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O-acetyl-ADP-ribose deacetylase MACROD1 (EC 3.2.2.-) (EC 3.5.1.-) (MACRO domain-containing protein 1) (Protein LRP16) ([Protein ADP-ribosylglutamate] hydrolase)

 MACD1_HUMAN             Reviewed;         325 AA.
Q9BQ69; Q9UH96;
16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
16-JUN-2003, sequence version 2.
13-FEB-2019, entry version 139.
RecName: Full=ADP-ribose glycohydrolase MACROD1 {ECO:0000305};
AltName: Full=MACRO domain-containing protein 1 {ECO:0000303|PubMed:23474712};
AltName: Full=O-acetyl-ADP-ribose deacetylase MACROD1;
EC=3.5.1.- {ECO:0000305|PubMed:21257746};
AltName: Full=Protein LRP16;
AltName: Full=[Protein ADP-ribosylaspartate] hydrolase MACROD1 {ECO:0000305};
EC=3.2.2.- {ECO:0000269|PubMed:23474714};
AltName: Full=[Protein ADP-ribosylglutamate] hydrolase MACROD1 {ECO:0000305};
EC=3.2.2.- {ECO:0000269|PubMed:23474712, ECO:0000269|PubMed:23474714};
Name=MACROD1 {ECO:0000303|PubMed:23474712,
ECO:0000312|HGNC:HGNC:29598}; Synonyms=LRP16;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lymphocyte;
PubMed=12578638;
Han W.-D., Yu L., Lou F.D., Wang Q.S., Zhao Y., Shi Z.J., Jin H.J.;
"The application of RACE technique to clone the full-length cDNA of a
novel leukemia associated gene LRP16.";
Zhongguo Shi Yan Xue Ye Xue Za Zhi 9:18-21(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
INDUCTION.
PubMed=12790785; DOI=10.1677/erc.0.0100217;
Han W.-D., Mu Y.-M., Lu X.-C., Xu Z.-M., Li X.-J., Yu L., Song H.-J.,
Li M., Lu J.-M., Zhao Y.-L., Pan C.-Y.;
"Up-regulation of LRP16 mRNA by 17beta-estradiol through activation of
estrogen receptor alpha (ERalpha), but not ERbeta, and promotion of
human breast cancer MCF-7 cell proliferation: a preliminary report.";
Endocr. Relat. Cancer 10:217-224(2003).
[4]
INDUCTION, AND FUNCTION.
PubMed=17893710; DOI=10.1038/cr.2007.79;
Meng Y.G., Han W.-D., Zhao Y.-L., Huang K., Si Y.-L., Wu Z.-Q.,
Mu Y.-M.;
"Induction of the LRP16 gene by estrogen promotes the invasive growth
of Ishikawa human endometrial cancer cells through the downregulation
of E-cadherin.";
Cell Res. 17:869-880(2007).
[5]
INTERACTION WITH ESR1, AND FUNCTION.
PubMed=17914104; DOI=10.1677/ERC-06-0082;
Han W.-D., Zhao Y.-L., Meng Y.G., Zang L., Wu Z.-Q., Li Q., Si Y.-L.,
Huang K., Ba J.-M., Morinaga H., Nomura M., Mu Y.-M.;
"Estrogenically regulated LRP16 interacts with estrogen receptor alpha
and enhances the receptor's transcriptional activity.";
Endocr. Relat. Cancer 14:741-753(2007).
[6]
CHROMOSOMAL TRANSLOCATION WITH RUNX1.
PubMed=17532767; DOI=10.1111/j.1600-0609.2007.00858.x;
Imagama S., Abe A., Suzuki M., Hayakawa F., Katsumi A., Emi N.,
Kiyoi H., Naoe T.;
"LRP16 is fused to RUNX1 in monocytic leukemia cell line with
t(11;21)(q13;q22).";
Eur. J. Haematol. 79:25-31(2007).
[7]
FUNCTION, INTERACTION WITH ANDROGENE RECEPTOR, AND INDUCTION BY
ANDROGEN.
PubMed=19022849; DOI=10.1677/ERC-08-0150;
Yang J., Zhao Y.-L., Wu Z.-Q., Si Y.-L., Meng Y.G., Fu X.B., Mu Y.-M.,
Han W.-D.;
"The single-macro domain protein LRP16 is an essential cofactor of
androgen receptor.";
Endocr. Relat. Cancer 16:139-153(2009).
[8]
INDUCTION, AND FUNCTION.
PubMed=19403568; DOI=10.1677/JOE-09-0054;
Tian L., Wu Z., Zhao Y., Meng Y., Si Y., Fu X., Mu Y., Han W.;
"Differential induction of LRP16 by liganded and unliganded estrogen
receptor alpha in SKOV3 ovarian carcinoma cells.";
J. Endocrinol. 202:167-177(2009).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-184 AND HIS-188.
PubMed=23474714; DOI=10.1038/nsmb.2521;
Rosenthal F., Feijs K.L., Frugier E., Bonalli M., Forst A.H.,
Imhof R., Winkler H.C., Fischer D., Caflisch A., Hassa P.O.,
Luescher B., Hottiger M.O.;
"Macrodomain-containing proteins are new mono-ADP-ribosylhydrolases.";
Nat. Struct. Mol. Biol. 20:502-507(2013).
[11]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
ASN-174; ASP-184 AND GLY-270.
PubMed=23474712; DOI=10.1038/nsmb.2523;
Jankevicius G., Hassler M., Golia B., Rybin V., Zacharias M.,
Timinszky G., Ladurner A.G.;
"A family of macrodomain proteins reverses cellular mono-ADP-
ribosylation.";
Nat. Struct. Mol. Biol. 20:508-514(2013).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[13]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-138, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[14]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 91-325, FUNCTION, CATALYTIC
ACTIVITY, MUTAGENESIS OF ASP-160; ASP-167; ASN-171; ASN-174; ASP-184;
HIS-188; SER-268 AND GLY-270, BIOPHYSICOCHEMICAL PROPERTIES, AND
ACTIVITY REGULATION.
PubMed=21257746; DOI=10.1074/jbc.M110.206771;
Chen D., Vollmar M., Rossi M.N., Phillips C., Kraehenbuehl R.,
Slade D., Mehrotra P.V., von Delft F., Crosthwaite S.K., Gileadi O.,
Denu J.M., Ahel I.;
"Identification of macrodomain proteins as novel O-acetyl-ADP-ribose
deacetylases.";
J. Biol. Chem. 286:13261-13271(2011).
-!- FUNCTION: Removes ADP-ribose from asparatate and glutamate
residues in proteins bearing a single ADP-ribose moiety
(PubMed:23474714, PubMed:23474712). Inactive towards proteins
bearing poly-ADP-ribose (PubMed:23474714, PubMed:23474712).
Deacetylates O-acetyl-ADP ribose, a signaling molecule generated
by the deacetylation of acetylated lysine residues in histones and
other proteins (PubMed:21257746). Plays a role in estrogen
signaling (PubMed:17893710, PubMed:17914104, PubMed:19403568).
Binds to androgen receptor (AR) and amplifies the transactivation
function of AR in response to androgen (PubMed:19022849). May play
an important role in carcinogenesis and/or progression of hormone-
dependent cancers by feed-forward mechanism that activates ESR1
transactivation (PubMed:17893710, PubMed:17914104). Could be an
ESR1 coactivator, providing a positive feedback regulatory loop
for ESR1 signal transduction (PubMed:17914104). Could be involved
in invasive growth by down-regulating CDH1 in endometrial cancer
cells (PubMed:17893710). Enhances ESR1-mediated transcription
activity (PubMed:17914104). {ECO:0000269|PubMed:17893710,
ECO:0000269|PubMed:17914104, ECO:0000269|PubMed:19022849,
ECO:0000269|PubMed:19403568, ECO:0000269|PubMed:21257746,
ECO:0000269|PubMed:23474712, ECO:0000269|PubMed:23474714}.
-!- CATALYTIC ACTIVITY:
Reaction=2''-O-acetyl-ADP-D-ribose + H2O = acetate + ADP-D-ribose
+ H(+); Xref=Rhea:RHEA:57060, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57967,
ChEBI:CHEBI:83767; Evidence={ECO:0000305|PubMed:21257746};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57061;
Evidence={ECO:0000305|PubMed:21257746};
-!- CATALYTIC ACTIVITY:
Reaction=4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + H2O = ADP-D-
ribose + H(+) + L-aspartyl-[protein]; Xref=Rhea:RHEA:54428,
Rhea:RHEA-COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:29961, ChEBI:CHEBI:57967,
ChEBI:CHEBI:138102; Evidence={ECO:0000269|PubMed:23474714};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54429;
Evidence={ECO:0000269|PubMed:23474714};
-!- CATALYTIC ACTIVITY:
Reaction=5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + H2O = ADP-D-
ribose + H(+) + L-glutamyl-[protein]; Xref=Rhea:RHEA:58248,
Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:57967,
ChEBI:CHEBI:142540; Evidence={ECO:0000269|PubMed:23474712,
ECO:0000269|PubMed:23474714};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58249;
Evidence={ECO:0000269|PubMed:23474712,
ECO:0000269|PubMed:23474714};
-!- ACTIVITY REGULATION: Subject to competitive inhibition by the
product ADP-ribose. {ECO:0000269|PubMed:21257746}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=373 uM for O-acetyl-ADP-ribose {ECO:0000269|PubMed:21257746};
-!- SUBUNIT: Interacts with ESR1; Interacts in a manner that is
estrogen independent but is enhanced by estrogen. Interacts (via
macro domain) with AR. {ECO:0000269|PubMed:17914104,
ECO:0000269|PubMed:19022849}.
-!- INTERACTION:
P03372:ESR1; NbExp=6; IntAct=EBI-5324932, EBI-78473;
P05783:KRT18; NbExp=7; IntAct=EBI-5324932, EBI-297888;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23474712}.
Note=Recruited to DNA lesions, probably via mono-APD-ribosylated
proteins. {ECO:0000269|PubMed:23474712}.
-!- INDUCTION: Overexpressed by estrogens in breast cancer MCF-7
cells, probably via an activation of nuclear receptors for
steroids (ESR1 but not ESR2). Significantly increased by estrogens
in ESR1-positive Ishikawa endometrial cancer cells. Up-regulated
in 17-beta-estradiol-responsive BG-1 ovarian cancer cells but
down-regulated in estrogen-resistant SKOV3 ovarian cancer cells.
Induced by androgen. {ECO:0000269|PubMed:12790785,
ECO:0000269|PubMed:17893710, ECO:0000269|PubMed:19022849,
ECO:0000269|PubMed:19403568}.
-!- DISEASE: Note=A chromosomal aberration involving MACROD1 is found
in acute leukemia. Translocation t(11;21)(q13;q22) that forms a
RUNX1-MACROD1 fusion protein. {ECO:0000269|PubMed:17532767}.
-!- MISCELLANEOUS: Overexpression may promote MCF-7 cells
proliferation. There is an approximate one-third increase of the
invasive capacity of MACROD1-overexpressing cells. The expression
of CDH1 is repressed by MACROD1. Further analyzes demonstrats that
MACROD1 inhibits CDH1 transactivation in a dose dependent manner.
Inhibition is abolished by estrogen deprivation, indicating that
the down-regulation of CDH1 transcription by MACROD1 requires ESR1
mediation. Binding of ESR1 to the CDH1 promoter is antagonized by
MACROD1, suggesting that MACROD1 could interfere with ESR1-
mediated transcription. Knockdown of MACROD1 leads to impaired AR
function and greatly attenuates the coactivation of AR by other AR
coactivators such as UXT and NCOA1. This interference also
markedly inhibits the androgen-stimulated proliferation of
androgen-sensitive LNCaP prostate cancer cells. MACROD1 knockdown
does not significantly affect the growth rate of AR-negative PC-3
prostate cancer cells. {ECO:0000269|PubMed:12790785}.
-!- SEQUENCE CAUTION:
Sequence=AAH03188.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH03188.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MACROD1ID50947ch11q13.html";
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EMBL; AF202922; AAF15294.2; -; mRNA.
EMBL; BC000270; AAH00270.2; -; mRNA.
EMBL; BC003188; AAH03188.1; ALT_INIT; mRNA.
EMBL; BC007297; AAH07297.1; -; mRNA.
EMBL; BC008316; AAH08316.1; -; mRNA.
CCDS; CCDS8056.1; -.
RefSeq; NP_054786.2; NM_014067.3.
UniGene; Hs.602898; -.
PDB; 2X47; X-ray; 1.70 A; A=91-325.
PDBsum; 2X47; -.
ProteinModelPortal; Q9BQ69; -.
SMR; Q9BQ69; -.
BioGrid; 118813; 32.
IntAct; Q9BQ69; 5.
STRING; 9606.ENSP00000255681; -.
iPTMnet; Q9BQ69; -.
PhosphoSitePlus; Q9BQ69; -.
BioMuta; MACROD1; -.
DMDM; 32129719; -.
EPD; Q9BQ69; -.
jPOST; Q9BQ69; -.
MaxQB; Q9BQ69; -.
PaxDb; Q9BQ69; -.
PeptideAtlas; Q9BQ69; -.
PRIDE; Q9BQ69; -.
ProteomicsDB; 78637; -.
Ensembl; ENST00000255681; ENSP00000255681; ENSG00000133315.
GeneID; 28992; -.
KEGG; hsa:28992; -.
UCSC; uc001nyh.4; human.
CTD; 28992; -.
DisGeNET; 28992; -.
EuPathDB; HostDB:ENSG00000133315.10; -.
GeneCards; MACROD1; -.
HGNC; HGNC:29598; MACROD1.
HPA; HPA041031; -.
HPA; HPA071075; -.
MIM; 610400; gene.
neXtProt; NX_Q9BQ69; -.
OpenTargets; ENSG00000133315; -.
PharmGKB; PA162394816; -.
eggNOG; KOG2633; Eukaryota.
eggNOG; COG2110; LUCA.
GeneTree; ENSGT00940000161450; -.
HOGENOM; HOG000086960; -.
HOVERGEN; HBG052356; -.
InParanoid; Q9BQ69; -.
OMA; KITCGYR; -.
OrthoDB; 937161at2759; -.
PhylomeDB; Q9BQ69; -.
TreeFam; TF341440; -.
ChiTaRS; MACROD1; human.
EvolutionaryTrace; Q9BQ69; -.
GenomeRNAi; 28992; -.
PRO; PR:Q9BQ69; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000133315; Expressed in 189 organ(s), highest expression level in gastrocnemius.
Genevisible; Q9BQ69; HS.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0140293; F:ADP-ribosylglutamate hydrolase activity; IDA:UniProtKB.
GO; GO:0019213; F:deacetylase activity; IDA:UniProtKB.
GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
GO; GO:0140291; P:peptidyl-glutamate ADP-deribosylation; IDA:UniProtKB.
GO; GO:0051725; P:protein de-ADP-ribosylation; IDA:UniProtKB.
GO; GO:0042278; P:purine nucleoside metabolic process; IDA:UniProtKB.
InterPro; IPR002589; Macro_dom.
InterPro; IPR039658; Macro_domain_protein.
PANTHER; PTHR11106; PTHR11106; 1.
Pfam; PF01661; Macro; 1.
SMART; SM00506; A1pp; 1.
PROSITE; PS51154; MACRO; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Chromosomal rearrangement;
Complete proteome; DNA damage; Hydrolase; Isopeptide bond; Nucleus;
Reference proteome; Ubl conjugation.
CHAIN 1 325 ADP-ribose glycohydrolase MACROD1.
/FTId=PRO_0000084485.
DOMAIN 141 322 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
REGION 159 161 Substrate binding.
{ECO:0000250|UniProtKB:A1Z1Q3}.
REGION 172 174 Substrate binding.
{ECO:0000250|UniProtKB:A1Z1Q3}.
REGION 179 184 Substrate binding.
{ECO:0000250|UniProtKB:A1Z1Q3}.
REGION 267 273 Substrate binding.
{ECO:0000250|UniProtKB:A1Z1Q3}.
BINDING 306 306 Substrate.
{ECO:0000250|UniProtKB:A1Z1Q3}.
SITE 100 100 Breakpoint for translocation to form
RUNX1-MACROD1.
{ECO:0000269|PubMed:17532767}.
MOD_RES 96 96 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q922B1}.
MOD_RES 103 103 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q922B1}.
MOD_RES 129 129 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q922B1}.
MOD_RES 163 163 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q922B1}.
CROSSLNK 138 138 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
MUTAGEN 160 160 D->A: Reduced enzyme activity.
{ECO:0000269|PubMed:21257746}.
MUTAGEN 167 167 D->A: Reduced enzyme activity.
{ECO:0000269|PubMed:21257746}.
MUTAGEN 171 171 N->A: Reduced enzyme activity. No
significant effect on affinity for
substrate. {ECO:0000269|PubMed:21257746}.
MUTAGEN 174 174 N->A: Slightly reduced ADP-ribosyl
hydrolase activity; when associated with
A-184. Reduces O-acetyl-ADP-ribose
deacetylase activity by 93%; when
associated with A-184. No significant
effect on affinity for substrate.
{ECO:0000269|PubMed:21257746,
ECO:0000269|PubMed:23474712}.
MUTAGEN 184 184 D->A: Slightly reduced ADP-ribosyl
hydrolase activity; when associated with
A-174. Reduces O-acetyl-ADP-ribose
deacetylase activity by 93%; when
associated with A-174. No significant
effect on affinity for substrate.
{ECO:0000269|PubMed:21257746,
ECO:0000269|PubMed:23474712,
ECO:0000269|PubMed:23474714}.
MUTAGEN 188 188 H->A: Reduced enzyme activity.
{ECO:0000269|PubMed:21257746,
ECO:0000269|PubMed:23474714}.
MUTAGEN 268 268 S->A: No significant effect on enzyme
activity. {ECO:0000269|PubMed:21257746}.
MUTAGEN 270 270 G->E: Loss of enzyme activity.
{ECO:0000269|PubMed:21257746,
ECO:0000269|PubMed:23474712}.
HELIX 94 103 {ECO:0000244|PDB:2X47}.
HELIX 107 110 {ECO:0000244|PDB:2X47}.
HELIX 111 113 {ECO:0000244|PDB:2X47}.
HELIX 122 124 {ECO:0000244|PDB:2X47}.
HELIX 128 132 {ECO:0000244|PDB:2X47}.
HELIX 148 151 {ECO:0000244|PDB:2X47}.
STRAND 154 159 {ECO:0000244|PDB:2X47}.
HELIX 161 163 {ECO:0000244|PDB:2X47}.
STRAND 164 172 {ECO:0000244|PDB:2X47}.
HELIX 182 191 {ECO:0000244|PDB:2X47}.
HELIX 193 200 {ECO:0000244|PDB:2X47}.
STRAND 210 214 {ECO:0000244|PDB:2X47}.
STRAND 218 227 {ECO:0000244|PDB:2X47}.
HELIX 237 256 {ECO:0000244|PDB:2X47}.
STRAND 261 264 {ECO:0000244|PDB:2X47}.
HELIX 276 294 {ECO:0000244|PDB:2X47}.
HELIX 295 297 {ECO:0000244|PDB:2X47}.
STRAND 299 305 {ECO:0000244|PDB:2X47}.
HELIX 308 321 {ECO:0000244|PDB:2X47}.
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


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CSB-EL013300HU Human MACRO domain containing 1 (MACROD1) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL013300BO Bovine MACRO domain containing 1 (MACROD1) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
CSB-EL013300MO Mouse MACRO domain containing 1 (MACROD1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CF130_HUMAN Human ELISA Kit FOR O-acetyl-ADP-ribose deacetylase C6orf130 96T
EIAAB26277 Amdhd2,Amidohydrolase domain-containing protein 2,GlcNAc 6-P deacetylase,Mouse,Mus musculus,Putative N-acetylglucosamine-6-phosphate deacetylase
EIAAB26278 AMDHD2,Amidohydrolase domain-containing protein 2,Bos taurus,Bovine,GlcNAc 6-P deacetylase,Putative N-acetylglucosamine-6-phosphate deacetylase
EIAAB26279 Amdhd2,Amidohydrolase domain-containing protein 2,GlcNAc 6-P deacetylase,Putative N-acetylglucosamine-6-phosphate deacetylase,Rat,Rattus norvegicus
EIAAB26280 AMDHD2,Amidohydrolase domain-containing protein 2,CGI-14,GlcNAc 6-P deacetylase,Homo sapiens,Human,Putative N-acetylglucosamine-6-phosphate deacetylase
EIAAB14350 C16orf36,FAHD1,Fumarylacetoacetate hydrolase domain-containing protein 1,Homo sapiens,Human,YISKL,YisK-like protein

Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP1493: Carbon assimilation C4 pathway
WP1689: Porphyrin and chlorophyll metabolism
WP1690: Propanoate metabolism
WP1713: Two-component system
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation

Related Genes :
[MACROD1 LRP16] ADP-ribose glycohydrolase MACROD1 (MACRO domain-containing protein 1) (O-acetyl-ADP-ribose deacetylase MACROD1) (EC 3.5.1.-) (Protein LRP16) ([Protein ADP-ribosylaspartate] hydrolase MACROD1) (EC 3.2.2.-) ([Protein ADP-ribosylglutamate] hydrolase MACROD1) (EC 3.2.2.-)
[Macrod1 Lrp16] ADP-ribose glycohydrolase MACROD1 (MACRO domain-containing protein 1) (O-acetyl-ADP-ribose deacetylase MACROD1) (EC 3.5.1.-) (Protein LRP16) ([Protein ADP-ribosylaspartate] hydrolase MACROD1) (EC 3.2.2.-) ([Protein ADP-ribosylglutamate] hydrolase MACROD1) (EC 3.2.2.-)
[Macrod1 Lrp16] ADP-ribose glycohydrolase MACROD1 (MACRO domain-containing protein 1) (O-acetyl-ADP-ribose deacetylase MACROD1) (EC 3.5.1.-) (Protein LRP16) ([Protein ADP-ribosylaspartate] hydrolase MACROD1) (EC 3.2.2.-) ([Protein ADP-ribosylglutamate] hydrolase MACROD1) (EC 3.2.2.-) (Fragment)
[MACROD1 LRP16] ADP-ribose glycohydrolase MACROD1 (MACRO domain-containing protein 1) (O-acetyl-ADP-ribose deacetylase MACROD1) (EC 3.5.1.-) (Protein LRP16) ([Protein ADP-ribosylaspartate] hydrolase MACROD1) (EC 3.2.2.-) ([Protein ADP-ribosylglutamate] hydrolase MACROD1) (EC 3.2.2.-)
[Adprhl2 Arh3] ADP-ribose glycohydrolase ARH3 (ADP-ribosylhydrolase 3) (O-acetyl-ADP-ribose deacetylase ARH3) (EC 3.5.1.-) (Poly(ADP-ribose) glycohydrolase ARH3) (EC 3.2.1.143) ([Protein ADP-ribosylarginine] hydrolase-like protein 2) ([Protein ADP-ribosylserine] hydrolase) (EC 3.2.2.-)
[ADPRHL2 ARH3] ADP-ribose glycohydrolase ARH3 (ADP-ribosylhydrolase 3) (O-acetyl-ADP-ribose deacetylase ARH3) (EC 3.5.1.-) (Poly(ADP-ribose) glycohydrolase ARH3) (EC 3.2.1.143) ([Protein ADP-ribosylarginine] hydrolase-like protein 2) ([Protein ADP-ribosylserine] hydrolase) (EC 3.2.2.-)
[adprhl2 arh3] ADP-ribose glycohydrolase ARH3 (LchARH3) (ADP-ribosylhydrolase 3) (O-acetyl-ADP-ribose deacetylase ARH3) (EC 3.5.1.-) (Poly(ADP-ribose) glycohydrolase ARH3) (EC 3.2.1.143) ([Protein ADP-ribosylarginine] hydrolase-like protein 2) ([Protein ADP-ribosylserine] hydrolase) (EC 3.2.2.-)
[adprhl2 arh3 zgc:92867] ADP-ribose glycohydrolase ARH3 (ADP-ribosylhydrolase 3) (O-acetyl-ADP-ribose deacetylase ARH3) (EC 3.5.1.-) (Poly(ADP-ribose) glycohydrolase ARH3) (EC 3.2.1.143) ([Protein ADP-ribosylarginine] hydrolase-like protein 2) ([Protein ADP-ribosylserine] hydrolase) (EC 3.2.2.-)
[ADPRHL2 ARH3] ADP-ribose glycohydrolase ARH3 (ADP-ribosylhydrolase 3) (O-acetyl-ADP-ribose deacetylase ARH3) (EC 3.5.1.-) (Poly(ADP-ribose) glycohydrolase ARH3) (EC 3.2.1.143) ([Protein ADP-ribosylarginine] hydrolase-like protein 2) ([Protein ADP-ribosylserine] hydrolase) (EC 3.2.2.-)
[RUNX1 AML1 CBFA2] Runt-related transcription factor 1 (Acute myeloid leukemia 1 protein) (Core-binding factor subunit alpha-2) (CBF-alpha-2) (Oncogene AML-1) (Polyomavirus enhancer-binding protein 2 alpha B subunit) (PEA2-alpha B) (PEBP2-alpha B) (SL3-3 enhancer factor 1 alpha B subunit) (SL3/AKV core-binding factor alpha B subunit)
[ADPRHL2 ARH3 RCJMB04_30e5] ADP-ribose glycohydrolase ARH3 (ADP-ribosylhydrolase 3) (O-acetyl-ADP-ribose deacetylase ARH3) (EC 3.5.1.-) (Poly(ADP-ribose) glycohydrolase ARH3) (EC 3.2.1.143) ([Protein ADP-ribosylarginine] hydrolase-like protein 2) ([Protein ADP-ribosylserine] hydrolase) (EC 3.2.2.-)
[adprhl2 arh3 TGas084j22.1] ADP-ribose glycohydrolase ARH3 (ADP-ribosylhydrolase 3) (O-acetyl-ADP-ribose deacetylase ARH3) (EC 3.5.1.-) (Poly(ADP-ribose) glycohydrolase ARH3) (EC 3.2.1.143) ([Protein ADP-ribosylarginine] hydrolase-like protein 2) ([Protein ADP-ribosylserine] hydrolase) (EC 3.2.2.-)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[CDH1 CDHE UVO] Cadherin-1 (CAM 120/80) (Epithelial cadherin) (E-cadherin) (Uvomorulin) (CD antigen CD324) [Cleaved into: E-Cad/CTF1; E-Cad/CTF2; E-Cad/CTF3]
[hchA A8C65_13880 A9R57_25255 AKG99_20940 AMK83_16550 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BMT53_00170 BUE81_10670 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 CDL37_00765 CG691_19145 CG705_13560 CG706_14580 CIJ94_05515 COD46_23180 CRD98_26150 D3I61_11545 DL800_09215 DNQ41_14245 DQE83_22775 DTL43_21780 DTL84_23375 DTM25_06080 EC95NR1_00961 ERS085379_01273 ERS085386_05041 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC13462_05714 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PU06_24500 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 SAMEA3753106_00003 SAMEA3753391_00513 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO) (SARS coronavirus main proteinase); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[PARP3 ADPRT3 ADPRTL3] Protein mono-ADP-ribosyltransferase PARP3 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 3) (ARTD3) (DNA ADP-ribosyltransferase PARP3) (EC 2.4.2.-) (IRT1) (NAD(+) ADP-ribosyltransferase 3) (ADPRT-3) (Poly [ADP-ribose] polymerase 3) (PARP-3) (hPARP-3) (Poly[ADP-ribose] synthase 3) (pADPRT-3)
[] ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase (EC 3.2.2.6) (2'-phospho-ADP-ribosyl cyclase) (2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase) (EC 2.4.99.20) (2'-phospho-cyclic-ADP-ribose transferase) (ADP-ribosyl cyclase) (ADPRC) (ADRC) (NAD glycohydrolase) (NAD(+) nucleosidase) (NADase)
[Parp3 Adprt3] Protein mono-ADP-ribosyltransferase PARP3 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 3) (ARTD3) (DNA ADP-ribosyltransferase PARP3) (EC 2.4.2.-) (NAD(+) ADP-ribosyltransferase 3) (ADPRT-3) (Poly [ADP-ribose] polymerase 3) (PARP-3) (Poly[ADP-ribose] synthase 3) (pADPRT-3)
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (p9); Non-structural protein 2 (nsp2) (p87); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.-) (PL1-PRO/PL2-PRO) (PLP1/PLP2) (Papain-like proteinases 1/2) (p195); Non-structural protein 4 (nsp4) (Peptide HD2); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p34); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7) (p5); Non-structural protein 8 (nsp8) (p23); Non-structural protein 9 (nsp9) (p12); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p14); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (nsp12) (p100); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (nsp13) (p66) (p66-HEL); Exoribonuclease (ExoN) (EC 3.1.13.-) (nsp14); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (nsp15) (p41); Putative 2'-O-methyl transferase (EC 2.1.1.-) (nsp16)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Non-structural protein 2A-alpha (NS2A-alpha); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Non-structural protein 1 (nsp1); Non-structural protein 2 (nsp2); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.-) (PL1-PRO/PL2-PRO) (PLP1/PLP2) (Papain-like proteinases 1/2) (p195); Non-structural protein 4 (nsp4) (Peptide HD2); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10); Non-structural protein 11 (nsp11); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (nsp12); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (nsp13); Exoribonuclease (ExoN) (EC 3.1.13.-) (nsp14); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (nsp15); Putative 2'-O-methyl transferase (EC 2.1.1.-) (nsp16)]
[NUDT2 NUDX2 At5g47650 MNJ7.24] Nudix hydrolase 2 (AtNUDT2) (EC 3.6.1.-) (ADP-ribose pyrophosphatase) (EC 3.6.1.13) (NADH pyrophosphatase) (EC 3.6.1.22)
[HST2 YPL015C LPA2C] NAD-dependent protein deacetylase HST2 (EC 3.5.1.-) (Homologous to SIR2 protein 2) (Regulatory protein SIR2 homolog 2)
[PARP9 BAL BAL1] Protein mono-ADP-ribosyltransferase PARP9 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 9) (ARTD9) (B aggressive lymphoma protein) (Poly [ADP-ribose] polymerase 9) (PARP-9)
[hchA ECH74115_2746] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[PARP4 ADPRTL1 KIAA0177 PARPL] Protein mono-ADP-ribosyltransferase PARP4 (EC 2.4.2.-) (193 kDa vault protein) (ADP-ribosyltransferase diphtheria toxin-like 4) (ARTD4) (PARP-related/IalphaI-related H5/proline-rich) (PH5P) (Poly [ADP-ribose] polymerase 4) (PARP-4) (Vault poly(ADP-ribose) polymerase) (VPARP)

Bibliography :
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