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Argininosuccinate synthase (EC 6.3.4.5) (Citrulline--aspartate ligase)

 ASSY_HUMAN              Reviewed;         412 AA.
P00966; Q6LDL2; Q86UZ0; Q96GT4;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
03-APR-2002, sequence version 2.
25-OCT-2017, entry version 200.
RecName: Full=Argininosuccinate synthase {ECO:0000305};
EC=6.3.4.5 {ECO:0000269|PubMed:18473344, ECO:0000269|PubMed:27287393, ECO:0000269|PubMed:8792870};
AltName: Full=Citrulline--aspartate ligase;
Name=ASS1 {ECO:0000312|HGNC:HGNC:758};
Synonyms=ASS {ECO:0000312|HGNC:HGNC:758};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6194510; DOI=10.1093/nar/11.18.6505;
Bock H.-G.O., Su T.-S., O'Brien W.E., Beaudet A.L.;
"Sequence for human argininosuccinate synthetase cDNA.";
Nucleic Acids Res. 11:6505-6512(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6321498;
Freytag S.O., Bock H.-G.O., Beaudet A.L., O'Brien W.E.;
"Molecular structures of human argininosuccinate synthetase
pseudogenes. Evolutionary and mechanistic implications.";
J. Biol. Chem. 259:3160-3166(1984).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CTLN1 LEU-108;
ARG-179; VAL-362 AND ARG-390.
PubMed=11941481; DOI=10.1007/s00439-002-0686-6;
Haeberle J., Pauli S., Linnebank M., Kleijer W.J., Bakker H.D.,
Wanders R.J.A., Harms E., Koch H.G.;
"Structure of the human argininosuccinate synthetase gene and an
improved system for molecular diagnostics in patients with classical
and mild citrullinemia.";
Hum. Genet. 110:327-333(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Small intestine;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney, and Muscle;
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).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
PubMed=3027451; DOI=10.1007/BF01819307;
Jinno Y., Nomiyama H., Matuo S., Shimada K., Matsuda I., Saheki T.;
"Structure of the 5' end region of the human argininosuccinate
synthetase gene.";
J. Inherit. Metab. Dis. 8:157-159(1985).
[7]
PROTEIN SEQUENCE OF 148-161.
PubMed=2788888;
Isashiki Y., Noda T., Kobayashi K., Sase M., Saheki T., Titani K.;
"Identification of essential arginine residue(s) for Mg-ATP binding of
human argininosuccinate synthetase.";
Protein Seq. Data Anal. 2:283-287(1989).
[8]
PROTEIN SEQUENCE OF 200-209.
TISSUE=Colon carcinoma;
PubMed=9150948; DOI=10.1002/elps.1150180344;
Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.;
"A two-dimensional gel database of human colon carcinoma proteins.";
Electrophoresis 18:605-613(1997).
[9]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=1708740; DOI=10.1016/0378-1119(91)90125-U;
Surh L.C., Beaudet A.L., O'Brien W.E.;
"Molecular characterization of the murine argininosuccinate synthetase
locus.";
Gene 99:181-189(1991).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180 AND THR-219, 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).
[11]
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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-219, 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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-113 AND THR-219, 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).
[14]
CHARACTERIZATION OF VARIANTS CLNT1 VAL-192; ARG-280; CYS-272 AND
TRP-304, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
PubMed=8792870;
Shaheen N., Kobayashi K., Terazono H., Fukushige T., Horiuchi M.,
Saheki T.;
"Characterization of human wild-type and mutant argininosuccinate
synthetase proteins expressed in bacterial cells.";
Enzyme Protein 48:251-264(1994).
[15]
INTERACTION WITH NMRAL1.
PubMed=17496144; DOI=10.1073/pnas.0700480104;
Zheng X., Dai X., Zhao Y., Chen Q., Lu F., Yao D., Yu Q., Liu X.,
Zhang C., Gu X., Luo M.;
"Restructuring of the dinucleotide-binding fold in an NADP(H) sensor
protein.";
Proc. Natl. Acad. Sci. U.S.A. 104:8809-8814(2007).
[16]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH CITRULLINE AND
ASPARTATE, AND SUBUNIT.
PubMed=18323623; DOI=10.1107/S0907444907067455;
Karlberg T., Collins R., van den Berg S., Flores A., Hammarstrom M.,
Hogbom M., Holmberg Schiavone L., Uppenberg J.;
"Structure of human argininosuccinate synthetase.";
Acta Crystallogr. D 64:279-286(2008).
[17]
INVOLVEMENT IN CTLN1, AND VARIANTS CTLN1 SER-14; HIS-157; ASN-180;
TRP-304; SER-324; TRP-363 AND ARG-390.
PubMed=2358466;
Kobayashi K., Jackson M.J., Tick D.B., O'Brien W.E., Beaudet A.L.;
"Heterogeneity of mutations in argininosuccinate synthetase causing
human citrullinemia.";
J. Biol. Chem. 265:11361-11367(1990).
[18]
VARIANTS CTLN1 LEU-18 AND CYS-86.
PubMed=1943692;
Kobayashi K., Rosenbloom C., Beaudet A.L., O'Brien W.E.;
"Additional mutations in argininosuccinate synthetase causing
citrullinemia.";
Mol. Biol. Med. 8:95-100(1991).
[19]
VARIANTS CTLN1 THR-118; VAL-192; CYS-272; ARG-280; TRP-304 AND
LEU-363.
PubMed=7977368;
Kobayashi K., Shaheen N., Terazono H., Saheki T.;
"Mutations in argininosuccinate synthetase mRNA of Japanese patients,
causing classical citrullinemia.";
Am. J. Hum. Genet. 55:1103-1112(1994).
[20]
VARIANTS CTLN1 ALA-69; LEU-108; ASP-117; ILE-119; GLN-270 AND ARG-390.
PubMed=11708871; DOI=10.1006/mgme.2001.3221;
Vilaseca M.A., Kobayashi K., Briones P., Lambruschini N.,
Campistol J., Tabata A., Alomar A., Rodes M., Lluch M., Saheki T.;
"Phenotype and genotype heterogeneity in Mediterranean
citrullinemia.";
Mol. Genet. Metab. 74:396-398(2001).
[21]
VARIANTS CTLN1 ARG-19; HIS-86; SER-95; SER-96; ASP-117; SER-117;
CYS-157; ARG-179; LYS-191; HIS-265; MET-269; CYS-272; LYS-283;
TRP-304; GLN-310; SER-324; VAL-362; GLN-363; TRP-363; ILE-389 AND
ARG-390.
PubMed=12815590; DOI=10.1002/humu.10230;
Gao H.-Z., Kobayashi K., Tabata A., Tsuge H., Iijima M., Yasuda T.,
Kalkanoglu H.S., Dursun A., Tokatli A., Coskun T., Trefz F.K.,
Skladal D., Mandel H., Seidel J., Kodama S., Shirane S., Ichida T.,
Makino S., Yoshino M., Kang J.-H., Mizuguchi M., Barshop B.A.,
Fuchinoue S., Seneca S., Zeesman S., Knerr I., Rodes M., Wasant P.,
Yoshida I., De Meirleir L., Abdul-Jalil M., Begum L., Horiuchi M.,
Katunuma N., Nakagawa S., Saheki T.;
"Identification of 16 novel mutations in the argininosuccinate
synthetase gene and genotype-phenotype correlation in 38 classical
citrullinemia patients.";
Hum. Mutat. 22:24-34(2003).
[22]
VARIANTS CTLN1 SER-14; LEU-40; GLN-127; ARG-179; ASP-190; GLU-202;
MET-263; MET-269; SER-324; GLY-345 AND VAL-362.
PubMed=14680976; DOI=10.1016/j.ymgme.2003.08.002;
Haeberle J., Pauli S., Schmidt E., Schulze-Eilfing B., Berning C.,
Koch H.G.;
"Mild citrullinemia in Caucasians is an allelic variant of
argininosuccinate synthetase deficiency (citrullinemia type 1).";
Mol. Genet. Metab. 80:302-306(2003).
[23]
VARIANT CTLN1 ARG-310.
PubMed=15863597; DOI=10.1097/01.AOG.0000157769.90230.24;
Enns G.M., O'Brien W.E., Kobayashi K., Shinzawa H., Pellegrino J.E.;
"Postpartum 'psychosis' in mild argininosuccinate synthetase
deficiency.";
Obstet. Gynecol. 105:1244-1246(2005).
[24]
VARIANTS CTLN1 ASN-124; HIS-157; GLN-270; GLN-279; LYS-283; SER-324;
GLY-363 AND ARG-390.
PubMed=16475226; DOI=10.1002/pd.1390;
Kleijer W.J., Garritsen V.H., van der Sterre M.L., Berning C.,
Haeberle J., Huijmans J.G.M.;
"Prenatal diagnosis of citrullinemia and argininosuccinic aciduria:
evidence for a transmission ratio distortion in citrullinemia.";
Prenat. Diagn. 26:242-247(2006).
[25]
VARIANTS CTLN1 CYS-265 AND VAL-302, CHARACTERIZATION OF VARIANTS CTLN1
THR-118; ARG-179; VAL-263; CYS-265; VAL-302; SER-324; VAL-362 AND
ARG-390, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND BIOPHYSICOCHEMICAL
PROPERTIES.
PubMed=18473344; DOI=10.1002/humu.20784;
Berning C., Bieger I., Pauli S., Vermeulen T., Vogl T., Rummel T.,
Hoehne W., Koch H.G., Rolinski B., Gempel K., Haeberle J.;
"Investigation of citrullinemia type I variants by in vitro expression
studies.";
Hum. Mutat. 29:1222-1227(2008).
[26]
VARIANTS CTLN1 PRO-79; HIS-96; GLN-127; TRP-127; PRO-160; GLN-191;
PRO-206; CYS-265; THR-277; ILE-284; SER-291; GLY-296; VAL-324;
PHE-341; ARG-347 AND ASP-359.
PubMed=19006241; DOI=10.1002/humu.20847;
Engel K., Hoehne W., Haeberle J.;
"Mutations and polymorphisms in the human argininosuccinate synthetase
(ASS1) gene.";
Hum. Mutat. 30:300-307(2009).
[27]
VARIANTS CTLN1 LYS-283 AND ARG-337.
PubMed=23611581; DOI=10.1016/j.braindev.2013.03.005;
Wu T.F., Liu Y.P., Li X.Y., Wang Q., Song J.Q., Yang Y.L.;
"Prenatal diagnosis of citrullinemia type 1: a Chinese family with a
novel mutation of the ASS1 gene.";
Brain Dev. 36:264-267(2014).
[28]
VARIANTS CTLN1 PRO-91; CYS-157; ILE-180; LYS-283 AND ARG-390, AND
VARIANT LEU-127.
PubMed=24889030; DOI=10.1016/j.ymgme.2014.05.004;
Miller M.J., Soler-Alfonso C.R., Grund J.E., Fang P., Sun Q.,
Elsea S.H., Sutton V.R.;
"Improved standards for prenatal diagnosis of citrullinemia.";
Mol. Genet. Metab. 112:205-209(2014).
[29]
VARIANTS CTLN1 GLY-141 AND CYS-265.
PubMed=25179242; DOI=10.1016/j.cca.2014.08.028;
Kimani J.K., Wei T., Chol K., Li Y., Yu P., Ye S., Huang X., Qi M.;
"Functional analysis of novel splicing and missense mutations
identified in the ASS1 gene in classical citrullinemia patients.";
Clin. Chim. Acta 438:323-329(2015).
[30]
VARIANTS CTLN1 PRO-91; LEU-96; SER-117; THR-118; ILE-119; ASN-124;
CYS-157; HIS-157; CYS-272; HIS-272 AND LEU-272, CHARACTERIZATION OF
VARIANTS CTLN1 PRO-91; SER-95; HIS-96; LEU-96; SER-96; SER-117;
THR-118; ILE-119; ASN-124; GLN-127; TRP-127; CYS-157; HIS-157;
ASN-180; ILE-180; GLN-191; GLN-270; CYS-272; HIS-272 AND LEU-272,
CHARACTERIZATION OF VARIANT LEU-127, CATALYTIC ACTIVITY, PATHWAY,
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=27287393; DOI=10.1136/jmedgenet-2016-103937;
Diez-Fernandez C., Wellauer O., Gemperle C., Ruefenacht V.,
Fingerhut R., Haeberle J.;
"Kinetic mutations in argininosuccinate synthetase deficiency:
characterisation and in vitro correction by substrate
supplementation.";
J. Med. Genet. 53:710-719(2016).
[31]
VARIANTS CTLN1 27-GLN--LYS-412 DEL; ILE-64; PRO-79; 97-CYS--LYS-412
DEL; CYS-100; HIS-100; ASP-111; CYS-117; 138-GLN--LYS-412 DEL;
SER-157; PRO-160; 163-TYR--LYS-412 DEL; PRO-164; LYS-184; ASP-190;
PRO-206; ARG-230; ILE-237; PRO-258; VAL-258; CYS-265; 275-GLY--LYS-412
DEL; THR-277; 279-ARG--LYS-412 DEL; ILE-284; PRO-290; SER-291;
GLY-296; ASP-299; VAL-302; GLY-306; CYS-307; 311-GLN--LYS-412 DEL;
MET-321; SER-324; VAL-324; HIS-335; PHE-341; 344-ARG--LYS-412 DEL;
ARG-347; VAL-356; 357-GLN--LYS-412 DEL; ASP-359; 380-GLN--LYS-412 DEL
AND PRO-389.
PubMed=28111830; DOI=10.1002/humu.23184;
Diez-Fernandez C., Ruefenacht V., Haeberle J.;
"Mutations in the human argininosuccinate synthetase (ASS1) gene,
impact on patients, common changes, and structural considerations.";
Hum. Mutat. 38:471-484(2017).
-!- FUNCTION: One of the enzymes of the urea cycle, the metabolic
pathway transforming neurotoxic amonia produced by protein
catabolism into inocuous urea in the liver of ureotelic animals.
Catalyzes the formation of arginosuccinate from aspartate,
citrulline and ATP and together with ASL it is responsible for the
biosynthesis of arginine in most body tissues.
{ECO:0000305|PubMed:18473344, ECO:0000305|PubMed:27287393,
ECO:0000305|PubMed:8792870}.
-!- CATALYTIC ACTIVITY: ATP + L-citrulline + L-aspartate = AMP +
diphosphate + N(omega)-(L-arginino)succinate.
{ECO:0000269|PubMed:18473344, ECO:0000269|PubMed:27287393,
ECO:0000269|PubMed:8792870}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=112 uM for citrulline (at pH 7.0 and 37 degrees Celsius)
{ECO:0000269|PubMed:18473344};
KM=68 uM for aspartate (at pH 7.0 and 37 degrees Celsius)
{ECO:0000269|PubMed:18473344};
Vmax=143 nmol/min/mg enzyme toward citrulline (at pH 7.0 and 37
degrees Celsius) {ECO:0000269|PubMed:18473344};
Vmax=116 nmol/min/mg enzyme toward aspartate (at pH 7.0 and 37
degrees {ECO:0000269|PubMed:18473344};
-!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
arginine from L-ornithine and carbamoyl phosphate: step 2/3.
{ECO:0000305|PubMed:18473344, ECO:0000305|PubMed:27287393,
ECO:0000305|PubMed:8792870}.
-!- PATHWAY: Nitrogen metabolism; urea cycle; (N(omega)-L-
arginino)succinate from L-aspartate and L-citrulline: step 1/1.
{ECO:0000305|PubMed:18473344, ECO:0000305|PubMed:27287393,
ECO:0000305|PubMed:8792870}.
-!- SUBUNIT: Homotetramer (PubMed:18323623). Interacts with NMRAL1
(PubMed:17496144). {ECO:0000269|PubMed:17496144,
ECO:0000269|PubMed:18323623}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-536842, EBI-536842;
P10398:ARAF; NbExp=4; IntAct=EBI-536842, EBI-365961;
Q9HBL8:NMRAL1; NbExp=3; IntAct=EBI-536842, EBI-2862643;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000305|PubMed:27287393}.
-!- TISSUE SPECIFICITY: Expressed in adult liver.
{ECO:0000269|PubMed:1708740}.
-!- DEVELOPMENTAL STAGE: Expressed in fetal liver and kidney.
{ECO:0000269|PubMed:1708740}.
-!- DISEASE: Citrullinemia 1 (CTLN1) [MIM:215700]: The classic form of
citrullinemia, an autosomal recessive disease characterized
primarily by elevated serum and urine citrulline levels. Ammonia
intoxication is another manifestation. It is a disorder of the
urea cycle, usually manifesting in the first few days of life.
Affected infants appear normal at birth, but as ammonia builds up
in the body they present symptoms such as lethargy, poor feeding,
vomiting, seizures and loss of consciousness. Less commonly, a
milder form can develop later in childhood or adulthood.
{ECO:0000269|PubMed:11708871, ECO:0000269|PubMed:11941481,
ECO:0000269|PubMed:12815590, ECO:0000269|PubMed:14680976,
ECO:0000269|PubMed:15863597, ECO:0000269|PubMed:16475226,
ECO:0000269|PubMed:18473344, ECO:0000269|PubMed:19006241,
ECO:0000269|PubMed:1943692, ECO:0000269|PubMed:2358466,
ECO:0000269|PubMed:23611581, ECO:0000269|PubMed:24889030,
ECO:0000269|PubMed:25179242, ECO:0000269|PubMed:27287393,
ECO:0000269|PubMed:28111830, ECO:0000269|PubMed:7977368}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type
1 subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Argininosuccinate synthetase 1 (ASS1);
Note=Leiden Open Variation Database (LOVD);
URL="http://www.lovd.nl/ASS1";
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EMBL; X01630; CAA25771.1; -; mRNA.
EMBL; L00084; AAA51783.1; -; Genomic_DNA.
EMBL; L00079; AAA51783.1; JOINED; Genomic_DNA.
EMBL; L00080; AAA51783.1; JOINED; Genomic_DNA.
EMBL; L00081; AAA51783.1; JOINED; Genomic_DNA.
EMBL; L00082; AAA51783.1; JOINED; Genomic_DNA.
EMBL; L00083; AAA51783.1; JOINED; Genomic_DNA.
EMBL; AY034076; AAK67487.1; -; Genomic_DNA.
EMBL; AK027126; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC009243; AAH09243.1; -; mRNA.
EMBL; BC021676; AAH21676.1; -; mRNA.
EMBL; M34903; AAA51782.1; -; Genomic_DNA.
CCDS; CCDS6933.1; -.
PIR; A01195; AJHURS.
RefSeq; NP_000041.2; NM_000050.4.
RefSeq; NP_446464.1; NM_054012.3.
RefSeq; XP_005272257.1; XM_005272200.3.
UniGene; Hs.160786; -.
PDB; 2NZ2; X-ray; 2.40 A; A=1-412.
PDBsum; 2NZ2; -.
ProteinModelPortal; P00966; -.
SMR; P00966; -.
BioGrid; 106937; 89.
DIP; DIP-34055N; -.
IntAct; P00966; 25.
MINT; MINT-5000467; -.
STRING; 9606.ENSP00000253004; -.
DrugBank; DB00171; Adenosine triphosphate.
DrugBank; DB00125; L-Arginine.
DrugBank; DB00128; L-Aspartic Acid.
DrugBank; DB00155; L-Citrulline.
iPTMnet; P00966; -.
PhosphoSitePlus; P00966; -.
BioMuta; ASS1; -.
DMDM; 20141195; -.
EPD; P00966; -.
PaxDb; P00966; -.
PeptideAtlas; P00966; -.
PRIDE; P00966; -.
DNASU; 445; -.
Ensembl; ENST00000352480; ENSP00000253004; ENSG00000130707.
Ensembl; ENST00000372393; ENSP00000361469; ENSG00000130707.
Ensembl; ENST00000372394; ENSP00000361471; ENSG00000130707.
GeneID; 445; -.
KEGG; hsa:445; -.
CTD; 445; -.
DisGeNET; 445; -.
EuPathDB; HostDB:ENSG00000130707.17; -.
GeneCards; ASS1; -.
GeneReviews; ASS1; -.
H-InvDB; HIX0025782; -.
HGNC; HGNC:758; ASS1.
HPA; HPA020896; -.
HPA; HPA020934; -.
MalaCards; ASS1; -.
MIM; 215700; phenotype.
MIM; 603470; gene.
neXtProt; NX_P00966; -.
OpenTargets; ENSG00000130707; -.
Orphanet; 247546; Acute neonatal citrullinemia type I.
Orphanet; 247573; Adult-onset citrullinemia type I.
PharmGKB; PA162376926; -.
eggNOG; KOG1706; Eukaryota.
eggNOG; COG0137; LUCA.
GeneTree; ENSGT00390000004524; -.
HOGENOM; HOG000230093; -.
HOVERGEN; HBG001717; -.
InParanoid; P00966; -.
KO; K01940; -.
OMA; GVGRIDM; -.
OrthoDB; EOG091G0AIR; -.
PhylomeDB; P00966; -.
TreeFam; TF300736; -.
BioCyc; MetaCyc:HS05425-MONOMER; -.
BRENDA; 6.3.4.5; 2681.
Reactome; R-HSA-70635; Urea cycle.
SABIO-RK; P00966; -.
UniPathway; UPA00068; UER00113.
UniPathway; UPA00158; UER00272.
EvolutionaryTrace; P00966; -.
GeneWiki; Argininosuccinate_synthetase_1; -.
GenomeRNAi; 445; -.
PRO; PR:P00966; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000130707; -.
CleanEx; HS_ASS1; -.
ExpressionAtlas; P00966; baseline and differential.
Genevisible; P00966; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0016597; F:amino acid binding; IMP:BHF-UCL.
GO; GO:0004055; F:argininosuccinate synthase activity; IMP:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0006526; P:arginine biosynthetic process; IMP:UniProtKB.
GO; GO:0000053; P:argininosuccinate metabolic process; IMP:BHF-UCL.
GO; GO:0006531; P:aspartate metabolic process; IMP:BHF-UCL.
GO; GO:0071499; P:cellular response to laminar fluid shear stress; IMP:BHF-UCL.
GO; GO:0000052; P:citrulline metabolic process; IMP:BHF-UCL.
GO; GO:1903038; P:negative regulation of leukocyte cell-cell adhesion; IMP:BHF-UCL.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:BHF-UCL.
GO; GO:0000050; P:urea cycle; IMP:UniProtKB.
CDD; cd01999; Argininosuccinate_Synthase; 1.
Gene3D; 3.40.50.620; -; 1.
Gene3D; 3.90.1260.10; -; 1.
HAMAP; MF_00005; Arg_succ_synth_type1; 1.
InterPro; IPR001518; Arginosuc_synth.
InterPro; IPR018223; Arginosuc_synth_CS.
InterPro; IPR023434; Arginosuc_synth_type_1_subfam.
InterPro; IPR024074; AS_cat/multimer_dom_body.
InterPro; IPR014729; Rossmann-like_a/b/a_fold.
PANTHER; PTHR11587; PTHR11587; 1.
Pfam; PF00764; Arginosuc_synth; 1.
TIGRFAMs; TIGR00032; argG; 1.
PROSITE; PS00564; ARGININOSUCCIN_SYN_1; 1.
PROSITE; PS00565; ARGININOSUCCIN_SYN_2; 1.
1: Evidence at protein level;
3D-structure; Amino-acid biosynthesis; Arginine biosynthesis;
ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing;
Disease mutation; Ligase; Nucleotide-binding; Phosphoprotein;
Polymorphism; Reference proteome; Urea cycle.
CHAIN 1 412 Argininosuccinate synthase.
/FTId=PRO_0000148554.
NP_BIND 10 18 ATP. {ECO:0000250}.
NP_BIND 115 123 ATP. {ECO:0000250}.
BINDING 36 36 ATP; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 87 87 Citrulline.
{ECO:0000269|PubMed:18323623}.
BINDING 92 92 Citrulline.
{ECO:0000269|PubMed:18323623}.
BINDING 119 119 Aspartate. {ECO:0000269|PubMed:18323623}.
BINDING 123 123 Aspartate. {ECO:0000269|PubMed:18323623}.
BINDING 123 123 Citrulline.
{ECO:0000269|PubMed:18323623}.
BINDING 124 124 Aspartate. {ECO:0000269|PubMed:18323623}.
BINDING 127 127 Citrulline.
{ECO:0000269|PubMed:18323623}.
BINDING 180 180 Citrulline.
{ECO:0000269|PubMed:18323623}.
BINDING 189 189 Citrulline.
{ECO:0000269|PubMed:18323623}.
BINDING 270 270 Citrulline.
{ECO:0000269|PubMed:18323623}.
BINDING 282 282 Citrulline.
{ECO:0000269|PubMed:18323623}.
MOD_RES 87 87 Phosphotyrosine.
{ECO:0000250|UniProtKB:P09034}.
MOD_RES 113 113 Phosphotyrosine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 180 180 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 219 219 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VARIANT 14 14 G -> S (in CTLN1; dbSNP:rs121908636).
{ECO:0000269|PubMed:14680976,
ECO:0000269|PubMed:2358466}.
/FTId=VAR_000681.
VARIANT 18 18 S -> L (in CTLN1; dbSNP:rs121908643).
{ECO:0000269|PubMed:1943692}.
/FTId=VAR_000682.
VARIANT 19 19 C -> R (in CTLN1).
{ECO:0000269|PubMed:12815590}.
/FTId=VAR_015891.
VARIANT 27 412 Missing (in CTLN1).
{ECO:0000269|PubMed:28111830}.
/FTId=VAR_078387.
VARIANT 40 40 Q -> L (in CTLN1).
{ECO:0000269|PubMed:14680976}.
/FTId=VAR_058337.
VARIANT 64 64 V -> I (in CTLN1; unknown pathological
significance; dbSNP:rs556297791).
{ECO:0000269|PubMed:28111830}.
/FTId=VAR_078388.
VARIANT 69 69 V -> A (in CTLN1; dbSNP:rs771594651).
{ECO:0000269|PubMed:11708871}.
/FTId=VAR_016013.
VARIANT 79 79 S -> P (in CTLN1).
{ECO:0000269|PubMed:19006241,
ECO:0000269|PubMed:28111830}.
/FTId=VAR_058338.
VARIANT 86 86 R -> C (in CTLN1; dbSNP:rs121908644).
{ECO:0000269|PubMed:1943692}.
/FTId=VAR_000683.
VARIANT 86 86 R -> H (in CTLN1; dbSNP:rs575001023).
{ECO:0000269|PubMed:12815590}.
/FTId=VAR_015892.
VARIANT 91 91 T -> P (in CTLN1; decreased affinity for
aspartate; decreased affinity for
citrulline; decreased argininosuccinate
synthase activity; dbSNP:rs769018733).
{ECO:0000269|PubMed:24889030,
ECO:0000269|PubMed:27287393}.
/FTId=VAR_078389.
VARIANT 95 95 R -> S (in CTLN1; increased thermal
stability; loss of argininosuccinate
synthase activity).
{ECO:0000269|PubMed:12815590,
ECO:0000269|PubMed:27287393}.
/FTId=VAR_015893.
VARIANT 96 96 P -> H (in CTLN1; decreased affinity for
aspartate; decreased affinity for
citrulline; decreased argininosuccinate
synthase activity).
{ECO:0000269|PubMed:19006241,
ECO:0000269|PubMed:27287393}.
/FTId=VAR_058339.
VARIANT 96 96 P -> L (in CTLN1; decreased thermal
stability; decreased affinity for
aspartate; decreased affinity for
citrulline; loss of argininosuccinate
synthase activity).
{ECO:0000269|PubMed:27287393}.
/FTId=VAR_078390.
VARIANT 96 96 P -> S (in CTLN1; no effect on thermal
stability; decreased argininosuccinate
synthase activity).
{ECO:0000269|PubMed:12815590,
ECO:0000269|PubMed:27287393}.
/FTId=VAR_015894.
VARIANT 97 412 Missing (in CTLN1).
{ECO:0000269|PubMed:28111830}.
/FTId=VAR_078391.
VARIANT 100 100 R -> C (in CTLN1; dbSNP:rs370695114).
{ECO:0000269|PubMed:28111830}.
/FTId=VAR_078392.
VARIANT 100 100 R -> H (in CTLN1; dbSNP:rs138279074).
{ECO:0000269|PubMed:28111830}.
/FTId=VAR_078393.
VARIANT 108 108 R -> L (in CTLN1; dbSNP:rs35269064).
{ECO:0000269|PubMed:11708871,
ECO:0000269|PubMed:11941481}.
/FTId=VAR_016014.
VARIANT 111 111 A -> D (in CTLN1).
{ECO:0000269|PubMed:28111830}.
/FTId=VAR_078394.
VARIANT 117 117 G -> C (in CTLN1).
{ECO:0000269|PubMed:28111830}.
/FTId=VAR_078395.
VARIANT 117 117 G -> D (in CTLN1).
{ECO:0000269|PubMed:11708871,
ECO:0000269|PubMed:12815590}.
/FTId=VAR_015896.
VARIANT 117 117 G -> S (in CTLN1; decreased thermal
stability; loss of argininosuccinate
synthase activity; dbSNP:rs770944877).
{ECO:0000269|PubMed:12815590,
ECO:0000269|PubMed:27287393}.
/FTId=VAR_015895.
VARIANT 118 118 A -> T (in CTLN1; decreased thermal
stability; decreased affinity for
aspartate; decreased affinity for
citrulline; decreased argininosuccinate
synthase activity; dbSNP:rs775305020).
{ECO:0000269|PubMed:18473344,
ECO:0000269|PubMed:27287393,
ECO:0000269|PubMed:7977368}.
/FTId=VAR_000684.
VARIANT 119 119 T -> I (in CTLN1; decreased thermal
stability; loss of argininosuccinate
synthase activity).
{ECO:0000269|PubMed:11708871,
ECO:0000269|PubMed:27287393}.
/FTId=VAR_016015.
VARIANT 124 124 D -> N (in CTLN1; loss of
argininosuccinate synthase activity).
{ECO:0000269|PubMed:16475226,
ECO:0000269|PubMed:27287393}.
/FTId=VAR_058340.
VARIANT 127 127 R -> L (increased thermal stability; loss
of argininosuccinate synthase activity;
dbSNP:rs201623252).
{ECO:0000269|PubMed:24889030,
ECO:0000269|PubMed:27287393}.
/FTId=VAR_078396.
VARIANT 127 127 R -> Q (in CTLN1; increased thermal
stability; loss of argininosuccinate
synthase activity; dbSNP:rs201623252).
{ECO:0000269|PubMed:14680976,
ECO:0000269|PubMed:19006241,
ECO:0000269|PubMed:27287393}.
/FTId=VAR_058341.
VARIANT 127 127 R -> W (in CTLN1; severe clinical course;
loss of argininosuccinate synthase
activity; dbSNP:rs771794639).
{ECO:0000269|PubMed:19006241,
ECO:0000269|PubMed:27287393}.
/FTId=VAR_058342.
VARIANT 138 412 Missing (in CTLN1).
{ECO:0000269|PubMed:28111830}.
/FTId=VAR_078397.
VARIANT 141 141 V -> G (in CTLN1).
{ECO:0000269|PubMed:25179242}.
/FTId=VAR_072792.
VARIANT 157 157 R -> C (in CTLN1; decreased thermal
stability; loss of argininosuccinate
synthase activity; dbSNP:rs770585183).
{ECO:0000269|PubMed:12815590,
ECO:0000269|PubMed:24889030,
ECO:0000269|PubMed:27287393}.
/FTId=VAR_015897.
VARIANT 157 157 R -> H (in CTLN1; loss of
argininosuccinate synthase activity;
dbSNP:rs121908637).
{ECO:0000269|PubMed:16475226,
ECO:0000269|PubMed:2358466,
ECO:0000269|PubMed:27287393}.
/FTId=VAR_000685.
VARIANT 157 157 R -> S (in CTLN1).
{ECO:0000269|PubMed:28111830}.
/FTId=VAR_078398.
VARIANT 160 160 L -> P (in CTLN1).
{ECO:0000269|PubMed:19006241,
ECO:0000269|PubMed:28111830}.
/FTId=VAR_058343.
VARIANT 163 412 Missing (in CTLN1).
{ECO:0000269|PubMed:28111830}.
/FTId=VAR_078399.
VARIANT 164 164 A -> P (in CTLN1).
{ECO:0000269|PubMed:28111830}.
/FTId=VAR_078400.
VARIANT 179 179 W -> R (in CTLN1; mild; decreased
affinity for aspartate; decreased
affinity for citrulline; decreased
argininosuccinate synthase activity;
dbSNP:rs121908646).
{ECO:0000269|PubMed:11941481,
ECO:0000269|PubMed:12815590,
ECO:0000269|PubMed:14680976,
ECO:0000269|PubMed:18473344}.
/FTId=VAR_015898.
VARIANT 180 180 S -> I (in CTLN1; increased thermal
stability; loss of argininosuccinate
synthase activity).
{ECO:0000269|PubMed:24889030,
ECO:0000269|PubMed:27287393}.
/FTId=VAR_078401.
VARIANT 180 180 S -> N (in CTLN1; decreased thermal
stability; decreased affinity for
aspartate; decreased affinity for
citrulline; decreased argininosuccinate
synthase activity; dbSNP:rs121908638).
{ECO:0000269|PubMed:2358466,
ECO:0000269|PubMed:27287393}.
/FTId=VAR_000686.
VARIANT 184 184 N -> K (in CTLN1).
{ECO:0000269|PubMed:28111830}.
/FTId=VAR_078402.
VARIANT 190 190 Y -> D (in CTLN1).
{ECO:0000269|PubMed:14680976,
ECO:0000269|PubMed:28111830}.
/FTId=VAR_058344.
VARIANT 191 191 E -> K (in CTLN1; dbSNP:rs777828000).
{ECO:0000269|PubMed:12815590}.
/FTId=VAR_015899.
VARIANT 191 191 E -> Q (in CTLN1; loss of
argininosuccinate synthase activity).
{ECO:0000269|PubMed:19006241,
ECO:0000269|PubMed:27287393}.
/FTId=VAR_058345.
VARIANT 192 192 A -> V (in CTLN1; decreased protein
abundance). {ECO:0000269|PubMed:7977368,
ECO:0000269|PubMed:8792870}.
/FTId=VAR_000687.
VARIANT 202 202 A -> E (in CTLN1; dbSNP:rs376371866).
{ECO:0000269|PubMed:14680976}.
/FTId=VAR_058346.
VARIANT 206 206 L -> P (in CTLN1).
{ECO:0000269|PubMed:19006241,
ECO:0000269|PubMed:28111830}.
/FTId=VAR_058347.
VARIANT 230 230 G -> R (in CTLN1).
{ECO:0000269|PubMed:28111830}.
/FTId=VAR_078403.
VARIANT 237 237 N -> I (in CTLN1).
{ECO:0000269|PubMed:28111830}.
/FTId=VAR_078404.
VARIANT 258 258 A -> P (in CTLN1).
{ECO:0000269|PubMed:28111830}.
/FTId=VAR_078405.
VARIANT 258 258 A -> V (in CTLN1; dbSNP:rs753078725).
{ECO:0000269|PubMed:28111830}.
/FTId=VAR_078406.
VARIANT 263 263 V -> M (in CTLN1; mild clinical course;
no effect on affinity for aspartate; no
effect on affinity for citrulline;
decreased argininosuccinate synthase
activity; dbSNP:rs192838388).
{ECO:0000269|PubMed:14680976,
ECO:0000269|PubMed:18473344}.
/FTId=VAR_058348.
VARIANT 265 265 R -> C (in CTLN1; severe clinical course;
loss of argininosuccinate synthase
activity; dbSNP:rs148918985).
{ECO:0000269|PubMed:18473344,
ECO:0000269|PubMed:19006241,
ECO:0000269|PubMed:25179242,
ECO:0000269|PubMed:28111830}.
/FTId=VAR_058349.
VARIANT 265 265 R -> H (in CTLN1; dbSNP:rs398123131).
{ECO:0000269|PubMed:12815590}.
/FTId=VAR_015900.
VARIANT 269 269 V -> M (in CTLN1; dbSNP:rs370595480).
{ECO:0000269|PubMed:12815590,
ECO:0000269|PubMed:14680976}.
/FTId=VAR_015901.
VARIANT 270 270 E -> Q (in CTLN1; loss of
argininosuccinate synthase activity;
dbSNP:rs775163147).
{ECO:0000269|PubMed:11708871,
ECO:0000269|PubMed:16475226,
ECO:0000269|PubMed:27287393}.
/FTId=VAR_016007.
VARIANT 272 272 R -> C (in CTLN1; increased thermal
stability; decreased affinity for
aspartate; decreased affinity for
citrulline; decreased argininosuccinate
synthase activity; dbSNP:rs762387914).
{ECO:0000269|PubMed:12815590,
ECO:0000269|PubMed:27287393,
ECO:0000269|PubMed:7977368,
ECO:0000269|PubMed:8792870}.
/FTId=VAR_000688.
VARIANT 272 272 R -> H (in CTLN1; increased thermal
stability; decreased affinity for
aspartate; decreased affinity for
citrulline; decreased argininosuccinate
synthase activity).
{ECO:0000269|PubMed:27287393}.
/FTId=VAR_078407.
VARIANT 272 272 R -> L (in CTLN1; increased thermal
stability; decreased affinity for
aspartate; decreased affinity for
citrulline; decreased argininosuccinate
synthase activity; dbSNP:rs768215008).
{ECO:0000269|PubMed:27287393}.
/FTId=VAR_078408.
VARIANT 275 412 Missing (in CTLN1).
{ECO:0000269|PubMed:28111830}.
/FTId=VAR_078409.
VARIANT 277 277 K -> T (in CTLN1).
{ECO:0000269|PubMed:19006241,
ECO:0000269|PubMed:28111830}.
/FTId=VAR_058350.
VARIANT 279 412 Missing (in CTLN1).
{ECO:0000269|PubMed:28111830}.
/FTId=VAR_078410.
VARIANT 279 279 R -> Q (in CTLN1; dbSNP:rs371265106).
{ECO:0000269|PubMed:16475226}.
/FTId=VAR_016008.
VARIANT 280 280 G -> R (in CTLN1; loss of
argininosuccinate synthase activity).
{ECO:0000269|PubMed:7977368,
ECO:0000269|PubMed:8792870}.
/FTId=VAR_000689.
VARIANT 283 283 E -> K (in CTLN1; dbSNP:rs765338121).
{ECO:0000269|PubMed:12815590,
ECO:0000269|PubMed:16475226,
ECO:0000269|PubMed:23611581,
ECO:0000269|PubMed:24889030}.
/FTId=VAR_015902.
VARIANT 284 284 T -> I (in CTLN1; mild clinical course).
{ECO:0000269|PubMed:19006241,
ECO:0000269|PubMed:28111830}.
/FTId=VAR_058351.
VARIANT 290 290 L -> P (in CTLN1).
{ECO:0000269|PubMed:28111830}.
/FTId=VAR_078411.
VARIANT 291 291 Y -> S (in CTLN1).
{ECO:0000269|PubMed:19006241,
ECO:0000269|PubMed:28111830}.
/FTId=VAR_058352.
VARIANT 296 296 D -> G (in CTLN1).
{ECO:0000269|PubMed:19006241,
ECO:0000269|PubMed:28111830}.
/FTId=VAR_058353.
VARIANT 299 299 A -> D (in CTLN1; dbSNP:rs768394647).
{ECO:0000269|PubMed:28111830}.
/FTId=VAR_078412.
VARIANT 302 302 M -> V (in CTLN1; no effect on affinity
for aspartate; no effect on affinity for
citrulline; decreased argininosuccinate
synthase activity).
{ECO:0000269|PubMed:18473344,
ECO:0000269|PubMed:28111830}.
/FTId=VAR_058354.
VARIANT 304 304 R -> W (in CTLN1; decreased protein
abundance; dbSNP:rs121908642).
{ECO:0000269|PubMed:12815590,
ECO:0000269|PubMed:2358466,
ECO:0000269|PubMed:7977368}.
/FTId=VAR_000690.
VARIANT 306 306 V -> G (in CTLN1).
{ECO:0000269|PubMed:28111830}.
/FTId=VAR_078413.
VARIANT 307 307 R -> C (in CTLN1; dbSNP:rs183276875).
{ECO:0000269|PubMed:28111830}.
/FTId=VAR_058355.
VARIANT 310 310 K -> Q (in CTLN1; dbSNP:rs121908648).
{ECO:0000269|PubMed:12815590}.
/FTId=VAR_016009.
VARIANT 310 310 K -> R (in CTLN1; dbSNP:rs199751308).
{ECO:0000269|PubMed:15863597}.
/FTId=VAR_015903.
VARIANT 311 412 Missing (in CTLN1).
{ECO:0000269|PubMed:28111830}.
/FTId=VAR_078414.
VARIANT 321 321 V -> M (in CTLN1; dbSNP:rs727503813).
{ECO:0000269|PubMed:28111830}.
/FTId=VAR_078415.
VARIANT 324 324 G -> S (in CTLN1; loss of
argininosuccinate synthase activity;
dbSNP:rs121908639).
{ECO:0000269|PubMed:12815590,
ECO:0000269|PubMed:14680976,
ECO:0000269|PubMed:16475226,
ECO:0000269|PubMed:18473344,
ECO:0000269|PubMed:2358466,
ECO:0000269|PubMed:28111830}.
/FTId=VAR_000691.
VARIANT 324 324 G -> V (in CTLN1).
{ECO:0000269|PubMed:19006241,
ECO:0000269|PubMed:28111830}.
/FTId=VAR_058356.
VARIANT 335 335 R -> H (in CTLN1; dbSNP:rs555388438).
{ECO:0000269|PubMed:28111830}.
/FTId=VAR_078416.
VARIANT 337 337 C -> R (in CTLN1).
{ECO:0000269|PubMed:23611581}.
/FTId=VAR_078417.
VARIANT 341 341 S -> F (in CTLN1).
{ECO:0000269|PubMed:19006241,
ECO:0000269|PubMed:28111830}.
/FTId=VAR_058357.
VARIANT 344 412 Missing (in CTLN1).
{ECO:0000269|PubMed:28111830}.
/FTId=VAR_078418.
VARIANT 345 345 V -> G (in CTLN1).
{ECO:0000269|PubMed:14680976}.
/FTId=VAR_058358.
VARIANT 347 347 G -> R (in CTLN1; severe clinical
course). {ECO:0000269|PubMed:19006241,
ECO:0000269|PubMed:28111830}.
/FTId=VAR_058359.
VARIANT 356 356 G -> V (in CTLN1).
{ECO:0000269|PubMed:28111830}.
/FTId=VAR_078419.
VARIANT 357 412 Missing (in CTLN1).
{ECO:0000269|PubMed:28111830}.
/FTId=VAR_078420.
VARIANT 359 359 Y -> D (in CTLN1; mild clinical course).
{ECO:0000269|PubMed:19006241,
ECO:0000269|PubMed:28111830}.
/FTId=VAR_058360.
VARIANT 362 362 G -> V (in CTLN1; mild; no effect on
affinity for aspartate; no effect on
affinity for citrulline; decreased
argininosuccinate synthase activity;
dbSNP:rs121908647).
{ECO:0000269|PubMed:11941481,
ECO:0000269|PubMed:12815590,
ECO:0000269|PubMed:14680976,
ECO:0000269|PubMed:18473344}.
/FTId=VAR_015904.
VARIANT 363 363 R -> G (in CTLN1).
{ECO:0000269|PubMed:16475226}.
/FTId=VAR_016010.
VARIANT 363 363 R -> L (in CTLN1).
{ECO:0000269|PubMed:7977368}.
/FTId=VAR_000692.
VARIANT 363 363 R -> Q (in CTLN1; dbSNP:rs771937610).
{ECO:0000269|PubMed:12815590}.
/FTId=VAR_016011.
VARIANT 363 363 R -> W (in CTLN1; dbSNP:rs121908640).
{ECO:0000269|PubMed:12815590,
ECO:0000269|PubMed:2358466}.
/FTId=VAR_000693.
VARIANT 380 412 Missing (in CTLN1).
{ECO:0000269|PubMed:28111830}.
/FTId=VAR_078421.
VARIANT 389 389 T -> I (in CTLN1).
{ECO:0000269|PubMed:12815590}.
/FTId=VAR_016012.
VARIANT 389 389 T -> P (in CTLN1).
{ECO:0000269|PubMed:28111830}.
/FTId=VAR_078422.
VARIANT 390 390 G -> R (in CTLN1; loss of
argininosuccinate synthase activity;
dbSNP:rs121908641).
{ECO:0000269|PubMed:11708871,
ECO:0000269|PubMed:11941481,
ECO:0000269|PubMed:12815590,
ECO:0000269|PubMed:16475226,
ECO:0000269|PubMed:18473344,
ECO:0000269|PubMed:2358466,
ECO:0000269|PubMed:24889030}.
/FTId=VAR_000694.
CONFLICT 325 327 FWH -> LRP (in Ref. 1; CAA25771 and 2;
AAA51783). {ECO:0000305}.
STRAND 5 10 {ECO:0000244|PDB:2NZ2}.
HELIX 15 26 {ECO:0000244|PDB:2NZ2}.
STRAND 29 39 {ECO:0000244|PDB:2NZ2}.
HELIX 44 54 {ECO:0000244|PDB:2NZ2}.
STRAND 57 63 {ECO:0000244|PDB:2NZ2}.
HELIX 65 71 {ECO:0000244|PDB:2NZ2}.
HELIX 73 78 {ECO:0000244|PDB:2NZ2}.
TURN 84 86 {ECO:0000244|PDB:2NZ2}.
TURN 90 93 {ECO:0000244|PDB:2NZ2}.
HELIX 94 109 {ECO:0000244|PDB:2NZ2}.
STRAND 112 115 {ECO:0000244|PDB:2NZ2}.
HELIX 124 135 {ECO:0000244|PDB:2NZ2}.
STRAND 140 142 {ECO:0000244|PDB:2NZ2}.
HELIX 144 146 {ECO:0000244|PDB:2NZ2}.
HELIX 148 151 {ECO:0000244|PDB:2NZ2}.
HELIX 158 166 {ECO:0000244|PDB:2NZ2}.
STRAND 181 183 {ECO:0000244|PDB:2NZ2}.
STRAND 188 190 {ECO:0000244|PDB:2NZ2}.
HELIX 193 196 {ECO:0000244|PDB:2NZ2}.
HELIX 204 206 {ECO:0000244|PDB:2NZ2}.
TURN 213 215 {ECO:0000244|PDB:2NZ2}.
STRAND 221 228 {ECO:0000244|PDB:2NZ2}.
STRAND 231 237 {ECO:0000244|PDB:2NZ2}.
TURN 238 240 {ECO:0000244|PDB:2NZ2}.
HELIX 247 261 {ECO:0000244|PDB:2NZ2}.
STRAND 265 271 {ECO:0000244|PDB:2NZ2}.
STRAND 277 283 {ECO:0000244|PDB:2NZ2}.
HELIX 285 301 {ECO:0000244|PDB:2NZ2}.
HELIX 304 323 {ECO:0000244|PDB:2NZ2}.
STRAND 326 328 {ECO:0000244|PDB:2NZ2}.
HELIX 329 341 {ECO:0000244|PDB:2NZ2}.
TURN 342 344 {ECO:0000244|PDB:2NZ2}.
STRAND 347 354 {ECO:0000244|PDB:2NZ2}.
STRAND 357 364 {ECO:0000244|PDB:2NZ2}.
HELIX 372 375 {ECO:0000244|PDB:2NZ2}.
HELIX 385 404 {ECO:0000244|PDB:2NZ2}.
SEQUENCE 412 AA; 46530 MW; 47CAD2373AE47E47 CRC64;
MSSKGSVVLA YSGGLDTSCI LVWLKEQGYD VIAYLANIGQ KEDFEEARKK ALKLGAKKVF
IEDVSREFVE EFIWPAIQSS ALYEDRYLLG TSLARPCIAR KQVEIAQREG AKYVSHGATG
KGNDQVRFEL SCYSLAPQIK VIAPWRMPEF YNRFKGRNDL MEYAKQHGIP IPVTPKNPWS
MDENLMHISY EAGILENPKN QAPPGLYTKT QDPAKAPNTP DILEIEFKKG VPVKVTNVKD
GTTHQTSLEL FMYLNEVAGK HGVGRIDIVE NRFIGMKSRG IYETPAGTIL YHAHLDIEAF
TMDREVRKIK QGLGLKFAEL VYTGFWHSPE CEFVRHCIAK SQERVEGKVQ VSVLKGQVYI
LGRESPLSLY NEELVSMNVQ GDYEPTDATG FININSLRLK EYHRLQSKVT AK


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