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Carbamoyl-phosphate synthase [ammonia], mitochondrial (EC 6.3.4.16) (Carbamoyl-phosphate synthetase I) (CPSase I)

 CPSM_HUMAN              Reviewed;        1500 AA.
P31327; B7Z818; J3KQL0; O43774; Q53TL5; Q59HF8; Q7Z5I5;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
15-DEC-1998, sequence version 2.
25-OCT-2017, entry version 207.
RecName: Full=Carbamoyl-phosphate synthase [ammonia], mitochondrial;
EC=6.3.4.16 {ECO:0000269|PubMed:23649895, ECO:0000269|PubMed:24813853};
AltName: Full=Carbamoyl-phosphate synthetase I;
Short=CPSase I;
Flags: Precursor;
Name=CPS1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS SER-1266;
LEU-1283 AND ASN-1406.
TISSUE=Liver;
PubMed=1840546; DOI=10.1016/0378-1119(91)90336-A;
Haraguchi Y., Uchino T., Takiguchi M., Endo F., Mori M., Matsuda I.;
"Cloning and sequence of a cDNA encoding human carbamyl phosphate
synthetase I: molecular analysis of hyperammonemia.";
Gene 107:335-340(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT CPS1D MET-544, AND
VARIANT ALA-344.
TISSUE=Liver;
PubMed=9711878;
DOI=10.1002/(SICI)1098-1004(1998)12:3<206::AID-HUMU8>3.0.CO;2-E;
Finckh U., Kohlschuetter A., Schaefer H., Sperhake K., Colombo J.-P.,
Gal A.;
"Prenatal diagnosis of carbamoyl phosphate synthetase I deficiency by
identification of a missense mutation in CPS1.";
Hum. Mutat. 12:206-211(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ALA-344; SER-1376
AND ASN-1406.
PubMed=12853138; DOI=10.1016/S0378-1119(03)00528-6;
Summar M.L., Hall L.D., Eeds A.M., Hutcheson H.B., Kuo A.N.,
Willis A.S., Rubio V., Arvin M.K., Schofield J.P., Dawson E.P.;
"Characterization of genomic structure and polymorphisms in the human
carbamyl phosphate synthetase I gene.";
Gene 311:51-57(2003).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Testis;
Huo R., Zhu H., Huang X.Y., Xu Z.Y., Lu L., Xu M., Yin L.L., Li J.M.,
Zhou Z.M., Sha J.H.;
"Cloning of an isoform of CPS1 gene related to spermatogenesis.";
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS CPS1D GLY-457
AND ARG-810, AND VARIANT ASN-1406.
PubMed=12955727; DOI=10.1002/humu.9184;
Funghini S., Donati M.A., Pasquini E., Zammarchi E., Morrone A.;
"Structural organization of the human carbamyl phosphate synthetase I
gene (CPS1) and identification of two novel genetic lesions.";
Hum. Mutat. 22:340-341(2003).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANT CPS1D SER-843,
AND VARIANT GLU-875.
PubMed=12655559; DOI=10.1002/humu.9118;
Haeberle J., Schmidt E., Pauli S., Rapp B., Christensen E.,
Wermuth B., Koch H.G.;
"Gene structure of human carbamylphosphate synthetase 1 and novel
mutations in patients with neonatal onset.";
Hum. Mutat. 21:444-444(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
ALA-344.
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
"Homo sapiens protein coding cDNA.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 795-1500.
TISSUE=Small intestine;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[13]
ALLOSTERIC ACTIVATOR NAG BINDING SITE.
PubMed=19754428; DOI=10.1042/BJ20090888;
Pekkala S., Martinez A.I., Barcelona B., Gallego J., Bendala E.,
Yefimenko I., Rubio V., Cervera J.;
"Structural insight on the control of urea synthesis: identification
of the binding site for N-acetyl-L-glutamate, the essential allosteric
activator of mitochondrial carbamoyl phosphate synthetase.";
Biochem. J. 424:211-220(2009).
[14]
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).
[15]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=22002106; DOI=10.1074/mcp.M111.013680;
Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.;
"Systematic analysis of protein pools, isoforms, and modifications
affecting turnover and subcellular localization.";
Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1036 AND SER-1079, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
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).
[17]
GLUTARYLATION AT LYS-55; LYS-171; LYS-176; LYS-207; LYS-210; LYS-214;
LYS-219; LYS-228; LYS-237; LYS-280; LYS-307; LYS-310; LYS-402;
LYS-412; LYS-453; LYS-458; LYS-527; LYS-532; LYS-553; LYS-728;
LYS-757; LYS-772; LYS-793; LYS-811; LYS-841; LYS-856; LYS-869;
LYS-875; LYS-889; LYS-892; LYS-905; LYS-908; LYS-915; LYS-919;
LYS-1074; LYS-1150; LYS-1168; LYS-1183; LYS-1224; LYS-1356; LYS-1360;
LYS-1479 AND LYS-1486.
PubMed=24703693; DOI=10.1016/j.cmet.2014.03.014;
Tan M., Peng C., Anderson K.A., Chhoy P., Xie Z., Dai L., Park J.,
Chen Y., Huang H., Zhang Y., Ro J., Wagner G.R., Green M.F.,
Madsen A.S., Schmiesing J., Peterson B.S., Xu G., Ilkayeva O.R.,
Muehlbauer M.J., Braulke T., Muehlhausen C., Backos D.S., Olsen C.A.,
McGuire P.J., Pletcher S.D., Lombard D.B., Hirschey M.D., Zhao Y.;
"Lysine glutarylation is a protein posttranslational modification
regulated by SIRT5.";
Cell Metab. 19:605-617(2014).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148; SER-569; SER-835;
SER-1079; SER-1203; SER-1419 AND SER-1431, 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).
[19]
X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 1343-1478.
RIKEN structural genomics initiative (RSGI);
"Crystal structure of MGS domain of carbamoyl-phosphate synthetase
from Homo sapiens.";
Submitted (FEB-2009) to the PDB data bank.
[20]
VARIANT CPS1D ARG-1054.
PubMed=11388595; DOI=10.1007/s004310100725;
Rapp B., Haberle J., Linnebank M., Wermuth B., Marquardt T., Harms E.,
Koch H.G.;
"Genetic analysis of carbamoylphosphate synthetase I and ornithine
transcarbamylase deficiency using fibroblasts.";
Eur. J. Pediatr. 160:283-287(2001).
[21]
VARIANT CPS1D ARG-337.
PubMed=11474210; DOI=10.1159/000053360;
Aoshima T., Kajita M., Sekido Y., Kikuchi S., Yasuda I., Saheki T.,
Watanabe K., Shimokata K., Niwa T.;
"Novel mutations (H337R and 238-362del) in the CPS1 gene cause
carbamoyl phosphate synthetase I deficiency.";
Hum. Hered. 52:99-101(2001).
[22]
VARIANT ASN-1406, AND INVOLVEMENT IN PHN.
PubMed=11407344; DOI=10.1056/NEJM200106143442404;
Pearson D.L., Dawling S., Walsh W.F., Haines J.L., Christman B.W.,
Bazyk A., Scott N., Summar M.L.;
"Neonatal pulmonary hypertension -- urea-cycle intermediates, nitric
oxide production, and carbamoyl-phosphate synthetase function.";
N. Engl. J. Med. 344:1832-1838(2001).
[23]
VARIANTS CPS1D HIS-850 AND PRO-918.
PubMed=15617192; DOI=10.1023/B:BOLI.0000045842.59768.ea;
Wakutani Y., Nakayasu H., Takeshima T., Adachi M., Kawataki M.,
Kihira K., Sawada H., Bonno M., Yamamoto H., Nakashima K.;
"Mutational analysis of carbamoylphosphate synthetase I deficiency in
three Japanese patients.";
J. Inherit. Metab. Dis. 27:787-788(2004).
[24]
VARIANT CPS1D SER-843, AND VARIANT GLU-875.
PubMed=15164414; DOI=10.1002/pd.884;
Haeberle J., Koch H.G.;
"Genetic approach to prenatal diagnosis in urea cycle defects.";
Prenat. Diagn. 24:378-383(2004).
[25]
VARIANTS CPS1D GLU-301; CYS-389; ARG-390; THR-589; SER-640; LYS-716;
LEU-805; VAL-911; PRO-958; SER-982; PHE-998; LEU-1089; PRO-1203;
ASN-1205; PRO-1331; THR-1378; LEU-1411 AND ALA-1443.
PubMed=16737834; DOI=10.1016/j.ymgme.2006.04.006;
Eeds A.M., Hall L.D., Yadav M., Willis A., Summar S., Putnam A.,
Barr F., Summar M.L.;
"The frequent observation of evidence for nonsense-mediated decay in
RNA from patients with carbamyl phosphate synthetase I deficiency.";
Mol. Genet. Metab. 89:80-86(2006).
[26]
VARIANTS CPS1D GLU-79; ASN-212; ASN-280; PRO-438; HIS-587; ARG-593;
LYS-651; ILE-674; HIS-780; CYS-850; ASP-982; ARG-1103; GLY-1141;
PRO-1195; VAL-1215 AND LYS-1241.
PubMed=17310273; DOI=10.1007/s10038-007-0122-9;
Kurokawa K., Yorifuji T., Kawai M., Momoi T., Nagasaka H.,
Takayanagi M., Kobayashi K., Yoshino M., Kosho T., Adachi M.,
Otsuka H., Yamamoto S., Murata T., Suenaga A., Ishii T., Terada K.,
Shimura N., Kiwaki K., Shintaku H., Yamakawa M., Nakabayashi H.,
Wakutani Y., Nakahata T.;
"Molecular and clinical analyses of Japanese patients with
carbamoylphosphate synthetase 1 (CPS1) deficiency.";
J. Hum. Genet. 52:349-354(2007).
[27]
VARIANTS CPS1D PHE-123; ARG-337; ASN-471; PRO-678; LEU-774; LEU-1411;
GLN-1453; TRP-1453 AND HIS-1491, VARIANT SER-1376, CHARACTERIZATION OF
VARIANTS CPS1D PHE-123; ARG-337; ASN-471; PRO-678; LEU-774; LEU-1411;
GLN-1453; TRP-1453 AND HIS-1491, AND CHARACTERIZATION OF VARIANT
SER-1376.
PubMed=20578160; DOI=10.1002/humu.21272;
Pekkala S., Martinez A.I., Barcelona B., Yefimenko I., Finckh U.,
Rubio V., Cervera J.;
"Understanding carbamoyl-phosphate synthetase I (CPS1) deficiency by
using expression studies and structure-based analysis.";
Hum. Mutat. 31:801-808(2010).
[28]
VARIANT ASN-1406.
PubMed=20520828; DOI=10.1371/journal.pone.0010792;
Moonen R.M., Reyes I., Cavallaro G., Gonzalez-Luis G., Bakker J.A.,
Villamor E.;
"The T1405N carbamoyl phosphate synthetase polymorphism does not
affect plasma arginine concentrations in preterm infants.";
PLoS ONE 5:E10792-E10792(2010).
[29]
VARIANTS CPS1D VAL-43; ASP-58; PHE-65; GLY-71; SER-87; ASP-89;
GLY-165; VAL-224; CYS-233; PRO-243; GLU-258; GLU-263; VAL-304;
GLU-317; HIS-358; LEU-382; ARG-401; ARG-431; VAL-432; THR-438;
GLU-450; PRO-498; GLU-531; GLY-531; MET-544; CYS-587; HIS-587;
LEU-587; LEU-597; MET-622; ASP-628; ARG-632; PRO-638; TYR-648;
VAL-654; LYS-674; SER-698; LYS-718; GLN-721; PRO-724; THR-726;
VAL-767; HIS-780; ILE-792; SER-803; GLY-803; CYS-803; SER-805;
TRP-814; ARG-816; HIS-850; GLU-911; LEU-913; HIS-914; GLY-914;
THR-932; THR-949; CYS-959; CYS-962; GLU-978; VAL-982; HIS-984;
THR-986; CYS-987; SER-992; SER-1016; LEU-1017; ILE-1022; GLY-1034;
ARG-1045; ARG-1059; GLU-1065; CYS-1089; GLU-1155; VAL-1155; LEU-1203;
GLN-1228; ASP-1255; GLN-1262; PRO-1262; HIS-1274; ARG-1327; GLU-1333;
LEU-1371; MET-1391; VAL-1398; LEU-1439; TRP-1453 AND ARG-1462.
PubMed=21120950; DOI=10.1002/humu.21406;
Haberle J., Shchelochkov O.A., Wang J., Katsonis P., Hall L.,
Reiss S., Eeds A., Willis A., Yadav M., Summar S., Lichtarge O.,
Rubio V., Wong L.J., Summar M.;
"Molecular defects in human carbamoyl phosphate synthetase I:
mutational spectrum, diagnostic and protein structure
considerations.";
Hum. Mutat. 32:579-589(2011).
[30]
VARIANTS VAL-530 AND ASN-1406.
PubMed=21767969; DOI=10.1016/j.ymgme.2011.06.022;
NISC Comparative Sequencing Program;
Solomon B.D., Pineda-Alvarez D.E., Hadley D.W., Teer J.K.,
Cherukuri P.F., Hansen N.F., Cruz P., Young A.C., Blakesley R.W.,
Lanpher B., Mayfield Gibson S., Sincan M., Chandrasekharappa S.C.,
Mullikin J.C.;
"Personalized genomic medicine: lessons from the exome.";
Mol. Genet. Metab. 104:189-191(2011).
[31]
VARIANTS CPS1D SER-341; ARG-661; ASP-964 AND ARG-1167.
PubMed=22173106; DOI=10.1016/j.gene.2011.11.052;
Funghini S., Thusberg J., Spada M., Gasperini S., Parini R.,
Ventura L., Meli C., De Cosmo L., Sibilio M., Mooney S.D.,
Guerrini R., Donati M.A., Morrone A.;
"Carbamoyl phosphate synthetase 1 deficiency in Italy: clinical and
genetic findings in a heterogeneous cohort.";
Gene 493:228-234(2012).
[32]
VARIANTS CPS1D ASP-355; CYS-389; ARG-390; PRO-438; MET-544; THR-1378;
SER-1381 AND ALA-1443, VARIANTS ALA-344 AND SER-1376, CHARACTERIZATION
OF VARIANTS CPS1D ASP-355; CYS-389; ARG-390; PRO-438; MET-544;
THR-1378; SER-1381 AND ALA-1443, CHARACTERIZATION OF VARIANTS ALA-344
AND SER-1376, SUBUNIT, PROTEOLYTIC CLEAVAGE, BIOPHYSICOCHEMICAL
PROPERTIES, ENZYME REGULATION, AND CATALYTIC ACTIVITY.
PubMed=23649895; DOI=10.1002/humu.22349;
Diez-Fernandez C., Martinez A.I., Pekkala S., Barcelona B.,
Perez-Arellano I., Guadalajara A.M., Summar M., Cervera J., Rubio V.;
"Molecular characterization of carbamoyl-phosphate synthetase (CPS1)
deficiency using human recombinant CPS1 as a key tool.";
Hum. Mutat. 34:1149-1159(2013).
[33]
VARIANT ASN-1406.
PubMed=24237036; DOI=10.1021/pr400544j;
Song C., Wang F., Cheng K., Wei X., Bian Y., Wang K., Tan Y., Wang H.,
Ye M., Zou H.;
"Large-scale quantification of single amino-acid variations by a
variation-associated database search strategy.";
J. Proteome Res. 13:241-248(2014).
[34]
VARIANTS CPS1D ARG-401; ARG-632; SER-843; CYS-850; HIS-850; PRO-871;
VAL-911; GLU-911; LEU-913; HIS-914; GLY-914; PRO-918; THR-932;
ASN-937; THR-949; PRO-958; CYS-959; CYS-962; ASP-964; ASP-1194 AND
ARG-1462, VARIANT GLU-875, CHARACTERIZATION OF VARIANTS CPS1D SER-843;
CYS-850; HIS-850; PRO-871; VAL-911; GLU-911; LEU-913; HIS-914;
GLY-914; PRO-918; THR-932; ASN-937; THR-949; PRO-958; CYS-959; CYS-962
AND ASP-964, CATALYTIC ACTIVITY, AND CHARACTERIZATION OF VARIANT
GLU-875.
PubMed=24813853; DOI=10.1016/j.ymgme.2014.04.003;
Diez-Fernandez C., Hu L., Cervera J., Haeberle J., Rubio V.;
"Understanding carbamoyl phosphate synthetase (CPS1) deficiency by
using the recombinantly purified human enzyme: effects of CPS1
mutations that concentrate in a central domain of unknown function.";
Mol. Genet. Metab. 112:123-132(2014).
[35]
VARIANTS CPS1D TYR-123; TRP-174; GLY-803; HIS-850; PHE-1254 AND
1363-LEU--ILE-1366 DEL.
PubMed=26440671; DOI=10.1007/s00431-015-2644-z;
Ali E.Z., Khalid M.K., Yunus Z.M., Yakob Y., Chin C.B., Latif K.A.,
Hock N.L.;
"Carbamoylphosphate synthetase 1 (CPS1) deficiency: clinical,
biochemical, and molecular characterization in Malaysian patients.";
Eur. J. Pediatr. 175:339-346(2016).
[36]
VARIANT GLU-875.
PubMed=27535533; DOI=10.1038/nature19057;
Exome Aggregation Consortium;
Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E.,
Fennell T., O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B.,
Tukiainen T., Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K.,
Zhao F., Zou J., Pierce-Hoffman E., Berghout J., Cooper D.N.,
Deflaux N., DePristo M., Do R., Flannick J., Fromer M., Gauthier L.,
Goldstein J., Gupta N., Howrigan D., Kiezun A., Kurki M.I.,
Moonshine A.L., Natarajan P., Orozco L., Peloso G.M., Poplin R.,
Rivas M.A., Ruano-Rubio V., Rose S.A., Ruderfer D.M., Shakir K.,
Stenson P.D., Stevens C., Thomas B.P., Tiao G., Tusie-Luna M.T.,
Weisburd B., Won H.H., Yu D., Altshuler D.M., Ardissino D.,
Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S.,
Laakso M., McCarroll S., McCarthy M.I., McGovern D., McPherson R.,
Neale B.M., Palotie A., Purcell S.M., Saleheen D., Scharf J.M.,
Sklar P., Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C.,
Wilson J.G., Daly M.J., MacArthur D.G.;
"Analysis of protein-coding genetic variation in 60,706 humans.";
Nature 536:285-291(2016).
-!- FUNCTION: Involved in the urea cycle of ureotelic animals where
the enzyme plays an important role in removing excess ammonia from
the cell.
-!- CATALYTIC ACTIVITY: 2 ATP + NH(3) + HCO(3)(-) = 2 ADP + phosphate
+ carbamoyl phosphate. {ECO:0000269|PubMed:23649895,
ECO:0000269|PubMed:24813853}.
-!- ENZYME REGULATION: Requires N-acetyl-L-glutamate (NAG) as an
allosteric activator. Activated by glycerol in the absence of NAG,
whereas in the presence of NAG it is inhibited by increasing
concentrations of glycerol. {ECO:0000269|PubMed:19754428,
ECO:0000269|PubMed:23649895}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.47 mM for ATP {ECO:0000269|PubMed:23649895};
KM=4.0 mM for HCO(3)(-) {ECO:0000269|PubMed:23649895};
KM=1.00 mM for NH(4)(+) {ECO:0000269|PubMed:23649895};
Vmax=1.22 umol/min/mg enzyme for ATP
{ECO:0000269|PubMed:23649895};
Vmax=1.23 umol/min/mg enzyme for HCO(3)(-)
{ECO:0000269|PubMed:23649895};
Vmax=1.19 umol/min/mg enzyme for NH(4)(+)
{ECO:0000269|PubMed:23649895};
-!- SUBUNIT: Can form homooligomers (monomers as predominant form and
dimers). {ECO:0000269|PubMed:23649895}.
-!- INTERACTION:
P10398:ARAF; NbExp=3; IntAct=EBI-536811, EBI-365961;
P04049:RAF1; NbExp=4; IntAct=EBI-536811, EBI-365996;
P63104:YWHAZ; NbExp=2; IntAct=EBI-536811, EBI-347088;
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:22002106}.
Nucleus, nucleolus {ECO:0000269|PubMed:22002106}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P31327-1; Sequence=Displayed;
Name=2;
IsoId=P31327-2; Sequence=VSP_009332;
Name=3;
IsoId=P31327-3; Sequence=VSP_046685;
Note=Ref.11 (BAD92037) sequence is in conflict in position:
5:I->IF. {ECO:0000305};
-!- TISSUE SPECIFICITY: Primarily in the liver and small intestine.
-!- DOMAIN: The type-1 glutamine amidotransferase domain is defective.
-!- PTM: Undergoes proteolytic cleavage in the C-terminal region
corresponding to the loss of approximately 12 AA residues from the
C-terminus. {ECO:0000269|PubMed:23649895}.
-!- PTM: Succinylated at Lys-287 and Lys-1291. Desuccinylated at Lys-
1291 by SIRT5, leading to activation (By similarity).
{ECO:0000250|UniProtKB:Q8C196}.
-!- PTM: Glutarylated. Glutarylation levels increase during fasting.
Deglutarylated by SIRT5 at Lys-55, Lys-219, Lys-412, Lys-889, Lys-
892, Lys-915, Lys-1360 and Lys-1486, leading to activation.
{ECO:0000269|PubMed:24703693}.
-!- DISEASE: Carbamoyl phosphate synthetase 1 deficiency (CPS1D)
[MIM:237300]: An autosomal recessive disorder of the urea cycle
causing hyperammonemia. It can present as a devastating metabolic
disease dominated by severe hyperammonemia in neonates or as a
more insidious late-onset condition, generally manifesting as
life-threatening hyperammonemic crises under catabolic situations.
Clinical features include protein intolerance, intermittent
ataxia, seizures, lethargy, developmental delay and mental
retardation. {ECO:0000269|PubMed:11388595,
ECO:0000269|PubMed:11474210, ECO:0000269|PubMed:12655559,
ECO:0000269|PubMed:12955727, ECO:0000269|PubMed:15164414,
ECO:0000269|PubMed:15617192, ECO:0000269|PubMed:16737834,
ECO:0000269|PubMed:17310273, ECO:0000269|PubMed:20578160,
ECO:0000269|PubMed:21120950, ECO:0000269|PubMed:22173106,
ECO:0000269|PubMed:23649895, ECO:0000269|PubMed:24813853,
ECO:0000269|PubMed:26440671, ECO:0000269|PubMed:9711878}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Pulmonary hypertension, neonatal (PHN) [MIM:615371]: A
disease characterized by elevated pulmonary artery pressure.
Pulmonary hypertension in the neonate is associated with multiple
underlying problems such as respiratory distress syndrome,
meconium aspiration syndrome, congenital diaphragmatic hernia,
bronchopulmonary dysplasia, sepsis, or congenital heart disease.
{ECO:0000269|PubMed:11407344}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry. CPS1 variants influence the availability of precursors for
nitric oxide (NO) synthesis and play a role in clinical situations
where endogenous NO production is critically important, such as
neonatal pulmonary hypertension, increased pulmonary artery
pressure following surgical repair of congenital heart defects or
hepatovenocclusive disease following bone marrow transplantation.
Infants with neonatal pulmonary hypertension homozygous for Thr-
1406 have lower L-arginine concentrations than neonates homozygous
for Asn-1406 (PubMed:11407344). {ECO:0000269|PubMed:11407344}.
-!- SEQUENCE CAUTION:
Sequence=BAD92037.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=LOVD-Leiden Open Variation Database;
Note=Carbamoyl-Phosphate Synthetase 1 (CPS1);
URL="http://chromium.lovd.nl/lovd2/home.php?select_db=CPS1";
-----------------------------------------------------------------------
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EMBL; D90282; BAA14328.1; -; mRNA.
EMBL; Y15793; CAA75785.1; -; mRNA.
EMBL; AF154830; AAD38072.1; -; mRNA.
EMBL; AY317138; AAP84318.1; -; mRNA.
EMBL; AY167007; AAO31763.1; -; Genomic_DNA.
EMBL; AY166970; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY166971; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY166972; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY166973; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY166974; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY166975; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY166976; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY166977; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY166978; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY166979; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY166980; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY166981; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY166982; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY166983; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY166984; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY166985; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY166986; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY166987; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY166988; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY166989; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY166990; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY166991; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY166992; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY166993; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY166994; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY166995; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY166996; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY166997; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY166998; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY166999; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY167000; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY167001; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY167002; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY167003; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY167004; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY167005; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AY167006; AAO31763.1; JOINED; Genomic_DNA.
EMBL; AF536523; AAN77181.1; -; Genomic_DNA.
EMBL; AK302778; BAH13804.1; -; mRNA.
EMBL; AC007970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC008172; AAY14960.1; -; Genomic_DNA.
EMBL; CH471063; EAW70492.1; -; Genomic_DNA.
EMBL; BC140943; AAI40944.1; -; mRNA.
EMBL; AB208800; BAD92037.1; ALT_INIT; mRNA.
EMBL; BX640601; CAE45707.1; -; mRNA.
CCDS; CCDS2393.1; -. [P31327-1]
CCDS; CCDS46505.1; -. [P31327-3]
CCDS; CCDS46506.1; -. [P31327-2]
PIR; JQ1348; JQ1348.
RefSeq; NP_001116105.1; NM_001122633.2. [P31327-3]
RefSeq; NP_001116106.1; NM_001122634.3. [P31327-2]
RefSeq; NP_001866.2; NM_001875.4. [P31327-1]
RefSeq; XP_011508943.1; XM_011510641.2. [P31327-1]
RefSeq; XP_011508944.1; XM_011510642.2. [P31327-1]
RefSeq; XP_011508945.1; XM_011510643.2. [P31327-1]
RefSeq; XP_011508946.1; XM_011510644.2. [P31327-1]
UniGene; Hs.149252; -.
PDB; 2YVQ; X-ray; 1.98 A; A=1343-1478.
PDB; 4UTR; X-ray; 2.90 A; C=524-531.
PDB; 4UTV; X-ray; 2.40 A; C=524-531.
PDB; 4UTX; X-ray; 3.10 A; C=524-531.
PDB; 4UTZ; X-ray; 3.30 A; D=524-531.
PDB; 4UU7; X-ray; 3.00 A; D=524-531.
PDB; 4UU8; X-ray; 2.90 A; D=524-531.
PDB; 4UUA; X-ray; 2.80 A; D=524-531.
PDB; 4UUB; X-ray; 2.90 A; D=524-531.
PDB; 5DOT; X-ray; 2.40 A; A/B=40-1500.
PDB; 5DOU; X-ray; 2.60 A; A/B/C/D=40-1500.
PDBsum; 2YVQ; -.
PDBsum; 4UTR; -.
PDBsum; 4UTV; -.
PDBsum; 4UTX; -.
PDBsum; 4UTZ; -.
PDBsum; 4UU7; -.
PDBsum; 4UU8; -.
PDBsum; 4UUA; -.
PDBsum; 4UUB; -.
PDBsum; 5DOT; -.
PDBsum; 5DOU; -.
ProteinModelPortal; P31327; -.
SMR; P31327; -.
BioGrid; 107764; 66.
IntAct; P31327; 27.
MINT; MINT-4991575; -.
STRING; 9606.ENSP00000402608; -.
ChEMBL; CHEMBL2362990; -.
DrugBank; DB06775; Carglumic Acid.
MEROPS; C26.951; -.
iPTMnet; P31327; -.
PhosphoSitePlus; P31327; -.
SwissPalm; P31327; -.
BioMuta; CPS1; -.
DMDM; 4033707; -.
EPD; P31327; -.
PaxDb; P31327; -.
PeptideAtlas; P31327; -.
PRIDE; P31327; -.
Ensembl; ENST00000233072; ENSP00000233072; ENSG00000021826. [P31327-1]
Ensembl; ENST00000430249; ENSP00000402608; ENSG00000021826. [P31327-3]
Ensembl; ENST00000451903; ENSP00000406136; ENSG00000021826. [P31327-2]
GeneID; 1373; -.
KEGG; hsa:1373; -.
UCSC; uc002vee.5; human. [P31327-1]
CTD; 1373; -.
DisGeNET; 1373; -.
EuPathDB; HostDB:ENSG00000021826.14; -.
GeneCards; CPS1; -.
HGNC; HGNC:2323; CPS1.
HPA; CAB003781; -.
HPA; HPA021400; -.
MalaCards; CPS1; -.
MIM; 237300; phenotype.
MIM; 608307; gene.
MIM; 615371; phenotype.
neXtProt; NX_P31327; -.
OpenTargets; ENSG00000021826; -.
Orphanet; 147; Carbamoyl-phosphate synthase deficiency.
PharmGKB; PA26840; -.
eggNOG; KOG0370; Eukaryota.
eggNOG; COG0458; LUCA.
eggNOG; COG0505; LUCA.
GeneTree; ENSGT00900000141204; -.
HOGENOM; HOG000234583; -.
HOVERGEN; HBG000279; -.
InParanoid; P31327; -.
KO; K01948; -.
OMA; AVFPFNK; -.
OrthoDB; EOG091G00DC; -.
PhylomeDB; P31327; -.
TreeFam; TF331485; -.
BioCyc; MetaCyc:HS00415-MONOMER; -.
BRENDA; 6.3.4.16; 2681.
Reactome; R-HSA-70635; Urea cycle.
SABIO-RK; P31327; -.
ChiTaRS; CPS1; human.
EvolutionaryTrace; P31327; -.
GenomeRNAi; 1373; -.
PRO; PR:P31327; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000021826; -.
CleanEx; HS_CPS1; -.
ExpressionAtlas; P31327; baseline and differential.
Genevisible; P31327; HS.
GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
GO; GO:0004087; F:carbamoyl-phosphate synthase (ammonia) activity; IMP:BHF-UCL.
GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IBA:GO_Central.
GO; GO:0004175; F:endopeptidase activity; IEA:Ensembl.
GO; GO:0016595; F:glutamate binding; IEA:Ensembl.
GO; GO:0072341; F:modified amino acid binding; IDA:UniProtKB.
GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
GO; GO:0055081; P:anion homeostasis; IEA:Ensembl.
GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central.
GO; GO:0070409; P:carbamoyl phosphate biosynthetic process; IMP:UniProtKB.
GO; GO:1903718; P:cellular response to ammonia; IMP:BHF-UCL.
GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEA:Ensembl.
GO; GO:0071377; P:cellular response to glucagon stimulus; IEA:Ensembl.
GO; GO:0071400; P:cellular response to oleic acid; IEA:Ensembl.
GO; GO:0019240; P:citrulline biosynthetic process; NAS:BHF-UCL.
GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
GO; GO:0070365; P:hepatocyte differentiation; IEA:Ensembl.
GO; GO:0050667; P:homocysteine metabolic process; IDA:UniProtKB.
GO; GO:0007494; P:midgut development; IEA:Ensembl.
GO; GO:0046209; P:nitric oxide metabolic process; IMP:BHF-UCL.
GO; GO:0014075; P:response to amine; IEA:Ensembl.
GO; GO:0043200; P:response to amino acid; IEA:Ensembl.
GO; GO:0071548; P:response to dexamethasone; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0032094; P:response to food; IEA:Ensembl.
GO; GO:0060416; P:response to growth hormone; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IDA:UniProtKB.
GO; GO:0042594; P:response to starvation; IEA:Ensembl.
GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
GO; GO:0010043; P:response to zinc ion; IEA:Ensembl.
GO; GO:0019433; P:triglyceride catabolic process; IMP:BHF-UCL.
GO; GO:0000050; P:urea cycle; IBA:GO_Central.
GO; GO:0042311; P:vasodilation; IMP:BHF-UCL.
CDD; cd01744; GATase1_CPSase; 1.
Gene3D; 1.10.1030.10; -; 1.
Gene3D; 3.30.1490.20; -; 1.
Gene3D; 3.40.50.1380; -; 1.
Gene3D; 3.40.50.880; -; 1.
Gene3D; 3.50.30.20; -; 1.
HAMAP; MF_01209; CPSase_S_chain; 1.
InterPro; IPR011761; ATP-grasp.
InterPro; IPR013815; ATP_grasp_subdomain_1.
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; IPR017926; GATASE.
InterPro; IPR011607; MGS-like_dom.
InterPro; IPR036914; MGS-like_dom_sf.
InterPro; IPR016185; PreATP-grasp_dom.
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.
PRINTS; PR00098; CPSASE.
SMART; SM01096; CPSase_L_D3; 1.
SMART; SM01097; CPSase_sm_chain; 1.
SMART; SM00851; MGS; 1.
SUPFAM; SSF48108; SSF48108; 1.
SUPFAM; SSF52021; SSF52021; 1.
SUPFAM; SSF52317; SSF52317; 1.
SUPFAM; SSF52335; SSF52335; 1.
SUPFAM; SSF52440; SSF52440; 2.
TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
PROSITE; PS50975; ATP_GRASP; 2.
PROSITE; PS00866; CPSASE_1; 2.
PROSITE; PS00867; CPSASE_2; 2.
PROSITE; PS51273; GATASE_TYPE_1; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Allosteric enzyme; Alternative splicing;
ATP-binding; Complete proteome; Disease mutation; Glycoprotein;
Ligase; Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Transit peptide; Urea cycle.
TRANSIT 1 38 Mitochondrion. {ECO:0000250}.
CHAIN 39 1500 Carbamoyl-phosphate synthase [ammonia],
mitochondrial.
/FTId=PRO_0000029897.
DOMAIN 219 404 Glutamine amidotransferase type-1.
DOMAIN 551 743 ATP-grasp 1.
DOMAIN 1093 1284 ATP-grasp 2.
REGION 39 218 Anthranilate phosphoribosyltransferase
homolog.
BINDING 1391 1391 Allosteric activator. {ECO:0000305}.
BINDING 1394 1394 Allosteric activator. {ECO:0000305}.
BINDING 1410 1410 Allosteric activator. {ECO:0000305}.
BINDING 1437 1437 Allosteric activator. {ECO:0000305}.
BINDING 1440 1440 Allosteric activator. {ECO:0000305}.
BINDING 1449 1449 Allosteric activator. {ECO:0000305}.
MOD_RES 55 55 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 55 55 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 55 55 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 57 57 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 57 57 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 119 119 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 119 119 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 148 148 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 157 157 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 157 157 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 171 171 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 171 171 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 176 176 N6-glutaryllysine.
{ECO:0000269|PubMed:24703693}.
MOD_RES 182 182 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 197 197 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 207 207 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 207 207 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 207 207 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 210 210 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 210 210 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 214 214 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 214 214 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 214 214 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 219 219 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 219 219 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 228 228 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 228 228 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 237 237 N6-glutaryllysine.
{ECO:0000269|PubMed:24703693}.
MOD_RES 280 280 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 280 280 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 287 287 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 287 287 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 307 307 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 307 307 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 307 307 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 310 310 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 310 310 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 400 400 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 402 402 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 402 402 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 412 412 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 412 412 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 412 412 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 453 453 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 453 453 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 458 458 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 458 458 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 458 458 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 522 522 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 522 522 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 527 527 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 527 527 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 527 527 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 532 532 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 532 532 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 537 537 Phosphoserine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 540 540 Phosphoserine.
{ECO:0000250|UniProtKB:P07756}.
MOD_RES 553 553 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 553 553 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 553 553 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 560 560 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 560 560 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 569 569 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 575 575 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 575 575 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 612 612 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 612 612 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 630 630 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 728 728 N6-glutaryllysine.
{ECO:0000269|PubMed:24703693}.
MOD_RES 751 751 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 751 751 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 757 757 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 757 757 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 757 757 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 772 772 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 772 772 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 793 793 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 793 793 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 793 793 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 811 811 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 811 811 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 831 831 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 831 831 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 835 835 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 841 841 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 841 841 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 856 856 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 856 856 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 869 869 N6-glutaryllysine.
{ECO:0000269|PubMed:24703693}.
MOD_RES 875 875 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 875 875 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 875 875 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 889 889 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 889 889 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 889 889 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 892 892 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 892 892 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 892 892 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 896 896 Phosphoserine.
{ECO:0000250|UniProtKB:P07756}.
MOD_RES 898 898 Phosphoserine.
{ECO:0000250|UniProtKB:P07756}.
MOD_RES 905 905 N6-glutaryllysine.
{ECO:0000269|PubMed:24703693}.
MOD_RES 908 908 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 908 908 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 915 915 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 915 915 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 915 915 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 919 919 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 919 919 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 919 919 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 935 935 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 1036 1036 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1074 1074 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 1074 1074 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 1074 1074 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 1079 1079 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1090 1090 Phosphoserine.
{ECO:0000250|UniProtKB:P07756}.
MOD_RES 1093 1093 Phosphoserine.
{ECO:0000250|UniProtKB:P07756}.
MOD_RES 1100 1100 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 1100 1100 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 1149 1149 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 1150 1150 N6-glutaryllysine.
{ECO:0000269|PubMed:24703693}.
MOD_RES 1168 1168 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 1168 1168 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 1168 1168 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 1183 1183 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 1183 1183 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 1183 1183 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 1203 1203 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1222 1222 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 1224 1224 N6-glutaryllysine.
{ECO:0000269|PubMed:24703693}.
MOD_RES 1232 1232 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 1232 1232 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 1269 1269 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 1269 1269 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 1291 1291 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 1291 1291 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 1356 1356 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 1356 1356 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 1356 1356 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 1360 1360 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 1360 1360 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 1419 1419 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1431 1431 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1444 1444 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 1444 1444 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 1471 1471 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 1471 1471 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 1479 1479 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 1479 1479 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 1479 1479 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 1486 1486 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
MOD_RES 1486 1486 N6-glutaryllysine; alternate.
{ECO:0000269|PubMed:24703693}.
MOD_RES 1486 1486 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8C196}.
CARBOHYD 537 537 O-linked (GlcNAc) serine; alternate.
{ECO:0000250}.
CARBOHYD 1331 1331 O-linked (GlcNAc) serine. {ECO:0000250}.
CARBOHYD 1332 1332 O-linked (GlcNAc) threonine.
{ECO:0000250}.
VAR_SEQ 1 451 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.4}.
/FTId=VSP_009332.
VAR_SEQ 1 1 M -> MPQIIKM (in isoform 3).
{ECO:0000303|Ref.11}.
/FTId=VSP_046685.
VARIANT 43 43 A -> V (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066171.
VARIANT 58 58 G -> D (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066172.
VARIANT 65 65 S -> F (in CPS1D; dbSNP:rs375979196).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066173.
VARIANT 71 71 V -> G (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066174.
VARIANT 79 79 G -> E (in CPS1D).
{ECO:0000269|PubMed:17310273}.
/FTId=VAR_063560.
VARIANT 87 87 P -> S (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066175.
VARIANT 89 89 Y -> D (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066176.
VARIANT 123 123 S -> F (in CPS1D; modestly decreases
enzyme activity).
{ECO:0000269|PubMed:20578160}.
/FTId=VAR_064062.
VARIANT 123 123 S -> Y (in CPS1D; unknown pathological
significance).
{ECO:0000269|PubMed:26440671}.
/FTId=VAR_075404.
VARIANT 165 165 D -> G (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066177.
VARIANT 174 174 R -> W (in CPS1D; unknown pathological
significance).
{ECO:0000269|PubMed:26440671}.
/FTId=VAR_075405.
VARIANT 212 212 Y -> N (in CPS1D).
{ECO:0000269|PubMed:17310273}.
/FTId=VAR_063561.
VARIANT 224 224 D -> V (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066178.
VARIANT 233 233 R -> C (in CPS1D; dbSNP:rs767905306).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066179.
VARIANT 243 243 H -> P (in CPS1D; dbSNP:rs752902711).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066180.
VARIANT 258 258 G -> E (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066181.
VARIANT 263 263 G -> E (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066182.
VARIANT 280 280 K -> N (in CPS1D; dbSNP:rs753751183).
{ECO:0000269|PubMed:17310273}.
/FTId=VAR_063562.
VARIANT 301 301 G -> E (in CPS1D).
{ECO:0000269|PubMed:16737834}.
/FTId=VAR_066104.
VARIANT 304 304 A -> V (in CPS1D; associated with T-986;
dbSNP:rs775920437).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066183.
VARIANT 317 317 G -> E (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066184.
VARIANT 337 337 H -> R (in CPS1D; modestly decreases
enzyme activity; dbSNP:rs28940283).
{ECO:0000269|PubMed:11474210,
ECO:0000269|PubMed:20578160}.
/FTId=VAR_014077.
VARIANT 341 341 L -> S (in CPS1D).
{ECO:0000269|PubMed:22173106}.
/FTId=VAR_075806.
VARIANT 344 344 T -> A (polymorphism; no negative effect
on protein stability, enzyme activity and
thermal stability; dbSNP:rs1047883).
{ECO:0000269|PubMed:12853138,
ECO:0000269|PubMed:23649895,
ECO:0000269|PubMed:9711878,
ECO:0000269|Ref.11}.
/FTId=VAR_006834.
VARIANT 344 344 T -> S (in dbSNP:rs1047883).
/FTId=VAR_061752.
VARIANT 355 355 N -> D (in CPS1D; around 80% decrease in
enzyme activity; significant reduction in
thermal stability; approximately 4-fold
decrease in the apparent Vmax for ATP,
bicarbonate and ammonia).
{ECO:0000269|PubMed:23649895}.
/FTId=VAR_075406.
VARIANT 358 358 D -> H (in CPS1D; dbSNP:rs149930500).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066185.
VARIANT 382 382 P -> L (in CPS1D; dbSNP:rs201407486).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066186.
VARIANT 389 389 Y -> C (in CPS1D; around 40% decrease in
enzyme activity; significant loss of
thermal stability).
{ECO:0000269|PubMed:16737834,
ECO:0000269|PubMed:23649895}.
/FTId=VAR_066105.
VARIANT 390 390 L -> R (in CPS1D; significant loss of
protein stability).
{ECO:0000269|PubMed:16737834,
ECO:0000269|PubMed:23649895}.
/FTId=VAR_066106.
VARIANT 401 401 G -> R (in CPS1D; unknown pathological
significance; associated with N-937 in a
patient; dbSNP:rs760895692).
{ECO:0000269|PubMed:21120950,
ECO:0000269|PubMed:24813853}.
/FTId=VAR_066187.
VARIANT 431 431 G -> R (in CPS1D; dbSNP:rs778766382).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066188.
VARIANT 432 432 G -> V (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066189.
VARIANT 438 438 A -> P (in CPS1D; almost complete loss of
enzyme activity).
{ECO:0000269|PubMed:17310273,
ECO:0000269|PubMed:23649895}.
/FTId=VAR_063563.
VARIANT 438 438 A -> T (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066190.
VARIANT 450 450 K -> E (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066191.
VARIANT 457 457 V -> G (in CPS1D; dbSNP:rs371350538).
{ECO:0000269|PubMed:12955727}.
/FTId=VAR_017562.
VARIANT 471 471 T -> N (in CPS1D).
{ECO:0000269|PubMed:20578160}.
/FTId=VAR_064063.
VARIANT 498 498 A -> P (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066192.
VARIANT 530 530 G -> V (found in a patient with VACTERL
syndrome and postsurgical PHN; variant of
unknown pathological significance).
{ECO:0000269|PubMed:21767969}.
/FTId=VAR_070211.
VARIANT 531 531 V -> E (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066193.
VARIANT 531 531 V -> G (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066194.
VARIANT 544 544 T -> M (in CPS1D; almost complete loss of
enzyme activity; approximately 60-fold
increase in the apparent Km for
bicarbonate and approximately 4-fold
respective decrease and increase in the
apparent Vmax and Km for ammonia;
dbSNP:rs121912592).
{ECO:0000269|PubMed:21120950,
ECO:0000269|PubMed:23649895,
ECO:0000269|PubMed:9711878}.
/FTId=VAR_006835.
VARIANT 587 587 R -> C (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066195.
VARIANT 587 587 R -> H (in CPS1D).
{ECO:0000269|PubMed:17310273,
ECO:0000269|PubMed:21120950}.
/FTId=VAR_063564.
VARIANT 587 587 R -> L (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066196.
VARIANT 589 589 A -> T (in CPS1D; dbSNP:rs777233486).
{ECO:0000269|PubMed:16737834}.
/FTId=VAR_066142.
VARIANT 593 593 G -> R (in CPS1D).
{ECO:0000269|PubMed:17310273}.
/FTId=VAR_063565.
VARIANT 597 597 S -> L (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066197.
VARIANT 622 622 V -> M (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066198.
VARIANT 628 628 G -> D (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066199.
VARIANT 632 632 I -> R (in CPS1D).
{ECO:0000269|PubMed:21120950,
ECO:0000269|PubMed:24813853}.
/FTId=VAR_066200.
VARIANT 638 638 R -> P (in CPS1D; dbSNP:rs757205958).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066201.
VARIANT 640 640 A -> S (in CPS1D; dbSNP:rs142693704).
{ECO:0000269|PubMed:16737834}.
/FTId=VAR_066143.
VARIANT 648 648 C -> Y (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066202.
VARIANT 651 651 E -> K (in CPS1D).
{ECO:0000269|PubMed:17310273}.
/FTId=VAR_063566.
VARIANT 654 654 D -> V (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066203.
VARIANT 661 661 G -> R (in CPS1D).
{ECO:0000269|PubMed:22173106}.
/FTId=VAR_075807.
VARIANT 674 674 N -> I (in CPS1D).
{ECO:0000269|PubMed:17310273}.
/FTId=VAR_063567.
VARIANT 674 674 N -> K (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066204.
VARIANT 678 678 Q -> P (in CPS1D; results in a poor
enzyme expression and solubility; hampers
correct enzyme folding).
{ECO:0000269|PubMed:20578160}.
/FTId=VAR_064064.
VARIANT 698 698 N -> S (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066205.
VARIANT 716 716 N -> K (in CPS1D; dbSNP:rs369061090).
{ECO:0000269|PubMed:16737834}.
/FTId=VAR_066144.
VARIANT 718 718 R -> K (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066107.
VARIANT 721 721 R -> Q (in CPS1D; dbSNP:rs752339705).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066108.
VARIANT 724 724 A -> P (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066109.
VARIANT 726 726 A -> T (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066110.
VARIANT 767 767 D -> V (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066111.
VARIANT 774 774 P -> L (in CPS1D; the enzyme is
inactive). {ECO:0000269|PubMed:20578160}.
/FTId=VAR_064065.
VARIANT 780 780 R -> H (in CPS1D; dbSNP:rs758724746).
{ECO:0000269|PubMed:17310273,
ECO:0000269|PubMed:21120950}.
/FTId=VAR_063568.
VARIANT 792 792 M -> I (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066112.
VARIANT 803 803 R -> C (in CPS1D; dbSNP:rs201716417).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066145.
VARIANT 803 803 R -> G (in CPS1D; dbSNP:rs201716417).
{ECO:0000269|PubMed:21120950,
ECO:0000269|PubMed:26440671}.
/FTId=VAR_066146.
VARIANT 803 803 R -> S (in CPS1D; dbSNP:rs201716417).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066147.
VARIANT 805 805 F -> L (in CPS1D).
{ECO:0000269|PubMed:16737834}.
/FTId=VAR_066148.
VARIANT 805 805 F -> S (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066149.
VARIANT 810 810 Q -> R (in CPS1D).
{ECO:0000269|PubMed:12955727}.
/FTId=VAR_017563.
VARIANT 814 814 R -> W (in CPS1D; dbSNP:rs772782772).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066150.
VARIANT 816 816 C -> R (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066151.
VARIANT 843 843 L -> S (in CPS1D; associated in cis with
E-875; causes 70% decrease of enzyme
activity; significant decrease in protein
yield). {ECO:0000269|PubMed:12655559,
ECO:0000269|PubMed:15164414,
ECO:0000269|PubMed:24813853}.
/FTId=VAR_017564.
VARIANT 850 850 R -> C (in CPS1D; moderate decrease in
protein yield and partial loss of enzyme
activity). {ECO:0000269|PubMed:17310273,
ECO:0000269|PubMed:24813853}.
/FTId=VAR_063569.
VARIANT 850 850 R -> H (in CPS1D; partial loss of enzyme
activity; dbSNP:rs767694281).
{ECO:0000269|PubMed:15617192,
ECO:0000269|PubMed:21120950,
ECO:0000269|PubMed:24813853,
ECO:0000269|PubMed:26440671}.
/FTId=VAR_030675.
VARIANT 871 871 T -> P (in CPS1D; significant decrease in
protein yield and enzyme activity).
{ECO:0000269|PubMed:24813853}.
/FTId=VAR_075407.
VARIANT 875 875 K -> E (polymorphism; associated in cis
with S-843 in a patient with carbamoyl-
phosphate synthase deficiency; does not
affect enzyme activity; significant
decrease in protein yield and thermal
stability; dbSNP:rs147062907).
{ECO:0000269|PubMed:12655559,
ECO:0000269|PubMed:15164414,
ECO:0000269|PubMed:24813853,
ECO:0000269|PubMed:27535533}.
/FTId=VAR_017565.
VARIANT 911 911 G -> E (in CPS1D; significant decrease in
protein yield and enzyme activity).
{ECO:0000269|PubMed:21120950,
ECO:0000269|PubMed:24813853}.
/FTId=VAR_066152.
VARIANT 911 911 G -> V (in CPS1D; significant decrease in
protein yield and enzyme activity).
{ECO:0000269|PubMed:16737834,
ECO:0000269|PubMed:24813853}.
/FTId=VAR_066153.
VARIANT 913 913 S -> L (in CPS1D; significant decrease in
protein yield and partial loss of enzyme
activity; dbSNP:rs754706559).
{ECO:0000269|PubMed:21120950,
ECO:0000269|PubMed:24813853}.
/FTId=VAR_066154.
VARIANT 914 914 D -> G (in CPS1D; significant decrease in
protein yield and enzyme activity).
{ECO:0000269|PubMed:21120950,
ECO:0000269|PubMed:24813853}.
/FTId=VAR_066155.
VARIANT 914 914 D -> H (in CPS1D; significant decrease in
protein yield and enzyme activity;
dbSNP:rs765484849).
{ECO:0000269|PubMed:21120950,
ECO:0000269|PubMed:24813853}.
/FTId=VAR_066156.
VARIANT 918 918 S -> P (in CPS1D; significant decrease in
protein yield and enzyme activity).
{ECO:0000269|PubMed:15617192,
ECO:0000269|PubMed:24813853}.
/FTId=VAR_030676.
VARIANT 932 932 R -> T (in CPS1D; significant decrease in
protein yield and partial loss of enzyme
activity). {ECO:0000269|PubMed:21120950,
ECO:0000269|PubMed:24813853}.
/FTId=VAR_066157.
VARIANT 937 937 I -> N (in CPS1D; associated with R-401;
significant decrease in protein yield and
enzyme activity; dbSNP:rs760714614).
{ECO:0000269|PubMed:24813853}.
/FTId=VAR_075408.
VARIANT 949 949 A -> T (in CPS1D; partial loss of enzyme
activity and significant decrease in
thermal stability; dbSNP:rs537170841).
{ECO:0000269|PubMed:21120950,
ECO:0000269|PubMed:24813853}.
/FTId=VAR_066158.
VARIANT 958 958 L -> P (in CPS1D; significant decrease in
protein yield and enzyme activity).
{ECO:0000269|PubMed:16737834,
ECO:0000269|PubMed:24813853}.
/FTId=VAR_066159.
VARIANT 959 959 Y -> C (in CPS1D; significant decrease in
protein yield and thermal stability;
partial loss of enzyme activity).
{ECO:0000269|PubMed:21120950,
ECO:0000269|PubMed:24813853}.
/FTId=VAR_066160.
VARIANT 962 962 Y -> C (in CPS1D; significant decrease in
protein yield and partial loss of enzyme
activity). {ECO:0000269|PubMed:21120950,
ECO:0000269|PubMed:24813853}.
/FTId=VAR_066161.
VARIANT 964 964 G -> D (in CPS1D; significant decrease in
protein yield and enzyme activity;
dbSNP:rs534815243).
{ECO:0000269|PubMed:22173106,
ECO:0000269|PubMed:24813853}.
/FTId=VAR_075409.
VARIANT 978 978 V -> E (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066113.
VARIANT 982 982 G -> D (in CPS1D; dbSNP:rs121912595).
{ECO:0000269|PubMed:17310273}.
/FTId=VAR_063570.
VARIANT 982 982 G -> S (in CPS1D; dbSNP:rs757059355).
{ECO:0000269|PubMed:16737834}.
/FTId=VAR_066162.
VARIANT 982 982 G -> V (in CPS1D; dbSNP:rs121912595).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066114.
VARIANT 984 984 Y -> H (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066115.
VARIANT 986 986 I -> T (in CPS1D; associated with V-304).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066116.
VARIANT 987 987 G -> C (in CPS1D; may affect splicing).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066117.
VARIANT 992 992 F -> S (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066118.
VARIANT 998 998 S -> F (in CPS1D).
{ECO:0000269|PubMed:16737834}.
/FTId=VAR_066163.
VARIANT 1016 1016 N -> S (in CPS1D; dbSNP:rs749238466).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066119.
VARIANT 1017 1017 P -> L (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066120.
VARIANT 1022 1022 T -> I (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066121.
VARIANT 1034 1034 E -> G (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066122.
VARIANT 1045 1045 H -> R (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066123.
VARIANT 1054 1054 I -> R (in CPS1D).
{ECO:0000269|PubMed:11388595}.
/FTId=VAR_066164.
VARIANT 1059 1059 Q -> R (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066124.
VARIANT 1065 1065 A -> E (in CPS1D; dbSNP:rs770471782).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066125.
VARIANT 1089 1089 R -> C (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066126.
VARIANT 1089 1089 R -> L (in CPS1D).
{ECO:0000269|PubMed:16737834}.
/FTId=VAR_066165.
VARIANT 1103 1103 Q -> R (in CPS1D).
{ECO:0000269|PubMed:17310273}.
/FTId=VAR_063571.
VARIANT 1141 1141 V -> G (in CPS1D).
{ECO:0000269|PubMed:17310273}.
/FTId=VAR_063572.
VARIANT 1155 1155 A -> E (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066127.
VARIANT 1155 1155 A -> V (in CPS1D; dbSNP:rs766125631).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066128.
VARIANT 1167 1167 T -> R (in CPS1D).
{ECO:0000269|PubMed:22173106}.
/FTId=VAR_075808.
VARIANT 1194 1194 E -> D (in CPS1D).
{ECO:0000269|PubMed:24813853}.
/FTId=VAR_075410.
VARIANT 1195 1195 H -> P (in CPS1D).
{ECO:0000269|PubMed:17310273}.
/FTId=VAR_063573.
VARIANT 1203 1203 S -> L (in CPS1D; dbSNP:rs149518280).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066129.
VARIANT 1203 1203 S -> P (in CPS1D).
{ECO:0000269|PubMed:16737834}.
/FTId=VAR_066166.
VARIANT 1205 1205 D -> N (in CPS1D).
{ECO:0000269|PubMed:16737834}.
/FTId=VAR_066167.
VARIANT 1215 1215 I -> V (in CPS1D; dbSNP:rs141373204).
{ECO:0000269|PubMed:17310273}.
/FTId=VAR_063574.
VARIANT 1228 1228 R -> Q (in CPS1D; dbSNP:rs778117194).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066130.
VARIANT 1241 1241 N -> K (in CPS1D).
{ECO:0000269|PubMed:17310273}.
/FTId=VAR_063575.
VARIANT 1254 1254 I -> F (in CPS1D; unknown pathological
significance).
{ECO:0000269|PubMed:26440671}.
/FTId=VAR_075411.
VARIANT 1255 1255 E -> D (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066131.
VARIANT 1262 1262 R -> P (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066132.
VARIANT 1262 1262 R -> Q (in CPS1D; dbSNP:rs750670270).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066133.
VARIANT 1266 1266 F -> S (in dbSNP:rs1047886).
{ECO:0000269|PubMed:1840546}.
/FTId=VAR_017566.
VARIANT 1274 1274 D -> H (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066134.
VARIANT 1283 1283 M -> L (in dbSNP:rs1047887).
{ECO:0000269|PubMed:1840546}.
/FTId=VAR_017567.
VARIANT 1327 1327 C -> R (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066135.
VARIANT 1331 1331 S -> P (in CPS1D).
{ECO:0000269|PubMed:16737834}.
/FTId=VAR_066168.
VARIANT 1333 1333 G -> E (in CPS1D; dbSNP:rs372645328).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066136.
VARIANT 1363 1366 Missing (in CPS1D; unknown pathological
significance).
{ECO:0000269|PubMed:26440671}.
/FTId=VAR_075412.
VARIANT 1371 1371 R -> L (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066137.
VARIANT 1376 1376 G -> S (polymorphism; no functional
consequences; no negative effect on
protein stability, enzyme activity and
thermal stability; dbSNP:rs140578009).
{ECO:0000269|PubMed:12853138,
ECO:0000269|PubMed:20578160,
ECO:0000269|PubMed:23649895}.
/FTId=VAR_017568.
VARIANT 1378 1378 A -> T (in CPS1D; significant reduction
in thermal stability).
{ECO:0000269|PubMed:16737834,
ECO:0000269|PubMed:23649895}.
/FTId=VAR_066169.
VARIANT 1381 1381 L -> S (in CPS1D; significant loss of
protein stability).
{ECO:0000269|PubMed:23649895}.
/FTId=VAR_075413.
VARIANT 1391 1391 T -> M (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066138.
VARIANT 1398 1398 L -> V (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066139.
VARIANT 1406 1406 T -> N (polymorphism; associated with
susceptibility to neonatal pulmonary
hypertension; also highly associated with
hepatocellular carcinoma progression;
dbSNP:rs1047891).
{ECO:0000269|PubMed:11407344,
ECO:0000269|PubMed:12853138,
ECO:0000269|PubMed:12955727,
ECO:0000269|PubMed:1840546,
ECO:0000269|PubMed:20520828,
ECO:0000269|PubMed:21767969,
ECO:0000269|PubMed:24237036}.
/FTId=VAR_017569.
VARIANT 1411 1411 P -> L (in CPS1D; modestly decreases
enzyme activity).
{ECO:0000269|PubMed:16737834,
ECO:0000269|PubMed:20578160}.
/FTId=VAR_064066.
VARIANT 1439 1439 P -> L (in CPS1D).
{ECO:0000269|PubMed:21120950}.
/FTId=VAR_066140.
VARIANT 1443 1443 T -> A (in CPS1D; almost complete loss of
enzyme activity; approximately 10-fold
decrease in the apparent Vmax for
bicarbonate, ammonia and ATP; decreased
affinity for NAG).
{ECO:0000269|PubMed:16737834,
ECO:0000269|PubMed:23649895}.
/FTId=VAR_066170.
VARIANT 1453 1453 R -> Q (in CPS1D; the enzyme is
inactive). {ECO:0000269|PubMed:20578160}.
/FTId=VAR_064067.
VARIANT 1453 1453 R -> W (in CPS1D; the enzyme is
inactive). {ECO:0000269|PubMed:20578160,
ECO:0000269|PubMed:21120950}.
/FTId=VAR_064068.
VARIANT 1462 1462 P -> R (in CPS1D).
{ECO:0000269|PubMed:21120950,
ECO:0000269|PubMed:24813853}.
/FTId=VAR_066141.
VARIANT 1491 1491 Y -> H (in CPS1D; triggers a large
decrease in the apparent affinity for N-
acetyl-L-glutamate (NAG)).
{ECO:0000269|PubMed:20578160}.
/FTId=VAR_064069.
CONFLICT 111 111 A -> S (in Ref. 1; BAA14328).
{ECO:0000305}.
CONFLICT 279 279 R -> Q (in Ref. 1; BAA14328).
{ECO:0000305}.
CONFLICT 338 338 G -> C (in Ref. 1; BAA14328).
{ECO:0000305}.
CONFLICT 718 722 RLSRS -> KMSPN (in Ref. 1; BAA14328).
{ECO:0000305}.
CONFLICT 729 729 A -> T (in Ref. 1; BAA14328).
{ECO:0000305}.
CONFLICT 749 749 E -> G (in Ref. 1; BAA14328).
{ECO:0000305}.
CONFLICT 912 912 F -> L (in Ref. 6; CAE45707).
{ECO:0000305}.
CONFLICT 1161 1162 EH -> AT (in Ref. 1; BAA14328).
{ECO:0000305}.
CONFLICT 1204 1205 GD -> EN (in Ref. 1; BAA14328).
{ECO:0000305}.
CONFLICT 1254 1254 I -> N (in Ref. 1; BAA14328).
{ECO:0000305}.
CONFLICT 1303 1303 A -> V (in Ref. 1; BAA14328).
{ECO:0000305}.
STRAND 45 50 {ECO:0000244|PDB:5DOT}.
STRAND 55 60 {ECO:0000244|PDB:5DOT}.
STRAND 67 74 {ECO:0000244|PDB:5DOT}.
HELIX 80 83 {ECO:0000244|PDB:5DOT}.
HELIX 87 89 {ECO:0000244|PDB:5DOT}.
STRAND 92 101 {ECO:0000244|PDB:5DOT}.
STRAND 116 125 {ECO:0000244|PDB:5DOT}.
STRAND 129 132 {ECO:0000244|PDB:5DOT}.
STRAND 134 136 {ECO:0000244|PDB:5DOT}.
HELIX 149 155 {ECO:0000244|PDB:5DOT}.
STRAND 160 163 {ECO:0000244|PDB:5DOT}.
HELIX 166 173 {ECO:0000244|PDB:5DOT}.
STRAND 179 185 {ECO:0000244|PDB:5DOT}.
HELIX 195 197 {ECO:0000244|PDB:5DOT}.
HELIX 200 204 {ECO:0000244|PDB:5DOT}.
STRAND 210 213 {ECO:0000244|PDB:5DOT}.
STRAND 217 226 {ECO:0000244|PDB:5DOT}.
HELIX 229 237 {ECO:0000244|PDB:5DOT}.
STRAND 240 246 {ECO:0000244|PDB:5DOT}.
STRAND 257 263 {ECO:0000244|PDB:5DOT}.
HELIX 268 270 {ECO:0000244|PDB:5DOT}.
HELIX 272 283 {ECO:0000244|PDB:5DOT}.
STRAND 290 294 {ECO:0000244|PDB:5DOT}.
HELIX 295 304 {ECO:0000244|PDB:5DOT}.
STRAND 308 324 {ECO:0000244|PDB:5DOT}.
TURN 325 327 {ECO:0000244|PDB:5DOT}.
STRAND 330 341 {ECO:0000244|PDB:5DOT}.
STRAND 349 355 {ECO:0000244|PDB:5DOT}.
TURN 356 358 {ECO:0000244|PDB:5DOT}.
STRAND 361 376 {ECO:0000244|PDB:5DOT}.
STRAND 381 383 {ECO:0000244|PDB:5DOT}.
HELIX 389 400 {ECO:0000244|PDB:5DOT}.
HELIX 407 409 {ECO:0000244|PDB:5DOT}.
STRAND 423 428 {ECO:0000244|PDB:5DOT}.
STRAND 435 437 {ECO:0000244|PDB:5DOT}.
HELIX 445 454 {ECO:0000244|PDB:5DOT}.
STRAND 458 462 {ECO:0000244|PDB:5DOT}.
HELIX 469 471 {ECO:0000244|PDB:5DOT}.
STRAND 473 475 {ECO:0000244|PDB:5DOU}.
STRAND 480 483 {ECO:0000244|PDB:5DOT}.
HELIX 489 499 {ECO:0000244|PDB:5DOT}.
STRAND 502 505 {ECO:0000244|PDB:5DOT}.
STRAND 507 509 {ECO:0000244|PDB:5DOT}.
HELIX 510 522 {ECO:0000244|PDB:5DOT}.
HELIX 527 530 {ECO:0000244|PDB:4UTV}.
HELIX 538 545 {ECO:0000244|PDB:5DOT}.
HELIX 547 555 {ECO:0000244|PDB:5DOT}.
TURN 556 558 {ECO:0000244|PDB:5DOT}.
STRAND 563 569 {ECO:0000244|PDB:5DOU}.
HELIX 570 580 {ECO:0000244|PDB:5DOU}.
STRAND 582 590 {ECO:0000244|PDB:5DOU}.
TURN 593 596 {ECO:0000244|PDB:5DOU}.
STRAND 598 602 {ECO:0000244|PDB:5DOU}.
HELIX 603 614 {ECO:0000244|PDB:5DOU}.
STRAND 620 624 {ECO:0000244|PDB:5DOU}.
STRAND 629 638 {ECO:0000244|PDB:5DOT}.
STRAND 644 653 {ECO:0000244|PDB:5DOT}.
HELIX 660 662 {ECO:0000244|PDB:5DOU}.
STRAND 665 668 {ECO:0000244|PDB:5DOT}.
HELIX 674 690 {ECO:0000244|PDB:5DOT}.
STRAND 695 703 {ECO:0000244|PDB:5DOT}.
STRAND 710 716 {ECO:0000244|PDB:5DOT}.
HELIX 721 730 {ECO:0000244|PDB:5DOT}.
HELIX 734 742 {ECO:0000244|PDB:5DOT}.
HELIX 747 749 {ECO:0000244|PDB:5DOT}.
TURN 753 755 {ECO:0000244|PDB:5DOT}.
STRAND 756 760 {ECO:0000244|PDB:5DOT}.
STRAND 767 775 {ECO:0000244|PDB:5DOT}.
STRAND 796 804 {ECO:0000244|PDB:5DOT}.
HELIX 805 816 {ECO:0000244|PDB:5DOT}.
HELIX 828 830 {ECO:0000244|PDB:5DOT}.
HELIX 839 844 {ECO:0000244|PDB:5DOT}.
HELIX 850 859 {ECO:0000244|PDB:5DOT}.
HELIX 864 871 {ECO:0000244|PDB:5DOT}.
HELIX 875 892 {ECO:0000244|PDB:5DOT}.
TURN 896 898 {ECO:0000244|PDB:5DOT}.
HELIX 901 909 {ECO:0000244|PDB:5DOT}.
HELIX 914 921 {ECO:0000244|PDB:5DOT}.
HELIX 925 934 {ECO:0000244|PDB:5DOT}.
STRAND 940 943 {ECO:0000244|PDB:5DOT}.
STRAND 957 963 {ECO:0000244|PDB:5DOT}.
STRAND 976 979 {ECO:0000244|PDB:5DOT}.
HELIX 991 1005 {ECO:0000244|PDB:5DOT}.
STRAND 1010 1014 {ECO:0000244|PDB:5DOT}.
TURN 1024 1026 {ECO:0000244|PDB:5DOT}.
STRAND 1027 1032 {ECO:0000244|PDB:5DOT}.
HELIX 1037 1047 {ECO:0000244|PDB:5DOT}.
STRAND 1050 1053 {ECO:0000244|PDB:5DOT}.
STRAND 1055 1057 {ECO:0000244|PDB:5DOU}.
HELIX 1059 1063 {ECO:0000244|PDB:5DOT}.
HELIX 1065 1070 {ECO:0000244|PDB:5DOT}.
HELIX 1080 1087 {ECO:0000244|PDB:5DOT}.
HELIX 1089 1098 {ECO:0000244|PDB:5DOT}.
STRAND 1106 1109 {ECO:0000244|PDB:5DOT}.
HELIX 1112 1122 {ECO:0000244|PDB:5DOT}.
STRAND 1126 1129 {ECO:0000244|PDB:5DOT}.
STRAND 1140 1142 {ECO:0000244|PDB:5DOT}.
HELIX 1145 1151 {ECO:0000244|PDB:5DOT}.
STRAND 1164 1167 {ECO:0000244|PDB:5DOT}.
STRAND 1174 1183 {ECO:0000244|PDB:5DOT}.
STRAND 1186 1197 {ECO:0000244|PDB:5DOT}.
HELIX 1203 1205 {ECO:0000244|PDB:5DOU}.
STRAND 1208 1211 {ECO:0000244|PDB:5DOT}.
HELIX 1217 1233 {ECO:0000244|PDB:5DOT}.
STRAND 1238 1247 {ECO:0000244|PDB:5DOT}.
STRAND 1250 1259 {ECO:0000244|PDB:5DOT}.
HELIX 1264 1271 {ECO:0000244|PDB:5DOT}.
HELIX 1275 1283 {ECO:0000244|PDB:5DOT}.
STRAND 1296 1298 {ECO:0000244|PDB:5DOT}.
STRAND 1306 1310 {ECO:0000244|PDB:5DOT}.
STRAND 1312 1318 {ECO:0000244|PDB:5DOT}.
STRAND 1322 1324 {ECO:0000244|PDB:5DOT}.
STRAND 1327 1332 {ECO:0000244|PDB:5DOT}.
STRAND 1335 1341 {ECO:0000244|PDB:5DOT}.
HELIX 1344 1350 {ECO:0000244|PDB:2YVQ}.
STRAND 1360 1365 {ECO:0000244|PDB:2YVQ}.
HELIX 1368 1370 {ECO:0000244|PDB:2YVQ}.
HELIX 1371 1382 {ECO:0000244|PDB:2YVQ}.
TURN 1383 1385 {ECO:0000244|PDB:2YVQ}.
STRAND 1387 1391 {ECO:0000244|PDB:2YVQ}.
HELIX 1392 1400 {ECO:0000244|PDB:2YVQ}.
STRAND 1406 1408 {ECO:0000244|PDB:2YVQ}.
HELIX 1411 1413 {ECO:0000244|PDB:2YVQ}.
STRAND 1418 1421 {ECO:0000244|PDB:5DOT}.
HELIX 1423 1428 {ECO:0000244|PDB:2YVQ}.
STRAND 1434 1437 {ECO:0000244|PDB:2YVQ}.
HELIX 1443 1445 {ECO:0000244|PDB:2YVQ}.
HELIX 1446 1458 {ECO:0000244|PDB:2YVQ}.
HELIX 1467 1475 {ECO:0000244|PDB:2YVQ}.
TURN 1486 1491 {ECO:0000244|PDB:5DOT}.
SEQUENCE 1500 AA; 164939 MW; E53A22D77563961D CRC64;
MTRILTAFKV VRTLKTGFGF TNVTAHQKWK FSRPGIRLLS VKAQTAHIVL EDGTKMKGYS
FGHPSSVAGE VVFNTGLGGY PEAITDPAYK GQILTMANPI IGNGGAPDTT ALDELGLSKY
LESNGIKVSG LLVLDYSKDY NHWLATKSLG QWLQEEKVPA IYGVDTRMLT KIIRDKGTML
GKIEFEGQPV DFVDPNKQNL IAEVSTKDVK VYGKGNPTKV VAVDCGIKNN VIRLLVKRGA
EVHLVPWNHD FTKMEYDGIL IAGGPGNPAL AEPLIQNVRK ILESDRKEPL FGISTGNLIT
GLAAGAKTYK MSMANRGQNQ PVLNITNKQA FITAQNHGYA LDNTLPAGWK PLFVNVNDQT
NEGIMHESKP FFAVQFHPEV TPGPIDTEYL FDSFFSLIKK GKATTITSVL PKPALVASRV
EVSKVLILGS GGLSIGQAGE FDYSGSQAVK AMKEENVKTV LMNPNIASVQ TNEVGLKQAD
TVYFLPITPQ FVTEVIKAEQ PDGLILGMGG QTALNCGVEL FKRGVLKEYG VKVLGTSVES
IMATEDRQLF SDKLNEINEK IAPSFAVESI EDALKAADTI GYPVMIRSAY ALGGLGSGIC
PNRETLMDLS TKAFAMTNQI LVEKSVTGWK EIEYEVVRDA DDNCVTVCNM ENVDAMGVHT
GDSVVVAPAQ TLSNAEFQML RRTSINVVRH LGIVGECNIQ FALHPTSMEY CIIEVNARLS
RSSALASKAT GYPLAFIAAK IALGIPLPEI KNVVSGKTSA CFEPSLDYMV TKIPRWDLDR
FHGTSSRIGS SMKSVGEVMA IGRTFEESFQ KALRMCHPSI EGFTPRLPMN KEWPSNLDLR
KELSEPSSTR IYAIAKAIDD NMSLDEIEKL TYIDKWFLYK MRDILNMEKT LKGLNSESMT
EETLKRAKEI GFSDKQISKC LGLTEAQTRE LRLKKNIHPW VKQIDTLAAE YPSVTNYLYV
TYNGQEHDVN FDDHGMMVLG CGPYHIGSSV EFDWCAVSSI RTLRQLGKKT VVVNCNPETV
STDFDECDKL YFEELSLERI LDIYHQEACG GCIISVGGQI PNNLAVPLYK NGVKIMGTSP
LQIDRAEDRS IFSAVLDELK VAQAPWKAVN TLNEALEFAK SVDYPCLLRP SYVLSGSAMN
VVFSEDEMKK FLEEATRVSQ EHPVVLTKFV EGAREVEMDA VGKDGRVISH AISEHVEDAG
VHSGDATLML PTQTISQGAI EKVKDATRKI AKAFAISGPF NVQFLVKGND VLVIECNLRA
SRSFPFVSKT LGVDFIDVAT KVMIGENVDE KHLPTLDHPI IPADYVAIKA PMFSWPRLRD
ADPILRCEMA STGEVACFGE GIHTAFLKAM LSTGFKIPQK GILIGIQQSF RPRFLGVAEQ
LHNEGFKLFA TEATSDWLNA NNVPATPVAW PSQEGQNPSL SSIRKLIRDG SIDLVINLPN
NNTKFVHDNY VIRRTAVDSG IPLLTNFQVT KLFAEAVQKS RKVDSKSLFH YRQYSAGKAA


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