ZMIZ1_MOUSE
ID ZMIZ1_MOUSE Reviewed; 1072 AA.
AC Q6P1E1; Q6PDK9; Q6PF85; Q8BW47;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Zinc finger MIZ domain-containing protein 1;
DE AltName: Full=PIAS-like protein Zimp10;
DE AltName: Full=Retinoic acid-induced protein 17;
GN Name=Zmiz1; Synonyms=Rai17, Zimp10;
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 MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, and Mammary tumor;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-416 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Ovary;
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 DISRUPTION PHENOTYPE.
RX PubMed=16862223; DOI=10.1621/nrs.04017;
RA Beliakoff J., Sun Z.;
RT "Zimp7 and Zimp10, two novel PIAS-like proteins, function as androgen
RT receptor coregulators.";
RL Nucl. Recept. Signal. 4:17-17(2006).
RN [4]
RP FUNCTION.
RX PubMed=23161489; DOI=10.1158/0008-5472.can-12-1389;
RA Rakowski L.A., Garagiola D.D., Li C.M., Decker M., Caruso S., Jones M.,
RA Kuick R., Cierpicki T., Maillard I., Chiang M.Y.;
RT "Convergence of the ZMIZ1 and NOTCH1 pathways at C-MYC in acute T
RT lymphoblastic leukemias.";
RL Cancer Res. 73:930-941(2013).
RN [5]
RP FUNCTION.
RX PubMed=26522984; DOI=10.1016/j.immuni.2015.10.007;
RA Pinnell N., Yan R., Cho H.J., Keeley T., Murai M.J., Liu Y., Alarcon A.S.,
RA Qin J., Wang Q., Kuick R., Elenitoba-Johnson K.S., Maillard I.,
RA Samuelson L.C., Cierpicki T., Chiang M.Y.;
RT "The PIAS-like coactivator Zmiz1 is a direct and selective cofactor of
RT Notch1 in T cell development and leukemia.";
RL Immunity 43:870-883(2015).
RN [6]
RP INTERACTION WITH SMARCA4, AND TISSUE SPECIFICITY.
RX PubMed=26163108; DOI=10.1007/s10048-015-0452-2;
RA Cordova-Fletes C., Dominguez M.G., Delint-Ramirez I.,
RA Martinez-Rodriguez H.G., Rivas-Estilla A.M., Barros-Nunez P.,
RA Ortiz-Lopez R., Neira V.A.;
RT "A de novo t(10;19)(q22.3;q13.33) leads to ZMIZ1/PRR12 reciprocal fusion
RT transcripts in a girl with intellectual disability and neuropsychiatric
RT alterations.";
RL Neurogenetics 16:287-298(2015).
CC -!- FUNCTION: Acts as transcriptional coactivator. Increases ligand-
CC dependent transcriptional activity of AR and promotes AR sumoylation.
CC The stimulation of AR activity is dependent upon sumoylation (By
CC similarity). Also functions as a transcriptional coactivator in the
CC TGF-beta signaling pathway by increasing the activity of the
CC SMAD3/SMAD4 transcriptional complex (By similarity). Involved in
CC transcriptional activation of a subset of NOTCH1 target genes including
CC MYC. Involved in thymocyte and T cell development (PubMed:26522984).
CC Involved in the regulation of postmitotic positioning of pyramidal
CC neurons in the developing cerebral cortex (By similarity).
CC {ECO:0000250|UniProtKB:Q9ULJ6, ECO:0000269|PubMed:26522984}.
CC -!- SUBUNIT: Interacts with AR, but not with ESR1, NR3C1, PGR, THRB nor
CC VDR. Interacts with NOTCH1 and RBPJ (By similarity). Interacts with
CC SMARCA4. Interacts (via SP-RING-type domain) with SMAD3 and SMAD4 (via
CC MH2 domain) (By similarity). {ECO:0000250|UniProtKB:Q9ULJ6,
CC ECO:0000269|PubMed:26163108}.
CC -!- INTERACTION:
CC Q6P1E1; Q3TKT4: Smarca4; NbExp=2; IntAct=EBI-647033, EBI-1210244;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q9ULJ6}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9ULJ6}. Note=Enriched at replication foci
CC throughout S phase. {ECO:0000250|UniProtKB:Q9ULJ6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P1E1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P1E1-2; Sequence=VSP_012187;
CC -!- TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:26163108}.
CC -!- DOMAIN: The C-terminal proline-rich domain possesses a significant
CC intrinsic transcriptional activity. This activity is inhibited by the
CC N-terminus in the full-length protein. {ECO:0000250|UniProtKB:Q9ULJ6}.
CC -!- DOMAIN: The SP-RING-type domain mediates interaction with SMAD3 and
CC SMAD4. {ECO:0000250|UniProtKB:Q9ULJ6}.
CC -!- DISRUPTION PHENOTYPE: Death between 9.5-10.5 dpc. Mice are
CC approximately half the size of wild-type littermates and display
CC vascular and cell viability defects. Some heterozygotes also do not
CC survive but those that do have no apparent defects.
CC {ECO:0000269|PubMed:16862223}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH57691.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC35753.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC35753.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; BC057691; AAH57691.1; ALT_INIT; mRNA.
DR EMBL; BC058646; AAH58646.1; -; mRNA.
DR EMBL; BC065120; AAH65120.1; -; mRNA.
DR EMBL; AK054366; BAC35753.1; ALT_SEQ; mRNA.
DR CCDS; CCDS26873.1; -. [Q6P1E1-1]
DR CCDS; CCDS79280.1; -. [Q6P1E1-2]
DR RefSeq; NP_001297595.1; NM_001310666.1. [Q6P1E1-2]
DR RefSeq; NP_899031.2; NM_183208.4. [Q6P1E1-1]
DR AlphaFoldDB; Q6P1E1; -.
DR SMR; Q6P1E1; -.
DR BioGRID; 236589; 1.
DR IntAct; Q6P1E1; 5.
DR STRING; 10090.ENSMUSP00000124863; -.
DR iPTMnet; Q6P1E1; -.
DR PhosphoSitePlus; Q6P1E1; -.
DR EPD; Q6P1E1; -.
DR MaxQB; Q6P1E1; -.
DR PaxDb; Q6P1E1; -.
DR PeptideAtlas; Q6P1E1; -.
DR PRIDE; Q6P1E1; -.
DR ProteomicsDB; 302065; -. [Q6P1E1-1]
DR ProteomicsDB; 302066; -. [Q6P1E1-2]
DR Antibodypedia; 29855; 169 antibodies from 26 providers.
DR DNASU; 328365; -.
DR Ensembl; ENSMUST00000007961; ENSMUSP00000007961; ENSMUSG00000007817. [Q6P1E1-2]
DR Ensembl; ENSMUST00000162645; ENSMUSP00000124863; ENSMUSG00000007817. [Q6P1E1-1]
DR GeneID; 328365; -.
DR KEGG; mmu:328365; -.
DR UCSC; uc007srn.2; mouse. [Q6P1E1-1]
DR UCSC; uc007sro.2; mouse. [Q6P1E1-2]
DR CTD; 57178; -.
DR MGI; MGI:3040693; Zmiz1.
DR VEuPathDB; HostDB:ENSMUSG00000007817; -.
DR eggNOG; KOG2169; Eukaryota.
DR GeneTree; ENSGT01030000234539; -.
DR HOGENOM; CLU_009461_1_0_1; -.
DR InParanoid; Q6P1E1; -.
DR OMA; PPMAMNQ; -.
DR PhylomeDB; Q6P1E1; -.
DR TreeFam; TF316952; -.
DR BioGRID-ORCS; 328365; 8 hits in 73 CRISPR screens.
DR ChiTaRS; Zmiz1; mouse.
DR PRO; PR:Q6P1E1; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q6P1E1; protein.
DR Bgee; ENSMUSG00000007817; Expressed in humerus cartilage element and 244 other tissues.
DR Genevisible; Q6P1E1; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IBA:GO_Central.
DR GO; GO:0046332; F:SMAD binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030521; P:androgen receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0048844; P:artery morphogenesis; IMP:MGI.
DR GO; GO:0090398; P:cellular senescence; IDA:MGI.
DR GO; GO:0048589; P:developmental growth; IMP:MGI.
DR GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:MGI.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IMP:UniProtKB.
DR GO; GO:1903508; P:positive regulation of nucleic acid-templated transcription; ISS:UniProtKB.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0021852; P:pyramidal neuron migration to cerebral cortex; ISO:MGI.
DR GO; GO:0033233; P:regulation of protein sumoylation; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0060395; P:SMAD protein signal transduction; ISS:UniProtKB.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR GO; GO:0007296; P:vitellogenesis; IMP:MGI.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR040797; Zmiz1_N.
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF02891; zf-MIZ; 1.
DR Pfam; PF18028; Zmiz1_N; 1.
DR PROSITE; PS51044; ZF_SP_RING; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cytoplasm; Isopeptide bond; Metal-binding;
KW Nucleus; Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1072
FT /note="Zinc finger MIZ domain-containing protein 1"
FT /id="PRO_0000218988"
FT ZN_FING 734..815
FT /note="SP-RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT REGION 1..120
FT /note="Sufficient for transactivation activity; sufficient
FT for interaction with NOTCH1"
FT /evidence="ECO:0000250|UniProtKB:Q9ULJ6"
FT REGION 112..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..1072
FT /note="Transactivation domain"
FT /evidence="ECO:0000250|UniProtKB:Q9ULJ6"
FT REGION 875..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..450
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..538
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..1002
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1023
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1072
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 765
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 767
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 788
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 791
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT CROSSLNK 91
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULJ6"
FT CROSSLNK 841
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULJ6"
FT CROSSLNK 850
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULJ6"
FT VAR_SEQ 320..325
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012187"
SQ SEQUENCE 1072 AA; 115851 MW; 53B1AF1338EBDB17 CRC64;
MNSMDRHIQQ TNDRLQCIKQ HLQNPANFHN AATELLDWCG DPRAFQRPFE QSLMGCLTVV
SRVAAQQGFD LDLGYRLLAV CAANRDKFTP KSAALLSSWC EELGRLLLLR HQKSRQNDPP
GKLPMQPPLS SMSSMKPTLS HSDGSFPYDS VPWQQNTNQP PGSLSVVTTV WGVTNTSQSQ
VLGNPMANAN NPMNPGGNPM ASGMSTSNPG INSPQFAGQQ QQFSTKAGPA QPYIQPNMYG
RPGYPGSGGF GASYPGGPSA PAGMGIPPHT RPPADFTQPA AAAAAAAVAA AAATATATAT
ATVAALQETQ NKDINQYGPV CSSFQMGPTQ AYNSQFMNQP GPRGPASMGG SLNPAGMAAG
MTPSGMSGPP MGMNQPRPPG ISPFGTHGQR MPQQTYPGPR PQSLPIQSIK RPYPGEPNYG
NQQYGPNSQF PTQPGQYPTP NPPRPLTSPN YPGQRMPSQP STGQYPPPTV NMGQYYKPEQ
FNGQNNTFSS GSSYSSYSQG SVNRPPRPVP VANYPHSPVP GNPTPPMTPG SSIPPYLSPS
QDVKPPFPPD IKPNMSALPP PPANHNDELR LTFPVRDGVV LEPFRLEHNL AVSNHVFHLR
PTVHQTLMWR SDLELQFKCY HHEDRQMNTN WPASVQVSVN ATPLTIERGD NKTSHKPLHL
KHVCQPGRNT IQITVTACCC SHLFVLQLVH RPSVRSVLQG LLKKRLLPAE HCITKIKRNF
SSVAASSGNT TLNGEDGVEQ TAIKVSLKCP ITFRRIQLPA RGHDCKHVQC FDLESYLQLN
CERGTWRCPV CNKTALLEGL EVDQYMWGIL NAIQHSEFEE VTIDPTCSWR PVPIKSDLHI
KDDPDGIPSK RFKTMSPSQM IMPNVMEMIA ALGPGPSPYP LPPPPGGTSS NDYSSQGNNY
QGHGNFDFPH GNPGGTSMND FMHGPPQLSH PPDMPNNMAA LEKPLSHPMQ ETMPHAGSSD
QPHPSIQQGL HVPHPSSQAG PPLHHSGAPP PSQPPRQPPQ AAPGNHPHSD LTFNPSSALE
GQAGAQGASD MPEPSLDLLP ELTNPDELLS YLDPPDLPSN SNDDLLSLFE NN
