CHD4_MOUSE
ID CHD4_MOUSE Reviewed; 1915 AA.
AC Q6PDQ2;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Chromodomain-helicase-DNA-binding protein 4;
DE Short=CHD-4;
DE EC=3.6.4.12;
GN Name=Chd4;
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 [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [2]
RP INTERACTION WITH IKFZ1 IN THE NURD COMPLEX.
RX PubMed=11003653; DOI=10.1128/mcb.20.20.7572-7582.2000;
RA O'Neill D.W., Schoetz S.S., Lopez R.A., Castle M., Rabinowitz L., Shor E.,
RA Krawchuk D., Goll M.G., Renz M., Seelig H.P., Han S., Seong R.H.,
RA Park S.D., Agalioti T., Munshi N., Thanos D., Erdjument-Bromage H.,
RA Tempst P., Bank A.;
RT "An ikaros-containing chromatin-remodeling complex in adult-type erythroid
RT cells.";
RL Mol. Cell. Biol. 20:7572-7582(2000).
RN [3]
RP INTERACTION WITH KLF1, AND FUNCTION.
RX PubMed=17938210; DOI=10.1128/mcb.00589-07;
RA Siatecka M., Xue L., Bieker J.J.;
RT "Sumoylation of EKLF promotes transcriptional repression and is involved in
RT inhibition of megakaryopoiesis.";
RL Mol. Cell. Biol. 27:8547-8560(2007).
RN [4]
RP 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-421 AND SER-1528, AND
RP IDENTIFICATION BY 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-301; SER-302; SER-303;
RP SER-312; SER-421; SER-508; THR-522; SER-524; SER-1202; SER-1301; SER-1524;
RP SER-1528; SER-1530; THR-1535; THR-1542 AND THR-1546, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [7]
RP ABSENCE OF INTERACTION WITH PWWP2A AND PWWP2B.
RX PubMed=30228260; DOI=10.1038/s41467-018-06235-9;
RA Zhang T., Wei G., Millard C.J., Fischer R., Konietzny R., Kessler B.M.,
RA Schwabe J.W.R., Brockdorff N.;
RT "A variant NuRD complex containing PWWP2A/B excludes MBD2/3 to regulate
RT transcription at active genes.";
RL Nat. Commun. 9:3798-3798(2018).
RN [8]
RP ABSENCE OF INTERACTION WITH PWWP2A.
RX PubMed=30327463; DOI=10.1038/s41467-018-06665-5;
RA Link S., Spitzer R.M.M., Sana M., Torrado M., Voelker-Albert M.C.,
RA Keilhauer E.C., Burgold T., Puenzeler S., Low J.K.K., Lindstroem I.,
RA Nist A., Regnard C., Stiewe T., Hendrich B., Imhof A., Mann M.,
RA Mackay J.P., Bartkuhn M., Hake S.B.;
RT "PWWP2A binds distinct chromatin moieties and interacts with an MTA1-
RT specific core NuRD complex.";
RL Nat. Commun. 9:4300-4300(2018).
CC -!- FUNCTION: Component of the histone deacetylase NuRD complex which
CC participates in the remodeling of chromatin by deacetylating histones.
CC {ECO:0000269|PubMed:17938210}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBUNIT: Central component of the nucleosome remodeling and histone
CC deacetylase (NuRD) repressor complex (PubMed:11003653). Interacts with
CC KLF1; the interaction depends on sumoylation of KLF1, and leads to its
CC transcriptional repression (PubMed:17938210). Interacts with ZGPAT; the
CC interaction is direct. Interacts with BCL6, BRD4 and PCNT. Interacts
CC directly with IKFZ1 in the NuRD complex. Interacts with TRIM27. Part of
CC a complex containing ATR and HDAC2. Interacts with HDAC2; the
CC interaction is direct (By similarity). Interacts with SETX (By
CC similarity). Interacts with HDAC1 (By similarity). Interacts with the
CC ISWI chromatin remodeling complex component SMARCA5; the interaction is
CC direct (By similarity). Interacts with the cohesin complex component
CC RAD21; the interaction is direct (By similarity). Does not interact
CC with PWWP2A and PWWP2B (PubMed:30228260, PubMed:30327463).
CC {ECO:0000250|UniProtKB:Q14839, ECO:0000269|PubMed:11003653,
CC ECO:0000269|PubMed:17938210, ECO:0000269|PubMed:30228260,
CC ECO:0000269|PubMed:30327463}.
CC -!- INTERACTION:
CC Q6PDQ2; Q60I23: Sox2; NbExp=3; IntAct=EBI-3043852, EBI-6120118;
CC Q6PDQ2; P70326: Tbx5; NbExp=3; IntAct=EBI-3043852, EBI-8411807;
CC Q6PDQ2; Q80V81: Zfp819; NbExp=4; IntAct=EBI-3043852, EBI-6394055;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000250}.
CC Note=Associates with centrosomes in interphase. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; BC058578; AAH58578.1; -; mRNA.
DR CCDS; CCDS20543.1; -.
DR RefSeq; NP_001333539.1; NM_001346610.1.
DR RefSeq; NP_666091.1; NM_145979.2.
DR AlphaFoldDB; Q6PDQ2; -.
DR BMRB; Q6PDQ2; -.
DR SMR; Q6PDQ2; -.
DR BioGRID; 223700; 44.
DR ComplexPortal; CPX-953; MBD2/NuRD nucleosome remodeling and deacetylase complex.
DR ComplexPortal; CPX-954; MBD3/NuRD nucleosome remodeling and deacetylase complex.
DR CORUM; Q6PDQ2; -.
DR DIP; DIP-59651N; -.
DR IntAct; Q6PDQ2; 28.
DR MINT; Q6PDQ2; -.
DR STRING; 10090.ENSMUSP00000060054; -.
DR iPTMnet; Q6PDQ2; -.
DR PhosphoSitePlus; Q6PDQ2; -.
DR SwissPalm; Q6PDQ2; -.
DR EPD; Q6PDQ2; -.
DR jPOST; Q6PDQ2; -.
DR MaxQB; Q6PDQ2; -.
DR PaxDb; Q6PDQ2; -.
DR PRIDE; Q6PDQ2; -.
DR ProteomicsDB; 281602; -.
DR DNASU; 107932; -.
DR Ensembl; ENSMUST00000056889; ENSMUSP00000060054; ENSMUSG00000063870.
DR GeneID; 107932; -.
DR KEGG; mmu:107932; -.
DR UCSC; uc009dtk.1; mouse.
DR CTD; 1108; -.
DR MGI; MGI:1344380; Chd4.
DR VEuPathDB; HostDB:ENSMUSG00000063870; -.
DR eggNOG; KOG0383; Eukaryota.
DR GeneTree; ENSGT00940000155088; -.
DR InParanoid; Q6PDQ2; -.
DR OMA; HMEEDFG; -.
DR PhylomeDB; Q6PDQ2; -.
DR TreeFam; TF106448; -.
DR Reactome; R-MMU-3214815; HDACs deacetylate histones.
DR Reactome; R-MMU-6804758; Regulation of TP53 Activity through Acetylation.
DR Reactome; R-MMU-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-MMU-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-MMU-9031628; NGF-stimulated transcription.
DR BioGRID-ORCS; 107932; 20 hits in 79 CRISPR screens.
DR ChiTaRS; Chd4; mouse.
DR PRO; PR:Q6PDQ2; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q6PDQ2; protein.
DR Bgee; ENSMUSG00000063870; Expressed in ileal epithelium and 267 other tissues.
DR ExpressionAtlas; Q6PDQ2; baseline and differential.
DR Genevisible; Q6PDQ2; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0016581; C:NuRD complex; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0032993; C:protein-DNA complex; IDA:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0001221; F:transcription coregulator binding; ISO:MGI.
DR GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
DR GO; GO:0016575; P:histone deacetylation; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0042659; P:regulation of cell fate specification; IC:ComplexPortal.
DR GO; GO:2000736; P:regulation of stem cell differentiation; IC:ComplexPortal.
DR GO; GO:0072553; P:terminal button organization; ISO:MGI.
DR Gene3D; 3.30.40.10; -; 2.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR012957; CHD_C2.
DR InterPro; IPR009462; CHD_II_SANT-like.
DR InterPro; IPR012958; CHD_N.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR009463; DUF1087.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF08074; CHDCT2; 1.
DR Pfam; PF08073; CHDNT; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF06461; DUF1086; 1.
DR Pfam; PF06465; DUF1087; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01146; DUF1086; 1.
DR SMART; SM01147; DUF1087; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54160; SSF54160; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS00598; CHROMO_1; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Chromatin regulator; Cytoplasm; Cytoskeleton;
KW DNA-binding; Helicase; Hydrolase; Isopeptide bond; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1915
FT /note="Chromodomain-helicase-DNA-binding protein 4"
FT /id="PRO_0000080229"
FT DOMAIN 522..579
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 615..676
FT /note="Chromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 731..915
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1047..1196
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 363..410
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 442..489
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1337..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1518..1694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1570..1915
FT /note="Required for interaction with PCNT"
FT /evidence="ECO:0000250"
FT MOTIF 866..869
FT /note="DEAH box"
FT COMPBIAS 52..66
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..95
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..527
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1337..1353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1372..1393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1529..1551
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1558..1580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1609..1694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 744..751
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 360
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 510
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT MOD_RES 522
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 696
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT MOD_RES 1202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT MOD_RES 1363
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12873"
FT MOD_RES 1524
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1528
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1530
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1535
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1542
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1546
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1563
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT MOD_RES 1569
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT MOD_RES 1646
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT MOD_RES 1656
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT MOD_RES 1682
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 126
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 172
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 290
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 611
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q12873"
FT CROSSLNK 689
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 704
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q12873"
FT CROSSLNK 704
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 1205
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 1221
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 1232
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 1297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 1521
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 1522
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 1558
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 1565
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 1577
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 1609
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 1620
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 1639
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 1646
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 1650
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 1663
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 1673
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 1690
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 1868
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
SQ SEQUENCE 1915 AA; 217751 MW; CFCB83B419AE6B5A CRC64;
MASGLGSPSP CSAGSEEEDM DALLNNSLPP PHPENEEDPD EDLSEAETPK LKKKKKPKKP
RDPKIPKSKR QKKELGDSSG EGPEFVEEEE EVALRSDSEG SDYTPGKKKK KKLGPKKEKK
SKSKRKEEEE EEDEDDDSKE PKSSAQLLED WGMEDIDHVF SEEDYRTLTN YKAFSQFVRP
LIAAKNPKIA VSKMMMVLGA KWREFSTNNP FKGSSGASVA AAAAAAVAVV ESMVTATEVA
PPPPPVEVPI RKAKTKEGKG PNARRKPKGS PRVPDAKKPK PKKVAPLKIK LGGFGSKRKR
SSSEDDDLDV ESDFDDASIN SYSVSDGSTS RSSRSRKKLR TAKKKKKGEE EVTAVDGYET
DHQDYCEVCQ QGGEIILCDT CPRAYHMVCL DPDMEKAPEG KWSCPHCEKE GIQWEAKEDN
SEGEEILEEV GGDPEEEDDH HMEFCRVCKD GGELLCCDTC PSSYHIHCLN PPLPEIPNGE
WLCPRCTCPA LKGKVQKILI WKWGQPPSPT PVPRPPDADP NTPSPKPLEG RPERQFFVKW
QGMSYWHCSW VSELQLELHC QVMFRNYQRK NDMDEPPSGD FGGDEEKSRK RKNKDPKFAE
MEERFYRYGI KPEWMMIHRI LNHSVDKKGH VHYLIKWRDL PYDQASWESE DVEIQDYDLF
KQSYWNHREL MRGEEGRPGK KLKKVKLRKL ERPPETPTVD PTVKYERQPE YLDATGGTLH
PYQMEGLNWL RFSWAQGTDT ILADEMGLGK TVQTAVFLYS LYKEGHSKGP FLVSAPLSTI
INWEREFEMW APDMYVVTYV GDKDSRAIIR ENEFSFEDNA IRGGKKASRM KKEASVKFHV
LLTSYELITI DMAILGSIDW ACLIVDEAHR LKNNQSKFFR VLNGYSLQHK LLLTGTPLQN
NLEELFHLLN FLTPERFHNL EGFLEEFADI AKEDQIKKLH DMLGPHMLRR LKADVFKNMP
SKTELIVRVE LSPMQKKYYK YILTRNFEAL NARGGGNQVS LLNVVMDLKK CCNHPYLFPV
AAMEAPKMPN GMYDGSALIR ASGKLLLLQK MLKNLKEGGH RVLIFSQMTK MLDLLEDFLE
HEGYKYERID GGITGNMRQE AIDRFNAPGA QQFCFLLSTR AGGLGINLAT ADTVIIYDSD
WNPHNDIQAF SRAHRIGQNK KVMIYRFVTR ASVEERITQV AKKKMMLTHL VVRPGLGSKT
GSMSKQELDD ILKFGTEELF KDEATDGGGD NKEGEDSSVI HYDDKAIERL LDRNQDETED
TELQGMNEYL SSFKVAQYVV REEEMGEEEE VEREIIKQEE SVDPDYWEKL LRHHYEQQQE
DLARNLGKGK RIRKQVNYND GSQEDRDWQD DQSDNQSDYS VASEEGDEDF DERSEAPRRP
SRKGLRNDKD KPLPPLLARV GGNIEVLGFN ARQRKAFLNA IMRYGMPPQD AFTTQWLVRD
LRGKSEKEFK AYVSLFMRHL CEPGADGAET FADGVPREGL SRQHVLTRIG VMSLIRKKVQ
EFEHVNGRWS MPELAEVEEN KKMSQPGSPS PKTPTPSTPG DTQPNTPAPV PPAEDGIKIE
ENSLKEEEST EGEKEVKSTA PEATVECAQP PAPAPATAPA TATAPEDDKA PAEPPEGEEK
VEKAEVKERT EEPMETEAKG TTEVEKVEEK SAVDLTPIVV EDKEEKKEEE EKKDVMLQNG
ETPKDLSDEK QKKNSKQRFM FNIADGGFTE LHSLWQNEER AATVTKKTYE IWHRRHDYWL
LAGIINHGYA RWQDIQNDPR YAILNEPFKG EMNRGNFLEI KNKFLARRFK LLEQALVIEE
QLRRAAYLNM SEDPSHPSMA LNTRFAEVEC LAESHQHLSK ESMAGNKPAN AVLHKVLKQL
EELLSDMKAD VTRLPATIAR IPPVAVRLQM SERNILSRLA NRAPEPPPQQ VAQQQ
