ID   HIC2_HUMAN              Reviewed;         615 AA.
AC   Q96JB3; Q504T6; Q96KR3; Q9NSM9; Q9UPX9;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2002, sequence version 2.
DT   24-JAN-2024, entry version 198.
DE   RecName: Full=Hypermethylated in cancer 2 protein;
DE            Short=Hic-2;
DE   AltName: Full=HIC1-related gene on chromosome 22 protein;
DE   AltName: Full=Hic-3;
DE   AltName: Full=Zinc finger and BTB domain-containing protein 30;
GN   Name=HIC2; Synonyms=HRG22, KIAA1020, ZBTB30;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-85 (ISOFORM 1), ALTERNATIVE SPLICING,
RP   SELF-ASSOCIATION, AND INTERACTION WITH HIC1.
RX   PubMed=11554746; DOI=10.1006/bbrc.2001.5624;
RA   Deltour S., Pinte S., Guerardel C., Leprince D.;
RT   "Characterization of HRG22, a human homologue of the putative tumor
RT   suppressor gene HIC1.";
RL   Biochem. Biophys. Res. Commun. 287:427-434(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RA   Alliel P.M., Goudou D., Bitoun M., Seddiqi N., Rieger F., Perin J.-P.;
RT   "Complete deduced structure of HIC-3, a novel human btb/poz and ZF factor
RT   of the HIC family.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA   Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA   Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XIV. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 6:197-205(1999).
RN   [4]
RP   SEQUENCE REVISION.
RX   PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA   Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT   "Construction of expression-ready cDNA clones for KIAA genes: manual
RT   curation of 330 KIAA cDNA clones.";
RL   DNA Res. 9:99-106(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA   Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA   Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA   Beare D.M., Dunham I.;
RT   "A genome annotation-driven approach to cloning the human ORFeome.";
RL   Genome Biol. 5:R84.1-R84.11(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA   Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA   Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA   Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA   Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA   Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA   Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA   Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA   Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA   Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA   Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA   Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA   Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA   Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA   Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA   Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA   Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA   Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA   Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA   Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA   Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA   Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA   Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA   Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA   Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA   Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA   Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA   McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA   Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA   Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA   Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA   Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 301-615.
RC   TISSUE=Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166; SER-169; SER-197;
RP   SER-348 AND SER-412, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
CC   -!- FUNCTION: Transcriptional repressor.
CC   -!- SUBUNIT: Self-associates. Interacts with HIC1.
CC       {ECO:0000269|PubMed:11554746}.
CC   -!- INTERACTION:
CC       Q96JB3; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-726282, EBI-739624;
CC       Q96JB3; Q96KQ7: EHMT2; NbExp=3; IntAct=EBI-726282, EBI-744366;
CC       Q96JB3; Q96BR9: ZBTB8A; NbExp=5; IntAct=EBI-726282, EBI-742740;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q96JB3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96JB3-2; Sequence=VSP_006829;
CC   -!- TISSUE SPECIFICITY: Highest levels in cerebellum.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. Hic subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA82972.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ313204; CAC70715.1; -; mRNA.
DR   EMBL; AF349035; AAK72951.1; -; mRNA.
DR   EMBL; AB028943; BAA82972.2; ALT_INIT; mRNA.
DR   EMBL; CR456377; CAG30263.1; -; mRNA.
DR   EMBL; AP000557; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC094787; AAH94787.1; -; mRNA.
DR   EMBL; AL162003; CAB82344.1; -; mRNA.
DR   CCDS; CCDS13789.1; -. [Q96JB3-1]
DR   PIR; T47181; T47181.
DR   RefSeq; NP_055909.2; NM_015094.2. [Q96JB3-1]
DR   RefSeq; XP_011528309.1; XM_011530007.2.
DR   RefSeq; XP_011528310.1; XM_011530008.2. [Q96JB3-1]
DR   RefSeq; XP_011528311.1; XM_011530009.2. [Q96JB3-1]
DR   RefSeq; XP_011528312.1; XM_011530010.2.
DR   RefSeq; XP_016884158.1; XM_017028669.1. [Q96JB3-2]
DR   PDB; 7TXC; X-ray; 3.04 A; E=503-615.
DR   PDBsum; 7TXC; -.
DR   AlphaFoldDB; Q96JB3; -.
DR   SMR; Q96JB3; -.
DR   BioGRID; 116741; 52.
DR   IntAct; Q96JB3; 28.
DR   MINT; Q96JB3; -.
DR   STRING; 9606.ENSP00000387757; -.
DR   iPTMnet; Q96JB3; -.
DR   PhosphoSitePlus; Q96JB3; -.
DR   SwissPalm; Q96JB3; -.
DR   BioMuta; HIC2; -.
DR   DMDM; 20454983; -.
DR   EPD; Q96JB3; -.
DR   jPOST; Q96JB3; -.
DR   MassIVE; Q96JB3; -.
DR   MaxQB; Q96JB3; -.
DR   PaxDb; 9606-ENSP00000387757; -.
DR   PeptideAtlas; Q96JB3; -.
DR   ProteomicsDB; 76928; -. [Q96JB3-1]
DR   ProteomicsDB; 76929; -. [Q96JB3-2]
DR   Pumba; Q96JB3; -.
DR   Antibodypedia; 8461; 280 antibodies from 31 providers.
DR   DNASU; 23119; -.
DR   Ensembl; ENST00000407464.7; ENSP00000385319.2; ENSG00000169635.10. [Q96JB3-1]
DR   Ensembl; ENST00000407598.2; ENSP00000384889.2; ENSG00000169635.10. [Q96JB3-1]
DR   Ensembl; ENST00000443632.2; ENSP00000387757.2; ENSG00000169635.10. [Q96JB3-1]
DR   GeneID; 23119; -.
DR   KEGG; hsa:23119; -.
DR   MANE-Select; ENST00000407464.7; ENSP00000385319.2; NM_015094.3; NP_055909.2.
DR   UCSC; uc002zur.5; human. [Q96JB3-1]
DR   AGR; HGNC:18595; -.
DR   CTD; 23119; -.
DR   DisGeNET; 23119; -.
DR   GeneCards; HIC2; -.
DR   HGNC; HGNC:18595; HIC2.
DR   HPA; ENSG00000169635; Low tissue specificity.
DR   MIM; 607712; gene.
DR   neXtProt; NX_Q96JB3; -.
DR   OpenTargets; ENSG00000169635; -.
DR   PharmGKB; PA38357; -.
DR   VEuPathDB; HostDB:ENSG00000169635; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000159978; -.
DR   HOGENOM; CLU_015352_1_0_1; -.
DR   InParanoid; Q96JB3; -.
DR   OMA; GTPNEPM; -.
DR   OrthoDB; 1378030at2759; -.
DR   PhylomeDB; Q96JB3; -.
DR   TreeFam; TF333488; -.
DR   PathwayCommons; Q96JB3; -.
DR   SignaLink; Q96JB3; -.
DR   BioGRID-ORCS; 23119; 26 hits in 1212 CRISPR screens.
DR   ChiTaRS; HIC2; human.
DR   GeneWiki; HIC2; -.
DR   GenomeRNAi; 23119; -.
DR   Pharos; Q96JB3; Tbio.
DR   PRO; PR:Q96JB3; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   RNAct; Q96JB3; Protein.
DR   Bgee; ENSG00000169635; Expressed in secondary oocyte and 188 other cell types or tissues.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; NAS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0001817; P:regulation of cytokine production; IBA:GO_Central.
DR   GO; GO:0002682; P:regulation of immune system process; IBA:GO_Central.
DR   CDD; cd18334; BTB_POZ_ZBTB30_HIC2; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 5.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR24394:SF22; HYPERMETHYLATED IN CANCER 2 PROTEIN; 1.
DR   PANTHER; PTHR24394; ZINC FINGER PROTEIN; 1.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF00096; zf-C2H2; 4.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR   SUPFAM; SSF54695; POZ domain; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
DR   Genevisible; Q96JB3; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..615
FT                   /note="Hypermethylated in cancer 2 protein"
FT                   /id="PRO_0000046945"
FT   DOMAIN          46..109
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   ZN_FING         442..469
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         505..532
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         533..560
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         561..588
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         589..615
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          144..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          182..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          229..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          246..250
FT                   /note="Binding to CtBP"
FT   COMPBIAS        270..298
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         166
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         169
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         197
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         348
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         412
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..18
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_006829"
FT   CONFLICT        49..51
FT                   /note="IIM -> TIR (in Ref. 1; CAC70715)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        176
FT                   /note="Q -> R (in Ref. 3; BAA82972)"
FT                   /evidence="ECO:0000305"
FT   STRAND          508..511
FT                   /evidence="ECO:0007829|PDB:7TXC"
FT   STRAND          513..516
FT                   /evidence="ECO:0007829|PDB:7TXC"
FT   HELIX           517..524
FT                   /evidence="ECO:0007829|PDB:7TXC"
FT   HELIX           525..528
FT                   /evidence="ECO:0007829|PDB:7TXC"
FT   STRAND          536..538
FT                   /evidence="ECO:0007829|PDB:7TXC"
FT   STRAND          541..544
FT                   /evidence="ECO:0007829|PDB:7TXC"
FT   HELIX           545..555
FT                   /evidence="ECO:0007829|PDB:7TXC"
FT   STRAND          556..558
FT                   /evidence="ECO:0007829|PDB:7TXC"
FT   STRAND          560..562
FT                   /evidence="ECO:0007829|PDB:7TXC"
FT   TURN            564..566
FT                   /evidence="ECO:0007829|PDB:7TXC"
FT   STRAND          569..572
FT                   /evidence="ECO:0007829|PDB:7TXC"
FT   HELIX           573..579
FT                   /evidence="ECO:0007829|PDB:7TXC"
FT   HELIX           580..583
FT                   /evidence="ECO:0007829|PDB:7TXC"
SQ   SEQUENCE   615 AA;  66156 MW;  B0368C631B198C95 CRC64;
     MVSGPLALRW CAWAGRGDMG PDMELPSHSK QLLLQLNQQR TKGFLCDVII MVENSIFRAH
     KNVLAASSIY FKSLVLHDNL INLDTDMVSS TVFQQILDFI YTGKLLPSDQ PAEPNFSTLL
     TAASYLQLPE LAALCRRKLK RAGKPFGSGR AGSTGMGRPP RSQRLSTASV IQARYQGLVD
     GRKGAHAPQE LPQAKGSDDE LFLGGSNQDS VQGLGRAVCP AGGEAGLGGC SSSTNGSSGG
     CEQELGLDLS KKSPPLPPAT PGPHLTPDDA AQLSDSQHGS PPAASAPPVA NSASYSELGG
     TPDEPMDLEG AEDNHLSLLE APGGQPRKSL RHSTRKKEWG KKEPVAGSPF ERREAGPKGP
     CPGEEGEGVG DRVPNGILAS GAGPSGPYGE PPYPCKEEEE NGKDASEDSA QSGSEGGSGH
     ASAHYMYRQE GYETVSYGDN LYVCIPCAKG FPSSEQLNAH VETHTEEELF IKEEGAYETG
     SGGAEEEAED LSAPSAAYTA EPRPFKCSVC EKTYKDPATL RQHEKTHWLT RPFPCNICGK
     MFTQRGTMTR HMRSHLGLKP FACDECGMRF TRQYRLTEHM RVHSGEKPYE CQLCGGKFTQ
     QRNLISHLRM HTSPS
//