ZMIZ2_MOUSE
ID ZMIZ2_MOUSE Reviewed; 920 AA.
AC Q8CIE2; Q5SVX4; Q5SVX5; Q5SVX6; Q6P558; Q6P9Q5; Q8BJ00;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Zinc finger MIZ domain-containing protein 2;
DE AltName: Full=PIAS-like protein Zimp7;
GN Name=Zmiz2; Synonyms=D11Bwg0280e, Zimp7;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 10-920 (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Embryonic brain, and Liver;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 628-920.
RC STRAIN=C57BL/6J; TISSUE=Embryonic head;
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 [4]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-111; ARG-245 AND ARG-262, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Increases ligand-dependent transcriptional activity of AR and
CC other nuclear hormone receptors. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with AR, SMARCA4/BRG1 and SMARCE1/BAF57. Interaction
CC with either SMARCA4 and SMARCE1 enhances AR-mediated transcription (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Detected at
CC replication foci throughout S phase. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8CIE2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CIE2-2; Sequence=VSP_012191;
CC Name=3;
CC IsoId=Q8CIE2-3; Sequence=VSP_024919;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC33364.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL607152; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024081; AAH24081.1; -; mRNA.
DR EMBL; BC060652; AAH60652.1; -; mRNA.
DR EMBL; BC063069; AAH63069.1; -; mRNA.
DR EMBL; AK048533; BAC33364.1; ALT_INIT; mRNA.
DR CCDS; CCDS24417.1; -. [Q8CIE2-2]
DR CCDS; CCDS24418.1; -. [Q8CIE2-1]
DR RefSeq; NP_001005867.1; NM_001005867.1. [Q8CIE2-2]
DR RefSeq; NP_082877.2; NM_028601.3. [Q8CIE2-1]
DR RefSeq; XP_006514811.1; XM_006514748.2. [Q8CIE2-1]
DR RefSeq; XP_006514813.1; XM_006514750.3. [Q8CIE2-1]
DR RefSeq; XP_011242034.1; XM_011243732.1. [Q8CIE2-1]
DR RefSeq; XP_011242035.1; XM_011243733.2. [Q8CIE2-3]
DR AlphaFoldDB; Q8CIE2; -.
DR SMR; Q8CIE2; -.
DR IntAct; Q8CIE2; 1.
DR STRING; 10090.ENSMUSP00000012612; -.
DR iPTMnet; Q8CIE2; -.
DR PhosphoSitePlus; Q8CIE2; -.
DR EPD; Q8CIE2; -.
DR MaxQB; Q8CIE2; -.
DR PaxDb; Q8CIE2; -.
DR PeptideAtlas; Q8CIE2; -.
DR PRIDE; Q8CIE2; -.
DR ProteomicsDB; 299564; -. [Q8CIE2-1]
DR ProteomicsDB; 299565; -. [Q8CIE2-2]
DR ProteomicsDB; 299566; -. [Q8CIE2-3]
DR Antibodypedia; 27318; 105 antibodies from 23 providers.
DR DNASU; 52915; -.
DR Ensembl; ENSMUST00000012612; ENSMUSP00000012612; ENSMUSG00000041164. [Q8CIE2-1]
DR Ensembl; ENSMUST00000102914; ENSMUSP00000099978; ENSMUSG00000041164. [Q8CIE2-2]
DR Ensembl; ENSMUST00000109785; ENSMUSP00000105408; ENSMUSG00000041164. [Q8CIE2-3]
DR Ensembl; ENSMUST00000109786; ENSMUSP00000105409; ENSMUSG00000041164. [Q8CIE2-1]
DR Ensembl; ENSMUST00000109787; ENSMUSP00000105410; ENSMUSG00000041164. [Q8CIE2-1]
DR GeneID; 52915; -.
DR KEGG; mmu:52915; -.
DR UCSC; uc007hym.1; mouse. [Q8CIE2-2]
DR UCSC; uc056yjq.1; mouse. [Q8CIE2-1]
DR CTD; 83637; -.
DR MGI; MGI:106374; Zmiz2.
DR VEuPathDB; HostDB:ENSMUSG00000041164; -.
DR eggNOG; KOG2169; Eukaryota.
DR GeneTree; ENSGT01030000234539; -.
DR HOGENOM; CLU_009461_1_0_1; -.
DR InParanoid; Q8CIE2; -.
DR OMA; GPPSISY; -.
DR OrthoDB; 273193at2759; -.
DR PhylomeDB; Q8CIE2; -.
DR TreeFam; TF316952; -.
DR BioGRID-ORCS; 52915; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Zmiz2; mouse.
DR PRO; PR:Q8CIE2; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8CIE2; protein.
DR Bgee; ENSMUSG00000041164; Expressed in perirhinal cortex and 284 other tissues.
DR Genevisible; Q8CIE2; MM.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0043596; C:nuclear replication fork; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF02891; zf-MIZ; 1.
DR PROSITE; PS51044; ZF_SP_RING; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Isopeptide bond; Metal-binding; Methylation; Nucleus;
KW Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..920
FT /note="Zinc finger MIZ domain-containing protein 2"
FT /id="PRO_0000218990"
FT ZN_FING 585..671
FT /note="SP-RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..506
FT /note="Interaction with AR"
FT /evidence="ECO:0000250"
FT REGION 732..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..383
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 616
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 618
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 639
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 642
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT MOD_RES 111
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 245
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 262
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 402
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NF64"
FT CROSSLNK 457
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NF64"
FT CROSSLNK 692
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NF64"
FT VAR_SEQ 56..87
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012191"
FT VAR_SEQ 333..358
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_024919"
SQ SEQUENCE 920 AA; 96719 MW; 0F9C6A6D53146279 CRC64;
MNPMNPMKPA LPPAPHGDGS FAYESVPWQQ SATQPAGSLS VVTTVWGVGN ATQSQVLGNP
MGPAGSPPGG SMMPGVAGGS SALTSPQCLG QQAFAEGGAS KSYVQQGVYG RGSYPGGSSF
TTGYAGGPAG LGLPTHAARP STDFTQAAAA AAMAAAAATA TATATATVAA LQEKQSQELS
QYGAMGTGQS FNSQFLQHGG PRGPSVPPGM NPSGMGGMMG PSGLSSMAMT PTRAAGMTPL
YAGQRLPQHG YPGPPQGQPL PRQGIKRAYS EVYPGQQYLQ GGQYAANTAQ YAPGPGQPPG
PASSYAGHRL PLQQGMAQSL SAPGPTGLHY KPTEQFNGQG ASFNGGSISY SQPGLSGPSR
SIPGYPSSPL PGNPTPPMTP SSNVPYMSPS QEVKSPFLPD LKPGLSSLHP SPSASVHCDE
LRLTFPVRDG VVLEPFRLQH NLAVSNHVFQ LRDSVYKTLM LRPDLELQFK CYHHEDRQMN
TNWPASVQVS VNATPLSIER GDNKTSHKPL YLKHVCQPGR NTIQITVTAC CCSHLFVLQL
VHRPSVRSVL QGLLKKRLLP AEHCITKIKR NFSSGTIPGT PGPNGEDGVE QTAIKVSLKC
PITFRRIQLP ARGHDCRHIQ CFDLESYLQL NCERGTWRCP VCNKTALLEG LEVDQYMLGI
LIYIQNSDYE EITIDPTCSW KPVPVKPDLH IKEEPDGPVL KRCRTVSPAH VLMPSVMEMI
AALGPGAAPF APLQPPSAPT PSDYPSQGSN FMGPGTFPES FPSATPTTPN LAEFTQGPPP
ISYQSDIPSS LLTPDKSTPC LPGQMAPAGH LDPAHNPGPP GLHTPNLGPT PGTQLHHPNP
SPASRQPLGQ PNTGPISELA FNPASGMMGP PSMTGAGEAS EPALDLLPEL TNPDELLSYL
GPPDLPTNSS DDLLSLFENN
