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Q96JB3 (HIC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hypermethylated in cancer 2 protein

Short name=Hic-2
Alternative name(s):
HIC1-related gene on chromosome 22 protein
Hic-3
Zinc finger and BTB domain-containing protein 30
Gene names
Name:HIC2
Synonyms:HRG22, KIAA1020, ZBTB30
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length615 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional repressor.

Subunit structure

Self-associates. Interacts with HIC1. Ref.1

Subcellular location

Nucleus.

Tissue specificity

Highest levels in cerebellum.

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.

Sequence caution

The sequence BAA82972.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96JB3-1)

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: Q96JB3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-18: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 615615Hypermethylated in cancer 2 protein
PRO_0000046945

Regions

Domain46 – 10964BTB
Zinc finger442 – 46928C2H2-type 1
Zinc finger505 – 53228C2H2-type 2
Zinc finger533 – 56028C2H2-type 3
Zinc finger561 – 58828C2H2-type 4
Zinc finger589 – 61527C2H2-type 5
Region246 – 2505Binding to CtBP

Natural variations

Alternative sequence1 – 1818Missing in isoform 2.
VSP_006829

Experimental info

Sequence conflict49 – 513IIM → TIR in CAC70715. Ref.1
Sequence conflict1761Q → R in BAA82972. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 2, 2002. Version 2.
Checksum: B0368C631B198C95

FASTA61566,156
        10         20         30         40         50         60 
MVSGPLALRW CAWAGRGDMG PDMELPSHSK QLLLQLNQQR TKGFLCDVII MVENSIFRAH 

        70         80         90        100        110        120 
KNVLAASSIY FKSLVLHDNL INLDTDMVSS TVFQQILDFI YTGKLLPSDQ PAEPNFSTLL 

       130        140        150        160        170        180 
TAASYLQLPE LAALCRRKLK RAGKPFGSGR AGSTGMGRPP RSQRLSTASV IQARYQGLVD 

       190        200        210        220        230        240 
GRKGAHAPQE LPQAKGSDDE LFLGGSNQDS VQGLGRAVCP AGGEAGLGGC SSSTNGSSGG 

       250        260        270        280        290        300 
CEQELGLDLS KKSPPLPPAT PGPHLTPDDA AQLSDSQHGS PPAASAPPVA NSASYSELGG 

       310        320        330        340        350        360 
TPDEPMDLEG AEDNHLSLLE APGGQPRKSL RHSTRKKEWG KKEPVAGSPF ERREAGPKGP 

       370        380        390        400        410        420 
CPGEEGEGVG DRVPNGILAS GAGPSGPYGE PPYPCKEEEE NGKDASEDSA QSGSEGGSGH 

       430        440        450        460        470        480 
ASAHYMYRQE GYETVSYGDN LYVCIPCAKG FPSSEQLNAH VETHTEEELF IKEEGAYETG 

       490        500        510        520        530        540 
SGGAEEEAED LSAPSAAYTA EPRPFKCSVC EKTYKDPATL RQHEKTHWLT RPFPCNICGK 

       550        560        570        580        590        600 
MFTQRGTMTR HMRSHLGLKP FACDECGMRF TRQYRLTEHM RVHSGEKPYE CQLCGGKFTQ 

       610 
QRNLISHLRM HTSPS 

« Hide

Isoform 2 [UniParc].

Checksum: C536567FC3A1AAC8
Show »

FASTA59764,228

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA] OF 1-85 (ISOFORM 1), ALTERNATIVE SPLICING, SELF-ASSOCIATION, INTERACTION WITH HIC1.
[2]"Complete deduced structure of HIC-3, a novel human btb/poz and ZF factor of the HIC family."
Alliel P.M., Goudou D., Bitoun M., Seddiqi N., Rieger F., Perin J.-P.
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Brain.
[3]"Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[4]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[5]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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: Placenta.
[8]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 301-615.
Tissue: Testis.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ313204 mRNA. Translation: CAC70715.1.
AF349035 mRNA. Translation: AAK72951.1.
AB028943 mRNA. Translation: BAA82972.2. Different initiation.
CR456377 mRNA. Translation: CAG30263.1.
AP000557 Genomic DNA. No translation available.
BC094787 mRNA. Translation: AAH94787.1.
AL162003 mRNA. Translation: CAB82344.1.
PIRT47181.
RefSeqNP_055909.2. NM_015094.2.
XP_005261452.1. XM_005261395.1.
UniGeneHs.632767.

3D structure databases

ProteinModelPortalQ96JB3.
SMRQ96JB3. Positions 23-135, 392-614.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116741. 5 interactions.
IntActQ96JB3. 4 interactions.
MINTMINT-1397107.
STRING9606.ENSP00000302994.

PTM databases

PhosphoSiteQ96JB3.

Polymorphism databases

DMDM20454983.

Proteomic databases

PaxDbQ96JB3.
PRIDEQ96JB3.

Protocols and materials databases

DNASU23119.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000407464; ENSP00000385319; ENSG00000169635. [Q96JB3-1]
ENST00000407598; ENSP00000384889; ENSG00000169635. [Q96JB3-1]
ENST00000443632; ENSP00000387757; ENSG00000169635. [Q96JB3-1]
GeneID23119.
KEGGhsa:23119.
UCSCuc002zur.4. human. [Q96JB3-1]

Organism-specific databases

CTD23119.
GeneCardsGC22P021771.
HGNCHGNC:18595. HIC2.
HPAHPA031884.
MIM607712. gene.
neXtProtNX_Q96JB3.
PharmGKBPA38357.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5048.
HOGENOMHOG000026793.
HOVERGENHBG079492.
InParanoidQ96JB3.
OMAIMVENSI.
OrthoDBEOG7T1R9Z.
PhylomeDBQ96JB3.
TreeFamTF333488.

Gene expression databases

BgeeQ96JB3.
CleanExHS_HIC2.
GenevestigatorQ96JB3.

Family and domain databases

Gene3D3.30.160.60. 5 hits.
3.30.710.10. 1 hit.
InterProIPR000210. 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]
PfamPF00651. BTB. 1 hit.
PF00096. zf-C2H2. 2 hits.
[Graphical view]
SMARTSM00225. BTB. 1 hit.
SM00355. ZnF_C2H2. 5 hits.
[Graphical view]
SUPFAMSSF54695. SSF54695. 1 hit.
PROSITEPS50097. BTB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 5 hits.
PS50157. ZINC_FINGER_C2H2_2. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiHIC2.
GenomeRNAi23119.
NextBio44339.
PROQ96JB3.
SOURCESearch...

Entry information

Entry nameHIC2_HUMAN
AccessionPrimary (citable) accession number: Q96JB3
Secondary accession number(s): Q504T6 expand/collapse secondary AC list , Q96KR3, Q9NSM9, Q9UPX9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: May 2, 2002
Last modified: April 16, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM