WDHD1_HUMAN
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 03-AUG-2022, entry version 197.
DE RecName: Full=WD repeat and HMG-box DNA-binding protein 1;
DE AltName: Full=Acidic nucleoplasmic DNA-binding protein 1;
DE Short=And-1;
GN Name=WDHD1; 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 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.
CC -!- FUNCTION: Acts as a replication initiation factor that brings together
CC the MCM2-7 helicase and the DNA polymerase alpha/primase complex in
CC order to initiate DNA replication. {ECO:0000269|PubMed:19805216}.
CC -!- SUBUNIT: Interacts with the polymerase alpha catalytic subunit POLA1.
CC Interacts with MCM10. Interacts with DNA2.
CC {ECO:0000269|PubMed:17761813, ECO:0000269|PubMed:22570476}.
CC -!- INTERACTION:
CC O75717; Q92830: KAT2A; NbExp=5; IntAct=EBI-3951691, EBI-477622;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}.
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 PDBsum; 2D7L; -.
DR PDBsum; 5GVA; -.
DR PDBsum; 5GVB; -.
DR PDBsum; 5OGS; -.
DR PDBsum; 6XTY; -.
DR PDBsum; 7PFO; -.
DR PDBsum; 7PLO; -.
DR AlphaFoldDB; O75717; -.
DR BMRB; O75717; -.
DR SMR; O75717; -.
DR BioGRID; 116340; 99.
DR CORUM; O75717; -.
DR IntAct; O75717; 22.
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 BioMuta; WDHD1; -.
DR EPD; O75717; -.
DR jPOST; O75717; -.
DR MassIVE; O75717; -.
DR MaxQB; O75717; -.
DR PaxDb; O75717; -.
DR PeptideAtlas; O75717; -.
DR PRIDE; O75717; -.
DR ProteomicsDB; 11926; -.
DR ProteomicsDB; 50175; -. [O75717-1]
DR Antibodypedia; 44; 175 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 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; 155530at2759; -.
DR PhylomeDB; O75717; -.
DR TreeFam; TF105988; -.
DR PathwayCommons; O75717; -.
DR SignaLink; O75717; -.
DR SIGNOR; O75717; -.
DR BioGRID-ORCS; 11169; 728 hits in 1083 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 ventricular zone and 115 other tissues.
DR ExpressionAtlas; O75717; baseline and differential.
DR Genevisible; O75717; HS.
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 Gene3D; 1.10.30.10; -; 1.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR024977; Apc4_WD40_dom.
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; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12894; ANAPC4_WD40; 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; SSF47095; 1.
DR SUPFAM; SSF50978; SSF50978; 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.
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
