FOG2_MOUSE
ID FOG2_MOUSE Reviewed; 1151 AA.
AC Q8CCH7; Q9Z0F2;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Zinc finger protein ZFPM2;
DE AltName: Full=Friend of GATA protein 2;
DE Short=FOG-2;
DE Short=Friend of GATA 2;
DE Short=mFOG-2;
DE AltName: Full=Zinc finger protein multitype 2;
GN Name=Zfpm2; Synonyms=Fog2;
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), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND INTERACTION WITH GATA4.
RC TISSUE=Heart;
RX PubMed=9927675; DOI=10.1073/pnas.96.3.956;
RA Svensson E.C., Tufts R.L., Polk C.E., Leiden J.M.;
RT "Molecular cloning of FOG-2: a modulator of transcription factor GATA-4 in
RT cardiomyocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:956-961(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND INTERACTION WITH GATA4.
RC TISSUE=Embryo;
RX PubMed=9927674; DOI=10.1073/pnas.96.3.950;
RA Tevosian S.G., Deconinck A.E., Cantor A.B., Rieff H.I., Fujiwara Y.,
RA Corfas G., Orkin S.H.;
RT "FOG-2: a novel GATA-family cofactor related to multitype zinc-finger
RT proteins Friend of GATA-1 and U-shaped.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:950-955(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND INTERACTION WITH GATA4 AND GATA5.
RC TISSUE=Embryonic heart;
RX PubMed=10330188; DOI=10.1128/mcb.19.6.4495;
RA Lu J.-R., McKinsey T.A., Xu H., Wang D.-Z., Richardson J.A., Olson E.N.;
RT "FOG-2, a heart- and brain-enriched cofactor for GATA transcription
RT factors.";
RL Mol. Cell. Biol. 19:4495-4502(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [6]
RP DOMAIN.
RX PubMed=10329627; DOI=10.1093/emboj/18.10.2812;
RA Fox A.H., Liew C., Holmes M., Kowalski K., Mackay J., Crossley M.;
RT "Transcriptional cofactors of the FOG family interact with GATA proteins by
RT means of multiple zinc fingers.";
RL EMBO J. 18:2812-2822(1999).
RN [7]
RP INTERACTION WITH CTBP2.
RX PubMed=10801815; DOI=10.1074/jbc.m001522200;
RA Svensson E.C., Huggins G.S., Dardik F.B., Polk C.E., Leiden J.M.;
RT "A functionally conserved N-terminal domain of the friend of GATA-2 (FOG-2)
RT protein represses GATA4-dependent transcription.";
RL J. Biol. Chem. 275:20762-20769(2000).
RN [8]
RP FUNCTION.
RX PubMed=10892744; DOI=10.1016/s0092-8674(00)80885-5;
RA Tevosian S.G., Deconinck A.E., Tanaka M., Schinke M., Litovsky S.H.,
RA Izumo S., Fujiwara Y., Orkin S.H.;
RT "FOG-2, a cofactor for GATA transcription factors, is essential for heart
RT morphogenesis and development of coronary vessels from epicardium.";
RL Cell 101:729-739(2000).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10888889; DOI=10.1038/77146;
RA Svensson E.C., Huggins G.S., Lin H., Clendenin C., Jiang F., Tufts R.,
RA Dardik F.B., Leiden J.M.;
RT "A syndrome of tricuspid atresia in mice with a targeted mutation of the
RT gene encoding Fog-2.";
RL Nat. Genet. 25:353-356(2000).
RN [10]
RP INTERACTION WITH NR2F1; NR2F2 AND NR2F6.
RX PubMed=11382775; DOI=10.1074/jbc.m103577200;
RA Huggins G.S., Bacani C.J., Boltax J., Aikawa R., Leiden J.M.;
RT "Friend of GATA 2 physically interacts with chicken ovalbumin upstream
RT promoter-TF2 (COUP-TF2) and COUP-TF3 and represses COUP-TF2-dependent
RT activation of the atrial natriuretic factor promoter.";
RL J. Biol. Chem. 276:28029-28036(2001).
RN [11]
RP FUNCTION.
RX PubMed=12223418; DOI=10.1242/dev.129.19.4627;
RA Tevosian S.G., Albrecht K.H., Crispino J.D., Fujiwara Y., Eicher E.M.,
RA Orkin S.H.;
RT "Gonadal differentiation, sex determination and normal Sry expression in
RT mice require direct interaction between transcription partners GATA4 and
RT FOG2.";
RL Development 129:4627-4634(2002).
RN [12]
RP INTERACTION WITH RXRA.
RX PubMed=10999851; DOI=10.1210/jcem.85.9.6828;
RA Laitinen M.P., Anttonen M., Ketola I., Wilson D.B., Ritvos O., Butzow R.,
RA Heikinheimo M.;
RT "Transcription factors GATA-4 and GATA-6 and a GATA family cofactor, FOG-2,
RT are expressed in human ovary and sex cord-derived ovarian tumors.";
RL J. Clin. Endocrinol. Metab. 85:3476-3483(2000).
RN [13]
RP INTERACTION WITH ATOH8.
RX PubMed=23836893; DOI=10.1074/jbc.m113.463083;
RA Rawnsley D.R., Xiao J., Lee J.S., Liu X., Mericko-Ishizuka P., Kumar V.,
RA He J., Basu A., Lu M., Lynn F.C., Pack M., Gasa R., Kahn M.L.;
RT "The transcription factor Atonal homolog 8 regulates Gata4 and Friend of
RT Gata-2 during vertebrate development.";
RL J. Biol. Chem. 288:24429-24440(2013).
CC -!- FUNCTION: Transcription regulator that plays a central role in heart
CC morphogenesis and development of coronary vessels from epicardium, by
CC regulating genes that are essential during cardiogenesis. Essential
CC cofactor that acts via the formation of a heterodimer with
CC transcription factors of the GATA family GATA4, GATA5 and GATA6. Such
CC heterodimer can both activate or repress transcriptional activity,
CC depending on the cell and promoter context. Also required in gonadal
CC differentiation, possibly be regulating expression of SRY. Probably
CC acts a corepressor of NR2F2. {ECO:0000269|PubMed:10330188,
CC ECO:0000269|PubMed:10888889, ECO:0000269|PubMed:10892744,
CC ECO:0000269|PubMed:12223418, ECO:0000269|PubMed:9927674,
CC ECO:0000269|PubMed:9927675}.
CC -!- SUBUNIT: Interacts with the N-terminal zinc-finger of GATA4, GATA5 and
CC probably GATA6. Interacts with retinoid nuclear receptor RXRA when
CC ligand bound. Interacts with corepressor CTBP2; this interaction is
CC however not essential for corepressor activity. Interacts with NR2F2
CC and NR2F6. Interacts with ATOH8; mediates indirect interaction with
CC GATA4. {ECO:0000269|PubMed:10330188, ECO:0000269|PubMed:10801815,
CC ECO:0000269|PubMed:10999851, ECO:0000269|PubMed:11382775,
CC ECO:0000269|PubMed:23836893, ECO:0000269|PubMed:9927674,
CC ECO:0000269|PubMed:9927675}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10330188,
CC ECO:0000269|PubMed:9927674, ECO:0000269|PubMed:9927675}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8CCH7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CCH7-2; Sequence=VSP_009703, VSP_009704;
CC Name=3;
CC IsoId=Q8CCH7-3; Sequence=VSP_009705;
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain and testis. Weakly
CC expressed in lung and liver. First expressed at approximately E8.5 in
CC the developing ventral heart tube and septum transversum. Cardiac
CC expression persists throughout the remainder of embryonic development
CC in the atria as well as in all layers of the ventricles (endocardium,
CC myocardium, and pericardium). Expressed in the neuroepithelium of the
CC developing midbrain and hindbrain from 11.5 dpc and increased in
CC intensity between 12 dpc and 16.5 dpc. Also expressed in the urogenital
CC ridge beginning at 11.5 dpc and subsequently localized to the gonads by
CC 16.5 dpc. Colocalizes with GATA4 GATA5 and GATA6 in the developing
CC heart, GATA3 in the brain, and GATA4 in the gonads.
CC {ECO:0000269|PubMed:10330188, ECO:0000269|PubMed:9927674,
CC ECO:0000269|PubMed:9927675}.
CC -!- DOMAIN: The CCHC FOG-type zinc fingers 1, 2, 3 and 5 directly bind to
CC GATA-type zinc fingers. The Tyr residue adjacent to the last Cys of the
CC CCHC FOG-type zinc finger is probably essential for the interaction
CC with GATA-type zinc fingers. {ECO:0000269|PubMed:10329627}.
CC -!- PTM: Sumoylation reduces transcriptional repression activity.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice die of congestive heart failure at 13 dpc
CC with a syndrome of tricuspid atresia that includes an absent tricuspid
CC valve, a large atrial and ventricular spetal defects, an elongated left
CC ventricular outflow tract, rightward displacement of the aortic valve
CC and pulmonic stenosis. These mice also display hypoplasia of the
CC compact zone of the left ventricle. {ECO:0000269|PubMed:10888889}.
CC -!- MISCELLANEOUS: [Isoform 3]: Splicing donor site between exon 3 and 4 is
CC not canonical. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FOG (Friend of GATA) family.
CC {ECO:0000255|PROSITE-ProRule:PRU01153}.
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DR EMBL; AF118845; AAD17251.1; -; mRNA.
DR EMBL; AF107306; AAD12182.1; -; mRNA.
DR EMBL; AF125166; AAD33250.1; -; mRNA.
DR EMBL; AK033131; BAC28166.1; -; mRNA.
DR EMBL; BC059241; AAH59241.1; -; mRNA.
DR CCDS; CCDS27447.1; -. [Q8CCH7-1]
DR PIR; T18297; T18297.
DR RefSeq; NP_035896.1; NM_011766.5. [Q8CCH7-1]
DR AlphaFoldDB; Q8CCH7; -.
DR BioGRID; 204688; 2.
DR STRING; 10090.ENSMUSP00000051335; -.
DR iPTMnet; Q8CCH7; -.
DR PhosphoSitePlus; Q8CCH7; -.
DR MaxQB; Q8CCH7; -.
DR PaxDb; Q8CCH7; -.
DR PRIDE; Q8CCH7; -.
DR ProteomicsDB; 267388; -. [Q8CCH7-1]
DR ProteomicsDB; 267389; -. [Q8CCH7-2]
DR ProteomicsDB; 267390; -. [Q8CCH7-3]
DR Antibodypedia; 1311; 144 antibodies from 27 providers.
DR DNASU; 22762; -.
DR Ensembl; ENSMUST00000053467; ENSMUSP00000051335; ENSMUSG00000022306. [Q8CCH7-1]
DR GeneID; 22762; -.
DR KEGG; mmu:22762; -.
DR UCSC; uc007voq.1; mouse. [Q8CCH7-2]
DR UCSC; uc007vos.1; mouse. [Q8CCH7-1]
DR CTD; 23414; -.
DR MGI; MGI:1334444; Zfpm2.
DR VEuPathDB; HostDB:ENSMUSG00000022306; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00530000063823; -.
DR HOGENOM; CLU_010755_0_0_1; -.
DR InParanoid; Q8CCH7; -.
DR OMA; LKHPMSI; -.
DR OrthoDB; 76702at2759; -.
DR PhylomeDB; Q8CCH7; -.
DR TreeFam; TF331342; -.
DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 22762; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Zfpm2; mouse.
DR PRO; PR:Q8CCH7; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8CCH7; protein.
DR Bgee; ENSMUSG00000022306; Expressed in ureter smooth muscle and 183 other tissues.
DR ExpressionAtlas; Q8CCH7; baseline and differential.
DR Genevisible; Q8CCH7; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR GO; GO:0003181; P:atrioventricular valve morphogenesis; TAS:BHF-UCL.
DR GO; GO:0048738; P:cardiac muscle tissue development; IMP:MGI.
DR GO; GO:0055008; P:cardiac muscle tissue morphogenesis; TAS:BHF-UCL.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0048568; P:embryonic organ development; IMP:MGI.
DR GO; GO:0007507; P:heart development; IDA:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:0003192; P:mitral valve formation; TAS:BHF-UCL.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:BHF-UCL.
DR GO; GO:2000195; P:negative regulation of female gonad development; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0003151; P:outflow tract morphogenesis; TAS:BHF-UCL.
DR GO; GO:0003148; P:outflow tract septum morphogenesis; ISO:MGI.
DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IGI:BHF-UCL.
DR GO; GO:2000020; P:positive regulation of male gonad development; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0003221; P:right ventricular cardiac muscle tissue morphogenesis; ISO:MGI.
DR GO; GO:0003195; P:tricuspid valve formation; TAS:BHF-UCL.
DR GO; GO:0001570; P:vasculogenesis; IDA:MGI.
DR GO; GO:0060979; P:vasculogenesis involved in coronary vascular morphogenesis; TAS:DFLAT.
DR GO; GO:0060412; P:ventricular septum morphogenesis; ISO:MGI.
DR InterPro; IPR039746; FOG.
DR InterPro; IPR034731; ZF_CCHC_FOG.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR12958; PTHR12958; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS51810; ZF_CCHC_FOG; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cardiomyopathy; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1151
FT /note="Zinc finger protein ZFPM2"
FT /id="PRO_0000221044"
FT ZN_FING 244..277
FT /note="CCHC FOG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT ZN_FING 296..320
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 335..357
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 363..385
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 542..575
FT /note="CCHC FOG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT ZN_FING 681..714
FT /note="CCHC FOG-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT ZN_FING 848..881
FT /note="CCHC FOG-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT ZN_FING 1113..1146
FT /note="CCHC FOG-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..835
FT /note="Interaction with CTBP2"
FT /evidence="ECO:0000305"
FT REGION 1004..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1049..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 736..740
FT /note="Nuclear localization signal"
FT COMPBIAS 65..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1025
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1073
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 550
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 553
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 566
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 571
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 689
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 692
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 705
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 710
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 856
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 859
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 872
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 877
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 1121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 1124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 1137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 1142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WW38"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WW38"
FT MOD_RES 904
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WW38"
FT MOD_RES 1014
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WW38"
FT CROSSLNK 324
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q8WW38"
FT CROSSLNK 444
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8WW38"
FT CROSSLNK 471
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q8WW38"
FT CROSSLNK 915
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q8WW38"
FT CROSSLNK 955
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q8WW38"
FT VAR_SEQ 102..111
FT /note="ELEVFQRDGE -> RTESTAFNPL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009703"
FT VAR_SEQ 112..1151
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009704"
FT VAR_SEQ 381..398
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009705"
SQ SEQUENCE 1151 AA; 127692 MW; 2759B0AA65D84F9E CRC64;
MSRRKQSKPR QIKRPLEDAI DDEEEECPVE EAEVISKGDF PLEGSFPAGF EPENLSCEDV
EFFCNKGDDE GIQEPAESDG DSHSDKPGQP GVETDDWDGP GELEVFQRDG ERKIQSRQQL
PVGTTWGPFA GKMDLNNNSL KTKAQVPMVL TAGPKWLLDV TWQGVEDSKN NCIVYSKGGQ
LWCTTTKAIS EGEELVAFVV DFDSRLQAAS HMTLTEGMYP ARLLDSIQLL PQQAAMASIL
PTAIVNKDIF PCKSCGIWYR SERNLQAHLM YYCSGRQREA APVSEENEDN SHQVSSLCPF
PQCTKSFSNA RALEMHLNSH SGVKMEEFLP PGASLKCTVC SYTADSVINF HQHLFSHLTQ
AAFRCNHCHF GFQTQRELLQ HQELHVPSGK LPRESDMEHS PSGTEDSLQP ATDLLARSDL
SQSQKAMPTK DASSDTELDK CEKKTQLFLT NQRPEIQPAA NKQNFSYTKI KSEPSSPRLA
SSPVQPNIGP SFPVGPFLSQ FAFPQDITMV PQASEILAKM SELVHRRLRH GSSSYPPVIY
SPLMPKGATC FECNITFNNL DNYLVHKKHY CSSRWQQMAK SPEFPSVSEK MPEAVSPNTG
QTSINLLNPA AHSSDPENPL LQTSCINSST VLDLIGPNGK GHEKDFSTQV KKLPTSNSSD
DKINGKPVDV KNPSGPLVDG ESDPNKTTCE ACNITFSRHE TYMVHKQYYC ATRHDPPLKR
SASNKVPAMQ RTMRTRKRRK MYEMCLPEQE QRPPLVQQRF LDVANLSNPC SSTQEPTEGL
GECYHPRCDI FPGIVSKHLE TSLAMNKCVP VPKCDTTHSN VSCLEMDVPI DLSKKCLSQS
ERTTASPKRL LDYHECTVCK ISFNKVENYL AHKQNFCPVT AHQRNDLGQL DGKVFPNPES
ERSSPEVSFE RNMIKCEKNG NPKQPSPNGN LFSSHLATLQ GLKVFSEAAQ LIATKEENKH
LFLPQCLYPG AIKKTKGADQ LSPYYGIKPS DYIASSLVIH NTDVEQSTNT ENESPKGQAS
SNGCAVPKKD SLPLLPKNRG MVIVNGGLKQ DERPTANPQQ ENISQNTQHE DGHKSPSWIS
ENPLAANENV SPGIPCAEEQ LSSIAKGVNG ASQAPSSGKY CRLCDIQFNN LSNFITHKKF
YCSSHAAEHV K
