Q14526 (HIC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Hypermethylated in cancer 1 protein
Short name=Hic-1

Alternative name(s):
Zinc finger and BTB domain-containing protein 29

Gene names

Name:	HIC1
Synonyms:	ZBTB29

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	733 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 CXCR7, FGFBP1 and EFNA1. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19
Subunit structure	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. Ref.5 Ref.6 Ref.10 Ref.11 Ref.13 Ref.16 Ref.18
Subcellular location	Nucleus Ref.5.
Tissue specificity	Ubiquitously expressed with highest levels found in lung, colon, prostate, thymus, testis and ovary. Expression is absent or decreased in many tumor cells.
Domain	The BTB domain inhibits the binding to a single consensus binding site, but mediates cooperative binding to multiple binding sites.
Post-translational modification	Acetylated on several residues, including Lys-333. Lys-333 is deacetylated by SIRT1. Sumoylated on Lys-333 by a PIAS family member, which enhances interaction with MTA1, positively regulates transcriptional repression activity and is enhanced by HDAC4. Ref.12
Miscellaneous	The HIC1 gene is frequently found epigenetically silenced or deleted in different types of solid tumors.
Sequence similarities	Belongs to the krueppel C2H2-type zinc-finger protein family. Hic subfamily. Contains 1 BTB (POZ) domain. Contains 5 C2H2-type zinc fingers.

Ontologies

Keywords
Biological process	Transcription Transcription regulation Wnt signaling pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Tumor suppressor
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Developmental protein Repressor
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Wnt receptor signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW intrinsic apoptotic signaling pathway in response to DNA damage Inferred from direct assay Ref.8. Source: UniProtKB multicellular organismal development Non-traceable author statement. Source: UniProtKB negative regulation of Wnt receptor signaling pathway Inferred from direct assay Ref.10. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.6Ref.7. Source: UniProtKB positive regulation of DNA damage response, signal transduction by p53 class mediator Inferred from sequence or structural similarity. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	chromatin Inferred from sequence or structural similarity. Source: UniProtKB cytoplasm Inferred from direct assay. Source: HPA nucleus Non-traceable author statement. Source: UniProtKB
Molecular_function	histone deacetylase binding Inferred from direct assay Ref.6. Source: UniProtKB sequence-specific DNA binding Inferred from direct assay Ref.7. Source: UniProtKB sequence-specific DNA binding transcription factor activity Inferred from direct assay Ref.7. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARID1A	O14497	2	EBI-2507362,EBI-637887
CTBP1	Q13363	4	EBI-2507362,EBI-908846
Ctbp1	O88712	8	EBI-2507362,EBI-604547	From a different organism.
CTBP2	P56545	2	EBI-2507362,EBI-741533
Ctbp2	P56546	2	EBI-2507362,EBI-1384883	From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q14526-1)

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.

Isoform 2 (identifier: Q14526-2)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 733	733	Hypermethylated in cancer 1 protein		PRO_0000046942
Regions
	Domain	47 – 110	64	BTB
	Zinc finger	439 – 459	21	C2H2-type 1
	Zinc finger	509 – 529	21	C2H2-type 2
	Zinc finger	537 – 557	21	C2H2-type 3
	Zinc finger	565 – 585	21	C2H2-type 4
	Zinc finger	593 – 613	21	C2H2-type 5
	Region	154 – 315	162	Mediates HDAC-dependent transcriptional repression
	Region	241 – 247	7	Interaction with CTBP1
	Compositional bias	110 – 119	10	Poly-Ala
	Compositional bias	160 – 167	8	Poly-Gly
	Compositional bias	195 – 199	5	Poly-Pro
Amino acid modifications
	Modified residue	313	1	Phosphoserine By similarity
	Modified residue	333	1	N6-acetyllysine; alternate Ref.12
	Cross-link	333		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate Ref.12
Natural variations
	Alternative sequence	1 – 19	19	Missing in isoform 2.		VSP_006826
	Natural variant	725	1	R → G. Ref.1 Corresponds to variant rs1063317 [ dbSNP | Ensembl ].		VAR_063109
Experimental info
	Mutagenesis	244	1	L → A: Abolishes interaction with CTBP1 and CTBP2. Impairs transcriptional repression. Ref.11
	Mutagenesis	333	1	K → Q: Mimicks acetylation. Impairs interaction with RBBP4 and MTA1 and no effect on interaction with CTBP2. Reduces transcriptional repression. Ref.12 Ref.18
	Mutagenesis	333	1	K → R: Abolishes sumoylation; impairs transcriptional repression activity. Ref.12 Ref.18
	Mutagenesis	335	1	E → A: Impairs transcriptional repression activity. Decreases interaction with MTA1. Ref.12 Ref.18
	Mutagenesis	336	1	P → A: Impairs K-333 acetylation; no effect on sumoylation. Decreases interaction with MTA1. Ref.12 Ref.18
	Mutagenesis	540	1	C → S: Abolishes repression activity. Ref.7
	Sequence conflict	190	1	P → R in AAD09201. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 18, 2010. Version 5. Checksum: 6DDD0F49C4E490D3	FASTA	733	76,508
	10 20 30 40 50 60 MTFPEADILL KSGECAGQTM LDTMEAPGHS RQLLLQLNNQ RTKGFLCDVI IVVQNALFRA 70 80 90 100 110 120 HKNVLAASSA YLKSLVVHDN LLNLDHDMVS PAVFRLVLDF IYTGRLADGA EAAAAAAVAP 130 140 150 160 170 180 GAEPSLGAVL AAASYLQIPD LVALCKKRLK RHGKYCHLRG GGGGGGGYAP YGRPGRGLRA 190 200 210 220 230 240 ATPVIQACYP SPVGPPPPPA AEPPSGPEAA VNTHCAELYA SGPGPAAALC ASERRCSPLC 250 260 270 280 290 300 GLDLSKKSPP GSAAPERPLA ERELPPRPDS PPSAGPAAYK EPPLALPSLP PLPFQKLEEA 310 320 330 340 350 360 APPSDPFRGG SGSPGPEPPG RPDGPSLLYR WMKHEPGLGS YGDELGRERG SPSERCEERG 370 380 390 400 410 420 GDAAVSPGGP PLGLAPPPRY PGSLDGPGAG GDGDDYKSSS EETGSSEDPS PPGGHLEGYP 430 440 450 460 470 480 CPHLAYGEPE SFGDNLYVCI PCGKGFPSSE QLNAHVEAHV EEEEALYGRA EAAEVAAGAA 490 500 510 520 530 540 GLGPPFGGGG DKVAGAPGGL GELLRPYRCA SCDKSYKDPA TLRQHEKTHW LTRPYPCTIC 550 560 570 580 590 600 GKKFTQRGTM TRHMRSHLGL KPFACDACGM RFTRQYRLTE HMRIHSGEKP YECQVCGGKF 610 620 630 640 650 660 AQQRNLISHM KMHAVGGAAG AAGALAGLGG LPGVPGPDGK GKLDFPEGVF AVARLTAEQL 670 680 690 700 710 720 SLKQQDKAAA AELLAQTTHF LHDPKVALES LYPLAKFTAE LGLSPDKAAE VLSQGAHLAA 730 GPDGRTIDRF SPT
	Isoform 2 [UniParc]. Checksum: 3AB8B6CB2C97218D	FASTA	714	74,514
	10 20 30 40 50 60 MLDTMEAPGH SRQLLLQLNN QRTKGFLCDV IIVVQNALFR AHKNVLAASS AYLKSLVVHD 70 80 90 100 110 120 NLLNLDHDMV SPAVFRLVLD FIYTGRLADG AEAAAAAAVA PGAEPSLGAV LAAASYLQIP 130 140 150 160 170 180 DLVALCKKRL KRHGKYCHLR GGGGGGGGYA PYGRPGRGLR AATPVIQACY PSPVGPPPPP 190 200 210 220 230 240 AAEPPSGPEA AVNTHCAELY ASGPGPAAAL CASERRCSPL CGLDLSKKSP PGSAAPERPL 250 260 270 280 290 300 AERELPPRPD SPPSAGPAAY KEPPLALPSL PPLPFQKLEE AAPPSDPFRG GSGSPGPEPP 310 320 330 340 350 360 GRPDGPSLLY RWMKHEPGLG SYGDELGRER GSPSERCEER GGDAAVSPGG PPLGLAPPPR 370 380 390 400 410 420 YPGSLDGPGA GGDGDDYKSS SEETGSSEDP SPPGGHLEGY PCPHLAYGEP ESFGDNLYVC 430 440 450 460 470 480 IPCGKGFPSS EQLNAHVEAH VEEEEALYGR AEAAEVAAGA AGLGPPFGGG GDKVAGAPGG 490 500 510 520 530 540 LGELLRPYRC ASCDKSYKDP ATLRQHEKTH WLTRPYPCTI CGKKFTQRGT MTRHMRSHLG 550 560 570 580 590 600 LKPFACDACG MRFTRQYRLT EHMRIHSGEK PYECQVCGGK FAQQRNLISH MKMHAVGGAA 610 620 630 640 650 660 GAAGALAGLG GLPGVPGPDG KGKLDFPEGV FAVARLTAEQ LSLKQQDKAA AAELLAQTTH 670 680 690 700 710 FLHDPKVALE SLYPLAKFTA ELGLSPDKAA EVLSQGAHLA AGPDGRTIDR FSPT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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]	Erratum 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. 22:1410-1410(2008)
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	L41919 Genomic DNA. Translation: AAD09201.1. AC090617 Genomic DNA. No translation available. CH471108 Genomic DNA. Translation: EAW90562.1. CH471108 Genomic DNA. Translation: EAW90563.1.
IPI	IPI00007993. IPI00219932.
RefSeq	NP_001091672.1. NM_001098202.1. NP_006488.2. NM_006497.3.
UniGene	Hs.695682. Hs.72956.
3D structure databases
ProteinModelPortal	Q14526.
SMR	Q14526. Positions 25-145, 429-613.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q14526. 9 interactions.
MINT	MINT-2730619.
STRING	9606.ENSP00000314080.
PTM databases
PhosphoSite	Q14526.
Polymorphism databases
DMDM	296439502.
Proteomic databases
PaxDb	Q14526.
PRIDE	Q14526.
Protocols and materials databases
DNASU	3090.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000322941; ENSP00000314080; ENSG00000177374. ENST00000399849; ENSP00000382742; ENSG00000177374.
GeneID	3090.
KEGG	hsa:3090.
UCSC	uc002fty.4. human.
Organism-specific databases
CTD	3090.
GeneCards	GC17P001958.
H-InvDB	HIX0039113.
HGNC	HGNC:4909. HIC1.
HPA	HPA043372.
MIM	603825. gene.
neXtProt	NX_Q14526.
Orphanet	531. Miller-Dieker syndrome.
PharmGKB	PA29282.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5048.
HOGENOM	HOG000026793.
HOVERGEN	HBG031606.
InParanoid	Q14526.
OMA	PPRYPGS.
PhylomeDB	Q14526.
Gene expression databases
ArrayExpress	Q14526.
Bgee	Q14526.
CleanEx	HS_HIC1.
Genevestigator	Q14526.
GermOnline	ENSG00000177374. Homo sapiens.
Family and domain databases
Gene3D	3.30.160.60. 4 hits. 3.30.710.10. 1 hit.
InterPro	IPR000210. BTB/POZ-like. IPR011333. BTB/POZ_fold. IPR013069. BTB_POZ. IPR007087. Znf_C2H2. IPR015880. Znf_C2H2-like. IPR013087. Znf_C2H2/integrase_DNA-bd. [Graphical view]
Pfam	PF00651. BTB. 1 hit. PF00096. zf-C2H2. 1 hit. [Graphical view]
SMART	SM00225. BTB. 1 hit. SM00355. ZnF_C2H2. 5 hits. [Graphical view]
SUPFAM	SSF54695. BTB/POZ_fold. 1 hit.
PROSITE	PS50097. BTB. 1 hit. PS00028. ZINC_FINGER_C2H2_1. 5 hits. PS50157. ZINC_FINGER_C2H2_2. 5 hits. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	3090.
NextBio	12259.
SOURCE	Search...

Entry information

Entry name

HIC1_HUMAN

Accession

Primary (citable) accession number: Q14526
Secondary accession number(s): D3DTI4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2002
Last sequence update:	May 18, 2010
Last modified:	May 1, 2013
This is version 123 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.