TYY1_MOUSE
ID TYY1_MOUSE Reviewed; 414 AA.
AC Q00899;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Transcriptional repressor protein YY1;
DE AltName: Full=Delta transcription factor;
DE AltName: Full=NF-E1;
DE AltName: Full=UCR-motif DNA-binding protein;
DE AltName: Full=Yin and yang 1;
DE Short=YY-1;
GN Name=Yy1; Synonyms=Ucrbp;
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].
RX PubMed=1309593; DOI=10.1128/mcb.12.1.38-44.1992;
RA Flanagan J.R., Becker K.G., Ennist D.L., Gleason S.L., Driggers P.H.,
RA Levi B.-Z., Appella E., Ozato K.;
RT "Cloning of a negative transcription factor that binds to the upstream
RT conserved region of Moloney murine leukemia virus.";
RL Mol. Cell. Biol. 12:38-44(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=8516301; DOI=10.1073/pnas.90.12.5559;
RA Safrany G., Perry R.P.;
RT "Characterization of the mouse gene that encodes the delta/YY1/NF-E1/UCRBP
RT transcription factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5559-5563(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1946404; DOI=10.1073/pnas.88.21.9799;
RA Hariharan N., Kelley D.E., Perry R.P.;
RT "Delta, a transcription factor that binds to downstream elements in several
RT polymerase II promoters, is a functionally versatile zinc finger protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:9799-9803(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 FUNCTION, DNA-BINDING, AND IDENTIFICATION IN A COMPLEX WITH SMAD1 AND
RP SMAD4.
RX PubMed=15329343; DOI=10.1242/dev.01344;
RA Lee K.H., Evans S., Ruan T.Y., Lassar A.B.;
RT "SMAD-mediated modulation of YY1 activity regulates the BMP response and
RT cardiac-specific expression of a GATA4/5/6-dependent chick Nkx2.5
RT enhancer.";
RL Development 131:4709-4723(2004).
RN [6]
RP FUNCTION IN DNA REPAIR.
RX PubMed=18026119; DOI=10.1038/nsmb1332;
RA Wu S., Shi Y., Mulligan P., Gay F., Landry J., Liu H., Lu J., Qi H.H.,
RA Wang W., Nickoloff J.A., Wu C., Shi Y.;
RT "A YY1-INO80 complex regulates genomic stability through homologous
RT recombination-based repair.";
RL Nat. Struct. Mol. Biol. 14:1165-1172(2007).
RN [7]
RP INTERACTION WITH SFMBT2, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=18024232; DOI=10.1016/j.modgep.2007.09.005;
RA Kuzmin A., Han Z., Golding M.C., Mann M.R., Latham K.E., Varmuza S.;
RT "The PcG gene Sfmbt2 is paternally expressed in extraembryonic tissues.";
RL Gene Expr. Patterns 8:107-116(2008).
RN [8]
RP FUNCTION IN SPERMATOGENESIS, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19786570; DOI=10.1128/mcb.00679-09;
RA Wu S., Hu Y.C., Liu H., Shi Y.;
RT "Loss of YY1 impacts the heterochromatic state and meiotic double-strand
RT breaks during mouse spermatogenesis.";
RL Mol. Cell. Biol. 29:6245-6256(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP IDENTIFICATION IN A COMPLEX WITH GON4L; SIN3A AND HDAC1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=21454521; DOI=10.1074/jbc.m110.133603;
RA Lu P., Hankel I.L., Hostager B.S., Swartzendruber J.A., Friedman A.D.,
RA Brenton J.L., Rothman P.B., Colgan J.D.;
RT "The developmental regulator protein Gon4l associates with protein YY1, co-
RT repressor Sin3a, and histone deacetylase 1 and mediates transcriptional
RT repression.";
RL J. Biol. Chem. 286:18311-18319(2011).
CC -!- FUNCTION: Multifunctional transcription factor that exhibits positive
CC and negative control on a large number of cellular and viral genes by
CC binding to sites overlapping the transcription start site. Binds to the
CC consensus sequence 5'-CCGCCATNTT-3'; some genes have been shown to
CC contain a longer binding motif allowing enhanced binding; the initial
CC CG dinucleotide can be methylated greatly reducing the binding
CC affinity. The effect on transcription regulation is depending upon the
CC context in which it binds and diverse mechanisms of action include
CC direct activation or repression, indirect activation or repression via
CC cofactor recruitment, or activation or repression by disruption of
CC binding sites or conformational DNA changes. Its activity is regulated
CC by transcription factors and cytoplasmic proteins that have been shown
CC to abrogate or completely inhibit YY1-mediated activation or
CC repression. Binds to the upstream conserved region (UCR) (5'-CGCCATTTT-
CC 3') of Moloney murine leukemia virus (MuLV). Acts synergistically with
CC the SMAD1 and SMAD4 in bone morphogenetic protein (BMP)-mediated
CC cardiac-specific gene expression (PubMed:15329343). Binds to SMAD
CC binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element
CC (BMPRE) of cardiac activating regions (PubMed:15329343). Proposed to
CC recruit the PRC2/EED-EZH2 complex to target genes that are
CC transcriptional repressed. Involved in DNA repair. In vitro, binds to
CC DNA recombination intermediate structures (Holliday junctions).
CC Involved in spermatogenesis and may play a role in meiotic DNA double-
CC strand break repair. Plays a role in regulating enhancer activation (By
CC similarity). {ECO:0000250|UniProtKB:P25490,
CC ECO:0000269|PubMed:15329343, ECO:0000269|PubMed:18026119,
CC ECO:0000269|PubMed:19786570}.
CC -!- FUNCTION: Proposed core component of the chromatin remodeling INO80
CC complex which is involved in transcriptional regulation, DNA
CC replication and probably DNA repair; proposed to target the INO80
CC complex to YY1-responsive elements. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with YAF2 through the region encompassing the first
CC and second zinc fingers. Component of the chromatin remodeling INO80
CC complex; specifically part of a complex module associated with the
CC DBINO domain of INO80. Interacts with EED and EZH2; the interactions
CC are indicative for an association with the PRC2/EED-EZH2 complex (By
CC similarity). Found in a complex with SMAD1 and SMAD4 (PubMed:15329343).
CC Interacts with SFMBT2 (PubMed:18024232). Found in a complex with YY1,
CC SIN3A and HDAC1 (PubMed:21454521). {ECO:0000250,
CC ECO:0000269|PubMed:15329343, ECO:0000269|PubMed:18024232,
CC ECO:0000269|PubMed:21454521}.
CC -!- INTERACTION:
CC Q00899; Q9JLN9: Mtor; NbExp=4; IntAct=EBI-6921536, EBI-1571628;
CC Q00899; O70343: Ppargc1a; NbExp=5; IntAct=EBI-6921536, EBI-1371053;
CC Q00899; Q8K4Q0: Rptor; NbExp=3; IntAct=EBI-6921536, EBI-4567273;
CC Q00899; Q8CG47: Smc4; NbExp=2; IntAct=EBI-6921536, EBI-6921575;
CC Q00899; P48432: Sox2; NbExp=2; IntAct=EBI-6921536, EBI-2313612;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21454521}. Nucleus
CC matrix {ECO:0000269|PubMed:19786570}. Cytoplasm
CC {ECO:0000269|PubMed:21454521}. Note=Associated with the nuclear matrix.
CC In testis, localized to heterochromatin of spermatocytes.
CC {ECO:0000269|PubMed:19786570}.
CC -!- TISSUE SPECIFICITY: Expressed in ovary and, at lower levels, in testis.
CC {ECO:0000269|PubMed:18024232}.
CC -!- DEVELOPMENTAL STAGE: At 7.5 dpc, highly expressed in the ectoplacental
CC cone and, at lower levels, in the embryonic and extraembryonic
CC ectoderm. At 14.5 dpc, highly expressed in placenta and yolk sac, and,
CC at lower levels, in brain and heart. {ECO:0000269|PubMed:18024232}.
CC -!- PTM: Transiently poly-ADP-ribosylated by PARP1 upon DNA damage, with
CC the effect of decreasing affinity of YY1 to its cognate DNA binding
CC sites. {ECO:0000250}.
CC -!- PTM: Ubiquitinated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Spermatocytes have a significant decrease in the
CC global level of the heterochromatin markers and increase in the
CC chromosomal double-strand break (DSB) signals at the leptotene/zygotene
CC stages. {ECO:0000269|PubMed:19786570}.
CC -!- SIMILARITY: Belongs to the YY transcription factor family.
CC {ECO:0000305}.
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DR EMBL; M73963; AAA40522.1; -; mRNA.
DR EMBL; L13968; AAA40477.1; -; Genomic_DNA.
DR EMBL; L13969; AAA40477.1; JOINED; Genomic_DNA.
DR EMBL; L13965; AAA40477.1; JOINED; Genomic_DNA.
DR EMBL; L13966; AAA40477.1; JOINED; Genomic_DNA.
DR EMBL; L13967; AAA40477.1; JOINED; Genomic_DNA.
DR EMBL; M74590; AAA37521.1; -; mRNA.
DR EMBL; BC055899; AAH55899.1; -; mRNA.
DR CCDS; CCDS26163.1; -.
DR PIR; A48273; A48273.
DR RefSeq; NP_033563.2; NM_009537.3.
DR AlphaFoldDB; Q00899; -.
DR SMR; Q00899; -.
DR BioGRID; 204624; 20.
DR ComplexPortal; CPX-878; INO80 chromatin remodeling complex.
DR CORUM; Q00899; -.
DR DIP; DIP-59285N; -.
DR IntAct; Q00899; 12.
DR MINT; Q00899; -.
DR STRING; 10090.ENSMUSP00000021692; -.
DR iPTMnet; Q00899; -.
DR PhosphoSitePlus; Q00899; -.
DR EPD; Q00899; -.
DR jPOST; Q00899; -.
DR MaxQB; Q00899; -.
DR PaxDb; Q00899; -.
DR PeptideAtlas; Q00899; -.
DR PRIDE; Q00899; -.
DR ProteomicsDB; 298052; -.
DR Antibodypedia; 9; 598 antibodies from 42 providers.
DR DNASU; 22632; -.
DR Ensembl; ENSMUST00000021692; ENSMUSP00000021692; ENSMUSG00000021264.
DR GeneID; 22632; -.
DR KEGG; mmu:22632; -.
DR UCSC; uc007pac.1; mouse.
DR CTD; 7528; -.
DR MGI; MGI:99150; Yy1.
DR VEuPathDB; HostDB:ENSMUSG00000021264; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000154763; -.
DR HOGENOM; CLU_002678_42_2_1; -.
DR InParanoid; Q00899; -.
DR OMA; DAGGRKW; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q00899; -.
DR TreeFam; TF106493; -.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR Reactome; R-MMU-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR BioGRID-ORCS; 22632; 19 hits in 112 CRISPR screens.
DR ChiTaRS; Yy1; mouse.
DR PRO; PR:Q00899; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q00899; protein.
DR Bgee; ENSMUSG00000021264; Expressed in indifferent gonad and 259 other tissues.
DR Genevisible; Q00899; MM.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005677; C:chromatin silencing complex; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031011; C:Ino80 complex; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0031519; C:PcG protein complex; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR GO; GO:0000400; F:four-way junction DNA binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0046332; F:SMAD binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR GO; GO:0030183; P:B cell differentiation; IMP:MGI.
DR GO; GO:0048593; P:camera-type eye morphogenesis; IGI:MGI.
DR GO; GO:0048468; P:cell development; IMP:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0071347; P:cellular response to interleukin-1; ISO:MGI.
DR GO; GO:0034644; P:cellular response to UV; ISO:MGI.
DR GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
DR GO; GO:0051276; P:chromosome organization; IMP:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISO:MGI.
DR GO; GO:0010467; P:gene expression; IDA:MGI.
DR GO; GO:0071707; P:immunoglobulin heavy chain V-D-J recombination; IMP:MGI.
DR GO; GO:0061052; P:negative regulation of cell growth involved in cardiac muscle cell development; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0032688; P:negative regulation of interferon-beta production; ISO:MGI.
DR GO; GO:1902894; P:negative regulation of miRNA transcription; IDA:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045739; P:positive regulation of DNA repair; IDA:ComplexPortal.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
DR GO; GO:1904507; P:positive regulation of telomere maintenance in response to DNA damage; IMP:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:0033044; P:regulation of chromosome organization; ISO:MGI.
DR GO; GO:0006282; P:regulation of DNA repair; IDA:ComplexPortal.
DR GO; GO:0006275; P:regulation of DNA replication; ISO:MGI.
DR GO; GO:0060382; P:regulation of DNA strand elongation; ISO:MGI.
DR GO; GO:0045995; P:regulation of embryonic development; IMP:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0034696; P:response to prostaglandin F; IEA:Ensembl.
DR GO; GO:0010225; P:response to UV-C; IMP:UniProtKB.
DR GO; GO:0006403; P:RNA localization; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR GO; GO:0000723; P:telomere maintenance; IMP:ComplexPortal.
DR InterPro; IPR017114; YY1-like.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR PIRSF; PIRSF037113; TF_Yin_yang; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW Activator; ADP-ribosylation; Cytoplasm; Differentiation; DNA damage;
KW DNA recombination; DNA repair; DNA-binding; Isopeptide bond; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Spermatogenesis; Transcription; Transcription regulation; Ubl conjugation;
KW Zinc; Zinc-finger.
FT CHAIN 1..414
FT /note="Transcriptional repressor protein YY1"
FT /id="PRO_0000047191"
FT ZN_FING 296..320
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 325..347
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 353..377
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 383..407
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..170
FT /note="Interaction with the SMAD1/SMAD4 complex"
FT /evidence="ECO:0000250"
FT REGION 32..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..341
FT /note="Involved in nuclear matrix association"
FT /evidence="ECO:0000250"
FT REGION 295..414
FT /note="Binding to DNA"
FT /evidence="ECO:0000250"
FT REGION 333..371
FT /note="Involved in repression of activated transcription"
FT /evidence="ECO:0000250"
FT REGION 371..397
FT /note="Involved in masking transactivation domain"
FT /evidence="ECO:0000250"
FT COMPBIAS 39..55
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..83
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 298
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 390
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 403
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 407
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25490"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 378
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P25490"
FT CROSSLNK 182
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P25490"
FT CROSSLNK 183
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P25490"
FT CROSSLNK 208
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P25490"
FT CROSSLNK 230
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P25490"
FT CROSSLNK 286
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P25490"
FT CROSSLNK 288
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P25490"
FT CROSSLNK 409
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P25490"
FT CROSSLNK 411
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P25490"
FT CONFLICT 219
FT /note="F -> S (in Ref. 3; AAA37521)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="R -> G (in Ref. 3; AAA37521)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 414 AA; 44717 MW; C012378288E984F9 CRC64;
MASGDTLYIA TDGSEMPAEI VELHEIEVET IPVETIETTV VGEEEEEDDD DEDGGGGDHG
GGGGGHGHAG HHHHHHHHHH HHPPMIALQP LVTDDPTQVH HHQEVILVQT REEVVGGDDS
DGLRAEDGFE DQILIPVPAP AGGDDDYIEQ TLVTVAAAGK SGGGASSGGG RVKKGGGKKS
GKKSYLGGGA GAAGGGGADP GNKKWEQKQV QIKTLEGEFS VTMWSSDEKK DIDHETVVEE
QIIGENSPPD YSEYMTGKKL PPGGIPGIDL SDPKQLAEFA RMKPRKIKED DAPRTIACPH
KGCTKMFRDN SAMRKHLHTH GPRVHVCAEC GKAFVESSKL KRHQLVHTGE KPFQCTFEGC
GKRFSLDFNL RTHVRIHTGD RPYVCPFDGC NKKFAQSTNL KSHILTHAKA KNNQ
