ID   WDHD1_HUMAN             Reviewed;        1129 AA.
AC   O75717; C9JW18; F6W0U7;
DT   22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 206.
DE   RecName: Full=WD repeat and HMG-box DNA-binding protein 1 {ECO:0000305};
DE   AltName: Full=Acidic nucleoplasmic DNA-binding protein 1;
DE            Short=And-1;
GN   Name=WDHD1 {ECO:0000312|HGNC:HGNC:23170}; Synonyms=AND1;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RA   Koehler A.;
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA   Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA   Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA   Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA   Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA   Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA   Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA   Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA   Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA   Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA   Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA   Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA   Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA   Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Liver, Skin, and Uterus;
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]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; SER-383 AND SER-868, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [5]
RP   INTERACTION WITH POLA1 AND MCM10.
RX   PubMed=17761813; DOI=10.1101/gad.1585607;
RA   Zhu W., Ukomadu C., Jha S., Senga T., Dhar S.K., Wohlschlegel J.A.,
RA   Nutt L.K., Kornbluth S., Dutta A.;
RT   "Mcm10 and And-1/CTF4 recruit DNA polymerase alpha to chromatin for
RT   initiation of DNA replication.";
RL   Genes Dev. 21:2288-2299(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-824, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA   Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA   Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-383; SER-387;
RP   SER-868 AND SER-1090, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [8]
RP   FUNCTION.
RX   PubMed=19805216; DOI=10.1073/pnas.0908039106;
RA   Im J.S., Ki S.H., Farina A., Jung D.S., Hurwitz J., Lee J.K.;
RT   "Assembly of the Cdc45-Mcm2-7-GINS complex in human cells requires the
RT   Ctf4/And-1, RecQL4, and Mcm10 proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:15628-15632(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-374 AND SER-383, 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   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-962, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-383 AND SER-387, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383; SER-868 AND SER-984, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [14]
RP   INTERACTION WITH DNA2.
RX   PubMed=22570476; DOI=10.1074/jbc.m112.359018;
RA   Duxin J.P., Moore H.R., Sidorova J., Karanja K., Honaker Y., Dao B.,
RA   Piwnica-Worms H., Campbell J.L., Monnat R.J. Jr., Stewart S.A.;
RT   "Okazaki fragment processing-independent role for human Dna2 enzyme during
RT   DNA replication.";
RL   J. Biol. Chem. 287:21980-21991(2012).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383; THR-826; SER-868;
RP   SER-917; SER-919; SER-932 AND SER-1041, AND IDENTIFICATION BY MASS
RP   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   [16]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1127, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA   Impens F., Radoshevich L., Cossart P., Ribet D.;
RT   "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT   external stimuli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN   [17]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1127, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA   Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL   Cell Rep. 10:1778-1791(2015).
RN   [18]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-397 AND LYS-1127, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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   [19]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=35585232; DOI=10.1038/s41586-022-04759-1;
RA   Baris Y., Taylor M.R.G., Aria V., Yeeles J.T.P.;
RT   "Fast and efficient DNA replication with purified human proteins.";
RL   Nature 606:204-210(2022).
RN   [20]
RP   STRUCTURE BY NMR OF 1017-1084.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the HMG box domain from human WD repeat and HMG-box
RT   DNA binding protein 1.";
RL   Submitted (MAY-2006) to the PDB data bank.
RN   [21] {ECO:0007744|PDB:6XTY}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.29 ANGSTROMS) IN COMPLEX WITH CMG
RP   COMPLEX, AND SUBUNIT.
RX   PubMed=32453425; DOI=10.1093/nar/gkaa429;
RA   Rzechorzek N.J., Hardwick S.W., Jatikusumo V.A., Chirgadze D.Y.,
RA   Pellegrini L.;
RT   "CryoEM structures of human CMG-ATPgammaS-DNA and CMG-AND-1 complexes.";
RL   Nucleic Acids Res. 48:6980-6995(2020).
RN   [22] {ECO:0007744|PDB:7PFO}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) IN REPLISOME, SUBUNIT,
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=34694004; DOI=10.15252/embj.2021108819;
RA   Jones M.L., Baris Y., Taylor M.R.G., Yeeles J.T.P.;
RT   "Structure of a human replisome shows the organisation and interactions of
RT   a DNA replication machine.";
RL   EMBO J. 40:e108819-e108819(2021).
RN   [23] {ECO:0007744|PDB:7PLO}
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) IN REPLISOME, AND
RP   SUBUNIT.
RX   PubMed=34700328; DOI=10.1038/s41586-021-04145-3;
RA   Jenkyn-Bedford M., Jones M.L., Baris Y., Labib K.P.M., Cannone G.,
RA   Yeeles J.T.P., Deegan T.D.;
RT   "A conserved mechanism for regulating replisome disassembly in
RT   eukaryotes.";
RL   Nature 600:743-747(2021).
CC   -!- FUNCTION: Core replisome component that acts as a replication
CC       initiation factor. Binds directly to the CMG complex and functions as a
CC       hub to recruit additional proteins to the replication fork.
CC       {ECO:0000269|PubMed:19805216, ECO:0000269|PubMed:34694004,
CC       ECO:0000269|PubMed:35585232}.
CC   -!- SUBUNIT: Trimer (PubMed:32453425, PubMed:34694004). Interacts with the
CC       polymerase alpha catalytic subunit POLA1. Interacts with MCM10
CC       (PubMed:17761813). Interacts with DNA2 (PubMed:22570476). Interacts
CC       with CDC45 and GINS2 subunit of GINS complex; these interactions
CC       associate WDHD1 with the CMG helicase complex (PubMed:32453425,
CC       PubMed:34694004). {ECO:0000269|PubMed:17761813,
CC       ECO:0000269|PubMed:22570476, ECO:0000269|PubMed:32453425,
CC       ECO:0000269|PubMed:34694004}.
CC   -!- INTERACTION:
CC       O75717; Q92830: KAT2A; NbExp=5; IntAct=EBI-3951691, EBI-477622;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC       {ECO:0000305|PubMed:34694004, ECO:0000305|PubMed:35585232}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O75717-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O75717-2; Sequence=VSP_054775;
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DR   EMBL; AJ006266; CAA06932.1; -; mRNA.
DR   EMBL; AL160471; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC000622; AAH00622.1; -; mRNA.
DR   EMBL; BC043349; AAH43349.1; -; mRNA.
DR   EMBL; BC063041; AAH63041.1; -; mRNA.
DR   CCDS; CCDS41955.1; -. [O75717-2]
DR   CCDS; CCDS9721.1; -. [O75717-1]
DR   RefSeq; NP_001008397.1; NM_001008396.2. [O75717-2]
DR   RefSeq; NP_009017.1; NM_007086.3. [O75717-1]
DR   PDB; 2D7L; NMR; -; A=1017-1084.
DR   PDB; 5GVA; X-ray; 1.85 A; A=1-330.
DR   PDB; 5GVB; X-ray; 2.75 A; A=416-850.
DR   PDB; 5OGS; X-ray; 2.50 A; A=329-826.
DR   PDB; 6XTY; EM; 6.77 A; F/G/H=1-1129.
DR   PDB; 7PFO; EM; 3.20 A; H/I/J=1-1129.
DR   PDB; 7PLO; EM; 2.80 A; H/I/J=1-1129.
DR   PDB; 8B9D; EM; 3.40 A; H/I/J=1-1129.
DR   PDBsum; 2D7L; -.
DR   PDBsum; 5GVA; -.
DR   PDBsum; 5GVB; -.
DR   PDBsum; 5OGS; -.
DR   PDBsum; 6XTY; -.
DR   PDBsum; 7PFO; -.
DR   PDBsum; 7PLO; -.
DR   PDBsum; 8B9D; -.
DR   AlphaFoldDB; O75717; -.
DR   BMRB; O75717; -.
DR   EMDB; EMD-10621; -.
DR   EMDB; EMD-13375; -.
DR   EMDB; EMD-13494; -.
DR   SMR; O75717; -.
DR   BioGRID; 116340; 170.
DR   CORUM; O75717; -.
DR   IntAct; O75717; 23.
DR   MINT; O75717; -.
DR   STRING; 9606.ENSP00000353793; -.
DR   ChEMBL; CHEMBL4295681; -.
DR   GlyGen; O75717; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O75717; -.
DR   MetOSite; O75717; -.
DR   PhosphoSitePlus; O75717; -.
DR   SwissPalm; O75717; -.
DR   BioMuta; WDHD1; -.
DR   EPD; O75717; -.
DR   jPOST; O75717; -.
DR   MassIVE; O75717; -.
DR   MaxQB; O75717; -.
DR   PaxDb; 9606-ENSP00000353793; -.
DR   PeptideAtlas; O75717; -.
DR   ProteomicsDB; 11926; -.
DR   ProteomicsDB; 50175; -. [O75717-1]
DR   Pumba; O75717; -.
DR   Antibodypedia; 44; 197 antibodies from 28 providers.
DR   DNASU; 11169; -.
DR   Ensembl; ENST00000360586.8; ENSP00000353793.3; ENSG00000198554.12. [O75717-1]
DR   Ensembl; ENST00000420358.2; ENSP00000399349.2; ENSG00000198554.12. [O75717-2]
DR   GeneID; 11169; -.
DR   KEGG; hsa:11169; -.
DR   MANE-Select; ENST00000360586.8; ENSP00000353793.3; NM_007086.4; NP_009017.1.
DR   UCSC; uc001xbm.3; human. [O75717-1]
DR   AGR; HGNC:23170; -.
DR   CTD; 11169; -.
DR   DisGeNET; 11169; -.
DR   GeneCards; WDHD1; -.
DR   HGNC; HGNC:23170; WDHD1.
DR   HPA; ENSG00000198554; Tissue enhanced (lymphoid).
DR   MIM; 608126; gene.
DR   neXtProt; NX_O75717; -.
DR   OpenTargets; ENSG00000198554; -.
DR   PharmGKB; PA134988782; -.
DR   VEuPathDB; HostDB:ENSG00000198554; -.
DR   eggNOG; KOG1274; Eukaryota.
DR   GeneTree; ENSGT00390000002030; -.
DR   HOGENOM; CLU_004219_0_0_1; -.
DR   InParanoid; O75717; -.
DR   OMA; NAWFPIC; -.
DR   OrthoDB; 3686044at2759; -.
DR   PhylomeDB; O75717; -.
DR   TreeFam; TF105988; -.
DR   PathwayCommons; O75717; -.
DR   SignaLink; O75717; -.
DR   SIGNOR; O75717; -.
DR   BioGRID-ORCS; 11169; 763 hits in 1168 CRISPR screens.
DR   ChiTaRS; WDHD1; human.
DR   EvolutionaryTrace; O75717; -.
DR   GeneWiki; WDHD1; -.
DR   GenomeRNAi; 11169; -.
DR   Pharos; O75717; Tbio.
DR   PRO; PR:O75717; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; O75717; Protein.
DR   Bgee; ENSG00000198554; Expressed in primordial germ cell in gonad and 116 other cell types or tissues.
DR   ExpressionAtlas; O75717; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR   GO; GO:0043596; C:nuclear replication fork; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR   GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR   CDD; cd21993; HMG-box_WDHD1; 1.
DR   CDD; cd00200; WD40; 1.
DR   Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
DR   InterPro; IPR024977; Apc4-like_WD40_dom.
DR   InterPro; IPR048591; Ctf4-like_C.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   InterPro; IPR022100; Mcl1_mid.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR19932; WD REPEAT AND HMG-BOX DNA BINDING PROTEIN; 1.
DR   PANTHER; PTHR19932:SF10; WD REPEAT AND HMG-BOX DNA-BINDING PROTEIN 1; 1.
DR   Pfam; PF12894; ANAPC4_WD40; 1.
DR   Pfam; PF20946; Ctf4_C; 1.
DR   Pfam; PF12341; Mcl1_mid; 1.
DR   Pfam; PF00400; WD40; 2.
DR   SMART; SM00398; HMG; 1.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF47095; HMG-box; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
DR   Genevisible; O75717; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; DNA-binding;
KW   Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Ubl conjugation; WD repeat.
FT   CHAIN           1..1129
FT                   /note="WD repeat and HMG-box DNA-binding protein 1"
FT                   /id="PRO_0000051338"
FT   REPEAT          11..50
FT                   /note="WD 1"
FT   REPEAT          52..91
FT                   /note="WD 2"
FT   REPEAT          92..131
FT                   /note="WD 3"
FT   REPEAT          134..173
FT                   /note="WD 4"
FT   REPEAT          184..223
FT                   /note="WD 5"
FT   REPEAT          228..267
FT                   /note="WD 6"
FT   REPEAT          271..310
FT                   /note="WD 7"
FT   DNA_BIND        1016..1079
FT                   /note="HMG box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   REGION          848..897
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          916..1017
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1068..1113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        883..897
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        916..959
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1068..1108
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         333
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT   MOD_RES         374
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:19690332"
FT   MOD_RES         383
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         387
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231"
FT   MOD_RES         671
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P59328"
FT   MOD_RES         824
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17525332"
FT   MOD_RES         826
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         868
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         917
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         919
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         932
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         962
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         984
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         1041
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1090
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   CROSSLNK        397
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1127
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0007744|PubMed:25114211"
FT   CROSSLNK        1127
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:25772364,
FT                   ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         1..123
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_054775"
FT   VARIANT         338
FT                   /note="F -> L (in dbSNP:rs8020032)"
FT                   /id="VAR_053422"
FT   VARIANT         411
FT                   /note="L -> P (in dbSNP:rs17128116)"
FT                   /id="VAR_053423"
FT   VARIANT         1102
FT                   /note="E -> K (in dbSNP:rs41309252)"
FT                   /id="VAR_062100"
FT   CONFLICT        612
FT                   /note="Q -> K (in Ref. 3; AAH43349/AAH00622)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        613
FT                   /note="I -> K (in Ref. 3; AAH00622)"
FT                   /evidence="ECO:0000305"
FT   STRAND          12..15
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   STRAND          18..21
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   STRAND          28..31
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   STRAND          35..42
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   STRAND          49..52
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   STRAND          57..63
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   STRAND          66..71
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   TURN            72..74
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   STRAND          75..80
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   TURN            81..83
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   STRAND          86..92
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   STRAND          97..102
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   STRAND          106..113
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   STRAND          118..122
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   STRAND          125..132
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   STRAND          139..144
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   STRAND          148..155
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   STRAND          160..164
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   TURN            165..168
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   STRAND          169..174
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   HELIX           183..185
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   STRAND          196..198
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   STRAND          201..206
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   STRAND          209..214
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   TURN            215..217
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   STRAND          220..224
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   STRAND          233..238
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   STRAND          242..249
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   STRAND          254..258
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   TURN            259..261
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   STRAND          264..268
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   STRAND          276..281
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   STRAND          283..292
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   STRAND          295..302
FT                   /evidence="ECO:0007829|PDB:5GVA"
FT   STRAND          442..449
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   STRAND          451..459
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   STRAND          464..472
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   TURN            473..475
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   STRAND          479..482
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   STRAND          489..492
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   STRAND          497..501
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   STRAND          505..507
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   STRAND          510..514
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   STRAND          519..521
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   STRAND          525..528
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   STRAND          535..540
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   STRAND          542..549
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   STRAND          552..558
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   STRAND          563..568
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   STRAND          573..579
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   STRAND          582..588
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   STRAND          599..605
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   STRAND          607..609
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   STRAND          611..618
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   STRAND          627..632
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   STRAND          638..642
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   STRAND          645..650
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   HELIX           652..654
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   STRAND          658..663
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   HELIX           664..667
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   STRAND          673..681
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   TURN            682..685
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   STRAND          686..697
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   STRAND          700..702
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   STRAND          707..709
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   TURN            716..719
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   HELIX           721..734
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   HELIX           737..744
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   HELIX           751..774
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   HELIX           778..786
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   HELIX           790..801
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   HELIX           802..804
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   HELIX           806..821
FT                   /evidence="ECO:0007829|PDB:5OGS"
FT   HELIX           1021..1036
FT                   /evidence="ECO:0007829|PDB:2D7L"
FT   HELIX           1043..1054
FT                   /evidence="ECO:0007829|PDB:2D7L"
FT   STRAND          1055..1057
FT                   /evidence="ECO:0007829|PDB:2D7L"
FT   HELIX           1059..1068
FT                   /evidence="ECO:0007829|PDB:2D7L"
FT   STRAND          1071..1076
FT                   /evidence="ECO:0007829|PDB:2D7L"
FT   HELIX           1081..1083
FT                   /evidence="ECO:0007829|PDB:2D7L"
SQ   SEQUENCE   1129 AA;  125967 MW;  DD3E3613CA6AE70A CRC64;
     MPATRKPMRY GHTEGHTEVC FDDSGSFIVT CGSDGDVRIW EDLDDDDPKF INVGEKAYSC
     ALKSGKLVTA VSNNTIQVHT FPEGVPDGIL TRFTTNANHV VFNGDGTKIA AGSSDFLVKI
     VDVMDSSQQK TFRGHDAPVL SLSFDPKDIF LASASCDGSV RVWQISDQTC AISWPLLQKC
     NDVINAKSIC RLAWQPKSGK LLAIPVEKSV KLYRRESWSH QFDLSDNFIS QTLNIVTWSP
     CGQYLAAGSI NGLIIVWNVE TKDCMERVKH EKGYAICGLA WHPTCGRISY TDAEGNLGLL
     ENVCDPSGKT SSSKVSSRVE KDYNDLFDGD DMSNAGDFLN DNAVEIPSFS KGIINDDEDD
     EDLMMASGRP RQRSHILEDD ENSVDISMLK TGSSLLKEEE EDGQEGSIHN LPLVTSQRPF
     YDGPMPTPRQ KPFQSGSTPL HLTHRFMVWN SIGIIRCYND EQDNAIDVEF HDTSIHHATH
     LSNTLNYTIA DLSHEAILLA CESTDELASK LHCLHFSSWD SSKEWIIDLP QNEDIEAICL
     GQGWAAAATS ALLLRLFTIG GVQKEVFSLA GPVVSMAGHG EQLFIVYHRG TGFDGDQCLG
     VQLLELGKKK KQILHGDPLP LTRKSYLAWI GFSAEGTPCY VDSEGIVRML NRGLGNTWTP
     ICNTREHCKG KSDHYWVVGI HENPQQLRCI PCKGSRFPPT LPRPAVAILS FKLPYCQIAT
     EKGQMEEQFW RSVIFHNHLD YLAKNGYEYE ESTKNQATKE QQELLMKMLA LSCKLEREFR
     CVELADLMTQ NAVNLAIKYA SRSRKLILAQ KLSELAVEKA AELTATQVEE EEEEEDFRKK
     LNAGYSNTAT EWSQPRFRNQ VEEDAEDSGE ADDEEKPEIH KPGQNSFSKS TNSSDVSAKS
     GAVTFSSQGR VNPFKVSASS KEPAMSMNSA RSTNILDNMG KSSKKSTALS RTTNNEKSPI
     IKPLIPKPKP KQASAASYFQ KRNSQTNKTE EVKEENLKNV LSETPAICPP QNTENQRPKT
     GFQMWLEENR SNILSDNPDF SDEADIIKEG MIRFRVLSTE ERKVWANKAK GETASEGTEA
     KKRKRVVDES DETENQEEKA KENLNLSKKQ KPLDFSTNQK LSAFAFKQE
//