ID   HIC2_MOUSE              Reviewed;         619 AA.
AC   Q9JLZ6; Q3U030; Q3ULP4; Q5K036; Q8BSZ9; Q8C3T5;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 4.
DT   24-JAN-2024, entry version 185.
DE   RecName: Full=Hypermethylated in cancer 2 protein;
DE            Short=Hic-2;
GN   Name=Hic2; Synonyms=Kiaa1020;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C3H/HeJ;
RA   Terzic A., Graw J.;
RT   "Characterization and expression analysis of the murine Hic2 gene.";
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Lung, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Embryonic tail;
RX   PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 354-619 (ISOFORM 1).
RC   STRAIN=Swiss Webster; TISSUE=Embryo;
RA   Grimm C., Graw J.;
RT   "Hic2, a novel homolog of Hic1 and gammaFBP.";
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcriptional repressor. {ECO:0000250}.
CC   -!- SUBUNIT: Self-associates. Interacts with HIC1 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9JLZ6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9JLZ6-2; Sequence=VSP_010499;
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. Hic subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98076.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAI30631.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR   EMBL; AJ868292; CAI30631.1; ALT_SEQ; mRNA.
DR   EMBL; AK084975; BAC39326.1; -; mRNA.
DR   EMBL; AK145386; BAE26404.1; -; mRNA.
DR   EMBL; AK156332; BAE33679.1; -; mRNA.
DR   EMBL; AK157276; BAE34025.1; -; mRNA.
DR   EMBL; AK129266; BAC98076.1; ALT_INIT; mRNA.
DR   EMBL; BC065124; AAH65124.1; -; mRNA.
DR   EMBL; AF117382; AAF28801.1; -; mRNA.
DR   CCDS; CCDS27999.1; -. [Q9JLZ6-1]
DR   RefSeq; NP_849253.2; NM_178922.3. [Q9JLZ6-1]
DR   AlphaFoldDB; Q9JLZ6; -.
DR   SMR; Q9JLZ6; -.
DR   BioGRID; 208374; 2.
DR   STRING; 10090.ENSMUSP00000087656; -.
DR   iPTMnet; Q9JLZ6; -.
DR   PhosphoSitePlus; Q9JLZ6; -.
DR   SwissPalm; Q9JLZ6; -.
DR   EPD; Q9JLZ6; -.
DR   MaxQB; Q9JLZ6; -.
DR   PaxDb; 10090-ENSMUSP00000087656; -.
DR   PeptideAtlas; Q9JLZ6; -.
DR   ProteomicsDB; 269745; -. [Q9JLZ6-1]
DR   ProteomicsDB; 269746; -. [Q9JLZ6-2]
DR   Pumba; Q9JLZ6; -.
DR   Antibodypedia; 8461; 280 antibodies from 31 providers.
DR   DNASU; 58180; -.
DR   Ensembl; ENSMUST00000090190.14; ENSMUSP00000087656.6; ENSMUSG00000050240.17. [Q9JLZ6-1]
DR   Ensembl; ENSMUST00000232082.2; ENSMUSP00000156293.2; ENSMUSG00000050240.17. [Q9JLZ6-2]
DR   GeneID; 58180; -.
DR   KEGG; mmu:58180; -.
DR   UCSC; uc007yko.1; mouse. [Q9JLZ6-1]
DR   AGR; MGI:1929869; -.
DR   CTD; 23119; -.
DR   MGI; MGI:1929869; Hic2.
DR   VEuPathDB; HostDB:ENSMUSG00000050240; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000159978; -.
DR   HOGENOM; CLU_015352_1_0_1; -.
DR   InParanoid; Q9JLZ6; -.
DR   OMA; GTPNEPM; -.
DR   OrthoDB; 1378030at2759; -.
DR   PhylomeDB; Q9JLZ6; -.
DR   TreeFam; TF333488; -.
DR   BioGRID-ORCS; 58180; 2 hits in 76 CRISPR screens.
DR   ChiTaRS; Hic2; mouse.
DR   PRO; PR:Q9JLZ6; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q9JLZ6; Protein.
DR   Bgee; ENSMUSG00000050240; Expressed in placenta labyrinth and 180 other cell types or tissues.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd18334; BTB_POZ_ZBTB30_HIC2; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 4.
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; Q9JLZ6; MM.
PE   2: Evidence at transcript level;
KW   Alternative splicing; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..619
FT                   /note="Hypermethylated in cancer 2 protein"
FT                   /id="PRO_0000046946"
FT   DOMAIN          46..109
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   ZN_FING         446..468
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         509..531
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         537..559
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         565..587
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         593..615
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          180..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          247..249
FT                   /note="Binding to CtBP"
FT                   /evidence="ECO:0000250"
FT   REGION          307..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..292
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         166
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96JB3"
FT   MOD_RES         169
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96JB3"
FT   MOD_RES         197
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96JB3"
FT   MOD_RES         349
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96JB3"
FT   MOD_RES         416
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96JB3"
FT   VAR_SEQ         544..619
FT                   /note="KMFTQRGTMTRHMRSHLGLKPFACDECGMRFTRQYRLTEHMRVHSGEKPYEC
FT                   QLCGGKFTQQRNLISHLRMHTSPS -> SEPTPSCPLQSSGMSGNLQQSQR (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_010499"
FT   CONFLICT        354..355
FT                   /note="RE -> AA (in Ref. 5; AAF28801)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   619 AA;  66766 MW;  AA7E58CC3BA8AB39 CRC64;
     MVSGPLALRW CPWAGHRDMG PDMELPSHSK QLLLQLNQQR AKGFLCDVII MVENSIFRAH
     KNVLAASSIY FKSLVLHDNL INLDTDMVSS TVFQQILDFI YTGKLLPSDQ PSEPNFSTLL
     TAASYLQLPE LAALCRRKLK RAGKPFGPGR VGTAGIGRPT RSQRLSTASV IQARFPGLVD
     VRKGHPAPQE LPQAKGSDDE LFLGTSTQES THGLGLGGPA GGEMGLGGCS TSTNGSSGGC
     EQELGLDLSK KSPPLPPTTP GPHLTPEDPA QLSDSQRESP APTSTSALPV GNSASFVELG
     ATPEEPMDVE GAEENHLSLL EGQGGQPRKS LRHSARKKDW NKKEPVAGSP FDRRETGSKG
     SCPGEEGEGT GDRVPNGVLA SSAGGGGPSA SYGEQSFPCK EEEENGKDGS EDSGQSGSEG
     GSGHTGAHYV YRQEGYETVS YGDNVYVCIP CAKGFPSSEQ LNAHVETHTE EELFIKEEGA
     YETGSGGAEE EAEDLSTPSA AYTADSRPFK CSVCEKTYKD PATLRQHEKT HWLTRPFPCN
     ICGKMFTQRG TMTRHMRSHL GLKPFACDEC GMRFTRQYRL TEHMRVHSGE KPYECQLCGG
     KFTQQRNLIS HLRMHTSPS
//