HIC2_MOUSE
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 03-AUG-2022, entry version 177.
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; Q9JLZ6; -.
DR PeptideAtlas; Q9JLZ6; -.
DR PRIDE; Q9JLZ6; -.
DR ProteomicsDB; 269745; -. [Q9JLZ6-1]
DR ProteomicsDB; 269746; -. [Q9JLZ6-2]
DR Antibodypedia; 8461; 246 antibodies from 31 providers.
DR DNASU; 58180; -.
DR Ensembl; ENSMUST00000090190; ENSMUSP00000087656; ENSMUSG00000050240. [Q9JLZ6-1]
DR Ensembl; ENSMUST00000232082; ENSMUSP00000156293; ENSMUSG00000050240. [Q9JLZ6-2]
DR GeneID; 58180; -.
DR KEGG; mmu:58180; -.
DR UCSC; uc007yko.1; mouse. [Q9JLZ6-1]
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; HTPQELP; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9JLZ6; -.
DR TreeFam; TF333488; -.
DR BioGRID-ORCS; 58180; 2 hits in 71 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 177 other tissues.
DR Genevisible; Q9JLZ6; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.710.10; -; 1.
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 Pfam; PF00651; BTB; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
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
