ZHX1_HUMAN
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 03-AUG-2022, entry version 188.
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}.
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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; 82.
DR IntAct; Q9UKY1; 79.
DR MINT; Q9UKY1; -.
DR STRING; 9606.ENSP00000297857; -.
DR GlyConnect; 2093; 1 N-Linked glycan (1 site), 1 O-Linked glycan (1 site).
DR GlyGen; Q9UKY1; 5 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (4 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; Q9UKY1; -.
DR PeptideAtlas; Q9UKY1; -.
DR PRIDE; Q9UKY1; -.
DR ProteomicsDB; 84909; -. [Q9UKY1-1]
DR ABCD; Q9UKY1; 4 sequenced antibodies.
DR Antibodypedia; 26954; 169 antibodies from 24 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 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; HSVVCSA; -.
DR PhylomeDB; Q9UKY1; -.
DR TreeFam; TF333363; -.
DR PathwayCommons; Q9UKY1; -.
DR SignaLink; Q9UKY1; -.
DR SIGNOR; Q9UKY1; -.
DR BioGRID-ORCS; 11244; 13 hits in 1090 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 196 other tissues.
DR ExpressionAtlas; Q9UKY1; baseline and differential.
DR Genevisible; Q9UKY1; HS.
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:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00086; homeodomain; 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 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; SSF46689; SSF46689; 5.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS50071; HOMEOBOX_2; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
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
