesi
    Name:SNAI1
    Synonyms:SNAH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:11128. SNAI1.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Once phosphorylated (probably on Ser-107, Ser-111, Ser-115 and Ser-119) it is exported from the nucleus to the cytoplasm where subsequent phosphorylation of the destruction motif and ubiquitination involving BTRC occurs.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2 – 21P → A: Abolishes repressor activity on E-cadherin/CDH1 promoter and binding to KDM1A. 1 Publication
    Mutagenesisi9 – 91K → R: Does not affect E-cadherin/CDH1 repression; when associated with R-16. 1 Publication
    Mutagenesisi11 – 111S → A: Abolishes PKA phosphorylation. Strongly decreases repressor activity on E-cadherin/CDH1 and CLDN1 promoters. Increases protein stability. Affects function in EMT. 1 Publication
    Mutagenesisi16 – 161K → R: Does not affect E-cadherin repression; when associated with R-9. 1 Publication
    Mutagenesisi92 – 921S → A: Abolishes CK2 phosphorylation. Strongly decreases repressor activity on E-cadherin/CDH1 and CLDN1 promoters. Increases protein stability. Affects function in cell survival. Abolishes phosphorylation in the serine-rich region; when associated with A-104 and A-107. 1 Publication
    Mutagenesisi92 – 921S → E: Does not affect repressor activity on E-cadherin/CDH1 promoter. 1 Publication
    Mutagenesisi96 – 961S → A: Abolishes recognition and ubiquitination by BTRC which increases steady state level and half-life. Preferentially localizes to the nucleus. Induces a more aggressive tissue invasion program. Lower sensitivity to BTRC-triggered degradation, impairs phosphorylation by GSK3B and does not affect NOTCH1-induced degradation; when associated with A-100. Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-100; A-107; A-111; A-115 and A-119. 4 Publications
    Mutagenesisi98 – 981K → R: No change. Complete loss of sensitivity to FBXL14- and BTRC-triggered degradation and loss of ability to repress E-cadherin/CDH1; when associated with R-137 and R-146. 2 Publications
    Mutagenesisi100 – 1001S → A: Lower sensitivity to BTRC-triggered degradation and impaired phosphorylation by GSK3B; when associated with A-96. Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-96; A-107; A-111; A-115 and A-119. Does not affect NOTCH1-induced degradation; when associated with A-96. Abolishes phosphorylation at S-96. 3 Publications
    Mutagenesisi104 – 1041S → A: Increases protein stability, does not affect repressor activity on E-cadherin/CDH1 promoter, preferentially localizes to the nucleus, induces a more aggressive tissue invasion program and impairs phosphorylation by GSK3B, binding to BTRC and ubiquitination; when associated with A-107. Impairs phosphorylation in the serine-rich domain/region; when associated with A-92 and A-107. Abolishes phosphorylation at S-96. 3 Publications
    Mutagenesisi107 – 1071S → A: Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-111; A-115 and A-119. Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-96; A-100; A-111; A-115 and A-119. Increases protein stability, does not affect repressor activity on E-cadherin promoter, preferentially localizes to the nucleus, induces a more aggressive tissue invasion program and impairs phosphorylation by GSK3B, binding to BTRC and ubiquitination; when associated with A-104. Impairs phosphorylation in the serine-rich region; when associated with A-92 and A-104. Abolishes phosphorylation at S-96. 4 Publications
    Mutagenesisi107 – 1071S → E: Predominantly localized to the cytoplasm; when associated with E-111; E-115 and E-119. 4 Publications
    Mutagenesisi111 – 1111S → A: Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-107; A-115 and A-119. Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-96; A-100; A-107; A-115 and A-119. 1 Publication
    Mutagenesisi111 – 1111S → E: Predominantly localized to the cytoplasm; when associated with E-107; E-115 and E-119. 1 Publication
    Mutagenesisi115 – 1151S → A: Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-107; A-111 and A-119. Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-96; A-100; A-107; A-111 and A-119. 1 Publication
    Mutagenesisi115 – 1151S → E: Predominantly localized to the cytoplasm; when associated with E-107; E-111 and E-119. 1 Publication
    Mutagenesisi119 – 1191S → A: Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-107; A-111 and A-119. Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-96; A-100; A-107; A-111 and A-115. 1 Publication
    Mutagenesisi119 – 1191S → E: Predominantly localized to the cytoplasm; when associated with E-107; E-111 and E-115. 1 Publication
    Mutagenesisi137 – 1371K → R: Lower sensitivity to FBXL14-triggered degradation. Lower sensitivity to FBXL14-triggered degradation; when associated to R-146. Complete loss of sensitivity to FBXL14- and BTRC-triggered degradation and loss of ability to repress E-cadherin; when associated with R-98 and R-146. 2 Publications
    Mutagenesisi146 – 1461K → R: Lower sensitivity to FBXL14-triggered degradation. Lower sensitivity to FBXL14-triggered degradation; when associated with R-137. Complete loss of sensitivity to FBXL14- and BTRC-triggered degradation; when associated with R-98 and R-137. 1 Publication
    Mutagenesisi151 – 1522RK → EE: Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1.
    Mutagenesisi156 – 1561C → A: Abolishes binding to KPNB1, KPNA2, IPO7 and TNPO1 and nuclear localization. 1 Publication
    Mutagenesisi161 – 1611K → E: Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. No change in subcellular localization. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1 and abolishes nuclear localization, DNA binding and repressor activity on E-cadherin/CDH1 promoter; when associated with E-170. Abolishes binding to KPNB1, KPNA2, IPO7 and TNPO1 and nuclear localization; when associated with E-187 and/or E-220. 1 Publication
    Mutagenesisi170 – 1701K → E: Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. No change in subcellular localization. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1 and abolishes nuclear localization, DNA binding and repressor activity on E-cadherin/CDH1 promoter; when associated with E-161. 1 Publication
    Mutagenesisi182 – 1821C → A: Impairs binding to KPNB1, IPO7 and TNPO1 and abolishes binding to KPNA2. Localizes to cytoplasm and nucleus. 1 Publication
    Mutagenesisi187 – 1871K → E: Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1 and abolishes nuclear localization, DNA binding and repressor activity on E-cadherin/CDH1 promoter; when associated with E-191. Abolishes binding to KPNB1, KPNA2, IPO7 and TNPO1 and nuclear localization; when associated with E-161 and/or E-220. 1 Publication
    Mutagenesisi191 – 1911R → E: Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. 1 Publication
    Mutagenesisi203 – 2031T → A: Abolishes LATS2 phosphorylation. Does not affect binding to LATS2. Reduces protein stability. Equally distributed between nucleus and cytoplasm. Increases capacity to associate with nuclear pore importins. Unable to accumulate in the nucleus. Does not abrogate function. 1 Publication
    Mutagenesisi203 – 2031T → E: Exclusively localizes to the cytoplasm. Reduces capacity to associate with nuclear pore importins. Unable to enter the nucleus. Does not abrogate function. 1 Publication
    Mutagenesisi210 – 2101C → A: Impairs binding to KPNB1, IPO7 and TNPO1 and abolishes binding to KPNA2. Localizes to cytoplasm and nucleus. 1 Publication
    Mutagenesisi215 – 2151R → E: Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1. No change in subcellular localization. 1 Publication
    Mutagenesisi220 – 2201R → E: Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. No change in subcellular localization. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1; when associated with E-222 and E-224. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1 and abolishes nuclear localization, DNA binding and repressor activity on E-cadherin/CDH1 promoter; when associated with E-224. Abolishes binding to KPNB1, KPNA2, IPO7 and TNPO1 and nuclear localization; when associated with E-161 and/or E-187. 1 Publication
    Mutagenesisi222 – 2221N → E: Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. No change in subcellular localization. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1; when associated with E-220 and E-224. 1 Publication
    Mutagenesisi224 – 2241R → E: Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. No change in subcellular localization. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1; when associated with E-220 and E-222. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1 and abolishes nuclear localization, DNA binding and repressor activity on E-cadherin/CDH1 promoter; when associated with E-220. 1 Publication
    Mutagenesisi232 – 2354DVKK → KVEE: Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1.
    Mutagenesisi238 – 2381C → A: Impairs binding to KPNB1 and IPO7 and abolishes binding to KPNA2 and TNPO1 and nuclear localization. 1 Publication
    Mutagenesisi239 – 2391Q → E: Does not affect binding to KPNB1, KPNA2, IPO7, TNPO1 or DNA. 1 Publication
    Mutagenesisi246 – 2461S → A: Decreases repression activity on E-cadherin/CDH1, occludin and aromatase promoters. Preferentially localizes to the cytoplasm. Abolishes phosphorylation by PAK1. 1 Publication

    Organism-specific databases

    PharmGKBiPA35977.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 264264Zinc finger protein SNAI1PRO_0000047029Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei11 – 111Phosphoserine; by PKA1 Publication
    Modified residuei82 – 821Phosphoserine1 Publication
    Modified residuei92 – 921Phosphoserine; by CK21 Publication
    Modified residuei96 – 961Phosphoserine1 Publication
    Cross-linki98 – 98Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
    Modified residuei100 – 1001PhosphoserineCurated
    Modified residuei104 – 1041Phosphoserine2 Publications
    Modified residuei107 – 1071Phosphoserine2 Publications
    Modified residuei111 – 1111PhosphoserineCurated
    Glycosylationi112 – 1121O-linked (GlcNAc)1 Publication
    Modified residuei115 – 1151PhosphoserineCurated
    Modified residuei119 – 1191PhosphoserineCurated
    Cross-linki137 – 137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
    Cross-linki146 – 146Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
    Modified residuei203 – 2031Phosphothreonine; by LATS21 Publication
    Modified residuei246 – 2461Phosphoserine; by PAK11 Publication

    Post-translational modificationi

    Phosphorylated by GSK3B. Once phosphorylated, it becomes a target for BTRC ubiquitination. Phosphorylation by CSNK1E, probably at Ser-104, provides the priming site for the subsequent phosphorylation by GSK3B, probably at Ser-100 and Ser-96. Phosphorylation by PAK1 may modulate its transcriptional activity by promoting increased accumulation in the nucleus. Phosphorylation at Ser-11 and Ser-92 positively regulates its functions in induction of EMT and cell survival, respectively. Phosphorylation by LATS2, upon mitotic stress, oncogenic stress or Hippo pathway activation, occurs in the nucleus and promotes nuclear retention and stabilization of total cellular protein level.3 Publications
    Ubiquitinated on Lys-98, Lys-137 and Lys-146 by FBXL14 and BTRC leading to degradation. BTRC-triggered ubiquitination requires previous GSK3B-mediated SNAI1 phosphorylation. Ubiquitination induced upon interaction with NOTCH1 or TP53/p53 is mediated by MDM2.
    O-GlcNAcylation at Ser-112 is enhanced in hyperglycaemic conditions, it opposes phosphorylation by GSK3B, and stabilizes the protein.
    ADP-ribosylation by PARP1 increases protein half-life and may be involved in TGFB-induced SNAI1 up-regulation.

    Keywords - PTMi

    ADP-ribosylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiO95863.
    PRIDEiO95863.

    PTM databases

    PhosphoSiteiO95863.

    Expressioni

    Tissue specificityi

    Expressed in a variety of tissues with the highest expression in kidney. Expressed in mesenchymal and epithelial cell lines.1 Publication

    Inductioni

    Induced by TPA maximally by 2.5-fold at 4 hours, in HepG2 cells (at protein level).1 Publication

    Gene expression databases

    BgeeiO95863.
    CleanExiHS_SNAI1.
    GenevestigatoriO95863.

    Organism-specific databases

    HPAiCAB005883.

    Interactioni

    Subunit structurei

    Interacts with FBXL14 and GSK3B. Interacts with BTRC; interaction occurs when it is phosphorylated on the destruction motif. Interacts (via SNAG domain) with WTIP (via LIM domains) By similarity. Interacts (via SNAG domain) with LIMD1 (via LIM domains), and AJUBA (via LIM domains). Interacts with LOXL2 and LOXL3. Interacts (via N-terminal region) with CSNK2A1. Interacts with EGR1 upon TPA induction. Interacts (via N-terminal region) with LATS2; the interaction is dependent on LATS2 kinase activity but independent of SNAI1 Thr-203 phosphorylation. Interacts (via zinc fingers) with KPNB1 and TNPO1; the interactions mediate nuclear import. Interacts (via zinc fingers) with KPNA1; the interaction disrupts the transport complex with KPNB1 and prevents nuclear import increasing SNAI1 degradation in the cytoplasm. Interacts (via zinc fingers) with KPNA2; the interaction, in combination with KPNB1, mediates nuclear import. Interacts with KPNA4; this interaction mediates nuclear import. May interact (via zinc fingers) with IPO7. Interacts (via zinc fingers) with PARP1; the interaction requires SNAI1 to be poly-ADP-ribosylated and non-phosphorylated (active) by GSK3B. Interacts (via SNAG domain) with KDM1A; the interaction is necessary for the down-regulation of dimethylated H3K4 mark and promoter activity of E-cadherin/CDH1, CDN7 and KRT8. Interacts with TP53/p53 and (via zinc fingers) with NOTCH1 (via intracellular domain); the interactions induce SNAI1 degradation via MDM2-mediated ubiquitination and inhibit SNAI1-induced cell invasion. Interacts with MDM2; the interaction promotes SNAI1 ubiquitination. Interacts (via zinc fingers) with CSNK1E. Interacts with PAK1.By similarity15 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BTRCQ9Y2972EBI-1045459,EBI-307461
    GSK3BP498415EBI-1045459,EBI-373586
    KDM1AO6034132EBI-1045459,EBI-710124
    PARP1P0987410EBI-1045459,EBI-355676
    TP53P046372EBI-1045459,EBI-366083

    Protein-protein interaction databases

    BioGridi112499. 30 interactions.
    DIPiDIP-50870N.
    IntActiO95863. 16 interactions.
    MINTiMINT-7384880.
    STRINGi9606.ENSP00000244050.

    Structurei

    Secondary structure

    1
    264
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 53
    Turni157 – 1593
    Beta strandi163 – 1653
    Helixi166 – 1738
    Helixi174 – 1763
    Beta strandi183 – 1853
    Beta strandi188 – 1914
    Helixi192 – 2009
    Turni211 – 2133
    Beta strandi216 – 2194
    Helixi220 – 2278
    Turni239 – 2413
    Beta strandi244 – 2474
    Helixi248 – 2569

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Y48X-ray3.00C2-21[»]
    3W5KX-ray2.60B1-264[»]
    ProteinModelPortaliO95863.
    SMRiO95863. Positions 116-264.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO95863.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 2020SNAG domainBy similarityAdd
    BLAST
    Regioni10 – 4031LATS2 bindingAdd
    BLAST
    Regioni120 – 15132Required for FBXL14-triggered degradationAdd
    BLAST
    Regioni151 – 264114Required for nuclear localization and interaction with KPNB1, NOTCH1 and PARP1Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi95 – 1006Destruction motif

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi90 – 12031Ser-richAdd
    BLAST

    Sequence similaritiesi

    Contains 4 C2H2-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri154 – 17623C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri178 – 20225C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri208 – 23023C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri236 – 25924C2H2-type 4; atypicalPROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5048.
    HOGENOMiHOG000261665.
    HOVERGENiHBG007477.
    InParanoidiO95863.
    KOiK05707.
    OMAiLPCVCGT.
    OrthoDBiEOG7P2XSG.
    PhylomeDBiO95863.
    TreeFamiTF315515.

    Family and domain databases

    Gene3Di3.30.160.60. 3 hits.
    InterProiIPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view]
    PfamiPF00096. zf-C2H2. 1 hit.
    [Graphical view]
    SMARTiSM00355. ZnF_C2H2. 4 hits.
    [Graphical view]
    PROSITEiPS00028. ZINC_FINGER_C2H2_1. 3 hits.
    PS50157. ZINC_FINGER_C2H2_2. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O95863-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPRSFLVRKP SDPNRKPNYS ELQDSNPEFT FQQPYDQAHL LAAIPPPEIL    50
    NPTASLPMLI WDSVLAPQAQ PIAWASLRLQ ESPRVAELTS LSDEDSGKGS 100
    QPPSPPSPAP SSFSSTSVSS LEAEAYAAFP GLGQVPKQLA QLSEAKDLQA 150
    RKAFNCKYCN KEYLSLGALK MHIRSHTLPC VCGTCGKAFS RPWLLQGHVR 200
    THTGEKPFSC PHCSRAFADR SNLRAHLQTH SDVKKYQCQA CARTFSRMSL 250
    LHKHQESGCS GCPR 264
    Length:264
    Mass (Da):29,083
    Last modified:December 1, 2000 - v2
    Checksum:i70E298C9BB154115
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti46 – 461P → L in BAG36039. (PubMed:14702039)Curated
    Sequence conflicti154 – 1541F → S in AAF32527. (PubMed:10655587)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti66 – 661A → V.
    Corresponds to variant rs34261470 [ dbSNP | Ensembl ].
    VAR_069162
    Natural varianti118 – 1181V → A.1 Publication
    Corresponds to variant rs4647958 [ dbSNP | Ensembl ].
    VAR_019969

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF125377 mRNA. Translation: AAD17332.1.
    AJ245657, AJ245658, AJ245659 Genomic DNA. Translation: CAB52414.1.
    AF155233 Genomic DNA. Translation: AAD52986.1.
    AF177731 Genomic DNA. Translation: AAD52996.1.
    AK313228 mRNA. Translation: BAG36039.1.
    AL121712 Genomic DNA. Translation: CAC07340.1.
    BC012910 mRNA. Translation: AAH12910.1.
    AF131208 mRNA. Translation: AAF32527.1.
    CCDSiCCDS13423.1.
    RefSeqiNP_005976.2. NM_005985.3.
    UniGeneiHs.48029.

    Genome annotation databases

    EnsembliENST00000244050; ENSP00000244050; ENSG00000124216.
    GeneIDi6615.
    KEGGihsa:6615.
    UCSCiuc002xuz.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF125377 mRNA. Translation: AAD17332.1 .
    AJ245657 , AJ245658 , AJ245659 Genomic DNA. Translation: CAB52414.1 .
    AF155233 Genomic DNA. Translation: AAD52986.1 .
    AF177731 Genomic DNA. Translation: AAD52996.1 .
    AK313228 mRNA. Translation: BAG36039.1 .
    AL121712 Genomic DNA. Translation: CAC07340.1 .
    BC012910 mRNA. Translation: AAH12910.1 .
    AF131208 mRNA. Translation: AAF32527.1 .
    CCDSi CCDS13423.1.
    RefSeqi NP_005976.2. NM_005985.3.
    UniGenei Hs.48029.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2Y48 X-ray 3.00 C 2-21 [» ]
    3W5K X-ray 2.60 B 1-264 [» ]
    ProteinModelPortali O95863.
    SMRi O95863. Positions 116-264.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112499. 30 interactions.
    DIPi DIP-50870N.
    IntActi O95863. 16 interactions.
    MINTi MINT-7384880.
    STRINGi 9606.ENSP00000244050.

    PTM databases

    PhosphoSitei O95863.

    Proteomic databases

    PaxDbi O95863.
    PRIDEi O95863.

    Protocols and materials databases

    DNASUi 6615.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000244050 ; ENSP00000244050 ; ENSG00000124216 .
    GeneIDi 6615.
    KEGGi hsa:6615.
    UCSCi uc002xuz.3. human.

    Organism-specific databases

    CTDi 6615.
    GeneCardsi GC20P048599.
    HGNCi HGNC:11128. SNAI1.
    HPAi CAB005883.
    MIMi 604238. gene.
    neXtProti NX_O95863.
    PharmGKBi PA35977.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5048.
    HOGENOMi HOG000261665.
    HOVERGENi HBG007477.
    InParanoidi O95863.
    KOi K05707.
    OMAi LPCVCGT.
    OrthoDBi EOG7P2XSG.
    PhylomeDBi O95863.
    TreeFami TF315515.

    Miscellaneous databases

    EvolutionaryTracei O95863.
    GeneWikii SNAI1.
    GenomeRNAii 6615.
    NextBioi 25757.
    PROi O95863.
    SOURCEi Search...

    Gene expression databases

    Bgeei O95863.
    CleanExi HS_SNAI1.
    Genevestigatori O95863.

    Family and domain databases

    Gene3Di 3.30.160.60. 3 hits.
    InterProi IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view ]
    Pfami PF00096. zf-C2H2. 1 hit.
    [Graphical view ]
    SMARTi SM00355. ZnF_C2H2. 4 hits.
    [Graphical view ]
    PROSITEi PS00028. ZINC_FINGER_C2H2_1. 3 hits.
    PS50157. ZINC_FINGER_C2H2_2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Down-regulation of promoter 1.3 activity of the human aromatase gene in breast tissue by zinc-finger protein, snail (SnaH)."
      Okubo T., Truong T.K., Yu B., Itoh T., Zhao J., Grube B., Zhou D., Chen S.
      Cancer Res. 61:1338-1346(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-118.
      Tissue: Mammary gland.
    2. "Characterisation of the human snail (SNAI1) gene and exclusion as a major disease gene in craniosynostosis."
      Twigg S.R., Wilkie A.O.M.
      Hum. Genet. 105:320-326(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Genomic organization, expression, and chromosome location of the human SNAIL gene (SNAI1) and a related processed pseudogene (SNAI1P)."
      Paznekas W.A., Okajima K., Schertzer M., Wood S., Jabs E.W.
      Genomics 62:42-49(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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.
      , 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].
      Tissue: Teratocarcinoma.
    5. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Testis.
    7. "The transcription factor Snail is a repressor of E-cadherin gene expression in epithelial tumour cells."
      Batlle E., Sancho E., Franci C., Dominguez D., Monfar M., Baulida J., Garcia de Herreros A.
      Nat. Cell Biol. 2:84-89(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-172, FUNCTION, TISSUE SPECIFICITY.
    8. "Dual regulation of Snail by GSK-3beta-mediated phosphorylation in control of epithelial-mesenchymal transition."
      Zhou B.P., Deng J., Xia W., Xu J., Li Y.M., Gunduz M., Hung M.C.
      Nat. Cell Biol. 6:931-940(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GSK3B AND BTRC, PHOSPHORYLATION BY GSK3B, UBIQUITINATION BY BTRC, MUTAGENESIS OF SER-96; SER-100; SER-107; SER-111; SER-115 AND SER-119, SUBCELLULAR LOCATION.
    9. "Pak1 phosphorylation of snail, a master regulator of epithelial-to-mesenchyme transition, modulates snail's subcellular localization and functions."
      Yang Z., Rayala S., Nguyen D., Vadlamudi R.K., Chen S., Kumar R.
      Cancer Res. 65:3179-3184(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-246 BY PAK1, MUTAGENESIS OF SER-246.
    10. "A molecular role for lysyl oxidase-like 2 enzyme in snail regulation and tumor progression."
      Peinado H., Del Carmen Iglesias-de la Cruz M., Olmeda D., Csiszar K., Fong K.S., Vega S., Nieto M.A., Cano A., Portillo F.
      EMBO J. 24:3446-3458(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH LOXL2 AND LOXL3, MUTAGENESIS OF LYS-9; LYS-16; LYS-98 AND LYS-137.
    11. "Zinc finger domain of Snail functions as a nuclear localization signal for importin beta-mediated nuclear import pathway."
      Yamasaki H., Sekimoto T., Ohkubo T., Douchi T., Nagata Y., Ozawa M., Yoneda Y.
      Genes Cells 10:455-464(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH KPNB1.
    12. "Wnt-dependent regulation of the E-cadherin repressor snail."
      Yook J.I., Li X.Y., Ota I., Fearon E.R., Weiss S.J.
      J. Biol. Chem. 280:11740-11748(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH GSK3B AND BTRC, PHOSPHORYLATION AT SER-104 AND SER-107, MUTAGENESIS OF SER-96; SER-104 AND SER-107.
    13. "Ajuba LIM proteins are snail/slug corepressors required for neural crest development in Xenopus."
      Langer E.M., Feng Y., Zhaoyuan H., Rauscher F.J. III, Kroll K.L., Longmore G.D.
      Dev. Cell 14:424-436(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LIMD1 AND AJUBA.
    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 151-ARG-LYS-152; CYS-156; LYS-161; LYS-170; CYS-182; LYS-187; ARG-191; CYS-210; ARG-215; ARG-220; ASN-222; ARG-224; 232-ASP--LYS-235; CYS-238 AND GLN-239.
    15. Cited for: GLYCOSYLATION AT SER-112.
    16. "Snail associates with EGR-1 and SP-1 to upregulate transcriptional activation of p15INK4b."
      Hu C.T., Chang T.Y., Cheng C.C., Liu C.S., Wu J.R., Li M.C., Wu W.S.
      FEBS J. 277:1202-1218(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EGR1, INDUCTION.
    17. "p53 inhibits tumor cell invasion via the degradation of snail protein in hepatocellular carcinoma."
      Lim S.O., Kim H., Jung G.
      FEBS Lett. 584:2231-2236(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TP53 AND MDM2, UBIQUITINATION BY MDM2.
    18. "The hypoxia-controlled FBXL14 ubiquitin ligase targets SNAIL1 for proteasome degradation."
      Vinas-Castells R., Beltran M., Valls G., Gomez I., Garcia J.M., Montserrat-Sentis B., Baulida J., Bonilla F., de Herreros A.G., Diaz V.M.
      J. Biol. Chem. 285:3794-3805(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY FBXL14 AND BTRC, INTERACTION WITH FBXL14, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-98; LYS-137 AND LYS-146.
    19. "Phosphorylation of serine 11 and serine 92 as new positive regulators of human Snail1 function: potential involvement of casein kinase-2 and the cAMP-activated kinase protein kinase A."
      MacPherson M.R., Molina P., Souchelnytskyi S., Wernstedt C., Martin-Perez J., Portillo F., Cano A.
      Mol. Biol. Cell 21:244-253(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CSNK2A1, PHOSPHORYLATION AT SER-11; SER-82; SER-92; SER-104 AND SER-107, MUTAGENESIS OF SER-11; SER-92; SER-104 AND SER-107.
    20. "Role of CK1 in GSK3beta-mediated phosphorylation and degradation of snail."
      Xu Y., Lee S.H., Kim H.S., Kim N.H., Piao S., Park S.H., Jung Y.S., Yook J.I., Park B.J., Ha N.C.
      Oncogene 29:3124-3133(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CSNK1E, PHOSPHORYLATION BY CSNK1E AND GSK3B, PHOSPHORYLATION AT SER-96, MUTAGENESIS OF SER-96; SER-100; SER-104 AND SER-107.
    21. "Requirement of the histone demethylase LSD1 in Snai1-mediated transcriptional repression during epithelial-mesenchymal transition."
      Lin T., Ponn A., Hu X., Law B.K., Lu J.
      Oncogene 29:4896-4904(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH KDM1A, MUTAGENESIS OF PRO-2.
    22. "Notch1 binds and induces degradation of Snail in hepatocellular carcinoma."
      Lim S.O., Kim H.S., Quan X., Ahn S.M., Kim H., Hsieh D., Seong J.K., Jung G.
      BMC Biol. 9:83-83(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH NOTCH1 AND MDM2, SUBCELLULAR LOCATION, UBIQUITINATION BY MDM2, MUTAGENESIS OF SER-96 AND SER-100.
    23. "Importin alpha protein acts as a negative regulator for Snail protein nuclear import."
      Sekimoto T., Miyamoto Y., Arai S., Yoneda Y.
      J. Biol. Chem. 286:15126-15131(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KPNB1; KPNA1; KPNA4 AND KPNA2.
    24. "Poly(ADP-ribose)-dependent regulation of Snail1 protein stability."
      Rodriguez M.I., Gonzalez-Flores A., Dantzer F., Collard J., de Herreros A.G., Oliver F.J.
      Oncogene 30:4365-4372(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PARP1, SUBCELLULAR LOCATION, ADP-RIBOSYLATION BY PARP1.
    25. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "Lats2 kinase potentiates Snail1 activity by promoting nuclear retention upon phosphorylation."
      Zhang K., Rodriguez-Aznar E., Yabuta N., Owen R.J., Mingot J.M., Nojima H., Nieto M.A., Longmore G.D.
      EMBO J. 31:29-43(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-203 BY LATS2, MUTAGENESIS OF THR-203.

    Entry informationi

    Entry nameiSNAI1_HUMAN
    AccessioniPrimary (citable) accession number: O95863
    Secondary accession number(s): B2R842
    , Q9P113, Q9UBP7, Q9UHH7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: December 1, 2000
    Last modified: October 1, 2014
    This is version 147 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Caution

    The interaction with mouse KPNA2 may prevent SNAI1 nuclear import.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3