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Q14526

- HIC1_HUMAN

UniProt

Q14526 - HIC1_HUMAN

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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

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. sequence-specific DNA binding Source: UniProtKB
  4. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ14526.
CleanExiHS_HIC1.
ExpressionAtlasiQ14526. baseline and differential.
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. 25 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.
GeneTreeiENSGT00760000119356.
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

        10         20         30         40         50
MTFPEADILL KSGECAGQTM LDTMEAPGHS RQLLLQLNNQ RTKGFLCDVI
60 70 80 90 100
IVVQNALFRA HKNVLAASSA YLKSLVVHDN LLNLDHDMVS PAVFRLVLDF
110 120 130 140 150
IYTGRLADGA EAAAAAAVAP GAEPSLGAVL AAASYLQIPD LVALCKKRLK
160 170 180 190 200
RHGKYCHLRG GGGGGGGYAP YGRPGRGLRA ATPVIQACYP SPVGPPPPPA
210 220 230 240 250
AEPPSGPEAA VNTHCAELYA SGPGPAAALC ASERRCSPLC GLDLSKKSPP
260 270 280 290 300
GSAAPERPLA ERELPPRPDS PPSAGPAAYK EPPLALPSLP PLPFQKLEEA
310 320 330 340 350
APPSDPFRGG SGSPGPEPPG RPDGPSLLYR WMKHEPGLGS YGDELGRERG
360 370 380 390 400
SPSERCEERG GDAAVSPGGP PLGLAPPPRY PGSLDGPGAG GDGDDYKSSS
410 420 430 440 450
EETGSSEDPS PPGGHLEGYP CPHLAYGEPE SFGDNLYVCI PCGKGFPSSE
460 470 480 490 500
QLNAHVEAHV EEEEALYGRA EAAEVAAGAA GLGPPFGGGG DKVAGAPGGL
510 520 530 540 550
GELLRPYRCA SCDKSYKDPA TLRQHEKTHW LTRPYPCTIC GKKFTQRGTM
560 570 580 590 600
TRHMRSHLGL KPFACDACGM RFTRQYRLTE HMRIHSGEKP YECQVCGGKF
610 620 630 640 650
AQQRNLISHM KMHAVGGAAG AAGALAGLGG LPGVPGPDGK GKLDFPEGVF
660 670 680 690 700
AVARLTAEQL SLKQQDKAAA AELLAQTTHF LHDPKVALES LYPLAKFTAE
710 720 730
LGLSPDKAAE VLSQGAHLAA GPDGRTIDRF SPT
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:
EMBLi
GenBanki
DDBJi
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]
ENST00000619757; ENSP00000477858; 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:
EMBLi
GenBanki
DDBJi
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. 25 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 ]
ENST00000619757 ; ENSP00000477858 ; ENSG00000177374 . [Q14526-2 ]
GeneIDi 3090.
KEGGi hsa:3090.
UCSCi uc002fty.4. human. [Q14526-1 ]

Organism-specific databases

CTDi 3090.
GeneCardsi GC17P001973.
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.
GeneTreei ENSGT00760000119356.
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

Bgeei Q14526.
CleanExi HS_HIC1.
ExpressionAtlasi Q14526. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 137 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