ID ZHX1_HUMAN Reviewed; 873 AA. AC Q9UKY1; Q8IWD8; DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 197. DE RecName: Full=Zinc fingers and homeoboxes protein 1; GN Name=ZHX1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000312|EMBL:AAF35183.1}; RN [1] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INTERACTION RP WITH NFYA. RC TISSUE=Liver {ECO:0000269|PubMed:10441475}; RX PubMed=10441475; DOI=10.1006/bbrc.1999.1087; RA Yamada K., Printz R.L., Osawa H., Granner D.K.; RT "Human ZHX1: cloning, chromosomal location, and interaction with RT transcription factor NF-Y."; RL Biochem. Biophys. Res. Commun. 261:614-621(1999). RN [2] {ECO:0000312|EMBL:AAF35183.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Mueller R., Ziegler B.L.; RT "Identification and cloning of the human ZHX1 gene."; RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis {ECO:0000312|EMBL:AAH40481.1}; 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 [4] {ECO:0000305} RP INTERACTION WITH NFYA. RX PubMed=10571058; DOI=10.1016/s0014-5793(99)01311-3; RA Yamada K., Osawa H., Granner D.K.; RT "Identification of proteins that interact with NF-YA."; RL FEBS Lett. 460:41-45(1999). RN [5] {ECO:0000305} RP FUNCTION, HOMODIMERIZATION, AND SUBCELLULAR LOCATION. RX PubMed=12237128; DOI=10.1016/s0006-291x(02)02203-9; RA Yamada K., Kawata H., Matsuura K., Shou Z., Hirano S., Mizutani T., RA Yazawa T., Yoshino M., Sekiguchi T., Kajitani T., Miyamoto K.; RT "Functional analysis and the molecular dissection of zinc-fingers and RT homeoboxes 1 (ZHX1)."; RL Biochem. Biophys. Res. Commun. 297:368-374(2002). RN [6] {ECO:0000305} RP HETERODIMERIZATION WITH ZHX3, AND INTERACTION WITH ATF7IP. RX PubMed=12659632; DOI=10.1042/bj20021866; RA Yamada K., Kawata H., Shou Z., Hirano S., Mizutani T., Yazawa T., RA Sekiguchi T., Yoshino M., Kajitani T., Miyamoto K.; RT "Analysis of zinc-fingers and homeoboxes (ZHX)-1-interacting proteins: RT molecular cloning and characterization of a member of the ZHX family, RT ZHX3."; RL Biochem. J. 373:167-178(2003). RN [7] {ECO:0000305} RP HETERODIMERIZATION WITH ZHX2. RX PubMed=12741956; DOI=10.1042/bj20030171; RA Kawata H., Yamada K., Shou Z., Mizutani T., Yazawa T., Yoshino M., RA Sekiguchi T., Kajitani T., Miyamoto K.; RT "Zinc-fingers and homeoboxes (ZHX) 2, a novel member of the ZHX family, RT functions as a transcriptional repressor."; RL Biochem. J. 373:747-757(2003). RN [8] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC TISSUE=Kidney; RX PubMed=17056598; DOI=10.1074/jbc.m606664200; RA Liu G., Clement L.C., Kanwar Y.S., Avila-Casado C., Chugh S.S.; RT "ZHX proteins regulate podocyte gene expression during the development of RT nephrotic syndrome."; RL J. Biol. Chem. 281:39681-39692(2006). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [10] RP INTERACTION WITH DNMT3B. RX PubMed=17303076; DOI=10.1016/j.bbrc.2007.01.187; RA Kim S.H., Park J., Choi M.C., Kim H.P., Park J.H., Jung Y., Lee J.H., RA Oh D.Y., Im S.A., Bang Y.J., Kim T.Y.; RT "Zinc-fingers and homeoboxes 1 (ZHX1) binds DNA methyltransferase (DNMT) 3B RT to enhance DNMT3B-mediated transcriptional repression."; RL Biochem. Biophys. Res. Commun. 355:318-323(2007). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-47 AND SER-48, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-48 AND SER-648, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 AND SER-774, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36 AND SER-48, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [16] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-454, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [17] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-159; LYS-441; LYS-454; LYS-485 RP AND LYS-629, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [18] {ECO:0000312|EMBL:AAF35183.1} RP STRUCTURE BY NMR OF 60-153. RG Structural proteomics in Europe (SPINE); RT "Solution structure of the zinc-finger region of human zinc-fingers and RT homeoboxes 1 (ZHX1)."; RL Submitted (APR-2006) to the PDB data bank. RN [19] {ECO:0000312|EMBL:AAF35183.1} RP STRUCTURE BY NMR OF 565-640. RG RIKEN structural genomics initiative (RSGI); RT "The solution structure of the third homeobox domain of human zinc fingers RT and homeoboxes protein."; RL Submitted (FEB-2007) to the PDB data bank. RN [20] RP STRUCTURE BY NMR OF 60-153. RX PubMed=19348505; DOI=10.1021/bi9001997; RA Wienk H., Lammers I., Hotze A., Wu J., Wechselberger R.W., Owens R., RA Stammers D.K., Stuart D., Kaptein R., Folkers G.E.; RT "The tandem zinc-finger region of human ZHX adopts a novel C2H2 zinc finger RT structure with a C-terminal extension."; RL Biochemistry 48:4431-4439(2009). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 655-731. RX PubMed=20509910; DOI=10.1186/1472-6807-10-13; RA Bird L.E., Ren J., Nettleship J.E., Folkers G.E., Owens R.J., RA Stammers D.K.; RT "Novel structural features in two ZHX homeodomains derived from a RT systematic study of single and multiple domains."; RL BMC Struct. Biol. 10:13-13(2010). CC -!- FUNCTION: Acts as a transcriptional repressor. Increases DNMT3B- CC mediated repressive transcriptional activity when DNMT3B is tethered to CC DNA. May link molecule between DNMT3B and other co-repressor proteins. CC {ECO:0000269|PubMed:12237128}. CC -!- SUBUNIT: Forms homodimers. Heterodimer (via HD1 domain) with ZHX2 (via CC HD1 domain). Also forms a heterodimer with ZHX3 which is a prerequisite CC for repressor activity. Interacts with ATF7IP and NFYA. Interacts (via CC homeobox domains) with DNMT3B (via PWWP domain). CC {ECO:0000269|PubMed:10441475, ECO:0000269|PubMed:10571058, CC ECO:0000269|PubMed:12659632, ECO:0000269|PubMed:17303076}. CC -!- INTERACTION: CC Q9UKY1; P54253: ATXN1; NbExp=11; IntAct=EBI-347767, EBI-930964; CC Q9UKY1; Q9UBC3-1: DNMT3B; NbExp=6; IntAct=EBI-347767, EBI-6083193; CC Q9UKY1; P42858: HTT; NbExp=6; IntAct=EBI-347767, EBI-466029; CC Q9UKY1; Q9Y6X8: ZHX2; NbExp=2; IntAct=EBI-347767, EBI-948566; CC Q9UKY1; Q15326: ZMYND11; NbExp=2; IntAct=EBI-347767, EBI-2623509; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, CC ECO:0000269|PubMed:12237128, ECO:0000269|PubMed:17056598}. CC Note=Colocalized in the nucleus with DNMT3B. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UKY1-1; Sequence=Displayed; CC Name=2; Synonyms=ZHX1-C8orf76; CC IsoId=Q96EF9-1; Sequence=External; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed in podocytes. CC {ECO:0000269|PubMed:10441475, ECO:0000269|PubMed:17056598}. CC -!- SIMILARITY: Belongs to the ZHX family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF106862; AAD50624.1; -; mRNA. DR EMBL; AF195766; AAF35183.1; -; mRNA. DR EMBL; BC040481; AAH40481.1; -; mRNA. DR CCDS; CCDS6342.1; -. [Q9UKY1-1] DR PIR; JC7079; JC7079. DR RefSeq; NP_001017926.1; NM_001017926.2. [Q9UKY1-1] DR RefSeq; NP_009153.3; NM_007222.4. [Q9UKY1-1] DR PDB; 2ECB; NMR; -; A=565-640. DR PDB; 2GHF; NMR; -; A=60-153. DR PDB; 2LY9; NMR; -; A=462-532. DR PDB; 3NAR; X-ray; 2.60 A; A/B=655-731. DR PDBsum; 2ECB; -. DR PDBsum; 2GHF; -. DR PDBsum; 2LY9; -. DR PDBsum; 3NAR; -. DR AlphaFoldDB; Q9UKY1; -. DR SMR; Q9UKY1; -. DR BioGRID; 116406; 91. DR IntAct; Q9UKY1; 79. DR MINT; Q9UKY1; -. DR STRING; 9606.ENSP00000297857; -. DR GlyConnect; 2093; 1 N-Linked glycan (1 site), 1 O-GlcNAc glycan (1 site). DR GlyCosmos; Q9UKY1; 5 sites, 3 glycans. DR GlyGen; Q9UKY1; 11 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (10 sites). DR iPTMnet; Q9UKY1; -. DR PhosphoSitePlus; Q9UKY1; -. DR BioMuta; ZHX1; -. DR DMDM; 44888551; -. DR EPD; Q9UKY1; -. DR jPOST; Q9UKY1; -. DR MassIVE; Q9UKY1; -. DR MaxQB; Q9UKY1; -. DR PaxDb; 9606-ENSP00000297857; -. DR PeptideAtlas; Q9UKY1; -. DR ProteomicsDB; 84909; -. [Q9UKY1-1] DR Pumba; Q9UKY1; -. DR ABCD; Q9UKY1; 4 sequenced antibodies. DR Antibodypedia; 26954; 187 antibodies from 23 providers. DR DNASU; 11244; -. DR Ensembl; ENST00000297857.3; ENSP00000297857.2; ENSG00000165156.15. [Q9UKY1-1] DR Ensembl; ENST00000395571.8; ENSP00000378938.2; ENSG00000165156.15. [Q9UKY1-1] DR Ensembl; ENST00000522655.5; ENSP00000428821.1; ENSG00000165156.15. [Q9UKY1-1] DR GeneID; 11244; -. DR KEGG; hsa:11244; -. DR MANE-Select; ENST00000395571.8; ENSP00000378938.2; NM_007222.5; NP_009153.3. DR UCSC; uc003yqe.4; human. [Q9UKY1-1] DR AGR; HGNC:12871; -. DR CTD; 11244; -. DR DisGeNET; 11244; -. DR GeneCards; ZHX1; -. DR HGNC; HGNC:12871; ZHX1. DR HPA; ENSG00000165156; Low tissue specificity. DR MIM; 604764; gene. DR neXtProt; NX_Q9UKY1; -. DR OpenTargets; ENSG00000165156; -. DR PharmGKB; PA37460; -. DR VEuPathDB; HostDB:ENSG00000165156; -. DR eggNOG; ENOG502QT3D; Eukaryota. DR GeneTree; ENSGT00950000182893; -. DR HOGENOM; CLU_009147_1_0_1; -. DR InParanoid; Q9UKY1; -. DR OMA; GKRINNW; -. DR OrthoDB; 3073996at2759; -. DR PhylomeDB; Q9UKY1; -. DR TreeFam; TF333363; -. DR PathwayCommons; Q9UKY1; -. DR SignaLink; Q9UKY1; -. DR SIGNOR; Q9UKY1; -. DR BioGRID-ORCS; 11244; 13 hits in 1168 CRISPR screens. DR EvolutionaryTrace; Q9UKY1; -. DR GeneWiki; ZHX1; -. DR GenomeRNAi; 11244; -. DR Pharos; Q9UKY1; Tbio. DR PRO; PR:Q9UKY1; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q9UKY1; Protein. DR Bgee; ENSG00000165156; Expressed in upper arm skin and 198 other cell types or tissues. DR ExpressionAtlas; Q9UKY1; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd00086; homeodomain; 5. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1. DR Gene3D; 1.10.10.60; Homeodomain-like; 5. DR InterPro; IPR009057; Homeobox-like_sf. DR InterPro; IPR001356; Homeobox_dom. DR InterPro; IPR024578; Homez_homeobox_dom. DR InterPro; IPR041057; ZHX_Znf_C2H2. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR15467:SF4; ZINC FINGERS AND HOMEOBOXES PROTEIN 1; 1. DR PANTHER; PTHR15467; ZINC-FINGERS AND HOMEOBOXES RELATED; 1. DR Pfam; PF00046; Homeodomain; 4. DR Pfam; PF11569; Homez; 1. DR Pfam; PF18387; zf_C2H2_ZHX; 1. DR SMART; SM00389; HOX; 5. DR SMART; SM00355; ZnF_C2H2; 2. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2. DR SUPFAM; SSF46689; Homeodomain-like; 5. DR PROSITE; PS50071; HOMEOBOX_2; 4. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1. DR Genevisible; Q9UKY1; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Differentiation; DNA-binding; Homeobox; KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Repressor; Transcription; KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..873 FT /note="Zinc fingers and homeoboxes protein 1" FT /id="PRO_0000049388" FT ZN_FING 70..93 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042, FT ECO:0000305" FT ZN_FING 102..125 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042, FT ECO:0000305" FT DNA_BIND 284..346 FT /note="Homeobox 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108, FT ECO:0000305" FT DNA_BIND 464..526 FT /note="Homeobox 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108, FT ECO:0000305" FT DNA_BIND 569..630 FT /note="Homeobox 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108, FT ECO:0000305" FT DNA_BIND 660..722 FT /note="Homeobox 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108, FT ECO:0000305" FT DNA_BIND 777..832 FT /note="Homeobox 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108, FT ECO:0000305" FT REGION 24..63 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 202..236 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 272..564 FT /note="Required for interaction with NFYA" FT REGION 272..432 FT /note="Required for dimerization" FT REGION 626..667 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 732..770 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 734..768 FT /note="Required for nuclear localization" FT REGION 829..873 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 831..873 FT /note="Required for repressor activity" FT COMPBIAS 44..63 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 202..224 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 626..648 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 742..762 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 831..855 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 856..873 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 36 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 45 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 47 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MOD_RES 48 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569" FT MOD_RES 202 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 648 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 774 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 159 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 441 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 454 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 485 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 629 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CONFLICT 263 FT /note="V -> M (in Ref. 3; AAH40481)" FT /evidence="ECO:0000305" FT CONFLICT 792 FT /note="H -> R (in Ref. 3; AAH40481)" FT /evidence="ECO:0000305" FT TURN 60..62 FT /evidence="ECO:0007829|PDB:2GHF" FT STRAND 68..71 FT /evidence="ECO:0007829|PDB:2GHF" FT STRAND 78..80 FT /evidence="ECO:0007829|PDB:2GHF" FT HELIX 82..92 FT /evidence="ECO:0007829|PDB:2GHF" FT STRAND 102..104 FT /evidence="ECO:0007829|PDB:2GHF" FT TURN 105..108 FT /evidence="ECO:0007829|PDB:2GHF" FT STRAND 109..113 FT /evidence="ECO:0007829|PDB:2GHF" FT HELIX 115..118 FT /evidence="ECO:0007829|PDB:2GHF" FT HELIX 120..123 FT /evidence="ECO:0007829|PDB:2GHF" FT STRAND 131..135 FT /evidence="ECO:0007829|PDB:2GHF" FT STRAND 144..150 FT /evidence="ECO:0007829|PDB:2GHF" FT HELIX 473..485 FT /evidence="ECO:0007829|PDB:2LY9" FT HELIX 491..501 FT /evidence="ECO:0007829|PDB:2LY9" FT HELIX 505..518 FT /evidence="ECO:0007829|PDB:2LY9" FT TURN 519..523 FT /evidence="ECO:0007829|PDB:2LY9" FT HELIX 577..589 FT /evidence="ECO:0007829|PDB:2ECB" FT HELIX 595..604 FT /evidence="ECO:0007829|PDB:2ECB" FT HELIX 609..624 FT /evidence="ECO:0007829|PDB:2ECB" FT STRAND 664..667 FT /evidence="ECO:0007829|PDB:3NAR" FT HELIX 669..681 FT /evidence="ECO:0007829|PDB:3NAR" FT HELIX 687..697 FT /evidence="ECO:0007829|PDB:3NAR" FT HELIX 701..715 FT /evidence="ECO:0007829|PDB:3NAR" FT TURN 716..718 FT /evidence="ECO:0007829|PDB:3NAR" FT HELIX 721..730 FT /evidence="ECO:0007829|PDB:3NAR" SQ SEQUENCE 873 AA; 98098 MW; 66CF1CEC5EF824E5 CRC64; MASRRKSTTP CMVLASEQDP DLELISDLDE GPPVLTPVEN TRAESISSDE EVHESVDSDN QQNKKVEGGY ECKYCTFQTP DLNMFTFHVD SEHPNVVLNS SYVCVECNFL TKRYDALSEH NLKYHPGEEN FKLTMVKRNN QTIFEQTIND LTFDGSFVKE ENAEQAESTE VSSSGISISK TPIMKMMKNK VENKRIAVHH NSVEDVPEEK ENEIKPDREE IVENPSSSAS ESNTSTSIVN RIHPSTASTV VTPAAVLPGL AQVITAVSAQ QNSNLIPKVL IPVNSIPTYN AALDNNPLLL NTYNKFPYPT MSEITVLSAQ AKYTEEQIKI WFSAQRLKHG VSWTPEEVEE ARRKQFNGTV HTVPQTITVI PTHISTGSNG LPSILQTCQI VGQPGLVLTQ VAGTNTLPVT APIALTVAGV PSQNNIQKSQ VPAAQPTAET KPATAAVPTS QSVKHETALV NPDSFGIRAK KTKEQLAELK VSYLKNQFPH DSEIIRLMKI TGLTKGEIKK WFSDTRYNQR NSKSNQCLHL NNDSSTTIII DSSDETTESP TVGTAQPKQS WNPFPDFTPQ KFKEKTAEQL RVLQASFLNS SVLTDEELNR LRAQTKLTRR EIDAWFTEKK KSKALKEEKM EIDESNAGSS KEEAGETSPA DESGAPKSGS TGKICKKTPE QLHMLKSAFV RTQWPSPEEY DKLAKESGLA RTDIVSWFGD TRYAWKNGNL KWYYYYQSAN SSSMNGLSSL RKRGRGRPKG RGRGRPRGRP RGSKRINNWD RGPSLIKFKT GTAILKDYYL KHKFLNEQDL DELVNKSHMG YEQVREWFAE RQRRSELGIE LFEENEEEDE VIDDQEEDEE ETDDSDTWEP PRHVKRKLSK SDD //