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Protein

Hypermethylated in cancer 2 protein

Gene

HIC2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcriptional repressor.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri442 – 46928C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri505 – 53228C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri533 – 56028C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri561 – 58828C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri589 – 61527C2H2-type 5PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. negative regulation of transcription, DNA-templated Source: UniProtKB
  2. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:HIC2
Synonyms:HRG22, KIAA1020, ZBTB30
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:18595. HIC2.

Subcellular locationi

GO - Cellular componenti

  1. nucleoplasm Source: HPA
  2. nucleus Source: UniProtKB
  3. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38357.

Polymorphism and mutation databases

BioMutaiHIC2.
DMDMi20454983.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 615615Hypermethylated in cancer 2 proteinPRO_0000046945Add
BLAST

Proteomic databases

MaxQBiQ96JB3.
PaxDbiQ96JB3.
PRIDEiQ96JB3.

PTM databases

PhosphoSiteiQ96JB3.

Expressioni

Tissue specificityi

Highest levels in cerebellum.

Gene expression databases

BgeeiQ96JB3.
CleanExiHS_HIC2.
GenevestigatoriQ96JB3.

Organism-specific databases

HPAiHPA031884.

Interactioni

Subunit structurei

Self-associates. Interacts with HIC1.1 Publication

Protein-protein interaction databases

BioGridi116741. 10 interactions.
IntActiQ96JB3. 4 interactions.
MINTiMINT-1397107.
STRINGi9606.ENSP00000302994.

Structurei

3D structure databases

ProteinModelPortaliQ96JB3.
SMRiQ96JB3. Positions 23-135, 442-613.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 10964BTBPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni246 – 2505Binding to CtBP

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 fingeri442 – 46928C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri505 – 53228C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri533 – 56028C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri561 – 58828C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri589 – 61527C2H2-type 5PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5048.
GeneTreeiENSGT00760000119063.
HOGENOMiHOG000026793.
HOVERGENiHBG079492.
InParanoidiQ96JB3.
OMAiMVENSIF.
OrthoDBiEOG7T1R9Z.
PhylomeDBiQ96JB3.
TreeFamiTF333488.

Family and domain databases

Gene3Di3.30.160.60. 5 hits.
InterProiIPR000210. 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]
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. AlignAdd to basket

Isoform 1 (identifier: Q96JB3-1) [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
MVSGPLALRW CAWAGRGDMG PDMELPSHSK QLLLQLNQQR TKGFLCDVII
60 70 80 90 100
MVENSIFRAH KNVLAASSIY FKSLVLHDNL INLDTDMVSS TVFQQILDFI
110 120 130 140 150
YTGKLLPSDQ PAEPNFSTLL TAASYLQLPE LAALCRRKLK RAGKPFGSGR
160 170 180 190 200
AGSTGMGRPP RSQRLSTASV IQARYQGLVD GRKGAHAPQE LPQAKGSDDE
210 220 230 240 250
LFLGGSNQDS VQGLGRAVCP AGGEAGLGGC SSSTNGSSGG CEQELGLDLS
260 270 280 290 300
KKSPPLPPAT PGPHLTPDDA AQLSDSQHGS PPAASAPPVA NSASYSELGG
310 320 330 340 350
TPDEPMDLEG AEDNHLSLLE APGGQPRKSL RHSTRKKEWG KKEPVAGSPF
360 370 380 390 400
ERREAGPKGP CPGEEGEGVG DRVPNGILAS GAGPSGPYGE PPYPCKEEEE
410 420 430 440 450
NGKDASEDSA QSGSEGGSGH ASAHYMYRQE GYETVSYGDN LYVCIPCAKG
460 470 480 490 500
FPSSEQLNAH VETHTEEELF IKEEGAYETG SGGAEEEAED LSAPSAAYTA
510 520 530 540 550
EPRPFKCSVC EKTYKDPATL RQHEKTHWLT RPFPCNICGK MFTQRGTMTR
560 570 580 590 600
HMRSHLGLKP FACDECGMRF TRQYRLTEHM RVHSGEKPYE CQLCGGKFTQ
610
QRNLISHLRM HTSPS
Length:615
Mass (Da):66,156
Last modified:May 2, 2002 - v2
Checksum:iB0368C631B198C95
GO
Isoform 2 (identifier: Q96JB3-2) [UniParc]FASTAAdd to basket

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

Show »
Length:597
Mass (Da):64,228
Checksum:iC536567FC3A1AAC8
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti49 – 513IIM → TIR in CAC70715 (PubMed:11554746).Curated
Sequence conflicti176 – 1761Q → R in BAA82972 (PubMed:10470851).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1818Missing in isoform 2. 1 PublicationVSP_006829Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13789.1. [Q96JB3-1]
PIRiT47181.
RefSeqiNP_055909.2. NM_015094.2. [Q96JB3-1]
XP_005261452.1. XM_005261395.2. [Q96JB3-1]
UniGeneiHs.632767.

Genome annotation databases

EnsembliENST00000407464; ENSP00000385319; ENSG00000169635. [Q96JB3-1]
ENST00000407598; ENSP00000384889; ENSG00000169635. [Q96JB3-1]
ENST00000443632; ENSP00000387757; ENSG00000169635. [Q96JB3-1]
GeneIDi23119.
KEGGihsa:23119.
UCSCiuc002zur.4. human. [Q96JB3-1]

Polymorphism and mutation databases

BioMutaiHIC2.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13789.1. [Q96JB3-1]
PIRiT47181.
RefSeqiNP_055909.2. NM_015094.2. [Q96JB3-1]
XP_005261452.1. XM_005261395.2. [Q96JB3-1]
UniGeneiHs.632767.

3D structure databases

ProteinModelPortaliQ96JB3.
SMRiQ96JB3. Positions 23-135, 442-613.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116741. 10 interactions.
IntActiQ96JB3. 4 interactions.
MINTiMINT-1397107.
STRINGi9606.ENSP00000302994.

PTM databases

PhosphoSiteiQ96JB3.

Polymorphism and mutation databases

BioMutaiHIC2.
DMDMi20454983.

Proteomic databases

MaxQBiQ96JB3.
PaxDbiQ96JB3.
PRIDEiQ96JB3.

Protocols and materials databases

DNASUi23119.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000407464; ENSP00000385319; ENSG00000169635. [Q96JB3-1]
ENST00000407598; ENSP00000384889; ENSG00000169635. [Q96JB3-1]
ENST00000443632; ENSP00000387757; ENSG00000169635. [Q96JB3-1]
GeneIDi23119.
KEGGihsa:23119.
UCSCiuc002zur.4. human. [Q96JB3-1]

Organism-specific databases

CTDi23119.
GeneCardsiGC22P021771.
HGNCiHGNC:18595. HIC2.
HPAiHPA031884.
MIMi607712. gene.
neXtProtiNX_Q96JB3.
PharmGKBiPA38357.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5048.
GeneTreeiENSGT00760000119063.
HOGENOMiHOG000026793.
HOVERGENiHBG079492.
InParanoidiQ96JB3.
OMAiMVENSIF.
OrthoDBiEOG7T1R9Z.
PhylomeDBiQ96JB3.
TreeFamiTF333488.

Miscellaneous databases

GeneWikiiHIC2.
GenomeRNAii23119.
NextBioi44339.
PROiQ96JB3.
SOURCEiSearch...

Gene expression databases

BgeeiQ96JB3.
CleanExiHS_HIC2.
GenevestigatoriQ96JB3.

Family and domain databases

Gene3Di3.30.160.60. 5 hits.
InterProiIPR000210. 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]
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 301-615.
    Tissue: Testis.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHIC2_HUMAN
AccessioniPrimary (citable) accession number: Q96JB3
Secondary accession number(s): Q504T6
, Q96KR3, Q9NSM9, Q9UPX9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: May 2, 2002
Last modified: April 29, 2015
This is version 134 of the entry and version 2 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.