DCA15_HUMAN
ID DCA15_HUMAN Reviewed; 600 AA.
AC Q66K64; B3KS86; Q96DW0; Q9BU31;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=DDB1- and CUL4-associated factor 15 {ECO:0000305};
GN Name=DCAF15 {ECO:0000303|PubMed:28437394, ECO:0000312|HGNC:HGNC:25095};
GN Synonyms=C19orf72;
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 [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary, and Skin;
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 FUNCTION, INTERACTION WITH DDB1 AND CUL4A, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16949367; DOI=10.1016/j.molcel.2006.08.010;
RA Jin J., Arias E.E., Chen J., Harper J.W., Walter J.C.;
RT "A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is
RT required for S phase destruction of the replication factor Cdt1.";
RL Mol. Cell 23:709-721(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-310, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP FUNCTION, PATHWAY, IDENTIFICATION IN THE DCX(DCAF15) COMPLEX, AND ACTIVITY
RP REGULATION.
RX PubMed=28437394; DOI=10.1038/nchembio.2363;
RA Uehara T., Minoshima Y., Sagane K., Sugi N.H., Mitsuhashi K.O.,
RA Yamamoto N., Kamiyama H., Takahashi K., Kotake Y., Uesugi M., Yokoi A.,
RA Inoue A., Yoshida T., Mabuchi M., Tanaka A., Owa T.;
RT "Selective degradation of splicing factor CAPERalpha by anticancer
RT sulfonamides.";
RL Nat. Chem. Biol. 13:675-680(2017).
RN [10]
RP FUNCTION, PATHWAY, IDENTIFICATION IN THE DCX(DCAF15) COMPLEX, AND ACTIVITY
RP REGULATION.
RX PubMed=28302793; DOI=10.1126/science.aal3755;
RA Han T., Goralski M., Gaskill N., Capota E., Kim J., Ting T.C., Xie Y.,
RA Williams N.S., Nijhawan D.;
RT "Anticancer sulfonamides target splicing by inducing RBM39 degradation via
RT recruitment to DCAF15.";
RL Science 356:0-0(2017).
RN [11]
RP ERRATUM OF PUBMED:28302793.
RX PubMed=28546157; DOI=10.1126/science.aan7977;
RA Han T., Goralski M., Gaskill N., Capota E., Kim J., Ting T.C., Xie Y.,
RA Williams N.S., Nijhawan D.;
RL Science 356:0-0(2017).
RN [12]
RP FUNCTION, PATHWAY, IDENTIFICATION IN THE DCX(DCAF15) COMPLEX, AND
RP MUTAGENESIS OF VAL-90; LEU-91; TRP-112; PHE-129; VAL-182; CYS-196; GLN-232;
RP LEU-244; LEU-392; THR-420; GLU-444; VAL-453 AND ASP-475.
RX PubMed=31693891; DOI=10.1016/j.celrep.2019.09.079;
RA Ting T.C., Goralski M., Klein K., Wang B., Kim J., Xie Y., Nijhawan D.;
RT "Aryl sulfonamides degrade RBM39 and RBM23 by recruitment to CRL4-DCAF15.";
RL Cell Rep. 29:1499-1510(2019).
RN [13]
RP FUNCTION, PATHWAY, AND IDENTIFICATION IN THE DCX(DCAF15) COMPLEX.
RX PubMed=31452512; DOI=10.7554/elife.47362;
RA Pech M.F., Fong L.E., Villalta J.E., Chan L.J., Kharbanda S., O'Brien J.J.,
RA McAllister F.E., Firestone A.J., Jan C.H., Settleman J.;
RT "Systematic identification of cancer cell vulnerabilities to natural killer
RT cell-mediated immune surveillance.";
RL Elife 8:0-0(2019).
RN [14]
RP FUNCTION.
RX PubMed=31626998; DOI=10.1016/j.jprot.2019.103545;
RA Jia X., Pan L., Zhu M., Hu H., Zhai L., Liu J., Hu M., Liu B., Tan M.;
RT "pSILAC method coupled with two complementary digestion approaches reveals
RT PRPF39 as a new E7070-dependent DCAF15 substrate.";
RL J. Proteomics 210:103545-103545(2020).
RN [15] {ECO:0007744|PDB:6Q0R, ECO:0007744|PDB:6Q0V, ECO:0007744|PDB:6Q0W}
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 34-290 AND 383-600 IN COMPLEX WITH
RP ZINC; ARYL-SULFONAMIDE E7820; DDB1; DDA1 AND RBM39, FUNCTION, ACTIVITY
RP REGULATION, AND IDENTIFICATION IN THE DCX(DCAF15) COMPLEX.
RX PubMed=31686031; DOI=10.1038/s41589-019-0378-3;
RA Faust T.B., Yoon H., Nowak R.P., Donovan K.A., Li Z., Cai Q.,
RA Eleuteri N.A., Zhang T., Gray N.S., Fischer E.S.;
RT "Structural complementarity facilitates E7820-mediated degradation of RBM39
RT by DCAF15.";
RL Nat. Chem. Biol. 16:7-14(2020).
RN [16] {ECO:0007744|PDB:6SJ7, ECO:0007744|PDB:6UD7, ECO:0007744|PDB:6UE5}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-600 IN COMPLEX WITH
RP ARYL-SULFONAMIDE E7820; DDB1; DDA1 AND RBM39, STRUCTURE BY ELECTRON
RP MICROSCOPY (3.54 ANGSTROMS) IN COMPLEX WITH ARYL-SULFONAMIDE E7820; DDB1;
RP DDA1 AND RBM39, FUNCTION, ACTIVITY REGULATION, AND IDENTIFICATION IN THE
RP DCX(DCAF15) COMPLEX.
RX PubMed=31819272; DOI=10.1038/s41589-019-0411-6;
RA Bussiere D.E., Xie L., Srinivas H., Shu W., Burke A., Be C., Zhao J.,
RA Godbole A., King D., Karki R.G., Hornak V., Xu F., Cobb J., Carte N.,
RA Frank A.O., Frommlet A., Graff P., Knapp M., Fazal A., Okram B., Jiang S.,
RA Michellys P.Y., Beckwith R., Voshol H., Wiesmann C., Solomon J.M.,
RA Paulk J.;
RT "Structural basis of indisulam-mediated RBM39 recruitment to DCAF15 E3
RT ligase complex.";
RL Nat. Chem. Biol. 16:15-23(2020).
RN [17] {ECO:0007744|PDB:6PAI}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 2-600 IN COMPLEX WITH ZINC;
RP ARYL-SULFONAMIDE E7820; DDB1; DDA1 AND RBM39, AND IDENTIFICATION IN THE
RP DCX(DCAF15) COMPLEX.
RX PubMed=31693911; DOI=10.1016/j.str.2019.10.005;
RA Du X., Volkov O.A., Czerwinski R.M., Tan H., Huerta C., Morton E.R.,
RA Rizzi J.P., Wehn P.M., Xu R., Nijhawan D., Wallace E.M.;
RT "Structural basis and kinetic pathway of RBM39 recruitment to DCAF15 by a
RT sulfonamide molecular glue E7820.";
RL Structure 27:1625-1633(2019).
CC -!- FUNCTION: Substrate-recognition component of the DCX(DCAF15) complex, a
CC cullin-4-RING E3 ubiquitin-protein ligase complex that mediates
CC ubiquitination and degradation of target proteins (PubMed:16949367,
CC PubMed:31452512). The DCX(DCAF15) complex acts as a regulator of the
CC natural killer (NK) cells effector functions, possibly by mediating
CC ubiquitination and degradation of cohesin subunits SMC1A and SMC3
CC (PubMed:31452512). May play a role in the activation of antigen-
CC presenting cells (APC) and their interaction with NK cells
CC (PubMed:31452512). {ECO:0000269|PubMed:16949367,
CC ECO:0000269|PubMed:31452512}.
CC -!- FUNCTION: Binding of aryl sulfonamide anticancer drugs, such as
CC indisulam (E7070) or E7820, change the substrate specificity of the
CC DCX(DCAF15) complex, leading to promote ubiquitination and degradation
CC of splicing factor RBM39 (PubMed:28437394, PubMed:28302793,
CC PubMed:31693891, PubMed:31452512). RBM39 degradation results in
CC splicing defects and death in cancer cell lines (PubMed:28437394,
CC PubMed:28302793, PubMed:31693891). Aryl sulfonamide anticancer drugs
CC change the substrate specificity of DCAF15 by acting as a molecular
CC glue that promotes binding between DCAF15 and weak affinity interactor
CC RBM39 (PubMed:31686031, PubMed:31819272). Aryl sulfonamide anticancer
CC drugs also promote ubiquitination and degradation of RBM23 and PRPF39
CC (PubMed:31693891, PubMed:31626998, PubMed:31686031).
CC {ECO:0000269|PubMed:28302793, ECO:0000269|PubMed:28437394,
CC ECO:0000269|PubMed:31452512, ECO:0000269|PubMed:31626998,
CC ECO:0000269|PubMed:31686031, ECO:0000269|PubMed:31693891,
CC ECO:0000269|PubMed:31819272}.
CC -!- ACTIVITY REGULATION: Aryl sulfonamide anticancer drugs change the
CC substrate specificity of DCAF15 by acting as a molecular glue that
CC promotes binding between DCAF15 and weak affinity interactors, such as
CC RBM39. {ECO:0000269|PubMed:28302793, ECO:0000269|PubMed:28437394,
CC ECO:0000269|PubMed:31686031, ECO:0000269|PubMed:31819272}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:28302793, ECO:0000269|PubMed:28437394,
CC ECO:0000269|PubMed:31452512, ECO:0000269|PubMed:31693891}.
CC -!- SUBUNIT: Component of the DCX(DCAF15) complex, also named CLR4(DCAF15)
CC complex, composed of DCAF15, DDB1, cullin-4 (CUL4A or CUL4B), DDA1 and
CC RBX1. {ECO:0000269|PubMed:28302793, ECO:0000269|PubMed:28437394,
CC ECO:0000269|PubMed:31452512, ECO:0000269|PubMed:31686031,
CC ECO:0000269|PubMed:31693891, ECO:0000269|PubMed:31693911,
CC ECO:0000269|PubMed:31819272, ECO:0000305|PubMed:16949367}.
CC -!- INTERACTION:
CC Q66K64; Q0D2K3: RIPPLY1; NbExp=3; IntAct=EBI-2559052, EBI-10226430;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH13280.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK093072; BAG52648.1; -; mRNA.
DR EMBL; CH471106; EAW84386.1; -; Genomic_DNA.
DR EMBL; BC002926; AAH02926.2; -; mRNA.
DR EMBL; BC013280; AAH13280.2; ALT_FRAME; mRNA.
DR EMBL; BC080575; AAH80575.1; -; mRNA.
DR CCDS; CCDS32926.1; -.
DR RefSeq; NP_612362.2; NM_138353.3.
DR PDB; 6PAI; X-ray; 2.90 A; C=2-600.
DR PDB; 6Q0R; X-ray; 2.90 A; B=34-260, C=383-600.
DR PDB; 6Q0V; X-ray; 2.90 A; B=34-260, C=383-600.
DR PDB; 6Q0W; X-ray; 2.90 A; B=34-260, C=383-600.
DR PDB; 6SJ7; EM; 3.54 A; A=1-600.
DR PDB; 6UD7; X-ray; 2.30 A; A=2-600.
DR PDB; 6UE5; X-ray; 2.61 A; A=2-600.
DR PDBsum; 6PAI; -.
DR PDBsum; 6Q0R; -.
DR PDBsum; 6Q0V; -.
DR PDBsum; 6Q0W; -.
DR PDBsum; 6SJ7; -.
DR PDBsum; 6UD7; -.
DR PDBsum; 6UE5; -.
DR AlphaFoldDB; Q66K64; -.
DR SMR; Q66K64; -.
DR BioGRID; 124705; 260.
DR IntAct; Q66K64; 13.
DR STRING; 9606.ENSP00000254337; -.
DR iPTMnet; Q66K64; -.
DR PhosphoSitePlus; Q66K64; -.
DR BioMuta; DCAF15; -.
DR DMDM; 74736316; -.
DR EPD; Q66K64; -.
DR jPOST; Q66K64; -.
DR MassIVE; Q66K64; -.
DR MaxQB; Q66K64; -.
DR PaxDb; Q66K64; -.
DR PeptideAtlas; Q66K64; -.
DR PRIDE; Q66K64; -.
DR ProteomicsDB; 65955; -.
DR Antibodypedia; 77450; 2 antibodies from 2 providers.
DR DNASU; 90379; -.
DR Ensembl; ENST00000254337.11; ENSP00000254337.5; ENSG00000132017.11.
DR Ensembl; ENST00000672437.1; ENSP00000500158.1; ENSG00000288453.1.
DR GeneID; 90379; -.
DR KEGG; hsa:90379; -.
DR MANE-Select; ENST00000254337.11; ENSP00000254337.5; NM_138353.4; NP_612362.2.
DR UCSC; uc002mxt.4; human.
DR CTD; 90379; -.
DR DisGeNET; 90379; -.
DR GeneCards; DCAF15; -.
DR HGNC; HGNC:25095; DCAF15.
DR HPA; ENSG00000132017; Low tissue specificity.
DR neXtProt; NX_Q66K64; -.
DR OpenTargets; ENSG00000132017; -.
DR PharmGKB; PA165393390; -.
DR VEuPathDB; HostDB:ENSG00000132017; -.
DR eggNOG; ENOG502QQCQ; Eukaryota.
DR GeneTree; ENSGT00390000011987; -.
DR HOGENOM; CLU_031970_0_0_1; -.
DR InParanoid; Q66K64; -.
DR OMA; QILYTKG; -.
DR OrthoDB; 471103at2759; -.
DR PhylomeDB; Q66K64; -.
DR TreeFam; TF329680; -.
DR PathwayCommons; Q66K64; -.
DR SignaLink; Q66K64; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 90379; 80 hits in 1116 CRISPR screens.
DR ChiTaRS; DCAF15; human.
DR GenomeRNAi; 90379; -.
DR Pharos; Q66K64; Tdark.
DR PRO; PR:Q66K64; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q66K64; protein.
DR Bgee; ENSG00000132017; Expressed in granulocyte and 92 other tissues.
DR ExpressionAtlas; Q66K64; baseline and differential.
DR Genevisible; Q66K64; HS.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0036094; F:small molecule binding; IPI:UniProtKB.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0032814; P:regulation of natural killer cell activation; IMP:UniProtKB.
DR InterPro; IPR038914; DCAF15.
DR InterPro; IPR032734; DCAF15_WD40.
DR PANTHER; PTHR28541; PTHR28541; 1.
DR Pfam; PF14939; DCAF15_WD40; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Immunity; Metal-binding; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway; Zinc.
FT CHAIN 1..600
FT /note="DDB1- and CUL4-associated factor 15"
FT /id="PRO_0000314485"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..299
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:31686031,
FT ECO:0000269|PubMed:31693911, ECO:0007744|PDB:6PAI,
FT ECO:0007744|PDB:6Q0R, ECO:0007744|PDB:6Q0V,
FT ECO:0007744|PDB:6Q0W"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:31686031,
FT ECO:0000269|PubMed:31693911, ECO:0007744|PDB:6PAI,
FT ECO:0007744|PDB:6Q0R, ECO:0007744|PDB:6Q0V,
FT ECO:0007744|PDB:6Q0W"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:31686031,
FT ECO:0000269|PubMed:31693911, ECO:0007744|PDB:6PAI,
FT ECO:0007744|PDB:6Q0R, ECO:0007744|PDB:6Q0V,
FT ECO:0007744|PDB:6Q0W"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:31686031,
FT ECO:0000269|PubMed:31693911, ECO:0007744|PDB:6PAI,
FT ECO:0007744|PDB:6Q0R, ECO:0007744|PDB:6Q0V,
FT ECO:0007744|PDB:6Q0W"
FT BINDING 231
FT /ligand="E7820"
FT /ligand_id="ChEBI:CHEBI:188454"
FT /evidence="ECO:0000269|PubMed:31686031,
FT ECO:0000269|PubMed:31693911, ECO:0000269|PubMed:31819272,
FT ECO:0007744|PDB:6PAI, ECO:0007744|PDB:6Q0R,
FT ECO:0007744|PDB:6Q0W"
FT BINDING 234..235
FT /ligand="E7820"
FT /ligand_id="ChEBI:CHEBI:188454"
FT /evidence="ECO:0000269|PubMed:31686031,
FT ECO:0000269|PubMed:31693911, ECO:0000269|PubMed:31819272,
FT ECO:0007744|PDB:6PAI, ECO:0007744|PDB:6Q0R,
FT ECO:0007744|PDB:6Q0V, ECO:0007744|PDB:6Q0W"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MUTAGEN 90
FT /note="V->D: Abolished interaction with DDB1, DDA1 and
FT RBM39 in presence of indisulam."
FT /evidence="ECO:0000269|PubMed:31693891"
FT MUTAGEN 91
FT /note="L->P: Abolished interaction with DDB1, DDA1 and
FT RBM39 in presence of indisulam."
FT /evidence="ECO:0000269|PubMed:31693891"
FT MUTAGEN 112
FT /note="W->R: Abolished interaction with DDB1, DDA1 and
FT RBM39 in presence of indisulam."
FT /evidence="ECO:0000269|PubMed:31693891"
FT MUTAGEN 129
FT /note="F->S,V: Abolished interaction with DDB1, DDA1 and
FT RBM39 in presence of indisulam."
FT /evidence="ECO:0000269|PubMed:31693891"
FT MUTAGEN 182
FT /note="V->D: Decreased interaction with DDB1, DDA1 and
FT RBM39 in presence of indisulam."
FT /evidence="ECO:0000269|PubMed:31693891"
FT MUTAGEN 196
FT /note="C->Y: Decreased interaction with DDB1, DDA1 and
FT RBM39 in presence of indisulam."
FT /evidence="ECO:0000269|PubMed:31693891"
FT MUTAGEN 232
FT /note="Q->R: Decreased interaction with RBM39 in presence
FT of indisulam, without affecting interaction with DDA1 and
FT DDB1."
FT /evidence="ECO:0000269|PubMed:31693891"
FT MUTAGEN 244
FT /note="L->P: Decreased interaction with DDB1, DDA1 and
FT RBM39 in presence of indisulam."
FT /evidence="ECO:0000269|PubMed:31693891"
FT MUTAGEN 392
FT /note="L->P: Decreased interaction with DDA1 and RBM39 in
FT presence of indisulam."
FT /evidence="ECO:0000269|PubMed:31693891"
FT MUTAGEN 420
FT /note="T->P: Decreased interaction with DDA1 and RBM39 in
FT presence of indisulam."
FT /evidence="ECO:0000269|PubMed:31693891"
FT MUTAGEN 444
FT /note="E->K: Decreased interaction with DDA1 and RBM39 in
FT presence of indisulam."
FT /evidence="ECO:0000269|PubMed:31693891"
FT MUTAGEN 453
FT /note="V->D: Decreased interaction with DDA1 and RBM39 in
FT presence of indisulam."
FT /evidence="ECO:0000269|PubMed:31693891"
FT MUTAGEN 475
FT /note="D->H,N,V: Decreased interaction with RBM39 in
FT presence of indisulam, without affecting interaction with
FT DDA1 and DDB1."
FT /evidence="ECO:0000269|PubMed:31693891"
FT HELIX 36..46
FT /evidence="ECO:0007829|PDB:6UD7"
FT TURN 51..56
FT /evidence="ECO:0007829|PDB:6UD7"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:6UD7"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:6UD7"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:6PAI"
FT TURN 74..77
FT /evidence="ECO:0007829|PDB:6PAI"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:6UD7"
FT STRAND 87..96
FT /evidence="ECO:0007829|PDB:6UD7"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:6UD7"
FT STRAND 105..113
FT /evidence="ECO:0007829|PDB:6UD7"
FT STRAND 121..129
FT /evidence="ECO:0007829|PDB:6UD7"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:6Q0W"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:6UD7"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:6UD7"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:6UD7"
FT STRAND 178..186
FT /evidence="ECO:0007829|PDB:6UD7"
FT HELIX 194..199
FT /evidence="ECO:0007829|PDB:6PAI"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:6PAI"
FT STRAND 217..224
FT /evidence="ECO:0007829|PDB:6UD7"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:6UD7"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:6UD7"
FT STRAND 248..259
FT /evidence="ECO:0007829|PDB:6UD7"
FT STRAND 389..395
FT /evidence="ECO:0007829|PDB:6UD7"
FT STRAND 420..427
FT /evidence="ECO:0007829|PDB:6UD7"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:6UD7"
FT STRAND 440..449
FT /evidence="ECO:0007829|PDB:6UD7"
FT HELIX 450..460
FT /evidence="ECO:0007829|PDB:6UD7"
FT TURN 463..467
FT /evidence="ECO:0007829|PDB:6UD7"
FT STRAND 468..482
FT /evidence="ECO:0007829|PDB:6UD7"
FT TURN 483..486
FT /evidence="ECO:0007829|PDB:6UD7"
FT STRAND 487..498
FT /evidence="ECO:0007829|PDB:6UD7"
FT STRAND 511..522
FT /evidence="ECO:0007829|PDB:6UD7"
FT TURN 523..525
FT /evidence="ECO:0007829|PDB:6UD7"
FT STRAND 528..533
FT /evidence="ECO:0007829|PDB:6UD7"
FT HELIX 544..561
FT /evidence="ECO:0007829|PDB:6UD7"
FT STRAND 568..571
FT /evidence="ECO:0007829|PDB:6UD7"
FT STRAND 573..575
FT /evidence="ECO:0007829|PDB:6UD7"
FT TURN 579..582
FT /evidence="ECO:0007829|PDB:6UD7"
FT STRAND 587..591
FT /evidence="ECO:0007829|PDB:6UD7"
FT TURN 592..595
FT /evidence="ECO:0007829|PDB:6UD7"
FT STRAND 596..599
FT /evidence="ECO:0007829|PDB:6UD7"
SQ SEQUENCE 600 AA; 66463 MW; 091BB2D0AADF3E6F CRC64;
MAPSSKSERN SGAGSGGGGP GGAGGKRAAG RRREHVLKQL ERVKISGQLS PRLFRKLPPR
VCVSLKNIVD EDFLYAGHIF LGFSKCGRYV LSYTSSSGDD DFSFYIYHLY WWEFNVHSKL
KLVRQVRLFQ DEEIYSDLYL TVCEWPSDAS KVIVFGFNTR SANGMLMNMM MMSDENHRDI
YVSTVAVPPP GRCAACQDAS RAHPGDPNAQ CLRHGFMLHT KYQVVYPFPT FQPAFQLKKD
QVVLLNTSYS LVACAVSVHS AGDRSFCQIL YDHSTCPLAP ASPPEPQSPE LPPALPSFCP
EAAPARSSGS PEPSPAIAKA KEFVADIFRR AKEAKGGVPE EARPALCPGP SGSRCRAHSE
PLALCGETAP RDSPPASEAP ASEPGYVNYT KLYYVLESGE GTEPEDELED DKISLPFVVT
DLRGRNLRPM RERTAVQGQY LTVEQLTLDF EYVINEVIRH DATWGHQFCS FSDYDIVILE
VCPETNQVLI NIGLLLLAFP SPTEEGQLRP KTYHTSLKVA WDLNTGIFET VSVGDLTEVK
GQTSGSVWSS YRKSCVDMVM KWLVPESSGR YVNRMTNEAL HKGCSLKVLA DSERYTWIVL
