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O75398

- DEAF1_HUMAN

UniProt

O75398 - DEAF1_HUMAN

Protein

Deformed epidermal autoregulatory factor 1 homolog

Gene

DEAF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    Functioni

    Transcription factor that binds to sequence with multiple copies of 5'-TTC[CG]G-3' present in its own promoter and that of the HNRPA2B1 gene. Down-regulates transcription of these genes. Binds to the retinoic acid response element (RARE) 5'-AGGGTTCACCGAAAGTTCA-3'. Activates the proenkephalin gene independently of promoter binding, probably through protein-protein interaction. When secreted, behaves as an inhibitor of cell proliferation, by arresting cells in the G0 or G1 phase. Required for neural tube closure and skeletal patterning. Regulates epithelial cell proliferation and side-branching in the mammary gland. Controls the expression of peripheral tissue antigens in pancreatic lymph nodes. Isoform 1 displays greater transcriptional activity than isoform 4. Isoform 4 may inhibit transcriptional activity of isoform 1 by interacting with isoform 1 and retaining it in the cytoplasm.5 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri504 – 54037MYND-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: IntAct

    GO - Biological processi

    1. anatomical structure morphogenesis Source: ProtInc
    2. embryonic skeletal system development Source: UniProtKB
    3. germ cell development Source: ProtInc
    4. neural tube closure Source: UniProtKB
    5. regulation of mammary gland epithelial cell proliferation Source: UniProtKB
    6. regulation of transcription from RNA polymerase II promoter Source: Ensembl
    7. transcription from RNA polymerase II promoter Source: ProtInc

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Neurogenesis, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Deformed epidermal autoregulatory factor 1 homolog
    Alternative name(s):
    Nuclear DEAF-1-related transcriptional regulator
    Short name:
    NUDR
    Suppressin
    Zinc finger MYND domain-containing protein 5
    Gene namesi
    Name:DEAF1
    Synonyms:SPN, ZMYND5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:14677. DEAF1.

    Subcellular locationi

    Isoform 1 : Nucleus. Cytoplasm
    Note: Cytoplasmic in non-mucinous colorectal carcinoma. When expressed alone, localized almost exclusively in the nucleus but, when expressed with isoform 4, nuclear expression decreases to 32% and cytoplasmic expression increases by 270%.
    Isoform 2 : Secreted
    Note: Secreted in some cell types.
    Isoform 3 : Secreted
    Note: Secreted in some cell types.
    Isoform 4 : Cytoplasm. Nucleus
    Note: When expressed alone, localizes mainly in the cytoplasm but, when expressed with isoform 1, nuclear localization is enhanced.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. extracellular region Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB
    4. transcription factor complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi215 – 2151Y → Q: Reduces transcription activation. 1 Publication
    Mutagenesisi226 – 2261R → A: Reduces transcription activation. 1 Publication
    Mutagenesisi246 – 2461R → A: Reduces transcription activation. 1 Publication
    Mutagenesisi250 – 2501K → A: Abolishes DNA-binding. 1 Publication
    Mutagenesisi252 – 2521W → Q: Abolishes DNA-binding. 1 Publication
    Mutagenesisi253 – 2531K → A: Abolishes DNA-binding. 1 Publication
    Mutagenesisi302 – 3021R → T: Abolishes nuclear localization. 1 Publication
    Mutagenesisi304 – 3041K → T: Abolishes nuclear localization. 1 Publication
    Mutagenesisi538 – 5381H → S: No effect on folding of MYND-type zinc finger. 1 Publication

    Organism-specific databases

    PharmGKBiPA27234.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 565565Deformed epidermal autoregulatory factor 1 homologPRO_0000074084Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei448 – 4481PhosphoserineBy similarity

    Post-translational modificationi

    May be phosphorylated by DNA-PK complex in a DNA independent manner (in vitro).1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO75398.
    PaxDbiO75398.
    PRIDEiO75398.

    PTM databases

    PhosphoSiteiO75398.

    Expressioni

    Tissue specificityi

    Expressed in various tissues and cells such as in peripheral mononuclear cells and hormone-secreting pituitary cells. Expression in pancreatic lymph nodes of patients with type 1 diabetes is 20 times higher than in healthy controls.1 Publication

    Gene expression databases

    ArrayExpressiO75398.
    BgeeiO75398.
    CleanExiHS_SPN.
    GenevestigatoriO75398.

    Organism-specific databases

    HPAiHPA030302.

    Interactioni

    Subunit structurei

    Homodimer. Isoform 1 and isoform 4 may form a heterodimer. Interacts with LMO2 and CLIM2 By similarity. Interacts with LMO4; LMO4 blocks export from nucleus By similarity. May interact with the corepressors NCOR1 and NCRO2. Identified in a complex with the XRCC5 and XRCC6 heterodimer. Interacts (via the SAND domain) with the DNA-PK complex subunit XRCC6; the interaction is direct and may be inhibited by DNA-binding.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDKN2AP427712EBI-718185,EBI-375053
    GSK3AP498402EBI-718185,EBI-1044067
    GSK3BP498412EBI-718185,EBI-373586

    Protein-protein interaction databases

    BioGridi115777. 21 interactions.
    IntActiO75398. 18 interactions.
    MINTiMINT-1420286.

    Structurei

    Secondary structure

    1
    565
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi505 – 5106
    Beta strandi512 – 5143
    Turni516 – 5183
    Beta strandi520 – 5256
    Helixi526 – 5327
    Turni533 – 5353
    Helixi536 – 5383
    Turni539 – 5413

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JW6NMR-A496-544[»]
    4A24NMR-A501-544[»]
    ProteinModelPortaliO75398.
    SMRiO75398. Positions 201-272, 501-544.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75398.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini193 – 27381SANDPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni403 – 47876Interaction with LMO4By similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi301 – 31616Nuclear localization signalSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi2 – 122121Ala-richAdd
    BLAST
    Compositional biasi383 – 43957Pro-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 MYND-type zinc finger.PROSITE-ProRule annotation
    Contains 1 SAND domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri504 – 54037MYND-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG291744.
    HOVERGENiHBG051335.
    InParanoidiO75398.
    OMAiQSCVNCG.
    OrthoDBiEOG7VQJF5.
    PhylomeDBiO75398.
    TreeFamiTF325664.

    Family and domain databases

    Gene3Di3.10.390.10. 1 hit.
    InterProiIPR000770. SAND_dom.
    IPR010919. SAND_dom-like.
    IPR024119. TF_DEAF-1.
    IPR002893. Znf_MYND.
    [Graphical view]
    PANTHERiPTHR10237. PTHR10237. 1 hit.
    PfamiPF01342. SAND. 1 hit.
    PF01753. zf-MYND. 1 hit.
    [Graphical view]
    SMARTiSM00258. SAND. 1 hit.
    [Graphical view]
    SUPFAMiSSF63763. SSF63763. 1 hit.
    PROSITEiPS50864. SAND. 1 hit.
    PS01360. ZF_MYND_1. 1 hit.
    PS50865. ZF_MYND_2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O75398-1) [UniParc]FASTAAdd to Basket

    Also known as: Hu-DF1

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEDSDSAAKQ LGLAEAAAVA AAAAVAAAAA AAAGGEAEEP VLSRDEDSEE    50
    DADSEAERET PRVTAVAVMA AEPGHMDMGA EALPGPDEAA AAAAFAEVTT 100
    VTVANVGAAA DNVFTTSVAN AASISGHVLS GRTALQIGDS LNTEKATLIV 150
    VHTDGSIVET TGLKGPAAPL TPGPQSPPTP LAPGQEKGGT KYNWDPSVYD 200
    SELPVRCRNI SGTLYKNRLG SGGRGRCIKQ GENWYSPTEF EAMAGRASSK 250
    DWKRSIRYAG RPLQCLIQDG ILNPHAASCT CAACCDDMTL SGPVRLFVPY 300
    KRRKKENELP TTPVKKDSPK NITLLPATAA TTFTVTPSGQ ITTSGALTFD 350
    RASTVEATAV ISESPAQGDV FAGATVQEAS VQPPCRASHP EPHYPGYQDS 400
    CQIAPFPEAA LPTSHPKIVL TSLPALAVPP PTPTKAAPPA LVNGLELSEP 450
    RSWLYLEEMV NSLLNTAQQL KTLFEQAKHA STYREAATNQ AKIHADAERK 500
    EQSCVNCGRE AMSECTGCHK VNYCSTFCQR KDWKDHQHIC GQSAAVTVQA 550
    DEVHVAESVM EKVTV 565
    Length:565
    Mass (Da):59,327
    Last modified:November 1, 1998 - v1
    Checksum:i3BDFEDBF6AD4BDDE
    GO
    Isoform 2 (identifier: O75398-3) [UniParc]FASTAAdd to Basket

    Also known as: NUDR8

    The sequence of this isoform differs from the canonical sequence as follows:
         15-29: EAAAVAAAAAVAAAA → D

    Show »
    Length:551
    Mass (Da):58,262
    Checksum:i9ABE2A02D3AA8DA1
    GO
    Isoform 3 (identifier: O75398-4) [UniParc]FASTAAdd to Basket

    Also known as: Suppressin

    The sequence of this isoform differs from the canonical sequence as follows:
         1-68: Missing.

    Note: Has no predictable signal peptide.Curated

    Show »
    Length:497
    Mass (Da):52,717
    Checksum:i4EC4279532D8A4DE
    GO
    Isoform 4 (identifier: O75398-5) [UniParc]FASTAAdd to Basket

    Also known as: Hu-DF1-VAR

    The sequence of this isoform differs from the canonical sequence as follows:
         223-333: GRGRCIKQGE...LLPATAATTF → WDLKPSRCLLHLCCLLRRHDLI
         501-501: E → EVIHPPRLPKVLGLQ

    Show »
    Length:490
    Mass (Da):51,277
    Checksum:iAD1869382C23FF2A
    GO

    Sequence cautioni

    The sequence AAC25718.1 differs from that shown. Reason: Several sequencing errors.
    The sequence AAC25719.1 differs from that shown. Reason: Frameshift at positions 222 and 236.
    Isoform 3 : The sequence AAC25718.1 differs from that shown. Reason: Frameshift at positions 222 and 236.
    Isoform 3 : The sequence AAC25719.1 differs from that shown. Reason: Frameshift at positions 222 and 236.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti65 – 651A → E in ACU88060. (PubMed:19668219)Curated
    Sequence conflicti72 – 721E → D in AAB62704. 1 PublicationCurated
    Sequence conflicti166 – 1661P → Q in ACU88060. (PubMed:19668219)Curated
    Sequence conflicti247 – 2471A → T in AAB62704. 1 PublicationCurated
    Sequence conflicti294 – 2941V → L in AAB62704. 1 PublicationCurated
    Sequence conflicti399 – 3991D → G in ACU88060. (PubMed:19668219)Curated
    Sequence conflicti522 – 5221N → K in AAB62704. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti186 – 1861E → V in a primary colorectal cancer. 1 Publication
    VAR_013725
    Natural varianti191 – 1911K → I in a primary colorectal cancer. 1 Publication
    VAR_013726
    Natural varianti191 – 1911K → N in a primary colorectal cancer. 1 Publication
    VAR_013727
    Natural varianti199 – 2024YDSE → CDND in a primary colorectal cancer.
    VAR_013728
    Natural varianti202 – 2021E → D in a primary colorectal cancer. 1 Publication
    VAR_013729
    Natural varianti218 – 2181R → K in a primary colorectal cancer. 1 Publication
    VAR_013730
    Natural varianti228 – 2281I → S De novo variant found in a patient with mental retardation. 1 Publication
    VAR_065089
    Natural varianti350 – 3523DRA → GQT in a primary colorectal cancer.
    VAR_013731
    Natural varianti356 – 3561E → H in a primary colorectal cancer; requires 2 nucleotide substitutions. 1 Publication
    VAR_013732
    Natural varianti364 – 3641S → N in a primary colorectal cancer. 1 Publication
    VAR_013733
    Natural varianti367 – 3671Q → H in a primary colorectal cancer. 1 Publication
    VAR_013734
    Natural varianti370 – 3701V → L in a primary colorectal cancer. 1 Publication
    VAR_013735
    Natural varianti397 – 3971Y → F in a primary colorectal cancer. 1 Publication
    VAR_013736
    Natural varianti442 – 4421V → A in a primary colorectal cancer. 1 Publication
    VAR_013737
    Natural varianti449 – 4491E → K in a primary colorectal cancer. 1 Publication
    VAR_013738
    Natural varianti451 – 4522RS → GI in a primary colorectal cancer.
    VAR_013739
    Natural varianti468 – 4681Q → H in a primary colorectal cancer. 1 Publication
    VAR_013740
    Natural varianti479 – 4791H → L in a primary colorectal cancer. 1 Publication
    VAR_013741
    Natural varianti498 – 4981E → K in a primary colorectal cancer. 1 Publication
    VAR_013742
    Natural varianti526 – 5261T → N in a primary colorectal cancer. 1 Publication
    VAR_013743
    Natural varianti530 – 5301R → L in a primary colorectal cancer. 1 Publication
    VAR_013744
    Natural varianti537 – 5382QH → HL in a primary colorectal cancer.
    VAR_013745
    Natural varianti542 – 5421Q → H in a primary colorectal cancer. 1 Publication
    VAR_013746
    Natural varianti545 – 5451A → G in a primary colorectal cancer. 1 Publication
    Corresponds to variant rs34114147 [ dbSNP | Ensembl ].
    VAR_013747
    Natural varianti545 – 5451A → V in a primary colorectal cancer. 1 Publication
    VAR_013748

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6868Missing in isoform 3. 3 PublicationsVSP_005966Add
    BLAST
    Alternative sequencei15 – 2915EAAAV…VAAAA → D in isoform 2. 1 PublicationVSP_005967Add
    BLAST
    Alternative sequencei223 – 333111GRGRC…AATTF → WDLKPSRCLLHLCCLLRRHD LI in isoform 4. 1 PublicationVSP_038701Add
    BLAST
    Alternative sequencei501 – 5011E → EVIHPPRLPKVLGLQ in isoform 4. 1 PublicationVSP_038702

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF049459 mRNA. Translation: AAC79676.1.
    AF049460 mRNA. Translation: AAC79677.1.
    AF068893 mRNA. Translation: AAC25715.1.
    AF068894 mRNA. Translation: AAC25716.1.
    AF068895 mRNA. Translation: AAC25717.1.
    AF068896 mRNA. Translation: AAC25718.1. Sequence problems.
    AF068897 mRNA. Translation: AAC25719.1. Frameshift.
    FJ985253 mRNA. Translation: ACU88060.1.
    AF007165 mRNA. Translation: AAB62704.1.
    AK291383 mRNA. Translation: BAF84072.1.
    AK289873 mRNA. Translation: BAF82562.1.
    BC053322 mRNA. Translation: AAH53322.1.
    CCDSiCCDS31327.1. [O75398-1]
    RefSeqiNP_066288.2. NM_021008.3. [O75398-1]
    UniGeneiHs.243994.

    Genome annotation databases

    EnsembliENST00000382409; ENSP00000371846; ENSG00000177030. [O75398-1]
    GeneIDi10522.
    KEGGihsa:10522.
    UCSCiuc001lqq.1. human. [O75398-1]
    uc021qbn.1. human. [O75398-5]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF049459 mRNA. Translation: AAC79676.1 .
    AF049460 mRNA. Translation: AAC79677.1 .
    AF068893 mRNA. Translation: AAC25715.1 .
    AF068894 mRNA. Translation: AAC25716.1 .
    AF068895 mRNA. Translation: AAC25717.1 .
    AF068896 mRNA. Translation: AAC25718.1 . Sequence problems.
    AF068897 mRNA. Translation: AAC25719.1 . Frameshift.
    FJ985253 mRNA. Translation: ACU88060.1 .
    AF007165 mRNA. Translation: AAB62704.1 .
    AK291383 mRNA. Translation: BAF84072.1 .
    AK289873 mRNA. Translation: BAF82562.1 .
    BC053322 mRNA. Translation: AAH53322.1 .
    CCDSi CCDS31327.1. [O75398-1 ]
    RefSeqi NP_066288.2. NM_021008.3. [O75398-1 ]
    UniGenei Hs.243994.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JW6 NMR - A 496-544 [» ]
    4A24 NMR - A 501-544 [» ]
    ProteinModelPortali O75398.
    SMRi O75398. Positions 201-272, 501-544.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115777. 21 interactions.
    IntActi O75398. 18 interactions.
    MINTi MINT-1420286.

    PTM databases

    PhosphoSitei O75398.

    Proteomic databases

    MaxQBi O75398.
    PaxDbi O75398.
    PRIDEi O75398.

    Protocols and materials databases

    DNASUi 10522.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000382409 ; ENSP00000371846 ; ENSG00000177030 . [O75398-1 ]
    GeneIDi 10522.
    KEGGi hsa:10522.
    UCSCi uc001lqq.1. human. [O75398-1 ]
    uc021qbn.1. human. [O75398-5 ]

    Organism-specific databases

    CTDi 10522.
    GeneCardsi GC11M000644.
    H-InvDB HIX0026125.
    HGNCi HGNC:14677. DEAF1.
    HPAi HPA030302.
    MIMi 602635. gene.
    neXtProti NX_O75398.
    PharmGKBi PA27234.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG291744.
    HOVERGENi HBG051335.
    InParanoidi O75398.
    OMAi QSCVNCG.
    OrthoDBi EOG7VQJF5.
    PhylomeDBi O75398.
    TreeFami TF325664.

    Miscellaneous databases

    EvolutionaryTracei O75398.
    GenomeRNAii 10522.
    NextBioi 39912.
    PROi O75398.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75398.
    Bgeei O75398.
    CleanExi HS_SPN.
    Genevestigatori O75398.

    Family and domain databases

    Gene3Di 3.10.390.10. 1 hit.
    InterProi IPR000770. SAND_dom.
    IPR010919. SAND_dom-like.
    IPR024119. TF_DEAF-1.
    IPR002893. Znf_MYND.
    [Graphical view ]
    PANTHERi PTHR10237. PTHR10237. 1 hit.
    Pfami PF01342. SAND. 1 hit.
    PF01753. zf-MYND. 1 hit.
    [Graphical view ]
    SMARTi SM00258. SAND. 1 hit.
    [Graphical view ]
    SUPFAMi SSF63763. SSF63763. 1 hit.
    PROSITEi PS50864. SAND. 1 hit.
    PS01360. ZF_MYND_1. 1 hit.
    PS50865. ZF_MYND_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of a nuclear deformed epidermal autoregulatory factor-1 (DEAF-1)-related (NUDR) transcriptional regulator protein."
      Huggenvik J.I., Michelson R.J., Collard M.W., Ziemba A.J., Gurley P., Mowen K.A.
      Mol. Endocrinol. 12:1619-1639(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), MUTAGENESIS OF ARG-302 AND LYS-304.
      Tissue: Choriocarcinoma.
    2. "Altered subcellular localization of suppressin, a novel inhibitor of cell-cycle entry, is an independent prognostic factor in colorectal adenocarcinomas."
      Manne U., Gary B.D., Oelschlager D.K., Weiss H.L., Frost A.R., Grizzle W.E.
      Clin. Cancer Res. 7:3495-3503(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), VARIANTS VAL-186; ASN-191; ILE-191; 199-CYS-ASP-ASN-ASP-202; ASP-202; LYS-218; 350-GLY-GLN-THR-352; HIS-356; ASN-364; HIS-367; LEU-370; PHE-397; ALA-442; LYS-449; 451-GLY-ILE-452; HIS-468; LEU-479; LYS-498; ASN-526; LEU-530; 537-HIS-LEU-538; HIS-542; GLY-545 AND VAL-545, ROLE IN NEOPLASIA.
      Tissue: Colon and Colon adenocarcinoma.
    3. "Deaf1 isoforms control the expression of genes encoding peripheral tissue antigens in the pancreatic lymph nodes during type 1 diabetes."
      Yip L., Su L., Sheng D., Chang P., Atkinson M., Czesak M., Albert P.R., Collier A.R., Turley S.J., Fathman C.G., Creusot R.J.
      Nat. Immunol. 10:1026-1033(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Pancreas.
    4. "Cloning and sequence analysis of the cDNA for human suppressin (spn)."
      LeBoeuf R.D., Blalock J.E., Tauber J.D.
      Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Tissue: Mammary gland.
    5. "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] (ISOFORMS 1 AND 3).
      Tissue: Brain and Caudate nucleus.
    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] (ISOFORM 1).
      Tissue: Ovary.
    7. "Nuclear DEAF-1-related (NUDR) protein contains a novel DNA binding domain and represses transcription of the heterogeneous nuclear ribonucleoprotein A2/B1 promoter."
      Michelson R.J., Collard M.W., Ziemba A.J., Persinger J., Bartholomew B., Huggenvik J.I.
      J. Biol. Chem. 274:30510-30519(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "The SAND domain structure defines a novel DNA-binding fold in transcriptional regulation."
      Bottomley M.J., Collard M.W., Huggenvik J.I., Liu Z., Gibson T.J., Sattler M.
      Nat. Struct. Biol. 8:626-633(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF SAND DOMAIN, MUTAGENESIS OF TYR-215; ARG-226; ARG-246; LYS-250; TRP-252 AND LYS-253.
    9. "Deaf-1 regulates epithelial cell proliferation and side-branching in the mammary gland."
      Barker H.E., Smyth G.K., Wettenhall J., Ward T.A., Bath M.L., Lindeman G.J., Visvader J.E.
      BMC Dev. Biol. 8:94-94(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Deformed epidermal autoregulatory factor-1 (DEAF1) interacts with the Ku70 subunit of the DNA-dependent protein kinase complex."
      Jensik P.J., Huggenvik J.I., Collard M.W.
      PLoS ONE 7:E33404-E33404(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING, IDENTIFICATION IN A COMPLEX WITH XRCC5 AND XRCC6, SUBCELLULAR LOCATION, PHOSPHORYLATION BY DNA-PK COMPLEX.
    12. Cited for: STRUCTURE BY NMR OF 496-544 IN COMPLEX WITH ZINC IONS.
    13. "Retraction notice to 'Structure and functional analysis of the MYND domain' [J. Mol. Biol. (2006) 358, 498-508]."
      Spadaccini R., Perrin H., Bottomley M.J., Ansieau S., Sattler M.
      J. Mol. Biol. 376:1523-1523(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: RETRACTION: STRUCTURE BY NMR OF 496-544 IN COMPLEX WITH ZINC IONS.
    14. Cited for: STRUCTURE BY NMR OF 501-544 IN COMPLEX WITH ZINC IONS, SUBUNIT, INTERACTION WITH NCOR1 AND NCOR2, MUTAGENESIS OF HIS-538.
    15. Cited for: VARIANT SER-228.

    Entry informationi

    Entry nameiDEAF1_HUMAN
    AccessioniPrimary (citable) accession number: O75398
    Secondary accession number(s): A8K1F8
    , A8K5R8, C7T5V5, O15152, O75399, O75510, O75511, O75512, O75513, Q9UET1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 2002
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 149 of the entry and version 1 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

    Miscellaneous

    Defective DEAF1 could confer a growth advantage to the mutated cells influencing the development and progression of neoplasia, e.g. in the case of colorectal carcinomas. Subcellular location in colorectal carcinomas (cytoplasmic or nuclear) is a prognostic factor that identifies a subgroup of patients with reduced survival. In addition, changes in the subcellular location correlates with the proliferative status of the cells.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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