MACD1_HUMAN
ID MACD1_HUMAN Reviewed; 325 AA.
AC Q9BQ69; Q9UH96;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=ADP-ribose glycohydrolase MACROD1 {ECO:0000305};
DE AltName: Full=MACRO domain-containing protein 1 {ECO:0000303|PubMed:23474712};
DE AltName: Full=O-acetyl-ADP-ribose deacetylase MACROD1;
DE EC=3.1.1.106 {ECO:0000305|PubMed:21257746};
DE AltName: Full=Protein LRP16;
DE AltName: Full=[Protein ADP-ribosylaspartate] hydrolase MACROD1 {ECO:0000305};
DE EC=3.2.2.- {ECO:0000269|PubMed:23474714};
DE AltName: Full=[Protein ADP-ribosylglutamate] hydrolase MACROD1 {ECO:0000305};
DE EC=3.2.2.- {ECO:0000269|PubMed:23474712, ECO:0000269|PubMed:23474714};
GN Name=MACROD1 {ECO:0000303|PubMed:23474712, ECO:0000312|HGNC:HGNC:29598};
GN Synonyms=LRP16;
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].
RC TISSUE=Lymphocyte;
RX PubMed=12578638;
RA Han W.-D., Yu L., Lou F.D., Wang Q.S., Zhao Y., Shi Z.J., Jin H.J.;
RT "The application of RACE technique to clone the full-length cDNA of a novel
RT leukemia associated gene LRP16.";
RL Zhongguo Shi Yan Xue Ye Xue Za Zhi 9:18-21(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and 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 [3]
RP INDUCTION.
RX PubMed=12790785; DOI=10.1677/erc.0.0100217;
RA Han W.-D., Mu Y.-M., Lu X.-C., Xu Z.-M., Li X.-J., Yu L., Song H.-J.,
RA Li M., Lu J.-M., Zhao Y.-L., Pan C.-Y.;
RT "Up-regulation of LRP16 mRNA by 17beta-estradiol through activation of
RT estrogen receptor alpha (ERalpha), but not ERbeta, and promotion of human
RT breast cancer MCF-7 cell proliferation: a preliminary report.";
RL Endocr. Relat. Cancer 10:217-224(2003).
RN [4]
RP INDUCTION, AND FUNCTION.
RX PubMed=17893710; DOI=10.1038/cr.2007.79;
RA Meng Y.G., Han W.-D., Zhao Y.-L., Huang K., Si Y.-L., Wu Z.-Q., Mu Y.-M.;
RT "Induction of the LRP16 gene by estrogen promotes the invasive growth of
RT Ishikawa human endometrial cancer cells through the downregulation of E-
RT cadherin.";
RL Cell Res. 17:869-880(2007).
RN [5]
RP INTERACTION WITH ESR1, AND FUNCTION.
RX PubMed=17914104; DOI=10.1677/erc-06-0082;
RA Han W.-D., Zhao Y.-L., Meng Y.G., Zang L., Wu Z.-Q., Li Q., Si Y.-L.,
RA Huang K., Ba J.-M., Morinaga H., Nomura M., Mu Y.-M.;
RT "Estrogenically regulated LRP16 interacts with estrogen receptor alpha and
RT enhances the receptor's transcriptional activity.";
RL Endocr. Relat. Cancer 14:741-753(2007).
RN [6]
RP CHROMOSOMAL TRANSLOCATION WITH RUNX1.
RX PubMed=17532767; DOI=10.1111/j.1600-0609.2007.00858.x;
RA Imagama S., Abe A., Suzuki M., Hayakawa F., Katsumi A., Emi N., Kiyoi H.,
RA Naoe T.;
RT "LRP16 is fused to RUNX1 in monocytic leukemia cell line with
RT t(11;21)(q13;q22).";
RL Eur. J. Haematol. 79:25-31(2007).
RN [7]
RP FUNCTION, INTERACTION WITH ANDROGENE RECEPTOR, AND INDUCTION BY ANDROGEN.
RX PubMed=19022849; DOI=10.1677/erc-08-0150;
RA Yang J., Zhao Y.-L., Wu Z.-Q., Si Y.-L., Meng Y.G., Fu X.B., Mu Y.-M.,
RA Han W.-D.;
RT "The single-macro domain protein LRP16 is an essential cofactor of androgen
RT receptor.";
RL Endocr. Relat. Cancer 16:139-153(2009).
RN [8]
RP INDUCTION, AND FUNCTION.
RX PubMed=19403568; DOI=10.1677/joe-09-0054;
RA Tian L., Wu Z., Zhao Y., Meng Y., Si Y., Fu X., Mu Y., Han W.;
RT "Differential induction of LRP16 by liganded and unliganded estrogen
RT receptor alpha in SKOV3 ovarian carcinoma cells.";
RL J. Endocrinol. 202:167-177(2009).
RN [9]
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 [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-184 AND HIS-188.
RX PubMed=23474714; DOI=10.1038/nsmb.2521;
RA Rosenthal F., Feijs K.L., Frugier E., Bonalli M., Forst A.H., Imhof R.,
RA Winkler H.C., Fischer D., Caflisch A., Hassa P.O., Luescher B.,
RA Hottiger M.O.;
RT "Macrodomain-containing proteins are new mono-ADP-ribosylhydrolases.";
RL Nat. Struct. Mol. Biol. 20:502-507(2013).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ASN-174; ASP-184 AND GLY-270.
RX PubMed=23474712; DOI=10.1038/nsmb.2523;
RA Jankevicius G., Hassler M., Golia B., Rybin V., Zacharias M., Timinszky G.,
RA Ladurner A.G.;
RT "A family of macrodomain proteins reverses cellular mono-ADP-
RT ribosylation.";
RL Nat. Struct. Mol. Biol. 20:508-514(2013).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-138, AND IDENTIFICATION BY MASS
RP 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 [14]
RP CATALYTIC ACTIVITY.
RX PubMed=31599159; DOI=10.1021/acschembio.9b00429;
RA Stevens L.A., Kato J., Kasamatsu A., Oda H., Lee D.Y., Moss J.;
RT "The ARH and Macrodomain Families of alpha-ADP-ribose-acceptor Hydrolases
RT Catalyze alpha-NAD+ Hydrolysis.";
RL ACS Chem. Biol. 14:2576-2584(2019).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 91-325, FUNCTION, CATALYTIC
RP ACTIVITY, MUTAGENESIS OF ASP-160; ASP-167; ASN-171; ASN-174; ASP-184;
RP HIS-188; SER-268 AND GLY-270, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=21257746; DOI=10.1074/jbc.m110.206771;
RA Chen D., Vollmar M., Rossi M.N., Phillips C., Kraehenbuehl R., Slade D.,
RA Mehrotra P.V., von Delft F., Crosthwaite S.K., Gileadi O., Denu J.M.,
RA Ahel I.;
RT "Identification of macrodomain proteins as novel O-acetyl-ADP-ribose
RT deacetylases.";
RL J. Biol. Chem. 286:13261-13271(2011).
CC -!- FUNCTION: Removes ADP-ribose from aspartate and glutamate residues in
CC proteins bearing a single ADP-ribose moiety (PubMed:23474714,
CC PubMed:23474712). Inactive towards proteins bearing poly-ADP-ribose
CC (PubMed:23474714, PubMed:23474712). Deacetylates O-acetyl-ADP ribose, a
CC signaling molecule generated by the deacetylation of acetylated lysine
CC residues in histones and other proteins (PubMed:21257746). Plays a role
CC in estrogen signaling (PubMed:17893710, PubMed:17914104,
CC PubMed:19403568). Binds to androgen receptor (AR) and amplifies the
CC transactivation function of AR in response to androgen
CC (PubMed:19022849). May play an important role in carcinogenesis and/or
CC progression of hormone-dependent cancers by feed-forward mechanism that
CC activates ESR1 transactivation (PubMed:17893710, PubMed:17914104).
CC Could be an ESR1 coactivator, providing a positive feedback regulatory
CC loop for ESR1 signal transduction (PubMed:17914104). Could be involved
CC in invasive growth by down-regulating CDH1 in endometrial cancer cells
CC (PubMed:17893710). Enhances ESR1-mediated transcription activity
CC (PubMed:17914104). {ECO:0000269|PubMed:17893710,
CC ECO:0000269|PubMed:17914104, ECO:0000269|PubMed:19022849,
CC ECO:0000269|PubMed:19403568, ECO:0000269|PubMed:21257746,
CC ECO:0000269|PubMed:23474712, ECO:0000269|PubMed:23474714}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3''-O-acetyl-ADP-D-ribose + H2O = acetate + ADP-D-ribose +
CC H(+); Xref=Rhea:RHEA:59244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:57967, ChEBI:CHEBI:142723;
CC EC=3.1.1.106; Evidence={ECO:0000305|PubMed:21257746};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59245;
CC Evidence={ECO:0000305|PubMed:21257746};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2''-O-acetyl-ADP-D-ribose + H2O = acetate + ADP-D-ribose +
CC H(+); Xref=Rhea:RHEA:57060, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:57967, ChEBI:CHEBI:83767;
CC EC=3.1.1.106; Evidence={ECO:0000305|PubMed:21257746};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57061;
CC Evidence={ECO:0000305|PubMed:21257746};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + H2O = ADP-D-ribose
CC + H(+) + L-aspartyl-[protein]; Xref=Rhea:RHEA:54428, Rhea:RHEA-
CC COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29961, ChEBI:CHEBI:57967,
CC ChEBI:CHEBI:138102; Evidence={ECO:0000269|PubMed:23474714};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54429;
CC Evidence={ECO:0000269|PubMed:23474714};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + H2O = ADP-D-ribose
CC + H(+) + L-glutamyl-[protein]; Xref=Rhea:RHEA:58248, Rhea:RHEA-
CC COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:57967,
CC ChEBI:CHEBI:142540; Evidence={ECO:0000269|PubMed:23474712,
CC ECO:0000269|PubMed:23474714};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58249;
CC Evidence={ECO:0000269|PubMed:23474712, ECO:0000269|PubMed:23474714};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-NAD(+) + H2O = ADP-D-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:68792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57967, ChEBI:CHEBI:77017;
CC Evidence={ECO:0000269|PubMed:31599159};
CC -!- ACTIVITY REGULATION: Subject to competitive inhibition by the product
CC ADP-ribose. {ECO:0000269|PubMed:21257746}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=373 uM for O-acetyl-ADP-ribose {ECO:0000269|PubMed:21257746};
CC -!- SUBUNIT: Interacts with ESR1; Interacts in a manner that is estrogen
CC independent but is enhanced by estrogen. Interacts (via macro domain)
CC with AR. {ECO:0000269|PubMed:17914104, ECO:0000269|PubMed:19022849}.
CC -!- INTERACTION:
CC Q9BQ69; P03372: ESR1; NbExp=6; IntAct=EBI-5324932, EBI-78473;
CC Q9BQ69; P52294: KPNA1; NbExp=3; IntAct=EBI-5324932, EBI-358383;
CC Q9BQ69; P05783: KRT18; NbExp=7; IntAct=EBI-5324932, EBI-297888;
CC Q9BQ69; Q04206: RELA; NbExp=7; IntAct=EBI-5324932, EBI-73886;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23474712}.
CC Note=Recruited to DNA lesions, probably via mono-APD-ribosylated
CC proteins. {ECO:0000269|PubMed:23474712}.
CC -!- INDUCTION: Overexpressed by estrogens in breast cancer MCF-7 cells,
CC probably via an activation of nuclear receptors for steroids (ESR1 but
CC not ESR2). Significantly increased by estrogens in ESR1-positive
CC Ishikawa endometrial cancer cells. Up-regulated in 17-beta-estradiol-
CC responsive BG-1 ovarian cancer cells but down-regulated in estrogen-
CC resistant SKOV3 ovarian cancer cells. Induced by androgen.
CC {ECO:0000269|PubMed:12790785, ECO:0000269|PubMed:17893710,
CC ECO:0000269|PubMed:19022849, ECO:0000269|PubMed:19403568}.
CC -!- DISEASE: Note=A chromosomal aberration involving MACROD1 is found in
CC acute leukemia. Translocation t(11;21)(q13;q22) that forms a RUNX1-
CC MACROD1 fusion protein. {ECO:0000269|PubMed:17532767}.
CC -!- MISCELLANEOUS: Overexpression may promote MCF-7 cells proliferation.
CC There is an approximate one-third increase of the invasive capacity of
CC MACROD1-overexpressing cells. The expression of CDH1 is repressed by
CC MACROD1. Further analysis demonstrates that MACROD1 inhibits CDH1
CC transactivation in a dose-dependent manner. Inhibition is abolished by
CC estrogen deprivation, indicating that the down-regulation of CDH1
CC transcription by MACROD1 requires ESR1 mediation. Binding of ESR1 to
CC the CDH1 promoter is antagonized by MACROD1, suggesting that MACROD1
CC could interfere with ESR1-mediated transcription. Knockdown of MACROD1
CC leads to impaired AR function and greatly attenuates the coactivation
CC of AR by other AR coactivators such as UXT and NCOA1. This interference
CC also markedly inhibits the androgen-stimulated proliferation of
CC androgen-sensitive LNCaP prostate cancer cells. MACROD1 knockdown does
CC not significantly affect the growth rate of AR-negative PC-3 prostate
CC cancer cells. {ECO:0000269|PubMed:12790785}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH03188.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH03188.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MACROD1ID50947ch11q13.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF202922; AAF15294.2; -; mRNA.
DR EMBL; BC000270; AAH00270.2; -; mRNA.
DR EMBL; BC003188; AAH03188.1; ALT_INIT; mRNA.
DR EMBL; BC007297; AAH07297.1; -; mRNA.
DR EMBL; BC008316; AAH08316.1; -; mRNA.
DR CCDS; CCDS8056.1; -.
DR RefSeq; NP_054786.2; NM_014067.3.
DR PDB; 2X47; X-ray; 1.70 A; A=91-325.
DR PDB; 6LH4; X-ray; 2.00 A; A/B/C/D=91-325.
DR PDBsum; 2X47; -.
DR PDBsum; 6LH4; -.
DR AlphaFoldDB; Q9BQ69; -.
DR SMR; Q9BQ69; -.
DR BioGRID; 118813; 51.
DR IntAct; Q9BQ69; 23.
DR STRING; 9606.ENSP00000255681; -.
DR BindingDB; Q9BQ69; -.
DR ChEMBL; CHEMBL4295934; -.
DR GlyGen; Q9BQ69; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BQ69; -.
DR PhosphoSitePlus; Q9BQ69; -.
DR BioMuta; MACROD1; -.
DR DMDM; 32129719; -.
DR EPD; Q9BQ69; -.
DR jPOST; Q9BQ69; -.
DR MassIVE; Q9BQ69; -.
DR MaxQB; Q9BQ69; -.
DR PaxDb; Q9BQ69; -.
DR PeptideAtlas; Q9BQ69; -.
DR PRIDE; Q9BQ69; -.
DR ProteomicsDB; 78637; -.
DR Antibodypedia; 51757; 58 antibodies from 12 providers.
DR DNASU; 28992; -.
DR Ensembl; ENST00000255681.7; ENSP00000255681.6; ENSG00000133315.12.
DR GeneID; 28992; -.
DR KEGG; hsa:28992; -.
DR MANE-Select; ENST00000255681.7; ENSP00000255681.6; NM_014067.4; NP_054786.2.
DR UCSC; uc001nyh.4; human.
DR CTD; 28992; -.
DR DisGeNET; 28992; -.
DR GeneCards; MACROD1; -.
DR HGNC; HGNC:29598; MACROD1.
DR HPA; ENSG00000133315; Tissue enhanced (skeletal).
DR MIM; 610400; gene.
DR neXtProt; NX_Q9BQ69; -.
DR OpenTargets; ENSG00000133315; -.
DR PharmGKB; PA162394816; -.
DR VEuPathDB; HostDB:ENSG00000133315; -.
DR eggNOG; KOG2633; Eukaryota.
DR GeneTree; ENSGT00940000161450; -.
DR HOGENOM; CLU_046550_4_1_1; -.
DR InParanoid; Q9BQ69; -.
DR OMA; DSAERDW; -.
DR OrthoDB; 937161at2759; -.
DR PhylomeDB; Q9BQ69; -.
DR TreeFam; TF341440; -.
DR BRENDA; 3.1.1.106; 2681.
DR PathwayCommons; Q9BQ69; -.
DR SignaLink; Q9BQ69; -.
DR BioGRID-ORCS; 28992; 17 hits in 1083 CRISPR screens.
DR ChiTaRS; MACROD1; human.
DR EvolutionaryTrace; Q9BQ69; -.
DR GenomeRNAi; 28992; -.
DR Pharos; Q9BQ69; Tchem.
DR PRO; PR:Q9BQ69; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9BQ69; protein.
DR Bgee; ENSG00000133315; Expressed in hindlimb stylopod muscle and 166 other tissues.
DR ExpressionAtlas; Q9BQ69; baseline and differential.
DR Genevisible; Q9BQ69; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0140293; F:ADP-ribosylglutamate hydrolase activity; IDA:UniProtKB.
DR GO; GO:0019213; F:deacetylase activity; IDA:UniProtKB.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0140291; P:peptidyl-glutamate ADP-deribosylation; IDA:UniProtKB.
DR GO; GO:0051725; P:protein de-ADP-ribosylation; IDA:UniProtKB.
DR GO; GO:0042278; P:purine nucleoside metabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.220.10; -; 1.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR Pfam; PF01661; Macro; 1.
DR SMART; SM00506; A1pp; 1.
DR SUPFAM; SSF52949; SSF52949; 1.
DR PROSITE; PS51154; MACRO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromosomal rearrangement; DNA damage;
KW Hydrolase; Isopeptide bond; Nucleus; Reference proteome; Ubl conjugation.
FT CHAIN 1..325
FT /note="ADP-ribose glycohydrolase MACROD1"
FT /id="PRO_0000084485"
FT DOMAIN 141..322
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT BINDING 159..161
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A1Z1Q3"
FT BINDING 172..174
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A1Z1Q3"
FT BINDING 179..184
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A1Z1Q3"
FT BINDING 267..273
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A1Z1Q3"
FT BINDING 306
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A1Z1Q3"
FT SITE 100
FT /note="Breakpoint for translocation to form RUNX1-MACROD1"
FT /evidence="ECO:0000269|PubMed:17532767"
FT MOD_RES 96
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q922B1"
FT MOD_RES 103
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q922B1"
FT MOD_RES 129
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q922B1"
FT MOD_RES 163
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q922B1"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT MUTAGEN 160
FT /note="D->A: Reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:21257746"
FT MUTAGEN 167
FT /note="D->A: Reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:21257746"
FT MUTAGEN 171
FT /note="N->A: Reduced enzyme activity. No significant effect
FT on affinity for substrate."
FT /evidence="ECO:0000269|PubMed:21257746"
FT MUTAGEN 174
FT /note="N->A: Slightly reduced ADP-ribosyl hydrolase
FT activity; when associated with A-184. Reduces O-acetyl-ADP-
FT ribose deacetylase activity by 93%; when associated with A-
FT 184. No significant effect on affinity for substrate."
FT /evidence="ECO:0000269|PubMed:21257746,
FT ECO:0000269|PubMed:23474712"
FT MUTAGEN 184
FT /note="D->A: Slightly reduced ADP-ribosyl hydrolase
FT activity; when associated with A-174. Reduces O-acetyl-ADP-
FT ribose deacetylase activity by 93%; when associated with A-
FT 174. No significant effect on affinity for substrate."
FT /evidence="ECO:0000269|PubMed:21257746,
FT ECO:0000269|PubMed:23474712, ECO:0000269|PubMed:23474714"
FT MUTAGEN 188
FT /note="H->A: Reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:21257746,
FT ECO:0000269|PubMed:23474714"
FT MUTAGEN 268
FT /note="S->A: No significant effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:21257746"
FT MUTAGEN 270
FT /note="G->E: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:21257746,
FT ECO:0000269|PubMed:23474712"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:2X47"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:2X47"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:2X47"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:2X47"
FT HELIX 128..132
FT /evidence="ECO:0007829|PDB:2X47"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:2X47"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:2X47"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:2X47"
FT STRAND 164..172
FT /evidence="ECO:0007829|PDB:2X47"
FT HELIX 182..191
FT /evidence="ECO:0007829|PDB:2X47"
FT HELIX 193..200
FT /evidence="ECO:0007829|PDB:2X47"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:2X47"
FT STRAND 218..227
FT /evidence="ECO:0007829|PDB:2X47"
FT HELIX 237..256
FT /evidence="ECO:0007829|PDB:2X47"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:2X47"
FT HELIX 276..294
FT /evidence="ECO:0007829|PDB:2X47"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:2X47"
FT STRAND 299..305
FT /evidence="ECO:0007829|PDB:2X47"
FT HELIX 308..321
FT /evidence="ECO:0007829|PDB:2X47"
SQ SEQUENCE 325 AA; 35505 MW; 82294BFC904FA4D0 CRC64;
MSLQSRLSGR LAQLRAAGQL LVPPRPRPGH LAGATRTRSS TCGPPAFLGV FGRRARTSAG
VGAWGAAAVG RTAGVRTWAP LAMAAKVDLS TSTDWKEAKS FLKGLSDKQR EEHYFCKDFV
RLKKIPTWKE MAKGVAVKVE EPRYKKDKQL NEKISLLRSD ITKLEVDAIV NAANSSLLGG
GGVDGCIHRA AGPLLTDECR TLQSCKTGKA KITGGYRLPA KYVIHTVGPI AYGEPSASQA
AELRSCYLSS LDLLLEHRLR SVAFPCISTG VFGYPCEAAA EIVLATLREW LEQHKDKVDR
LIICVFLEKD EDIYRSRLPH YFPVA
