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CAD protein [Includes: Glutamine-dependent carbamoyl-phosphate synthase (EC 6.3.5.5); Aspartate carbamoyltransferase (EC 2.1.3.2); Dihydroorotase (EC 3.5.2.3)]

 PYR1_HUMAN              Reviewed;        2225 AA.
P27708; D6W552; Q6P0Q0; Q96CK3;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
19-JUL-2004, sequence version 3.
22-NOV-2017, entry version 206.
RecName: Full=CAD protein;
Includes:
RecName: Full=Glutamine-dependent carbamoyl-phosphate synthase;
EC=6.3.5.5 {ECO:0000269|PubMed:24332717};
Includes:
RecName: Full=Aspartate carbamoyltransferase;
EC=2.1.3.2 {ECO:0000269|PubMed:24332717};
Includes:
RecName: Full=Dihydroorotase;
EC=3.5.2.3 {ECO:0000269|PubMed:24332717};
Name=CAD {ECO:0000312|HGNC:HGNC:1424};
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=Fetal lung fibroblast;
PubMed=8619816; DOI=10.1006/bbrc.1996.0213;
Iwahana H., Fujimura M., Ii S., Kondo M., Moritani M., Takahashi Y.,
Yamaoka T., Yoshimoto K., Itakura M.;
"Molecular cloning of a human cDNA encoding a trifunctional enzyme of
carbamoyl-phosphate synthetase-aspartate transcarbamoylase-
dihydroorotase in de Novo pyrimidine synthesis.";
Biochem. Biophys. Res. Commun. 219:249-255(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=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).
[4]
PROTEIN SEQUENCE OF 2-13; 157-165; 169-177; 359-371; 501-516; 548-555;
599-606; 697-719; 761-778; 843-854; 932-944; 1034-1048; 1067-1075;
1110-1127; 1229-1240; 1263-1270; 1313-1323; 1326-1333; 1658-1667;
1723-1731; 1840-1848; 1976-1986; 2025-2036; 2103-2110; 2179-2187 AND
2215-2225, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Colon adenocarcinoma, and Hepatoma;
Bienvenut W.V., Dhillon A.S., Matallanas D., Murray L., Brunton V.G.,
Cooper W.N., Boldt K., von Kriegsheim A.F., Kolch W., Frame M.C.;
Submitted (FEB-2008) to UniProtKB.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1752-2225.
PubMed=1979741; DOI=10.1089/dna.1990.9.667;
Davidson J.N., Rao G.N., Niswander L., Andreano C., Tamer C.,
Chen K.C.;
"Organization and nucleotide sequence of the 3' end of the human CAD
gene.";
DNA Cell Biol. 9:667-676(1990).
[6]
MUTAGENESIS OF HIS-1471; HIS-1473; ASP-1512; HIS-1590; HIS-1642 AND
HIS-1690, COFACTOR, AND ZINC-BINDING SITES.
PubMed=7766613; DOI=10.1021/bi00021a015;
Zimmermann B.H., Kemling N.M., Evans D.R.;
"Function of conserved histidine residues in mammalian
dihydroorotase.";
Biochemistry 34:7038-7046(1995).
[7]
ENZYME REGULATION.
PubMed=11872754; DOI=10.1074/jbc.M201112200;
Sigoillot F.D., Evans D.R., Guy H.I.;
"Growth-dependent regulation of mammalian pyrimidine biosynthesis by
the protein kinase A and MAPK signaling cascades.";
J. Biol. Chem. 277:15745-15751(2002).
[8]
SUBCELLULAR LOCATION.
PubMed=15890648; DOI=10.1074/jbc.M504581200;
Sigoillot F.D., Kotsis D.H., Serre V., Sigoillot S.M., Evans D.R.,
Guy H.I.;
"Nuclear localization and mitogen-activated protein kinase
phosphorylation of the multifunctional protein CAD.";
J. Biol. Chem. 280:25611-25620(2005).
[9]
INDUCTION.
PubMed=16155188; DOI=10.1093/nar/gki839;
Chen K.F., Lai Y.Y., Sun H.S., Tsai S.J.;
"Transcriptional repression of human cad gene by hypoxia inducible
factor-1alpha.";
Nucleic Acids Res. 33:5190-5198(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1859, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1859, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[12]
PHOSPHORYLATION AT THR-456; SER-1406; SER-1859 AND SER-1873, AND
MUTAGENESIS OF SER-1873.
PubMed=17485345; DOI=10.2741/2358;
Sigoillot F.D., Kotsis D.H., Masko E.M., Bame M., Evans D.R.,
Evans H.I.;
"Protein kinase C modulates the up-regulation of the pyrimidine
biosynthetic complex, CAD, by MAP kinase.";
Front. Biosci. 12:3892-3898(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1859 AND THR-1884, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1884, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-747 AND LYS-1411, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1859 AND SER-1900, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1406 AND SER-1859, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1038; SER-1406;
SER-1859; SER-1900 AND SER-1938, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[24]
PHOSPHORYLATION AT SER-1859.
PubMed=23429704; DOI=10.1126/science.1228771;
Robitaille A.M., Christen S., Shimobayashi M., Cornu M., Fava L.L.,
Moes S., Prescianotto-Baschong C., Sauer U., Jenoe P., Hall M.N.;
"Quantitative phosphoproteomics reveal mTORC1 activates de novo
pyrimidine synthesis.";
Science 339:1320-1323(2013).
[25]
PHOSPHORYLATION AT SER-1859 AND SER-1900.
PubMed=23429703; DOI=10.1126/science.1228792;
Ben-Sahra I., Howell J.J., Asara J.M., Manning B.D.;
"Stimulation of de novo pyrimidine synthesis by growth signaling
through mTOR and S6K1.";
Science 339:1323-1328(2013).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1859, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[27]
INTERACTION WITH CIPC.
PubMed=26657846; DOI=10.1016/j.bbrc.2015.11.117;
Matsunaga R., Nishino T., Yokoyama A., Nakashima A., Kikkawa U.,
Konishi H.;
"Versatile function of the circadian protein CIPC as a regulator of
Erk activation.";
Biochem. Biophys. Res. Commun. 469:377-383(2016).
[28]
X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 1456-1846 IN COMPLEX WITH
DIHYDROOROTATE; N-CARBAMOYL-L-ASPARTIC ACID AND ZINC, COFACTOR,
CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
MUTAGENESIS OF HIS-1471; THR-1562; PHE-1563; HIS-1590; CYS-1613;
HIS-1614; GLU-1637 AND ASP-1686, AND CARBAMYLATION AT LYS-1556.
PubMed=24332717; DOI=10.1016/j.str.2013.10.016;
Grande-Garcia A., Lallous N., Diaz-Tejada C., Ramon-Maiques S.;
"Structure, functional characterization, and evolution of the
dihydroorotase domain of human CAD.";
Structure 22:185-198(2014).
[29]
VARIANTS [LARGE SCALE ANALYSIS] GLN-177 AND CYS-735.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[30]
INVOLVEMENT IN EIEE50, AND VARIANT EIEE50 GLN-2024.
PubMed=25678555; DOI=10.1093/hmg/ddv057;
Ng B.G., Wolfe L.A., Ichikawa M., Markello T., He M., Tifft C.J.,
Gahl W.A., Freeze H.H.;
"Biallelic mutations in CAD, impair de novo pyrimidine biosynthesis
and decrease glycosylation precursors.";
Hum. Mol. Genet. 24:3050-3057(2015).
[31]
VARIANTS EIEE50 ARG-33 AND 1789-ARG--PHE-2225 DEL.
PubMed=28087732; DOI=10.1093/hmg/ddx018;
Lohmann K., Masuho I., Patil D.N., Baumann H., Hebert E.,
Steinruecke S., Trujillano D., Skamangas N.K., Dobricic V.,
Huening I., Gillessen-Kaesbach G., Westenberger A.,
Savic-Pavicevic D., Muenchau A., Oprea G., Klein C., Rolfs A.,
Martemyanov K.A.;
"Novel GNB1 mutations disrupt assembly and function of G protein
heterotrimers and cause global developmental delay in humans.";
Hum. Mol. Genet. 26:1078-1086(2017).
-!- FUNCTION: This protein is a "fusion" protein encoding four
enzymatic activities of the pyrimidine pathway (GATase, CPSase,
ATCase and DHOase). {ECO:0000269|PubMed:24332717}.
-!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2
ADP + phosphate + L-glutamate + carbamoyl phosphate.
{ECO:0000269|PubMed:24332717}.
-!- CATALYTIC ACTIVITY: Carbamoyl phosphate + L-aspartate = phosphate
+ N-carbamoyl-L-aspartate. {ECO:0000269|PubMed:24332717}.
-!- CATALYTIC ACTIVITY: (S)-dihydroorotate + H(2)O = N-carbamoyl-L-
aspartate. {ECO:0000269|PubMed:24332717}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:24332717,
ECO:0000269|PubMed:7766613};
Note=Binds 3 Zn(2+) ions per subunit (for dihydroorotase
activity). {ECO:0000269|PubMed:24332717,
ECO:0000269|PubMed:7766613};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
Note=Binds 4 magnesium or manganese ions per subunit.
{ECO:0000255|PROSITE-ProRule:PRU00409};
-!- ENZYME REGULATION: Allosterically regulated and controlled by
phosphorylation. 5-phosphoribose 1-diphosphate (PRPP) is an
activator while UMP and UTP are inhibitors of the CPSase reaction.
{ECO:0000269|PubMed:11872754}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=28 uM for dihydroorotate {ECO:0000269|PubMed:24332717};
KM=241 uM for N-carbamoyl-L-aspartate
{ECO:0000269|PubMed:24332717};
-!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
{ECO:0000269|PubMed:24332717}.
-!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
{ECO:0000269|PubMed:24332717}.
-!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
{ECO:0000269|PubMed:24332717}.
-!- SUBUNIT: Homohexamer (PubMed:24332717). Interacts with CIPC
(PubMed:26657846). {ECO:0000269|PubMed:24332717,
ECO:0000269|PubMed:26657846}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-355504, EBI-355504;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15890648}.
Nucleus {ECO:0000269|PubMed:15890648}. Note=Cytosolic and
unphosphorylated in resting cells, translocates to the nucleus in
response to EGF stimulation, nuclear import promotes optimal cell
growth.
-!- INDUCTION: Transcriptionally repressed following hypoxia by HIF1A.
{ECO:0000269|PubMed:16155188}.
-!- PTM: Activated by MAP kinase (Erk1/2) phosphorylation just prior
to the S phase of the cell cycle, when the demand for pyrimidine
nucleotides is greatest, and down-regulated as the cells emerge
from S phase by protein kinase A (PKA) phosphorylation.
Phosphorylation at Ser-1859 by RPS6KB1 downstream of MTOR promotes
oligomerization and stimulates dihydroorotase activity.
Phosphorylation at Ser-1406 reduces sensitivy to feedback
inhibition by UTP. {ECO:0000269|PubMed:17485345,
ECO:0000269|PubMed:23429703, ECO:0000269|PubMed:23429704}.
-!- DISEASE: Epileptic encephalopathy, early infantile, 50 (EIEE50)
[MIM:616457]: A form of epileptic encephalopathy, a heterogeneous
group of severe childhood onset epilepsies characterized by
refractory seizures, neurodevelopmental impairment, and poor
prognosis. Development is normal prior to seizure onset, after
which cognitive and motor delays become apparent. EIEE50 is an
autosomal recessive, progressive disease with onset in infancy and
favorable response to treatment with oral uridine.
{ECO:0000269|PubMed:25678555, ECO:0000269|PubMed:28087732}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- MISCELLANEOUS: GATase (glutamine amidotransferase) and CPSase
(carbamoyl phosphate synthase) form together the glutamine-
dependent CPSase (GD-CPSase) (EC 6.3.5.5). {ECO:0000305}.
-!- SIMILARITY: In the central section; belongs to the metallo-
dependent hydrolases superfamily. DHOase family. CAD subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Aspartate carbamoyltransferase
entry;
URL="https://en.wikipedia.org/wiki/Aspartate_carbamoyltransferase";
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EMBL; D78586; BAA11423.1; -; mRNA.
EMBL; CH471053; EAX00612.1; -; Genomic_DNA.
EMBL; CH471053; EAX00613.1; -; Genomic_DNA.
EMBL; CH471053; EAX00614.1; -; Genomic_DNA.
EMBL; BC014178; AAH14178.2; -; mRNA.
EMBL; BC065510; AAH65510.1; -; mRNA.
EMBL; M38561; AAA51907.1; -; Genomic_DNA.
CCDS; CCDS1742.1; -.
PIR; A36240; A36240.
RefSeq; NP_001293008.1; NM_001306079.1.
RefSeq; NP_004332.2; NM_004341.4.
UniGene; Hs.377010; -.
PDB; 4BY3; X-ray; 1.73 A; A=1456-1846.
PDB; 4C6B; X-ray; 1.66 A; A=1456-1846.
PDB; 4C6C; X-ray; 1.45 A; A=1456-1846.
PDB; 4C6D; X-ray; 1.30 A; A=1456-1846.
PDB; 4C6E; X-ray; 1.26 A; A=1456-1846.
PDB; 4C6F; X-ray; 1.26 A; A=1456-1846.
PDB; 4C6I; X-ray; 1.35 A; A=1456-1846.
PDB; 4C6J; X-ray; 1.30 A; A=1456-1846.
PDB; 4C6K; X-ray; 1.48 A; A=1456-1846.
PDB; 4C6L; X-ray; 1.55 A; A=1456-1846.
PDB; 4C6M; X-ray; 1.62 A; A=1456-1846.
PDB; 4C6N; X-ray; 1.90 A; A=1456-1846.
PDB; 4C6O; X-ray; 1.65 A; A=1456-1846.
PDB; 4C6P; X-ray; 1.52 A; A=1456-1846.
PDB; 4C6Q; X-ray; 1.66 A; A=1456-1846.
PDB; 5G1N; X-ray; 2.10 A; A/B/C/D/E/F=1915-2225.
PDB; 5G1O; X-ray; 2.10 A; A/B/C/D/E/F=1915-2225.
PDB; 5G1P; X-ray; 3.19 A; A/B/C/D/E/F=1915-2225.
PDBsum; 4BY3; -.
PDBsum; 4C6B; -.
PDBsum; 4C6C; -.
PDBsum; 4C6D; -.
PDBsum; 4C6E; -.
PDBsum; 4C6F; -.
PDBsum; 4C6I; -.
PDBsum; 4C6J; -.
PDBsum; 4C6K; -.
PDBsum; 4C6L; -.
PDBsum; 4C6M; -.
PDBsum; 4C6N; -.
PDBsum; 4C6O; -.
PDBsum; 4C6P; -.
PDBsum; 4C6Q; -.
PDBsum; 5G1N; -.
PDBsum; 5G1O; -.
PDBsum; 5G1P; -.
DisProt; DP01024; -.
ProteinModelPortal; P27708; -.
SMR; P27708; -.
BioGrid; 107243; 111.
DIP; DIP-39484N; -.
IntAct; P27708; 50.
MINT; MINT-5000537; -.
STRING; 9606.ENSP00000264705; -.
BindingDB; P27708; -.
ChEMBL; CHEMBL3093; -.
DrugBank; DB00128; L-Aspartic Acid.
DrugBank; DB00130; L-Glutamine.
DrugBank; DB03459; Sparfosic acid.
MEROPS; M38.972; -.
iPTMnet; P27708; -.
PhosphoSitePlus; P27708; -.
SwissPalm; P27708; -.
BioMuta; CAD; -.
DMDM; 50403731; -.
EPD; P27708; -.
MaxQB; P27708; -.
PaxDb; P27708; -.
PeptideAtlas; P27708; -.
PRIDE; P27708; -.
Ensembl; ENST00000264705; ENSP00000264705; ENSG00000084774.
GeneID; 790; -.
KEGG; hsa:790; -.
UCSC; uc002rji.4; human.
CTD; 790; -.
DisGeNET; 790; -.
EuPathDB; HostDB:ENSG00000084774.13; -.
GeneCards; CAD; -.
HGNC; HGNC:1424; CAD.
HPA; CAB007781; -.
HPA; HPA057266; -.
HPA; HPA069341; -.
MalaCards; CAD; -.
MIM; 114010; gene.
MIM; 616457; phenotype.
neXtProt; NX_P27708; -.
OpenTargets; ENSG00000084774; -.
PharmGKB; PA26023; -.
eggNOG; KOG0370; Eukaryota.
eggNOG; COG0458; LUCA.
eggNOG; COG0505; LUCA.
eggNOG; COG0540; LUCA.
GeneTree; ENSGT00900000141043; -.
HOGENOM; HOG000234584; -.
HOVERGEN; HBG000279; -.
InParanoid; P27708; -.
KO; K11540; -.
OrthoDB; EOG091G00DC; -.
PhylomeDB; P27708; -.
TreeFam; TF105604; -.
BioCyc; MetaCyc:ENSG00000084774-MONOMER; -.
BRENDA; 3.5.2.3; 2681.
Reactome; R-HSA-500753; Pyrimidine biosynthesis.
SIGNOR; P27708; -.
UniPathway; UPA00070; UER00115.
UniPathway; UPA00070; UER00116.
UniPathway; UPA00070; UER00117.
ChiTaRS; CAD; human.
GenomeRNAi; 790; -.
PMAP-CutDB; P27708; -.
PRO; PR:P27708; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000084774; -.
CleanEx; HS_CAD; -.
ExpressionAtlas; P27708; baseline and differential.
Genevisible; P27708; HS.
GO; GO:0042995; C:cell projection; ISS:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; ISS:BHF-UCL.
GO; GO:0016363; C:nuclear matrix; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0043195; C:terminal bouton; ISS:BHF-UCL.
GO; GO:0070335; F:aspartate binding; ISS:BHF-UCL.
GO; GO:0004070; F:aspartate carbamoyltransferase activity; ISS:BHF-UCL.
GO; GO:0005524; F:ATP binding; ISS:BHF-UCL.
GO; GO:0004087; F:carbamoyl-phosphate synthase (ammonia) activity; IBA:GO_Central.
GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; ISS:BHF-UCL.
GO; GO:0004151; F:dihydroorotase activity; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004672; F:protein kinase activity; ISS:BHF-UCL.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IDA:UniProtKB.
GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central.
GO; GO:0017144; P:drug metabolic process; ISS:BHF-UCL.
GO; GO:0006541; P:glutamine metabolic process; ISS:BHF-UCL.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISS:BHF-UCL.
GO; GO:0046777; P:protein autophosphorylation; ISS:BHF-UCL.
GO; GO:0046134; P:pyrimidine nucleoside biosynthetic process; TAS:Reactome.
GO; GO:0000050; P:urea cycle; IBA:GO_Central.
CDD; cd01744; GATase1_CPSase; 1.
Gene3D; 1.10.1030.10; -; 1.
Gene3D; 2.30.40.10; -; 2.
Gene3D; 3.40.50.1370; -; 2.
Gene3D; 3.40.50.1380; -; 1.
Gene3D; 3.40.50.880; -; 1.
Gene3D; 3.50.30.20; -; 1.
HAMAP; MF_00001; Asp_carb_tr; 1.
HAMAP; MF_01209; CPSase_S_chain; 1.
InterPro; IPR006680; Amidohydro-rel.
InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
InterPro; IPR002082; Asp_carbamoyltransf.
InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
InterPro; IPR011761; ATP-grasp.
InterPro; IPR006275; CarbamoylP_synth_lsu.
InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
InterPro; IPR006274; CarbamoylP_synth_ssu.
InterPro; IPR002474; CarbamoylP_synth_ssu_N.
InterPro; IPR036480; CarbP_synth_ssu_N_sf.
InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
InterPro; IPR029062; Class_I_gatase-like.
InterPro; IPR035686; CPSase_GATase1.
InterPro; IPR002195; Dihydroorotase_CS.
InterPro; IPR017926; GATASE.
InterPro; IPR011059; Metal-dep_hydrolase_composite.
InterPro; IPR032466; Metal_Hydrolase.
InterPro; IPR011607; MGS-like_dom.
InterPro; IPR036914; MGS-like_dom_sf.
InterPro; IPR016185; PreATP-grasp_dom_sf.
Pfam; PF01979; Amidohydro_1; 1.
Pfam; PF02786; CPSase_L_D2; 2.
Pfam; PF02787; CPSase_L_D3; 1.
Pfam; PF00988; CPSase_sm_chain; 1.
Pfam; PF00117; GATase; 1.
Pfam; PF02142; MGS; 1.
Pfam; PF00185; OTCace; 1.
Pfam; PF02729; OTCace_N; 1.
PRINTS; PR00100; AOTCASE.
PRINTS; PR00101; ATCASE.
PRINTS; PR00098; CPSASE.
SMART; SM01096; CPSase_L_D3; 1.
SMART; SM01097; CPSase_sm_chain; 1.
SMART; SM00851; MGS; 1.
SUPFAM; SSF48108; SSF48108; 1.
SUPFAM; SSF51338; SSF51338; 1.
SUPFAM; SSF51556; SSF51556; 1.
SUPFAM; SSF52021; SSF52021; 1.
SUPFAM; SSF52317; SSF52317; 1.
SUPFAM; SSF52335; SSF52335; 1.
SUPFAM; SSF52440; SSF52440; 2.
SUPFAM; SSF53671; SSF53671; 1.
TIGRFAMs; TIGR00670; asp_carb_tr; 1.
TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
PROSITE; PS50975; ATP_GRASP; 2.
PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PROSITE; PS00866; CPSASE_1; 2.
PROSITE; PS00867; CPSASE_2; 2.
PROSITE; PS00482; DIHYDROOROTASE_1; 1.
PROSITE; PS00483; DIHYDROOROTASE_2; 1.
PROSITE; PS51273; GATASE_TYPE_1; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Allosteric enzyme; ATP-binding;
Complete proteome; Congenital disorder of glycosylation; Cytoplasm;
Direct protein sequencing; Disease mutation; Epilepsy; Hydrolase;
Ligase; Magnesium; Manganese; Metal-binding; Multifunctional enzyme;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Pyrimidine biosynthesis; Reference proteome; Repeat; Transferase;
Zinc.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.4}.
CHAIN 2 2225 CAD protein.
/FTId=PRO_0000199506.
DOMAIN 177 363 Glutamine amidotransferase type-1.
{ECO:0000255|PROSITE-ProRule:PRU00605}.
DOMAIN 519 711 ATP-grasp 1. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
DOMAIN 1052 1243 ATP-grasp 2. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
NP_BIND 545 600 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
NP_BIND 1078 1135 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
REGION 2 365 GATase (Glutamine amidotransferase).
{ECO:0000250|UniProtKB:P08955}.
REGION 366 394 Linker. {ECO:0000250|UniProtKB:P08955}.
REGION 395 1455 CPSase (Carbamoyl-phosphate synthase).
{ECO:0000250|UniProtKB:P08955}.
REGION 395 933 CPSase A. {ECO:0000250|UniProtKB:P08955}.
REGION 934 1455 CPSase B. {ECO:0000250|UniProtKB:P08955}.
REGION 1456 1788 DHOase (dihydroorotase).
{ECO:0000250|UniProtKB:P08955}.
REGION 1789 1917 Linker. {ECO:0000250|UniProtKB:P08955}.
REGION 1918 2225 ATCase (Aspartate transcarbamylase).
{ECO:0000250|UniProtKB:P08955}.
ACT_SITE 252 252 Nucleophile; for GATase activity.
{ECO:0000255|PROSITE-ProRule:PRU00605}.
ACT_SITE 336 336 For GATase activity.
{ECO:0000255|PROSITE-ProRule:PRU00605}.
ACT_SITE 338 338 For GATase activity.
{ECO:0000255|PROSITE-ProRule:PRU00605}.
METAL 668 668 Magnesium or manganese 1.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
METAL 682 682 Magnesium or manganese 1.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
METAL 682 682 Magnesium or manganese 2.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
METAL 684 684 Magnesium or manganese 2.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
METAL 1202 1202 Magnesium or manganese 3.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
METAL 1214 1214 Magnesium or manganese 3.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
METAL 1214 1214 Magnesium or manganese 4.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
METAL 1216 1216 Magnesium or manganese 4.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
METAL 1471 1471 Zinc 1; via tele nitrogen.
{ECO:0000269|PubMed:24332717}.
METAL 1471 1471 Zinc 2; via pros nitrogen.
{ECO:0000269|PubMed:24332717}.
METAL 1473 1473 Zinc 1; via tele nitrogen.
{ECO:0000269|PubMed:24332717}.
METAL 1556 1556 Zinc 1; via carbamate group.
{ECO:0000269|PubMed:24332717}.
METAL 1556 1556 Zinc 3; via carbamate group.
{ECO:0000269|PubMed:24332717}.
METAL 1590 1590 Zinc 3; via pros nitrogen.
{ECO:0000269|PubMed:24332717}.
METAL 1613 1613 Zinc 2. {ECO:0000269|PubMed:24332717}.
METAL 1614 1614 Zinc 3; via tele nitrogen.
{ECO:0000269|PubMed:24332717}.
METAL 1637 1637 Zinc 2. {ECO:0000269|PubMed:24332717}.
METAL 1686 1686 Zinc 1. {ECO:0000269|PubMed:24332717}.
BINDING 1475 1475 N-carbamoyl-L-aspartate.
{ECO:0000269|PubMed:24332717}.
BINDING 1505 1505 N-carbamoyl-L-aspartate.
{ECO:0000269|PubMed:24332717}.
BINDING 1661 1661 N-carbamoyl-L-aspartate; via amide
nitrogen and carbonyl oxygen.
{ECO:0000269|PubMed:24332717}.
BINDING 1686 1686 N-carbamoyl-L-aspartate.
{ECO:0000269|PubMed:24332717}.
BINDING 1690 1690 N-carbamoyl-L-aspartate.
{ECO:0000269|PubMed:24332717}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.4}.
MOD_RES 456 456 Phosphothreonine; by MAPK1.
{ECO:0000269|PubMed:17485345}.
MOD_RES 747 747 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1038 1038 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1406 1406 Phosphoserine; by PKA.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:17485345}.
MOD_RES 1411 1411 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1556 1556 N6-carboxylysine.
{ECO:0000269|PubMed:24332717}.
MOD_RES 1859 1859 Phosphoserine; by RPS6KB1 and PKA.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:17485345,
ECO:0000269|PubMed:23429703,
ECO:0000269|PubMed:23429704}.
MOD_RES 1873 1873 Phosphoserine; by PKC; in vitro.
{ECO:0000269|PubMed:17485345}.
MOD_RES 1884 1884 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976}.
MOD_RES 1900 1900 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:23429703}.
MOD_RES 1938 1938 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 33 33 M -> R (in EIEE50; unknown pathological
significance; dbSNP:rs751610198).
{ECO:0000269|PubMed:28087732}.
/FTId=VAR_078289.
VARIANT 177 177 R -> Q (in a colorectal cancer sample;
somatic mutation; dbSNP:rs374122292).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035897.
VARIANT 735 735 Y -> C (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035898.
VARIANT 1789 2225 Missing (in EIEE50; unknown pathological
significance).
{ECO:0000269|PubMed:28087732}.
/FTId=VAR_078290.
VARIANT 2024 2024 R -> Q (in EIEE50; dbSNP:rs763410987).
{ECO:0000269|PubMed:25678555}.
/FTId=VAR_073955.
MUTAGEN 1471 1471 H->A: No zinc-binding and no catalytic
activity. {ECO:0000269|PubMed:24332717,
ECO:0000269|PubMed:7766613}.
MUTAGEN 1471 1471 H->N: Abolishes dihydroorotase activity.
{ECO:0000269|PubMed:24332717,
ECO:0000269|PubMed:7766613}.
MUTAGEN 1473 1473 H->A: No zinc-binding and no catalytic
activity. {ECO:0000269|PubMed:7766613}.
MUTAGEN 1512 1512 D->N: No change in catalytic activity.
{ECO:0000269|PubMed:7766613}.
MUTAGEN 1562 1562 T->A: Abolishes dihydroorotase activity.
{ECO:0000269|PubMed:24332717}.
MUTAGEN 1563 1563 F->A: Abolishes dihydroorotase activity.
{ECO:0000269|PubMed:24332717}.
MUTAGEN 1590 1590 H->A: Abolishes dihydroorotase activity.
{ECO:0000269|PubMed:24332717,
ECO:0000269|PubMed:7766613}.
MUTAGEN 1590 1590 H->N: No catalytic activity.
{ECO:0000269|PubMed:24332717,
ECO:0000269|PubMed:7766613}.
MUTAGEN 1613 1613 C->S: Reduces dihydroorotase activity.
{ECO:0000269|PubMed:24332717}.
MUTAGEN 1614 1614 H->A: Abolishes dihydroorotase activity.
{ECO:0000269|PubMed:24332717}.
MUTAGEN 1637 1637 E->T: Abolishes dihydroorotase activity.
{ECO:0000269|PubMed:24332717}.
MUTAGEN 1642 1642 H->N: 11.5% of wild-type catalytic
activity. {ECO:0000269|PubMed:7766613}.
MUTAGEN 1686 1686 D->N: Abolishes dihydroorotase activity.
{ECO:0000269|PubMed:24332717}.
MUTAGEN 1690 1690 H->N: 3% of wild-type catalytic activity.
{ECO:0000269|PubMed:7766613}.
MUTAGEN 1873 1873 S->A: Abolishes PMA-induced Thr-456
phosphorylation.
{ECO:0000269|PubMed:17485345}.
CONFLICT 505 505 P -> T (in Ref. 1; BAA11423).
{ECO:0000305}.
CONFLICT 535 535 A -> G (in Ref. 1; BAA11423).
{ECO:0000305}.
CONFLICT 560 560 L -> V (in Ref. 1; BAA11423).
{ECO:0000305}.
CONFLICT 1103 1103 T -> A (in Ref. 1; BAA11423).
{ECO:0000305}.
CONFLICT 1513 1513 A -> G (in Ref. 1; BAA11423).
{ECO:0000305}.
CONFLICT 1676 1676 N -> D (in Ref. 1; BAA11423).
{ECO:0000305}.
STRAND 1462 1465 {ECO:0000244|PDB:4C6F}.
STRAND 1467 1472 {ECO:0000244|PDB:4C6F}.
TURN 1476 1478 {ECO:0000244|PDB:4C6F}.
TURN 1480 1482 {ECO:0000244|PDB:4C6F}.
HELIX 1485 1494 {ECO:0000244|PDB:4C6F}.
STRAND 1497 1502 {ECO:0000244|PDB:4C6F}.
STRAND 1506 1508 {ECO:0000244|PDB:4C6F}.
HELIX 1513 1526 {ECO:0000244|PDB:4C6F}.
STRAND 1528 1533 {ECO:0000244|PDB:4C6F}.
TURN 1546 1548 {ECO:0000244|PDB:4C6F}.
HELIX 1549 1551 {ECO:0000244|PDB:4C6F}.
STRAND 1555 1558 {ECO:0000244|PDB:4C6F}.
STRAND 1560 1563 {ECO:0000244|PDB:4C6F}.
TURN 1564 1566 {ECO:0000244|PDB:4C6C}.
HELIX 1571 1580 {ECO:0000244|PDB:4C6F}.
STRAND 1587 1590 {ECO:0000244|PDB:4C6F}.
HELIX 1594 1605 {ECO:0000244|PDB:4C6F}.
STRAND 1610 1612 {ECO:0000244|PDB:4C6F}.
HELIX 1618 1629 {ECO:0000244|PDB:4C6F}.
STRAND 1634 1638 {ECO:0000244|PDB:4C6F}.
HELIX 1640 1644 {ECO:0000244|PDB:4C6F}.
HELIX 1647 1649 {ECO:0000244|PDB:4C6F}.
HELIX 1650 1657 {ECO:0000244|PDB:4C6F}.
HELIX 1667 1675 {ECO:0000244|PDB:4C6F}.
HELIX 1677 1679 {ECO:0000244|PDB:4C6F}.
HELIX 1692 1695 {ECO:0000244|PDB:4C6F}.
STRAND 1697 1699 {ECO:0000244|PDB:4C6F}.
HELIX 1707 1719 {ECO:0000244|PDB:4C6F}.
HELIX 1725 1732 {ECO:0000244|PDB:4C6F}.
HELIX 1734 1740 {ECO:0000244|PDB:4C6F}.
STRAND 1749 1759 {ECO:0000244|PDB:4C6F}.
TURN 1773 1776 {ECO:0000244|PDB:4C6F}.
STRAND 1778 1788 {ECO:0000244|PDB:4C6F}.
STRAND 1791 1795 {ECO:0000244|PDB:4C6F}.
HELIX 1809 1811 {ECO:0000244|PDB:4C6F}.
HELIX 1813 1815 {ECO:0000244|PDB:4C6F}.
HELIX 1929 1931 {ECO:0000244|PDB:5G1N}.
HELIX 1934 1952 {ECO:0000244|PDB:5G1N}.
TURN 1959 1962 {ECO:0000244|PDB:5G1N}.
STRAND 1964 1971 {ECO:0000244|PDB:5G1N}.
HELIX 1975 1986 {ECO:0000244|PDB:5G1N}.
STRAND 1990 1995 {ECO:0000244|PDB:5G1N}.
HELIX 1996 1998 {ECO:0000244|PDB:5G1N}.
HELIX 2000 2003 {ECO:0000244|PDB:5G1N}.
HELIX 2007 2014 {ECO:0000244|PDB:5G1N}.
TURN 2015 2017 {ECO:0000244|PDB:5G1N}.
STRAND 2019 2027 {ECO:0000244|PDB:5G1N}.
HELIX 2030 2035 {ECO:0000244|PDB:5G1N}.
STRAND 2042 2047 {ECO:0000244|PDB:5G1N}.
HELIX 2053 2067 {ECO:0000244|PDB:5G1N}.
STRAND 2074 2079 {ECO:0000244|PDB:5G1N}.
TURN 2081 2083 {ECO:0000244|PDB:5G1N}.
HELIX 2085 2094 {ECO:0000244|PDB:5G1N}.
STRAND 2100 2104 {ECO:0000244|PDB:5G1N}.
STRAND 2107 2109 {ECO:0000244|PDB:5G1P}.
HELIX 2113 2121 {ECO:0000244|PDB:5G1N}.
STRAND 2126 2131 {ECO:0000244|PDB:5G1N}.
HELIX 2132 2135 {ECO:0000244|PDB:5G1N}.
HELIX 2136 2138 {ECO:0000244|PDB:5G1O}.
STRAND 2140 2144 {ECO:0000244|PDB:5G1N}.
HELIX 2149 2151 {ECO:0000244|PDB:5G1N}.
HELIX 2155 2160 {ECO:0000244|PDB:5G1N}.
HELIX 2169 2172 {ECO:0000244|PDB:5G1N}.
STRAND 2180 2182 {ECO:0000244|PDB:5G1N}.
STRAND 2188 2191 {ECO:0000244|PDB:5G1N}.
HELIX 2193 2195 {ECO:0000244|PDB:5G1N}.
HELIX 2203 2221 {ECO:0000244|PDB:5G1N}.
SEQUENCE 2225 AA; 242984 MW; 2AB8E8413E825A8F CRC64;
MAALVLEDGS VLRGQPFGAA VSTAGEVVFQ TGMVGYPEAL TDPSYKAQIL VLTYPLIGNY
GIPPDEMDEF GLCKWFESSG IHVAALVVGE CCPTPSHWSA TRTLHEWLQQ HGIPGLQGVD
TRELTKKLRE QGSLLGKLVQ NGTEPSSLPF LDPNARPLVP EVSIKTPRVF NTGGAPRILA
LDCGLKYNQI RCLCQRGAEV TVVPWDHALD SQEYEGLFLS NGPGDPASYP SVVSTLSRVL
SEPNPRPVFG ICLGHQLLAL AIGAKTYKMR YGNRGHNQPC LLVGSGRCFL TSQNHGFAVE
TDSLPADWAP LFTNANDGSN EGIVHNSLPF FSVQFHPEHQ AGPSDMELLF DIFLETVKEA
TAGNPGGQTV RERLTERLCP PGIPTPGSGL PPPRKVLILG SGGLSIGQAG EFDYSGSQAI
KALKEENIQT LLINPNIATV QTSQGLADKV YFLPITPHYV TQVIRNERPD GVLLTFGGQT
ALNCGVELTK AGVLARYGVR VLGTPVETIE LTEDRRAFAA RMAEIGEHVA PSEAANSLEQ
AQAAAERLGY PVLVRAAFAL GGLGSGFASN REELSALVAP AFAHTSQVLV DKSLKGWKEI
EYEVVRDAYG NCVTVCNMEN LDPLGIHTGE SIVVAPSQTL NDREYQLLRQ TAIKVTQHLG
IVGECNVQYA LNPESEQYYI IEVNARLSRS SALASKATGY PLAYVAAKLA LGIPLPELRN
SVTGGTAAFE PSVDYCVVKI PRWDLSKFLR VSTKIGSCMK SVGEVMGIGR SFEEAFQKAL
RMVDENCVGF DHTVKPVSDM ELETPTDKRI FVVAAALWAG YSVDRLYELT RIDRWFLHRM
KRIIAHAQLL EQHRGQPLPP DLLQQAKCLG FSDKQIALAV LSTELAVRKL RQELGICPAV
KQIDTVAAEW PAQTNYLYLT YWGTTHDLTF RTPHVLVLGS GVYRIGSSVE FDWCAVGCIQ
QLRKMGYKTI MVNYNPETVS TDYDMCDRLY FDEISFEVVM DIYELENPEG VILSMGGQLP
NNMAMALHRQ QCRVLGTSPE AIDSAENRFK FSRLLDTIGI SQPQWRELSD LESARQFCQT
VGYPCVVRPS YVLSGAAMNV AYTDGDLERF LSSAAAVSKE HPVVISKFIQ EAKEIDVDAV
ASDGVVAAIA ISEHVENAGV HSGDATLVTP PQDITAKTLE RIKAIVHAVG QELQVTGPFN
LQLIAKDDQL KVIECNVRVS RSFPFVSKTL GVDLVALATR VIMGEEVEPV GLMTGSGVVG
VKVPQFSFSR LAGADVVLGV EMTSTGEVAG FGESRCEAYL KAMLSTGFKI PKKNILLTIG
SYKNKSELLP TVRLLESLGY SLYASLGTAD FYTEHGVKVT AVDWHFEEAV DGECPPQRSI
LEQLAEKNFE LVINLSMRGA GGRRLSSFVT KGYRTRRLAA DFSVPLIIDI KCTKLFVEAL
GQIGPAPPLK VHVDCMTSQK LVRLPGLIDV HVHLREPGGT HKEDFASGTA AALAGGITMV
CAMPNTRPPI IDAPALALAQ KLAEAGARCD FALFLGASSE NAGTLGTVAG SAAGLKLYLN
ETFSELRLDS VVQWMEHFET WPSHLPIVAH AEQQTVAAVL MVAQLTQRSV HICHVARKEE
ILLIKAAKAR GLPVTCEVAP HHLFLSHDDL ERLGPGKGEV RPELGSRQDV EALWENMAVI
DCFASDHAPH TLEEKCGSRP PPGFPGLETM LPLLLTAVSE GRLSLDDLLQ RLHHNPRRIF
HLPPQEDTYV EVDLEHEWTI PSHMPFSKAH WTPFEGQKVK GTVRRVVLRG EVAYIDGQVL
VPPGYGQDVR KWPQGAVPQL PPSAPATSEM TTTPERPRRG IPGLPDGRFH LPPRIHRASD
PGLPAEEPKE KSSRKVAEPE LMGTPDGTCY PPPPVPRQAS PQNLGTPGLL HPQTSPLLHS
LVGQHILSVQ QFTKDQMSHL FNVAHTLRMM VQKERSLDIL KGKVMASMFY EVSTRTSSSF
AAAMARLGGA VLSFSEATSS VQKGESLADS VQTMSCYADV VVLRHPQPGA VELAAKHCRR
PVINAGDGVG EHPTQALLDI FTIREELGTV NGMTITMVGD LKHGRTVHSL ACLLTQYRVS
LRYVAPPSLR MPPTVRAFVA SRGTKQEEFE SIEEALPDTD VLYMTRIQKE RFGSTQEYEA
CFGQFILTPH IMTRAKKKMV VMHPMPRVNE ISVEVDSDPR AAYFRQAENG MYIRMALLAT
VLGRF


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