MDC1_MOUSE
ID MDC1_MOUSE Reviewed; 1707 AA.
AC Q5PSV9; Q52KG1; Q5U4D3; Q6ZQH7;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Mediator of DNA damage checkpoint protein 1;
GN Name=Mdc1; Synonyms=Kiaa0170;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INTERACTION WITH H2AX AND NBN, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15611643; DOI=10.4161/cc.4.1.1354;
RA Lee A.C., Fernandez-Capetillo O., Pisupati V., Jackson S.P.,
RA Nussenzweig A.;
RT "Specific association of mouse MDC1/NFBD1 with NBS1 at sites of DNA-
RT damage.";
RL Cell Cycle 4:177-182(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 693-1707.
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168; SER-438; SER-442 AND
RP THR-444, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168; SER-438; SER-442;
RP THR-444; SER-461; THR-470; SER-492; SER-493; SER-591; SER-593; SER-595;
RP THR-1056; SER-1104; SER-1126; SER-1128; THR-1132; THR-1297; THR-1298;
RP SER-1435; SER-1436; SER-1439; SER-1443 AND THR-1480, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=23039116; DOI=10.1111/gtc.12005;
RA Kogo H., Tsutsumi M., Inagaki H., Ohye T., Kiyonari H., Kurahashi H.;
RT "HORMAD2 is essential for synapsis surveillance during meiotic prophase via
RT the recruitment of ATR activity.";
RL Genes Cells 17:897-912(2012).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1496, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Required for checkpoint mediated cell cycle arrest in
CC response to DNA damage within both the S phase and G2/M phases of the
CC cell cycle. May serve as a scaffold for the recruitment of DNA repair
CC and signal transduction proteins to discrete foci of DNA damage marked
CC by 'Ser-139' phosphorylation of histone H2AX. Also required for
CC downstream events subsequent to the recruitment of these proteins.
CC These include phosphorylation and activation of the ATM, CHEK1 and
CC CHEK2 kinases, and stabilization of TP53 and apoptosis. ATM and CHEK2
CC may also be activated independently by a parallel pathway mediated by
CC TP53BP1 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with several proteins involved in the DNA
CC damage response, although not all these interactions may be direct.
CC Interacts with CHEK2, which requires ATM-mediated phosphorylation
CC within the FHA domain of CHEK2. Interacts constitutively with the
CC BRCA1-BARD1 complex, SMC1A and TP53BP1. Interacts with ATM and FANCD2,
CC and these interactions are reduced upon DNA damage. Also interacts with
CC the PRKDC complex, composed of XRCC6/KU70, XRCC5/KU80 and PRKDC/XRCC7.
CC This interaction may be required for PRKDC autophosphorylation, which
CC is essential for DNA double strand break (DSB) repair. When
CC phosphorylated by ATM, interacts with RNF8 (via FHA domain). Interacts
CC with CEP164. When phosphorylated, interacts with APTX (via FHA-like
CC domain) (By similarity). Interacts with H2AX, which requires
CC phosphorylation of H2AX. Interacts with the MRN complex, composed of
CC MRE11, RAD50, and NBN. {ECO:0000250, ECO:0000269|PubMed:15611643}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Associated with
CC chromatin. Relocalizes to discrete nuclear foci following DNA damage,
CC this requires phosphorylation of H2AX. Colocalizes with APTX at sites
CC of DNA double-strand breaks (By similarity). {ECO:0000250}.
CC -!- DOMAIN: Tandemly repeated BRCT domains are characteristic of proteins
CC involved in DNA damage signaling. In MDC1, these repeats are required
CC for localization to chromatin which flanks sites of DNA damage marked
CC by 'Ser-139' phosphorylation of H2AX (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated upon exposure to ionizing radiation (IR),
CC ultraviolet radiation (UV), and hydroxyurea (HU). Phosphorylation in
CC response to IR requires ATM, NBN, and possibly CHEK2. Also
CC phosphorylated during the G2/M phase of the cell cycle and during
CC activation of the mitotic spindle checkpoint. Phosphorylation at Thr-4
CC by ATM stabilizes and enhances homodimerization via the FHA domain (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Sumoylation at Lys-1461 by PIAS4 following DNA damage promotes
CC ubiquitin-mediated degradation. {ECO:0000250}.
CC -!- PTM: Ubiquitinated by RNF4, leading to proteasomal degradation;
CC undergoes 'Lys-48'-linked polyubiquitination. {ECO:0000250}.
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DR EMBL; AY826432; AAV85449.1; -; Genomic_DNA.
DR EMBL; BC085140; AAH85140.1; -; mRNA.
DR EMBL; BC094363; AAH94363.1; -; mRNA.
DR EMBL; AK129074; BAC97884.1; -; mRNA.
DR RefSeq; NP_001010833.2; NM_001010833.2.
DR PDB; 3VA1; X-ray; 1.74 A; A/B=29-139.
DR PDB; 3VA4; X-ray; 1.54 A; A/B=29-139.
DR PDBsum; 3VA1; -.
DR PDBsum; 3VA4; -.
DR AlphaFoldDB; Q5PSV9; -.
DR SMR; Q5PSV9; -.
DR BioGRID; 232163; 6.
DR STRING; 10090.ENSMUSP00000080949; -.
DR iPTMnet; Q5PSV9; -.
DR PhosphoSitePlus; Q5PSV9; -.
DR EPD; Q5PSV9; -.
DR jPOST; Q5PSV9; -.
DR MaxQB; Q5PSV9; -.
DR PaxDb; Q5PSV9; -.
DR PeptideAtlas; Q5PSV9; -.
DR PRIDE; Q5PSV9; -.
DR ProteomicsDB; 293442; -.
DR GeneID; 240087; -.
DR KEGG; mmu:240087; -.
DR CTD; 9656; -.
DR MGI; MGI:3525201; Mdc1.
DR eggNOG; KOG2043; Eukaryota.
DR InParanoid; Q5PSV9; -.
DR OrthoDB; 670424at2759; -.
DR PhylomeDB; Q5PSV9; -.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-MMU-5693571; Nonhomologous End-Joining (NHEJ).
DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
DR BioGRID-ORCS; 240087; 28 hits in 110 CRISPR screens.
DR ChiTaRS; Mdc1; mouse.
DR PRO; PR:Q5PSV9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q5PSV9; protein.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0070975; F:FHA domain binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd00060; FHA; 1.
DR Gene3D; 3.40.50.10190; -; 2.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF16770; RTT107_BRCT_5; 1.
DR SMART; SM00292; BRCT; 2.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Chromosome; Coiled coil; DNA damage;
KW DNA repair; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Ubl conjugation.
FT CHAIN 1..1707
FT /note="Mediator of DNA damage checkpoint protein 1"
FT /id="PRO_0000096318"
FT DOMAIN 54..105
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT DOMAIN 1510..1588
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 1609..1700
FT /note="BRCT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 1..150
FT /note="Interaction with CHEK2"
FT /evidence="ECO:0000250"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..222
FT /note="Interaction with the MRN complex"
FT /evidence="ECO:0000250"
FT REGION 166..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..1510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..885
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..998
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1057
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1089
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1205..1254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1261..1276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1283..1313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1345..1375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1376..1390
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1423..1442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1443..1506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 146
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U2M8"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 300
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 315
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 362
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 387
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U2M8"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U2M8"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 444
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 470
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 735
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 750
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 769
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 885
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 929
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 962
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U2M8"
FT MOD_RES 991
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1056
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1132
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1173
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1234
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1297
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1298
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1352
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1359
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1375
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT MOD_RES 1435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1443
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1480
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1496
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CROSSLNK 1418
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT CROSSLNK 1461
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT CROSSLNK 1461
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14676"
FT CONFLICT 396
FT /note="E -> EE (in Ref. 2; AAH94363)"
FT /evidence="ECO:0000305"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:3VA4"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:3VA4"
FT STRAND 51..59
FT /evidence="ECO:0007829|PDB:3VA4"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:3VA4"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:3VA4"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:3VA4"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:3VA4"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:3VA4"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:3VA4"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:3VA4"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:3VA4"
SQ SEQUENCE 1707 AA; 184670 MW; F6ECCD30BBED265D CRC64;
MESTQVIDWD AEEEEETELS SGSLGYSVEP IGQLRLFSGT HGPERDFPLY LGKNVVGRSP
DCSVALPFPS ISKQHAVIEI SAWNKAPILQ DCGSLNGTQI VKPPRVLPPG VSHRLRDQEL
ILFADFPCQY HRLDVPPPLV PRSLLTIEKT PRIRIESQNS RVLLAADSEE EGDFPSGRCV
ANGQRNTASP SATVVPESDE EVSSPAPSVP GPSSPFGLGS DTDEEQGQQP GVEESSLADS
SGAAGEAEQP EANGTTAGIQ AQPTEHKLKD TKVKKEAGRA GVSDGSVLER SPTLGEDSDT
EVDEDHKPGF ADSETDVEEE RIPVTPPVAP VKKNQVLLAV GIGDPEAPGV AHLQDCLAGS
GTDVEDKTAL DVPLERNHTP MVINSDTDEE EEEEEEVSAA LTLAHLKERG IGLWSRDPGA
EEVKSQPQVL VEQSQSASGR DSDTDVEEES SGRKREIIPD SPMDVDEALT VTQPESQPPR
RPNDADEYMD MSSPGSHLVV NQASFAVVGK TRAQVEEEVP GPSVILGEKH QVPLEGAQPP
EEAWETAVQE GSSSPEAAAS VRPSQQPVAE DAGTECATAV SEQESTLEVR SQSGSPAAPV
EQVVIHTDTS GDPTLPQREG AQTPTGRERE AHVGRTKSAK ECCDAEPEDL CLPATQCFVE
GESQHPEAVQ SLENEPTQLF PCTLPQEPGP SHLSLQTPGA DTLDVPWEVL ATQPFCLREQ
SETSELHEAH GSQPSLPREP PGHQHLVHTS PVHTELLRIE GREIQTVEKA MGIPKEMADR
MTPEREPLER EIRGRTENSE RDVIGEELIQ GTKDREPKKV LARDSQRKEA DKDLEGNRES
LEVEIEMSKD SQKRERKVEK PEPKREWEPA DLEVTPDRGV TEEGSHDQKG QIASLTLKPG
VGVKDLEGLA SAPIITGSQA DGGKGDPLSP GRQQRGRLSC QTTPAGKASR GDPEPPDHCL
FSSVPEASTQ SLLTSQSQKQ STPQPLFSTS SSEIPLPESL HTKPNVRPRR SSRMTPSPHS
SAALKPNTTC PTNQPAASRP TSRPTRGRAN RSSTRTPELI VPVDPELQPS TSTEQPVIPK
LTSQVTEGRV QMPEPLLTGP EIQSPTSTEQ SVTPDRKPRA TRGRPSKSPN KTPEPLISTG
PELQPPTSIE QPVIPKPTSR VTRGRPRKSS VRTPESVVST GPELQPLTSI EQPVIPEPRA
TRGRPSKSSI KTPESVVPTG PELQPLTSAK QPVTPNLTSR ASRGRSSKSI RTPEPVVQTG
PEFHPSTSTE QPDTREPSSQ ARTRRSAVKT PEASVPTTPE LQPFTSKKQP APKPTALVTQ
GRTYKPSTED CESVGPVAPD FEPSTSTDHL VTPKVTDQSL TLQSSPLSAS PVSSTPDLKP
PVPIAQPVTP EPIPQANHQR KRRAAGKQGS RTVPLGHKSY SALSEPEPQS SASQSSGASE
ADSPRQKRPR RQASQKTVVI KEEPVETEVK EEPQETAIPT PEKRKRDHAE EVTQGKPTRS
RRTKPNQETA PKVLFTGVMD SRGERAVLAL GGSLASSVNE ASHLVTDRIR RTVKFLCALG
KGIPILSLNW LYQSRKAGCF LPPDDYLVTD PEQEKNFSFS LRDSLCRARE RRLLEDYEIH
VTPGVQPPPP QMGEIISCCG GTFLPSMPHS YKLHRVIITC TEDLPRCAIP SRLGLPLLSP
EFLLTGVLKQ EATPEAFVLS NLEMSST
