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Q14526

- HIC1_HUMAN

UniProt

Q14526 - HIC1_HUMAN

Protein

Hypermethylated in cancer 1 protein

Gene

HIC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 5 (18 May 2010)
      Previous versions | rss
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    Functioni

    Transcriptional repressor. Recognizes and binds to the consensus sequence '5-[CG]NG[CG]GGGCA[CA]CC-3'. May act as a tumor suppressor. May be involved in development of head, face, limbs and ventral body wall. Involved in down-regulation of SIRT1 and thereby is involved in regulation of p53/TP53-dependent apoptotic DNA-damage responses. The specific target gene promoter association seems to be depend on corepressors, such as CTBP1 or CTBP2 and MTA1. The regulation of SIRT1 transcription in response to nutrient deprivation seems to involve CTBP1. In cooperation with MTA1 (indicative for an association with the NuRD complex) represses transcription from CCND1/cyclin-D1 and CDKN1C/p57Kip2 specifically in quiescent cells. Involved in regulation of the Wnt signaling pathway probably by association with TCF7L2 and preventing TCF7L2 and CTNNB1 association with promoters of TCF-responsive genes. Seems to repress transcription from E2F1 and ATOH1 which involves ARID1A, indicative for the participation of a distinct SWI/SNF-type chromatin-remodeling complex. Probably represses transcription from ACKR3, FGFBP1 and EFNA1.11 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri439 – 45921C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri509 – 52921C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri537 – 55721C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri565 – 58521C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri593 – 61321C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. histone deacetylase binding Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. sequence-specific DNA binding Source: UniProtKB
    5. sequence-specific DNA binding transcription factor activity Source: UniProtKB

    GO - Biological processi

    1. intrinsic apoptotic signaling pathway in response to DNA damage Source: UniProtKB
    2. multicellular organismal development Source: UniProtKB-KW
    3. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    4. negative regulation of Wnt signaling pathway Source: UniProtKB
    5. positive regulation of DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
    6. regulation of transcription, DNA-templated Source: UniProtKB
    7. transcription, DNA-templated Source: UniProtKB-KW
    8. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Molecular functioni

    Developmental protein, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation, Wnt signaling pathway

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiQ14526.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hypermethylated in cancer 1 protein
    Short name:
    Hic-1
    Alternative name(s):
    Zinc finger and BTB domain-containing protein 29
    Gene namesi
    Name:HIC1
    Synonyms:ZBTB29
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:4909. HIC1.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. chromatin Source: UniProtKB
    2. cytoplasm Source: HPA
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi244 – 2441L → A: Abolishes interaction with CTBP1 and CTBP2. Impairs transcriptional repression. 1 Publication
    Mutagenesisi333 – 3331K → Q: Mimicks acetylation. Impairs interaction with RBBP4 and MTA1 and no effect on interaction with CTBP2. Reduces transcriptional repression. 2 Publications
    Mutagenesisi333 – 3331K → R: Abolishes sumoylation; impairs transcriptional repression activity. 2 Publications
    Mutagenesisi335 – 3351E → A: Impairs transcriptional repression activity. Decreases interaction with MTA1. 2 Publications
    Mutagenesisi336 – 3361P → A: Impairs K-333 acetylation; no effect on sumoylation. Decreases interaction with MTA1. 2 Publications
    Mutagenesisi540 – 5401C → S: Abolishes repression activity. 1 Publication

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    Orphaneti531. Miller-Dieker syndrome.
    PharmGKBiPA29282.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 733733Hypermethylated in cancer 1 proteinPRO_0000046942Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei333 – 3331N6-acetyllysine; alternate1 Publication
    Cross-linki333 – 333Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate

    Post-translational modificationi

    Acetylated on several residues, including Lys-333. Lys-333 is deacetylated by SIRT1.1 Publication
    Sumoylated on Lys-333 by a PIAS family member, which enhances interaction with MTA1, positively regulates transcriptional repression activity and is enhanced by HDAC4.1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Ubl conjugation

    Proteomic databases

    PaxDbiQ14526.
    PRIDEiQ14526.

    PTM databases

    PhosphoSiteiQ14526.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed with highest levels found in lung, colon, prostate, thymus, testis and ovary. Expression is absent or decreased in many tumor cells.

    Gene expression databases

    ArrayExpressiQ14526.
    BgeeiQ14526.
    CleanExiHS_HIC1.
    GenevestigatoriQ14526.

    Organism-specific databases

    HPAiHPA043372.

    Interactioni

    Subunit structurei

    Self-associates. Interacts with HIC2. Interacts with CTBP1 and CTBP2. Interacts with TCF7L2 and ARID1A. Interacts with MTA1 and MBD3; indicative for an association with the NuRD complex.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARID1AO144972EBI-2507362,EBI-637887
    CTBP1Q133634EBI-2507362,EBI-908846
    Ctbp1O8871210EBI-2507362,EBI-604547From a different organism.
    CTBP2P565452EBI-2507362,EBI-741533
    Ctbp2P565462EBI-2507362,EBI-1384883From a different organism.
    TCF7L2Q9NQB06EBI-2507362,EBI-924724

    Protein-protein interaction databases

    BioGridi109337. 24 interactions.
    IntActiQ14526. 11 interactions.
    MINTiMINT-2730619.
    STRINGi9606.ENSP00000314080.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14526.
    SMRiQ14526. Positions 25-145, 429-613.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini47 – 11064BTBPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni154 – 315162Mediates HDAC-dependent transcriptional repressionAdd
    BLAST
    Regioni241 – 2477Interaction with CTBP1

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi110 – 11910Poly-Ala
    Compositional biasi160 – 1678Poly-Gly
    Compositional biasi195 – 1995Poly-Pro

    Domaini

    The BTB domain inhibits the binding to a single consensus binding site, but mediates cooperative binding to multiple binding sites.

    Sequence similaritiesi

    Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation
    Contains 5 C2H2-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri439 – 45921C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri509 – 52921C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri537 – 55721C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri565 – 58521C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri593 – 61321C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5048.
    HOGENOMiHOG000026793.
    HOVERGENiHBG031606.
    InParanoidiQ14526.
    OMAiERCEERG.
    OrthoDBiEOG74J97F.
    PhylomeDBiQ14526.
    TreeFamiTF333488.

    Family and domain databases

    Gene3Di3.30.160.60. 4 hits.
    3.30.710.10. 1 hit.
    InterProiIPR000210. BTB/POZ-like.
    IPR011333. BTB/POZ_fold.
    IPR013069. BTB_POZ.
    IPR028424. HIC1.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view]
    PANTHERiPTHR11389:SF322. PTHR11389:SF322. 1 hit.
    PfamiPF00651. BTB. 1 hit.
    PF00096. zf-C2H2. 2 hits.
    [Graphical view]
    SMARTiSM00225. BTB. 1 hit.
    SM00355. ZnF_C2H2. 5 hits.
    [Graphical view]
    SUPFAMiSSF54695. SSF54695. 1 hit.
    PROSITEiPS50097. BTB. 1 hit.
    PS00028. ZINC_FINGER_C2H2_1. 5 hits.
    PS50157. ZINC_FINGER_C2H2_2. 5 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: Q14526-1) [UniParc]FASTAAdd to Basket

    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

    MTFPEADILL KSGECAGQTM LDTMEAPGHS RQLLLQLNNQ RTKGFLCDVI    50
    IVVQNALFRA HKNVLAASSA YLKSLVVHDN LLNLDHDMVS PAVFRLVLDF 100
    IYTGRLADGA EAAAAAAVAP GAEPSLGAVL AAASYLQIPD LVALCKKRLK 150
    RHGKYCHLRG GGGGGGGYAP YGRPGRGLRA ATPVIQACYP SPVGPPPPPA 200
    AEPPSGPEAA VNTHCAELYA SGPGPAAALC ASERRCSPLC GLDLSKKSPP 250
    GSAAPERPLA ERELPPRPDS PPSAGPAAYK EPPLALPSLP PLPFQKLEEA 300
    APPSDPFRGG SGSPGPEPPG RPDGPSLLYR WMKHEPGLGS YGDELGRERG 350
    SPSERCEERG GDAAVSPGGP PLGLAPPPRY PGSLDGPGAG GDGDDYKSSS 400
    EETGSSEDPS PPGGHLEGYP CPHLAYGEPE SFGDNLYVCI PCGKGFPSSE 450
    QLNAHVEAHV EEEEALYGRA EAAEVAAGAA GLGPPFGGGG DKVAGAPGGL 500
    GELLRPYRCA SCDKSYKDPA TLRQHEKTHW LTRPYPCTIC GKKFTQRGTM 550
    TRHMRSHLGL KPFACDACGM RFTRQYRLTE HMRIHSGEKP YECQVCGGKF 600
    AQQRNLISHM KMHAVGGAAG AAGALAGLGG LPGVPGPDGK GKLDFPEGVF 650
    AVARLTAEQL SLKQQDKAAA AELLAQTTHF LHDPKVALES LYPLAKFTAE 700
    LGLSPDKAAE VLSQGAHLAA GPDGRTIDRF SPT 733
    Length:733
    Mass (Da):76,508
    Last modified:May 18, 2010 - v5
    Checksum:i6DDD0F49C4E490D3
    GO
    Isoform 2 (identifier: Q14526-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-19: Missing.

    Show »
    Length:714
    Mass (Da):74,514
    Checksum:i3AB8B6CB2C97218D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti190 – 1901P → R in AAD09201. (PubMed:7585125)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti725 – 7251R → G.1 Publication
    Corresponds to variant rs1063317 [ dbSNP | Ensembl ].
    VAR_063109

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1919Missing in isoform 2. CuratedVSP_006826Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L41919 Genomic DNA. Translation: AAD09201.1.
    AC090617 Genomic DNA. No translation available.
    CH471108 Genomic DNA. Translation: EAW90562.1.
    CH471108 Genomic DNA. Translation: EAW90563.1.
    CCDSiCCDS42229.1. [Q14526-1]
    CCDS42230.1. [Q14526-2]
    RefSeqiNP_001091672.1. NM_001098202.1. [Q14526-1]
    NP_006488.2. NM_006497.3. [Q14526-2]
    UniGeneiHs.695682.
    Hs.72956.

    Genome annotation databases

    EnsembliENST00000322941; ENSP00000314080; ENSG00000177374. [Q14526-1]
    ENST00000399849; ENSP00000382742; ENSG00000177374. [Q14526-2]
    GeneIDi3090.
    KEGGihsa:3090.
    UCSCiuc002fty.4. human. [Q14526-1]

    Polymorphism databases

    DMDMi296439502.

    Keywords - Coding sequence diversityi

    Alternative splicing, 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
    L41919 Genomic DNA. Translation: AAD09201.1 .
    AC090617 Genomic DNA. No translation available.
    CH471108 Genomic DNA. Translation: EAW90562.1 .
    CH471108 Genomic DNA. Translation: EAW90563.1 .
    CCDSi CCDS42229.1. [Q14526-1 ]
    CCDS42230.1. [Q14526-2 ]
    RefSeqi NP_001091672.1. NM_001098202.1. [Q14526-1 ]
    NP_006488.2. NM_006497.3. [Q14526-2 ]
    UniGenei Hs.695682.
    Hs.72956.

    3D structure databases

    ProteinModelPortali Q14526.
    SMRi Q14526. Positions 25-145, 429-613.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109337. 24 interactions.
    IntActi Q14526. 11 interactions.
    MINTi MINT-2730619.
    STRINGi 9606.ENSP00000314080.

    PTM databases

    PhosphoSitei Q14526.

    Polymorphism databases

    DMDMi 296439502.

    Proteomic databases

    PaxDbi Q14526.
    PRIDEi Q14526.

    Protocols and materials databases

    DNASUi 3090.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000322941 ; ENSP00000314080 ; ENSG00000177374 . [Q14526-1 ]
    ENST00000399849 ; ENSP00000382742 ; ENSG00000177374 . [Q14526-2 ]
    GeneIDi 3090.
    KEGGi hsa:3090.
    UCSCi uc002fty.4. human. [Q14526-1 ]

    Organism-specific databases

    CTDi 3090.
    GeneCardsi GC17P001967.
    H-InvDB HIX0039113.
    HGNCi HGNC:4909. HIC1.
    HPAi HPA043372.
    MIMi 603825. gene.
    neXtProti NX_Q14526.
    Orphaneti 531. Miller-Dieker syndrome.
    PharmGKBi PA29282.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5048.
    HOGENOMi HOG000026793.
    HOVERGENi HBG031606.
    InParanoidi Q14526.
    OMAi ERCEERG.
    OrthoDBi EOG74J97F.
    PhylomeDBi Q14526.
    TreeFami TF333488.

    Enzyme and pathway databases

    SignaLinki Q14526.

    Miscellaneous databases

    GeneWikii HIC1.
    GenomeRNAii 3090.
    NextBioi 12259.
    PROi Q14526.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14526.
    Bgeei Q14526.
    CleanExi HS_HIC1.
    Genevestigatori Q14526.

    Family and domain databases

    Gene3Di 3.30.160.60. 4 hits.
    3.30.710.10. 1 hit.
    InterProi IPR000210. BTB/POZ-like.
    IPR011333. BTB/POZ_fold.
    IPR013069. BTB_POZ.
    IPR028424. HIC1.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view ]
    PANTHERi PTHR11389:SF322. PTHR11389:SF322. 1 hit.
    Pfami PF00651. BTB. 1 hit.
    PF00096. zf-C2H2. 2 hits.
    [Graphical view ]
    SMARTi SM00225. BTB. 1 hit.
    SM00355. ZnF_C2H2. 5 hits.
    [Graphical view ]
    SUPFAMi SSF54695. SSF54695. 1 hit.
    PROSITEi PS50097. BTB. 1 hit.
    PS00028. ZINC_FINGER_C2H2_1. 5 hits.
    PS50157. ZINC_FINGER_C2H2_2. 5 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "p53 activates expression of HIC-1, a new candidate tumour suppressor gene on 17p13.3."
      Wales M.M., Biel M.A., el Deiry W., Nelkin B.D., Issa J.-P., Cavenee W.K., Kuerbitz S.J., Baylin S.B.
      Nat. Med. 1:570-577(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), VARIANT GLY-725.
    2. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Recruitment of SMRT/N-CoR-mSin3A-HDAC-repressing complexes is not a general mechanism for BTB/POZ transcriptional repressors: the case of HIC-1 and gammaFBP-B."
      Deltour S., Guerardel C., Leprince D.
      Proc. Natl. Acad. Sci. U.S.A. 96:14831-14836(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SELF-ASSOCIATION.
    5. "Characterization of HRG22, a human homologue of the putative tumor suppressor gene HIC1."
      Deltour S., Pinte S., Guerardel C., Leprince D.
      Biochem. Biophys. Res. Commun. 287:427-434(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING, INTERACTION WITH HIC2, SUBCELLULAR LOCATION.
    6. "The human candidate tumor suppressor gene HIC1 recruits CtBP through a degenerate GLDLSKK motif."
      Deltour S., Pinte S., Guerardel C., Wasylyk B., Leprince D.
      Mol. Cell. Biol. 22:4890-4901(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SELF-ASSOCIATION, INTERACTION WITH CTBP1.
    7. "The tumor suppressor gene HIC1 (hypermethylated in cancer 1) is a sequence-specific transcriptional repressor: definition of its consensus binding sequence and analysis of its DNA binding and repressive properties."
      Pinte S., Stankovic-Valentin N., Deltour S., Rood B.R., Guerardel C., Leprince D.
      J. Biol. Chem. 279:38313-38324(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DNA-BINDING, MUTAGENESIS OF CYS-540.
    8. "Tumor suppressor HIC1 directly regulates SIRT1 to modulate p53-dependent DNA-damage responses."
      Chen W.Y., Wang D.H., Yen R.C., Luo J., Gu W., Baylin S.B.
      Cell 123:437-448(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Mechanism of fibroblast growth factor-binding protein 1 repression by TGF-beta."
      Briones V.R., Chen S., Riegel A.T., Lechleider R.J.
      Biochem. Biophys. Res. Commun. 345:595-601(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "HIC1 attenuates Wnt signaling by recruitment of TCF-4 and beta-catenin to the nuclear bodies."
      Valenta T., Lukas J., Doubravska L., Fafilek B., Korinek V.
      EMBO J. 25:2326-2337(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN WNT SIGNALING, INTERACTION WITH TCF7L2.
    11. "A L225A substitution in the human tumour suppressor HIC1 abolishes its interaction with the corepressor CtBP."
      Stankovic-Valentin N., Verger A., Deltour-Balerdi S., Quinlan K.G., Crossley M., Leprince D.
      FEBS J. 273:2879-2890(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CTBP1 AND CTBP2, MUTAGENESIS OF LEU-244.
    12. "An acetylation/deacetylation-SUMOylation switch through a phylogenetically conserved psiKXEP motif in the tumor suppressor HIC1 regulates transcriptional repression activity."
      Stankovic-Valentin N., Deltour S., Seeler J., Pinte S., Vergoten G., Guerardel C., Dejean A., Leprince D.
      Mol. Cell. Biol. 27:2661-2675(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-333, ACETYLATION AT LYS-333, MUTAGENESIS OF LYS-333; GLU-335 AND PRO-336.
    13. "Metabolic regulation of SIRT1 transcription via a HIC1:CtBP corepressor complex."
      Zhang Q., Wang S.Y., Fleuriel C., Leprince D., Rocheleau J.V., Piston D.W., Goodman R.H.
      Proc. Natl. Acad. Sci. U.S.A. 104:829-833(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CTBP1.
    14. "Cooperation between the Hic1 and Ptch1 tumor suppressors in medulloblastoma."
      Briggs K.J., Corcoran-Schwartz I.M., Zhang W., Harcke T., Devereux W.L., Baylin S.B., Eberhart C.G., Watkins D.N.
      Genes Dev. 22:770-785(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "HIC1 interacts with a specific subunit of SWI/SNF complexes, ARID1A/BAF250A."
      Van Rechem C., Boulay G., Leprince D.
      Biochem. Biophys. Res. Commun. 385:586-590(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ARID1A.
    16. "Scavenger chemokine (CXC motif) receptor 7 (CXCR7) is a direct target gene of HIC1 (hypermethylated in cancer 1)."
      Van Rechem C., Rood B.R., Touka M., Pinte S., Jenal M., Guerardel C., Ramsey K., Monte D., Begue A., Tschan M.P., Stephan D.A., Leprince D.
      J. Biol. Chem. 284:20927-20935(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "Differential regulation of HIC1 target genes by CtBP and NuRD, via an acetylation/SUMOylation switch, in quiescent versus proliferating cells."
      Van Rechem C., Boulay G., Pinte S., Stankovic-Valentin N., Guerardel C., Leprince D.
      Mol. Cell. Biol. 30:4045-4059(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MTA1 AND MBD3, MUTAGENESIS OF LYS-333; GLU-335 AND PRO-336.
    18. "A potential tumor suppressor role for Hic1 in breast cancer through transcriptional repression of ephrin-A1."
      Zhang W., Zeng X., Briggs K.J., Beaty R., Simons B., Chiu Yen R.W., Tyler M.A., Tsai H.C., Ye Y., Gesell G.S., Herman J.G., Baylin S.B., Watkins D.N.
      Oncogene 29:2467-2476(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiHIC1_HUMAN
    AccessioniPrimary (citable) accession number: Q14526
    Secondary accession number(s): D3DTI4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2002
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 136 of the entry and version 5 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

    The HIC1 gene is frequently found epigenetically silenced or deleted in different types of solid tumors.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3