UniProtKB - P00966 (ASSY_HUMAN)
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>sp|P00966|ASSY_HUMAN Argininosuccinate synthase OS=Homo sapiens OX=9606 GN=ASS1 PE=1 SV=2 MSSKGSVVLAYSGGLDTSCILVWLKEQGYDVIAYLANIGQKEDFEEARKKALKLGAKKVF IEDVSREFVEEFIWPAIQSSALYEDRYLLGTSLARPCIARKQVEIAQREGAKYVSHGATG KGNDQVRFELSCYSLAPQIKVIAPWRMPEFYNRFKGRNDLMEYAKQHGIPIPVTPKNPWS MDENLMHISYEAGILENPKNQAPPGLYTKTQDPAKAPNTPDILEIEFKKGVPVKVTNVKD GTTHQTSLELFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHLDIEAF TMDREVRKIKQGLGLKFAELVYTGFWHSPECEFVRHCIAKSQERVEGKVQVSVLKGQVYI LGRESPLSLYNEELVSMNVQGDYEPTDATGFININSLRLKEYHRLQSKVTAKCommunity curation ()Add a publicationFeedback
Argininosuccinate synthase
ASS1
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.15"Characterization of human wild-type and mutant argininosuccinate synthetase proteins expressed in bacterial cells."
Shaheen N., Kobayashi K., Terazono H., Fukushige T., Horiuchi M., Saheki T.
Enzyme Protein 48:251-264(1994) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANTS CLNT1 VAL-192; ARG-280; CYS-272 AND TRP-304, FUNCTION, CATALYTIC ACTIVITY, PATHWAY. - Ref.26"Investigation of citrullinemia type I variants by in vitro expression studies."
Berning C., Bieger I., Pauli S., Vermeulen T., Vogl T., Rummel T., Hoehne W., Koch H.G., Rolinski B., Gempel K., Haeberle J.
Hum. Mutat. 29:1222-1227(2008) [PubMed] [Europe PMC] [Abstract]Cited for: 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, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.31"Kinetic mutations in argininosuccinate synthetase deficiency: characterisation and in vitro correction by substrate supplementation."
Diez-Fernandez C., Wellauer O., Gemperle C., Ruefenacht V., Fingerhut R., Haeberle J.
J. Med. Genet. 53:710-719(2016) [PubMed] [Europe PMC] [Abstract]Cited for: 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, SUBCELLULAR LOCATION.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
- ATPEC:6.3.4.5
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<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.15"Characterization of human wild-type and mutant argininosuccinate synthetase proteins expressed in bacterial cells."
Shaheen N., Kobayashi K., Terazono H., Fukushige T., Horiuchi M., Saheki T.
Enzyme Protein 48:251-264(1994) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANTS CLNT1 VAL-192; ARG-280; CYS-272 AND TRP-304, FUNCTION, CATALYTIC ACTIVITY, PATHWAY. - Ref.26"Investigation of citrullinemia type I variants by in vitro expression studies."
Berning C., Bieger I., Pauli S., Vermeulen T., Vogl T., Rummel T., Hoehne W., Koch H.G., Rolinski B., Gempel K., Haeberle J.
Hum. Mutat. 29:1222-1227(2008) [PubMed] [Europe PMC] [Abstract]Cited for: 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, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.31"Kinetic mutations in argininosuccinate synthetase deficiency: characterisation and in vitro correction by substrate supplementation."
Diez-Fernandez C., Wellauer O., Gemperle C., Ruefenacht V., Fingerhut R., Haeberle J.
J. Med. Genet. 53:710-719(2016) [PubMed] [Europe PMC] [Abstract]Cited for: 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, SUBCELLULAR LOCATION.
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Manual assertion based on experiment ini
- Ref.15"Characterization of human wild-type and mutant argininosuccinate synthetase proteins expressed in bacterial cells."
Shaheen N., Kobayashi K., Terazono H., Fukushige T., Horiuchi M., Saheki T.
Enzyme Protein 48:251-264(1994) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANTS CLNT1 VAL-192; ARG-280; CYS-272 AND TRP-304, FUNCTION, CATALYTIC ACTIVITY, PATHWAY. - Ref.26"Investigation of citrullinemia type I variants by in vitro expression studies."
Berning C., Bieger I., Pauli S., Vermeulen T., Vogl T., Rummel T., Hoehne W., Koch H.G., Rolinski B., Gempel K., Haeberle J.
Hum. Mutat. 29:1222-1227(2008) [PubMed] [Europe PMC] [Abstract]Cited for: 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, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.31"Kinetic mutations in argininosuccinate synthetase deficiency: characterisation and in vitro correction by substrate supplementation."
Diez-Fernandez C., Wellauer O., Gemperle C., Ruefenacht V., Fingerhut R., Haeberle J.
J. Med. Genet. 53:710-719(2016) [PubMed] [Europe PMC] [Abstract]Cited for: 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, SUBCELLULAR LOCATION.
Source: Rhea- Search for this reaction in UniProtKB.
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+L-aspartate- Search proteins in UniProtKB for this molecule.
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+L-citrulline- Search proteins in UniProtKB for this molecule.
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=2-(Nω-L-arginino)succinate- Search proteins in UniProtKB for this molecule.
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<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
- KM=112 µM for citrulline (at pH 7.0 and 37 degrees Celsius)1 Publication
Manual assertion based on experiment ini
- Ref.26"Investigation of citrullinemia type I variants by in vitro expression studies."
Berning C., Bieger I., Pauli S., Vermeulen T., Vogl T., Rummel T., Hoehne W., Koch H.G., Rolinski B., Gempel K., Haeberle J.
Hum. Mutat. 29:1222-1227(2008) [PubMed] [Europe PMC] [Abstract]Cited for: 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, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=68 µM for aspartate (at pH 7.0 and 37 degrees Celsius)1 Publication
Manual assertion based on experiment ini
- Ref.26"Investigation of citrullinemia type I variants by in vitro expression studies."
Berning C., Bieger I., Pauli S., Vermeulen T., Vogl T., Rummel T., Hoehne W., Koch H.G., Rolinski B., Gempel K., Haeberle J.
Hum. Mutat. 29:1222-1227(2008) [PubMed] [Europe PMC] [Abstract]Cited for: 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, BIOPHYSICOCHEMICAL PROPERTIES.
- Vmax=143 nmol/min/mg enzyme toward citrulline (at pH 7.0 and 37 degrees Celsius)1 Publication
Manual assertion based on experiment ini
- Ref.26"Investigation of citrullinemia type I variants by in vitro expression studies."
Berning C., Bieger I., Pauli S., Vermeulen T., Vogl T., Rummel T., Hoehne W., Koch H.G., Rolinski B., Gempel K., Haeberle J.
Hum. Mutat. 29:1222-1227(2008) [PubMed] [Europe PMC] [Abstract]Cited for: 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, BIOPHYSICOCHEMICAL PROPERTIES.
- Vmax=116 nmol/min/mg enzyme toward aspartate (at pH 7.0 and 37 degrees1 Publication
Manual assertion based on experiment ini
- Ref.26"Investigation of citrullinemia type I variants by in vitro expression studies."
Berning C., Bieger I., Pauli S., Vermeulen T., Vogl T., Rummel T., Hoehne W., Koch H.G., Rolinski B., Gempel K., Haeberle J.
Hum. Mutat. 29:1222-1227(2008) [PubMed] [Europe PMC] [Abstract]Cited for: 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, BIOPHYSICOCHEMICAL PROPERTIES.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-arginine biosynthesis
This protein is involved in step 2 of the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate.3 PublicationsManual assertion inferred by curator fromi
- Ref.15"Characterization of human wild-type and mutant argininosuccinate synthetase proteins expressed in bacterial cells."
Shaheen N., Kobayashi K., Terazono H., Fukushige T., Horiuchi M., Saheki T.
Enzyme Protein 48:251-264(1994) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANTS CLNT1 VAL-192; ARG-280; CYS-272 AND TRP-304, FUNCTION, CATALYTIC ACTIVITY, PATHWAY. - Ref.26"Investigation of citrullinemia type I variants by in vitro expression studies."
Berning C., Bieger I., Pauli S., Vermeulen T., Vogl T., Rummel T., Hoehne W., Koch H.G., Rolinski B., Gempel K., Haeberle J.
Hum. Mutat. 29:1222-1227(2008) [PubMed] [Europe PMC] [Abstract]Cited for: 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, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.31"Kinetic mutations in argininosuccinate synthetase deficiency: characterisation and in vitro correction by substrate supplementation."
Diez-Fernandez C., Wellauer O., Gemperle C., Ruefenacht V., Fingerhut R., Haeberle J.
J. Med. Genet. 53:710-719(2016) [PubMed] [Europe PMC] [Abstract]Cited for: 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, SUBCELLULAR LOCATION.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
- no protein annotated in this organism
- Citrulline--aspartate ligase, Argininosuccinate synthase (ASS), Citrulline--aspartate ligase (ASS1), Citrulline--aspartate ligase (ASS1), Argininosuccinate synthase, Argininosuccinate synthase (ASS1), Citrulline--aspartate ligase (ASS1), Citrulline--aspartate ligase (LOC402295), Citrulline--aspartate ligase (ASS1)
- Argininosuccinate lyase (ASL)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.
Pathwayi: urea cycle
This protein is involved in step 1 of the subpathway that synthesizes (N(omega)-L-arginino)succinate from L-aspartate and L-citrulline.3 PublicationsManual assertion inferred by curator fromi
- Ref.15"Characterization of human wild-type and mutant argininosuccinate synthetase proteins expressed in bacterial cells."
Shaheen N., Kobayashi K., Terazono H., Fukushige T., Horiuchi M., Saheki T.
Enzyme Protein 48:251-264(1994) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANTS CLNT1 VAL-192; ARG-280; CYS-272 AND TRP-304, FUNCTION, CATALYTIC ACTIVITY, PATHWAY. - Ref.26"Investigation of citrullinemia type I variants by in vitro expression studies."
Berning C., Bieger I., Pauli S., Vermeulen T., Vogl T., Rummel T., Hoehne W., Koch H.G., Rolinski B., Gempel K., Haeberle J.
Hum. Mutat. 29:1222-1227(2008) [PubMed] [Europe PMC] [Abstract]Cited for: 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, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.31"Kinetic mutations in argininosuccinate synthetase deficiency: characterisation and in vitro correction by substrate supplementation."
Diez-Fernandez C., Wellauer O., Gemperle C., Ruefenacht V., Fingerhut R., Haeberle J.
J. Med. Genet. 53:710-719(2016) [PubMed] [Europe PMC] [Abstract]Cited for: 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, SUBCELLULAR LOCATION.
Proteins known to be involved in this subpathway in this organism are:
- Argininosuccinate synthase (ASS), Citrulline--aspartate ligase (ASS1), Argininosuccinate synthase 1 isoform 2 (ASS1), Citrulline--aspartate ligase (ASS1), Argininosuccinate synthase, Argininosuccinate synthase (ASS1), Citrulline--aspartate ligase (ASS1), Citrulline--aspartate ligase (ASS1)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (N(omega)-L-arginino)succinate from L-aspartate and L-citrulline, the pathway urea cycle and in Nitrogen metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 36 | ATP; via amide nitrogen and carbonyl oxygenBy similarity | 1 | |
Binding sitei | 87 | Citrulline1 Publication Manual assertion based on experiment ini
| 1 | |
Binding sitei | 92 | Citrulline1 Publication Manual assertion based on experiment ini
| 1 | |
Binding sitei | 119 | Aspartate1 Publication Manual assertion based on experiment ini
| 1 | |
Binding sitei | 123 | Aspartate1 Publication Manual assertion based on experiment ini
| 1 | |
Binding sitei | 123 | Citrulline1 Publication Manual assertion based on experiment ini
| 1 | |
Binding sitei | 124 | Aspartate1 Publication Manual assertion based on experiment ini
| 1 | |
Binding sitei | 127 | Citrulline1 Publication Manual assertion based on experiment ini
| 1 | |
Binding sitei | 180 | Citrulline1 Publication Manual assertion based on experiment ini
| 1 | |
Binding sitei | 189 | Citrulline1 Publication Manual assertion based on experiment ini
| 1 | |
Binding sitei | 270 | Citrulline1 Publication Manual assertion based on experiment ini
| 1 | |
Binding sitei | 282 | Citrulline1 Publication Manual assertion based on experiment ini
| 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 10 – 18 | ATPBy similarity | 9 | |
Nucleotide bindingi | 115 – 123 | ATPBy similarity | 9 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- amino acid binding Source: BHF-UCL
<p>Inferred from Mutant Phenotype</p>
<p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p>
Inferred from mutant phenotypei
- Ref.20"Mutations in argininosuccinate synthetase mRNA of Japanese patients, causing classical citrullinemia."
Kobayashi K., Shaheen N., Terazono H., Saheki T.
Am. J. Hum. Genet. 55:1103-1112(1994) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS CTLN1 THR-118; VAL-192; CYS-272; ARG-280; TRP-304 AND LEU-363.
- argininosuccinate synthase activity Source: UniProtKBInferred from mutant phenotypei
- Ref.26"Investigation of citrullinemia type I variants by in vitro expression studies."
Berning C., Bieger I., Pauli S., Vermeulen T., Vogl T., Rummel T., Hoehne W., Koch H.G., Rolinski B., Gempel K., Haeberle J.
Hum. Mutat. 29:1222-1227(2008) [PubMed] [Europe PMC] [Abstract]Cited for: 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, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.31"Kinetic mutations in argininosuccinate synthetase deficiency: characterisation and in vitro correction by substrate supplementation."
Diez-Fernandez C., Wellauer O., Gemperle C., Ruefenacht V., Fingerhut R., Haeberle J.
J. Med. Genet. 53:710-719(2016) [PubMed] [Europe PMC] [Abstract]Cited for: 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, SUBCELLULAR LOCATION. - Ref.14"CLOCK acetylates ASS1 to drive circadian rhythm of ureagenesis."
Lin R., Mo Y., Zha H., Qu Z., Xie P., Zhu Z.J., Xu Y., Xiong Y., Guan K.L.
Mol. Cell 68:198-209(2017) [PubMed] [Europe PMC] [Abstract]Cited for: ACETYLATION AT LYS-165 AND LYS-176, MUTAGENESIS OF LYS-165 AND LYS-176, INTERACTION WITH CLOCK, SUBCELLULAR LOCATION. - Ref.15"Characterization of human wild-type and mutant argininosuccinate synthetase proteins expressed in bacterial cells."
Shaheen N., Kobayashi K., Terazono H., Fukushige T., Horiuchi M., Saheki T.
Enzyme Protein 48:251-264(1994) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANTS CLNT1 VAL-192; ARG-280; CYS-272 AND TRP-304, FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
- ATP binding Source: UniProtKB-KW
- identical protein binding Source: IntAct
<p>Inferred from Physical Interaction</p>
<p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p>
Inferred from physical interactioni
- "Towards a proteome-scale map of the human protein-protein interaction network."
Rual J.F., Venkatesan K., Hao T., Hirozane-Kishikawa T., Dricot A., Li N., Berriz G.F., Gibbons F.D., Dreze M., Ayivi-Guedehoussou N., Klitgord N., Simon C., Boxem M., Milstein S., Rosenberg J., Goldberg D.S., Zhang L.V., Wong S.L. , Franklin G., Li S., Albala J.S., Lim J., Fraughton C., Llamosas E., Cevik S., Bex C., Lamesch P., Sikorski R.S., Vandenhaute J., Zoghbi H.Y., Smolyar A., Bosak S., Sequerra R., Doucette-Stamm L., Cusick M.E., Hill D.E., Roth F.P., Vidal M.
Nature 437:1173-1178(2005) [PubMed] [Europe PMC] [Abstract] - "Toward an understanding of the protein interaction network of the human liver."
Wang J., Huo K., Ma L., Tang L., Li D., Huang X., Yuan Y., Li C., Wang W., Guan W., Chen H., Jin C., Wei J., Zhang W., Yang Y., Liu Q., Zhou Y., Zhang C. , Wu Z., Xu W., Zhang Y., Liu T., Yu D., Zhang Y., Chen L., Zhu D., Zhong X., Kang L., Gan X., Yu X., Ma Q., Yan J., Zhou L., Liu Z., Zhu Y., Zhou T., He F., Yang X.
Mol Syst Biol 7:536-536(2011) [PubMed] [Europe PMC] [Abstract] - "A proteome-scale map of the human interactome network."
Rolland T., Tasan M., Charloteaux B., Pevzner S.J., Zhong Q., Sahni N., Yi S., Lemmens I., Fontanillo C., Mosca R., Kamburov A., Ghiassian S.D., Yang X., Ghamsari L., Balcha D., Begg B.E., Braun P., Brehme M. , Broly M.P., Carvunis A.R., Convery-Zupan D., Corominas R., Coulombe-Huntington J., Dann E., Dreze M., Dricot A., Fan C., Franzosa E., Gebreab F., Gutierrez B.J., Hardy M.F., Jin M., Kang S., Kiros R., Lin G.N., Luck K., MacWilliams A., Menche J., Murray R.R., Palagi A., Poulin M.M., Rambout X., Rasla J., Reichert P., Romero V., Ruyssinck E., Sahalie J.M., Scholz A., Shah A.A., Sharma A., Shen Y., Spirohn K., Tam S., Tejeda A.O., Trigg S.A., Twizere J.C., Vega K., Walsh J., Cusick M.E., Xia Y., Barabasi A.L., Iakoucheva L.M., Aloy P., De Las Rivas J., Tavernier J., Calderwood M.A., Hill D.E., Hao T., Roth F.P., Vidal M.
Cell 159:1212-1226(2014) [PubMed] [Europe PMC] [Abstract]
- RNA binding Source: UniProtKBInferred from high throughput direct assayi
- "Insights into RNA biology from an atlas of mammalian mRNA-binding proteins."
Castello A., Fischer B., Eichelbaum K., Horos R., Beckmann B.M., Strein C., Davey N.E., Humphreys D.T., Preiss T., Steinmetz L.M., Krijgsveld J., Hentze M.W.
Cell 149:1393-1406(2012) [PubMed] [Europe PMC] [Abstract]
- toxic substance binding Source: Ensembl
GO - Biological processi
- acute-phase response Source: Ensembl
- aging Source: Ensembl
- arginine biosynthetic process Source: UniProtKBInferred from mutant phenotypei
- Ref.26"Investigation of citrullinemia type I variants by in vitro expression studies."
Berning C., Bieger I., Pauli S., Vermeulen T., Vogl T., Rummel T., Hoehne W., Koch H.G., Rolinski B., Gempel K., Haeberle J.
Hum. Mutat. 29:1222-1227(2008) [PubMed] [Europe PMC] [Abstract]Cited for: 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, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.31"Kinetic mutations in argininosuccinate synthetase deficiency: characterisation and in vitro correction by substrate supplementation."
Diez-Fernandez C., Wellauer O., Gemperle C., Ruefenacht V., Fingerhut R., Haeberle J.
J. Med. Genet. 53:710-719(2016) [PubMed] [Europe PMC] [Abstract]Cited for: 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, SUBCELLULAR LOCATION. - Ref.15"Characterization of human wild-type and mutant argininosuccinate synthetase proteins expressed in bacterial cells."
Shaheen N., Kobayashi K., Terazono H., Fukushige T., Horiuchi M., Saheki T.
Enzyme Protein 48:251-264(1994) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANTS CLNT1 VAL-192; ARG-280; CYS-272 AND TRP-304, FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
- argininosuccinate metabolic process Source: BHF-UCLInferred from mutant phenotypei
- Ref.20"Mutations in argininosuccinate synthetase mRNA of Japanese patients, causing classical citrullinemia."
Kobayashi K., Shaheen N., Terazono H., Saheki T.
Am. J. Hum. Genet. 55:1103-1112(1994) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS CTLN1 THR-118; VAL-192; CYS-272; ARG-280; TRP-304 AND LEU-363.
- aspartate metabolic process Source: BHF-UCLInferred from mutant phenotypei
- Ref.20"Mutations in argininosuccinate synthetase mRNA of Japanese patients, causing classical citrullinemia."
Kobayashi K., Shaheen N., Terazono H., Saheki T.
Am. J. Hum. Genet. 55:1103-1112(1994) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS CTLN1 THR-118; VAL-192; CYS-272; ARG-280; TRP-304 AND LEU-363.
- cellular response to amine stimulus Source: Ensembl
- cellular response to amino acid stimulus Source: Ensembl
- cellular response to ammonium ion Source: Ensembl
- cellular response to cAMP Source: Ensembl
- cellular response to dexamethasone stimulus Source: Ensembl
- cellular response to glucagon stimulus Source: Ensembl
- cellular response to interferon-gamma Source: Ensembl
- cellular response to laminar fluid shear stress Source: BHF-UCLInferred from mutant phenotypei
- "Endothelial argininosuccinate synthetase 1 regulates nitric oxide production and monocyte adhesion under static and laminar shear stress conditions."
Mun G.I., Kim I.S., Lee B.H., Boo Y.C.
J Biol Chem 286:2536-2542(2011) [PubMed] [Europe PMC] [Abstract]
- cellular response to lipopolysaccharide Source: Ensembl
- cellular response to oleic acid Source: Ensembl
- cellular response to tumor necrosis factor Source: Ensembl
- circadian rhythm Source: UniProtKB
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.14"CLOCK acetylates ASS1 to drive circadian rhythm of ureagenesis."
Lin R., Mo Y., Zha H., Qu Z., Xie P., Zhu Z.J., Xu Y., Xiong Y., Guan K.L.
Mol. Cell 68:198-209(2017) [PubMed] [Europe PMC] [Abstract]Cited for: ACETYLATION AT LYS-165 AND LYS-176, MUTAGENESIS OF LYS-165 AND LYS-176, INTERACTION WITH CLOCK, SUBCELLULAR LOCATION.
- citrulline metabolic process Source: BHF-UCLInferred from mutant phenotypei
- Ref.20"Mutations in argininosuccinate synthetase mRNA of Japanese patients, causing classical citrullinemia."
Kobayashi K., Shaheen N., Terazono H., Saheki T.
Am. J. Hum. Genet. 55:1103-1112(1994) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS CTLN1 THR-118; VAL-192; CYS-272; ARG-280; TRP-304 AND LEU-363.
- diaphragm development Source: Ensembl
- kidney development Source: Ensembl
- liver development Source: Ensembl
- midgut development Source: Ensembl
- negative regulation of leukocyte cell-cell adhesion Source: BHF-UCLInferred from mutant phenotypei
- "Endothelial argininosuccinate synthetase 1 regulates nitric oxide production and monocyte adhesion under static and laminar shear stress conditions."
Mun G.I., Kim I.S., Lee B.H., Boo Y.C.
J Biol Chem 286:2536-2542(2011) [PubMed] [Europe PMC] [Abstract]
- positive regulation of nitric oxide biosynthetic process Source: BHF-UCLInferred from mutant phenotypei
- "Endothelial argininosuccinate synthetase 1 regulates nitric oxide production and monocyte adhesion under static and laminar shear stress conditions."
Mun G.I., Kim I.S., Lee B.H., Boo Y.C.
J Biol Chem 286:2536-2542(2011) [PubMed] [Europe PMC] [Abstract]
- response to drug Source: Ensembl
- response to estradiol Source: Ensembl
- response to growth hormone Source: Ensembl
- response to mycotoxin Source: Ensembl
- response to nutrient Source: Ensembl
- response to zinc ion Source: Ensembl
- urea cycle Source: UniProtKBInferred from mutant phenotypei
- Ref.26"Investigation of citrullinemia type I variants by in vitro expression studies."
Berning C., Bieger I., Pauli S., Vermeulen T., Vogl T., Rummel T., Hoehne W., Koch H.G., Rolinski B., Gempel K., Haeberle J.
Hum. Mutat. 29:1222-1227(2008) [PubMed] [Europe PMC] [Abstract]Cited for: 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, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.31"Kinetic mutations in argininosuccinate synthetase deficiency: characterisation and in vitro correction by substrate supplementation."
Diez-Fernandez C., Wellauer O., Gemperle C., Ruefenacht V., Fingerhut R., Haeberle J.
J. Med. Genet. 53:710-719(2016) [PubMed] [Europe PMC] [Abstract]Cited for: 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, SUBCELLULAR LOCATION. - Ref.15"Characterization of human wild-type and mutant argininosuccinate synthetase proteins expressed in bacterial cells."
Shaheen N., Kobayashi K., Terazono H., Fukushige T., Horiuchi M., Saheki T.
Enzyme Protein 48:251-264(1994) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANTS CLNT1 VAL-192; ARG-280; CYS-272 AND TRP-304, FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
Molecular function | Ligase |
Biological process | Amino-acid biosynthesis, Arginine biosynthesis, Urea cycle |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:HS05425-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 6.3.4.5, 2681 |
Pathway Commons web resource for biological pathway data More...PathwayCommonsi | P00966 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-70635, Urea cycle |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P00966 |
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00068;UER00113 UPA00158;UER00272 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Argininosuccinate synthaseCurated (EC:6.3.4.5
Manual assertion based on experiment ini
Alternative name(s): Citrulline--aspartate ligase |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen and Host Database Resources More...EuPathDBi | HostDB:ENSG00000130707.17 |
Human Gene Nomenclature Database More...HGNCi | HGNC:758, ASS1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 603470, gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P00966 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Cytosol
- cytosol 1 Publication
Manual assertion inferred by curator fromi
- Ref.31"Kinetic mutations in argininosuccinate synthetase deficiency: characterisation and in vitro correction by substrate supplementation."
Diez-Fernandez C., Wellauer O., Gemperle C., Ruefenacht V., Fingerhut R., Haeberle J.
J. Med. Genet. 53:710-719(2016) [PubMed] [Europe PMC] [Abstract]Cited for: 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, SUBCELLULAR LOCATION.
Manual assertion based on experiment ini
- Ref.14"CLOCK acetylates ASS1 to drive circadian rhythm of ureagenesis."
Lin R., Mo Y., Zha H., Qu Z., Xie P., Zhu Z.J., Xu Y., Xiong Y., Guan K.L.
Mol. Cell 68:198-209(2017) [PubMed] [Europe PMC] [Abstract]Cited for: ACETYLATION AT LYS-165 AND LYS-176, MUTAGENESIS OF LYS-165 AND LYS-176, INTERACTION WITH CLOCK, SUBCELLULAR LOCATION.
- cytosol 1 Publication
Cytosol
- cytosol Source: UniProtKBInferred from direct assayi
- Ref.14"CLOCK acetylates ASS1 to drive circadian rhythm of ureagenesis."
Lin R., Mo Y., Zha H., Qu Z., Xie P., Zhu Z.J., Xu Y., Xiong Y., Guan K.L.
Mol. Cell 68:198-209(2017) [PubMed] [Europe PMC] [Abstract]Cited for: ACETYLATION AT LYS-165 AND LYS-176, MUTAGENESIS OF LYS-165 AND LYS-176, INTERACTION WITH CLOCK, SUBCELLULAR LOCATION.
- cytosol Source: UniProtKBInferred from direct assayi
Endoplasmic reticulum
- endoplasmic reticulum Source: Ensembl
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
- "Large-scale proteomics and phosphoproteomics of urinary exosomes."
Gonzales P.A., Pisitkun T., Hoffert J.D., Tchapyjnikov D., Star R.A., Kleta R., Wang N.S., Knepper M.A.
J Am Soc Nephrol 20:363-379(2009) [PubMed] [Europe PMC] [Abstract] - "In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine."
Principe S., Jones E.E., Kim Y., Sinha A., Nyalwidhe J.O., Brooks J., Semmes O.J., Troyer D.A., Lance R.S., Kislinger T., Drake R.R.
Proteomics 13:1667-1671(2013) [PubMed] [Europe PMC] [Abstract]
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
Lysosome
- lysosome Source: Ensembl
Mitochondrion
- mitochondrial outer membrane Source: Ensembl
Nucleus
- nucleus Source: Ensembl
Other locations
- cell body fiber Source: Ensembl
- cytoplasm Source: GO_Central
<p>Inferred from Biological aspect of Ancestor</p>
<p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p>
Inferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
- perikaryon Source: Ensembl
Keywords - Cellular componenti
Cytoplasm<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Citrullinemia 1 (CTLN1)16 PublicationsManual assertion based on experiment ini
- Ref.3"Structure of the human argininosuccinate synthetase gene and an improved system for molecular diagnostics in patients with classical and mild citrullinemia."
Haeberle J., Pauli S., Linnebank M., Kleijer W.J., Bakker H.D., Wanders R.J.A., Harms E., Koch H.G.
Hum. Genet. 110:327-333(2002) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CTLN1 LEU-108; ARG-179; VAL-362 AND ARG-390. - Ref.18"Heterogeneity of mutations in argininosuccinate synthetase causing human citrullinemia."
Kobayashi K., Jackson M.J., Tick D.B., O'Brien W.E., Beaudet A.L.
J. Biol. Chem. 265:11361-11367(1990) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN CTLN1, VARIANTS CTLN1 SER-14; HIS-157; ASN-180; TRP-304; SER-324; TRP-363 AND ARG-390. - Ref.19"Additional mutations in argininosuccinate synthetase causing citrullinemia."
Kobayashi K., Rosenbloom C., Beaudet A.L., O'Brien W.E.
Mol. Biol. Med. 8:95-100(1991) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS CTLN1 LEU-18 AND CYS-86. - Ref.20"Mutations in argininosuccinate synthetase mRNA of Japanese patients, causing classical citrullinemia."
Kobayashi K., Shaheen N., Terazono H., Saheki T.
Am. J. Hum. Genet. 55:1103-1112(1994) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS CTLN1 THR-118; VAL-192; CYS-272; ARG-280; TRP-304 AND LEU-363. - Ref.21"Phenotype and genotype heterogeneity in Mediterranean citrullinemia."
Vilaseca M.A., Kobayashi K., Briones P., Lambruschini N., Campistol J., Tabata A., Alomar A., Rodes M., Lluch M., Saheki T.
Mol. Genet. Metab. 74:396-398(2001) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS CTLN1 ALA-69; LEU-108; ASP-117; ILE-119; GLN-270 AND ARG-390. - Ref.22"Identification of 16 novel mutations in the argininosuccinate synthetase gene and genotype-phenotype correlation in 38 classical citrullinemia patients."
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.
Hum. Mutat. 22:24-34(2003) [PubMed] [Europe PMC] [Abstract]Cited for: 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. - Ref.23"Mild citrullinemia in Caucasians is an allelic variant of argininosuccinate synthetase deficiency (citrullinemia type 1)."
Haeberle J., Pauli S., Schmidt E., Schulze-Eilfing B., Berning C., Koch H.G.
Mol. Genet. Metab. 80:302-306(2003) [PubMed] [Europe PMC] [Abstract]Cited for: 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. - Ref.24"Postpartum 'psychosis' in mild argininosuccinate synthetase deficiency."
Enns G.M., O'Brien W.E., Kobayashi K., Shinzawa H., Pellegrino J.E.
Obstet. Gynecol. 105:1244-1246(2005) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT CTLN1 ARG-310. - Ref.25"Prenatal diagnosis of citrullinemia and argininosuccinic aciduria: evidence for a transmission ratio distortion in citrullinemia."
Kleijer W.J., Garritsen V.H., van der Sterre M.L., Berning C., Haeberle J., Huijmans J.G.M.
Prenat. Diagn. 26:242-247(2006) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS CTLN1 ASN-124; HIS-157; GLN-270; GLN-279; LYS-283; SER-324; GLY-363 AND ARG-390. - Ref.26"Investigation of citrullinemia type I variants by in vitro expression studies."
Berning C., Bieger I., Pauli S., Vermeulen T., Vogl T., Rummel T., Hoehne W., Koch H.G., Rolinski B., Gempel K., Haeberle J.
Hum. Mutat. 29:1222-1227(2008) [PubMed] [Europe PMC] [Abstract]Cited for: 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, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.27"Mutations and polymorphisms in the human argininosuccinate synthetase (ASS1) gene."
Engel K., Hoehne W., Haeberle J.
Hum. Mutat. 30:300-307(2009) [PubMed] [Europe PMC] [Abstract]Cited for: 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. - Ref.28"Prenatal diagnosis of citrullinemia type 1: a Chinese family with a novel mutation of the ASS1 gene."
Wu T.F., Liu Y.P., Li X.Y., Wang Q., Song J.Q., Yang Y.L.
Brain Dev. 36:264-267(2014) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS CTLN1 LYS-283 AND ARG-337. - Ref.29"Improved standards for prenatal diagnosis of citrullinemia."
Miller M.J., Soler-Alfonso C.R., Grund J.E., Fang P., Sun Q., Elsea S.H., Sutton V.R.
Mol. Genet. Metab. 112:205-209(2014) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS CTLN1 PRO-91; CYS-157; ILE-180; LYS-283 AND ARG-390, VARIANT LEU-127. - Ref.30"Functional analysis of novel splicing and missense mutations identified in the ASS1 gene in classical citrullinemia patients."
Kimani J.K., Wei T., Chol K., Li Y., Yu P., Ye S., Huang X., Qi M.
Clin. Chim. Acta 438:323-329(2015) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS CTLN1 GLY-141 AND CYS-265. - Ref.31"Kinetic mutations in argininosuccinate synthetase deficiency: characterisation and in vitro correction by substrate supplementation."
Diez-Fernandez C., Wellauer O., Gemperle C., Ruefenacht V., Fingerhut R., Haeberle J.
J. Med. Genet. 53:710-719(2016) [PubMed] [Europe PMC] [Abstract]Cited for: 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, SUBCELLULAR LOCATION. - Ref.32"Mutations in the human argininosuccinate synthetase (ASS1) gene, impact on patients, common changes, and structural considerations."
Diez-Fernandez C., Ruefenacht V., Haeberle J.
Hum. Mutat. 38:471-484(2017) [PubMed] [Europe PMC] [Abstract]Cited for: 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.
Haeberle J., Pauli S., Linnebank M., Kleijer W.J., Bakker H.D., Wanders R.J.A., Harms E., Koch H.G.
Hum. Genet. 110:327-333(2002) [PubMed] [Europe PMC] [Abstract]
Kobayashi K., Jackson M.J., Tick D.B., O'Brien W.E., Beaudet A.L.
J. Biol. Chem. 265:11361-11367(1990) [PubMed] [Europe PMC] [Abstract]
Kobayashi K., Rosenbloom C., Beaudet A.L., O'Brien W.E.
Mol. Biol. Med. 8:95-100(1991) [PubMed] [Europe PMC] [Abstract]
Kobayashi K., Shaheen N., Terazono H., Saheki T.
Am. J. Hum. Genet. 55:1103-1112(1994) [PubMed] [Europe PMC] [Abstract]
Vilaseca M.A., Kobayashi K., Briones P., Lambruschini N., Campistol J., Tabata A., Alomar A., Rodes M., Lluch M., Saheki T.
Mol. Genet. Metab. 74:396-398(2001) [PubMed] [Europe PMC] [Abstract]
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.
Hum. Mutat. 22:24-34(2003) [PubMed] [Europe PMC] [Abstract]
Haeberle J., Pauli S., Schmidt E., Schulze-Eilfing B., Berning C., Koch H.G.
Mol. Genet. Metab. 80:302-306(2003) [PubMed] [Europe PMC] [Abstract]
Enns G.M., O'Brien W.E., Kobayashi K., Shinzawa H., Pellegrino J.E.
Obstet. Gynecol. 105:1244-1246(2005) [PubMed] [Europe PMC] [Abstract]
Kleijer W.J., Garritsen V.H., van der Sterre M.L., Berning C., Haeberle J., Huijmans J.G.M.
Prenat. Diagn. 26:242-247(2006) [PubMed] [Europe PMC] [Abstract]
Berning C., Bieger I., Pauli S., Vermeulen T., Vogl T., Rummel T., Hoehne W., Koch H.G., Rolinski B., Gempel K., Haeberle J.
Hum. Mutat. 29:1222-1227(2008) [PubMed] [Europe PMC] [Abstract]
Engel K., Hoehne W., Haeberle J.
Hum. Mutat. 30:300-307(2009) [PubMed] [Europe PMC] [Abstract]
Wu T.F., Liu Y.P., Li X.Y., Wang Q., Song J.Q., Yang Y.L.
Brain Dev. 36:264-267(2014) [PubMed] [Europe PMC] [Abstract]
Miller M.J., Soler-Alfonso C.R., Grund J.E., Fang P., Sun Q., Elsea S.H., Sutton V.R.
Mol. Genet. Metab. 112:205-209(2014) [PubMed] [Europe PMC] [Abstract]
Kimani J.K., Wei T., Chol K., Li Y., Yu P., Ye S., Huang X., Qi M.
Clin. Chim. Acta 438:323-329(2015) [PubMed] [Europe PMC] [Abstract]
Diez-Fernandez C., Wellauer O., Gemperle C., Ruefenacht V., Fingerhut R., Haeberle J.
J. Med. Genet. 53:710-719(2016) [PubMed] [Europe PMC] [Abstract]
Diez-Fernandez C., Ruefenacht V., Haeberle J.
Hum. Mutat. 38:471-484(2017) [PubMed] [Europe PMC] [Abstract]
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000681 | 14 | G → S in CTLN1. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_000682 | 18 | S → L in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015891 | 19 | C → R in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078387 | 27 – 412 | Missing in CTLN1. 1 Publication Manual assertion based on experiment ini
| 386 | |
Natural variantiVAR_058337 | 40 | Q → L in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078388 | 64 | V → I in CTLN1; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_016013 | 69 | V → A in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_058338 | 79 | S → P in CTLN1. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_000683 | 86 | R → C in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015892 | 86 | R → H in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078389 | 91 | T → P in CTLN1; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015893 | 95 | R → S in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_058339 | 96 | P → H in CTLN1; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078390 | 96 | P → L in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; loss of argininosuccinate synthase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015894 | 96 | P → S in CTLN1; no effect on thermal stability; decreased argininosuccinate synthase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078391 | 97 – 412 | Missing in CTLN1. 1 Publication Manual assertion based on experiment ini
| 316 | |
Natural variantiVAR_078392 | 100 | R → C in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078393 | 100 | R → H in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_016014 | 108 | R → L in CTLN1. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078394 | 111 | A → D in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078395 | 117 | G → C in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015896 | 117 | G → D in CTLN1. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015895 | 117 | G → S in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_000684 | 118 | A → T in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_016015 | 119 | T → I in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_058340 | 124 | D → N in CTLN1; loss of argininosuccinate synthase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_058341 | 127 | R → Q in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_058342 | 127 | R → W in CTLN1; severe clinical course; loss of argininosuccinate synthase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078397 | 138 – 412 | Missing in CTLN1. 1 Publication Manual assertion based on experiment ini
| 275 | |
Natural variantiVAR_072792 | 141 | V → G in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015897 | 157 | R → C in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_000685 | 157 | R → H in CTLN1; loss of argininosuccinate synthase activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078398 | 157 | R → S in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_058343 | 160 | L → P in CTLN1. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078399 | 163 – 412 | Missing in CTLN1. 1 Publication Manual assertion based on experiment ini
| 250 | |
Natural variantiVAR_078400 | 164 | A → P in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015898 | 179 | W → R in CTLN1; mild; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity. 4 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078401 | 180 | S → I in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_000686 | 180 | S → N in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078402 | 184 | N → K in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_058344 | 190 | Y → D in CTLN1. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015899 | 191 | E → K in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_058345 | 191 | E → Q in CTLN1; loss of argininosuccinate synthase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_000687 | 192 | A → V in CTLN1; decreased protein abundance. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_058346 | 202 | A → E in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_058347 | 206 | L → P in CTLN1. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078403 | 230 | G → R in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078404 | 237 | N → I in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078405 | 258 | A → P in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078406 | 258 | A → V in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_058348 | 263 | V → M in CTLN1; mild clinical course; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_058349 | 265 | R → C in CTLN1; severe clinical course; loss of argininosuccinate synthase activity. 4 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015900 | 265 | R → H in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015901 | 269 | V → M in CTLN1. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_016007 | 270 | E → Q in CTLN1; loss of argininosuccinate synthase activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_000688 | 272 | R → C in CTLN1; increased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity. 4 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078407 | 272 | R → H in CTLN1; increased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078408 | 272 | R → L in CTLN1; increased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078409 | 275 – 412 | Missing in CTLN1. 1 Publication Manual assertion based on experiment ini
| 138 | |
Natural variantiVAR_058350 | 277 | K → T in CTLN1. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078410 | 279 – 412 | Missing in CTLN1. 1 Publication Manual assertion based on experiment ini
| 134 | |
Natural variantiVAR_016008 | 279 | R → Q in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_000689 | 280 | G → R in CTLN1; loss of argininosuccinate synthase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015902 | 283 | E → K in CTLN1. 4 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_058351 | 284 | T → I in CTLN1; mild clinical course. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078411 | 290 | L → P in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_058352 | 291 | Y → S in CTLN1. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_058353 | 296 | D → G in CTLN1. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078412 | 299 | A → D in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_058354 | 302 | M → V in CTLN1; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_000690 | 304 | R → W in CTLN1; decreased protein abundance. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078413 | 306 | V → G in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_058355 | 307 | R → C in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_016009 | 310 | K → Q in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015903 | 310 | K → R in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078414 | 311 – 412 | Missing in CTLN1. 1 Publication Manual assertion based on experiment ini
| 102 | |
Natural variantiVAR_078415 | 321 | V → M in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_000691 | 324 | G → S in CTLN1; loss of argininosuccinate synthase activity. 6 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_058356 | 324 | G → V in CTLN1. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078416 | 335 | R → H in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078417 | 337 | C → R in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_058357 | 341 | S → F in CTLN1. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078418 | 344 – 412 | Missing in CTLN1. 1 Publication Manual assertion based on experiment ini
| 69 | |
Natural variantiVAR_058358 | 345 | V → G in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_058359 | 347 | G → R in CTLN1; severe clinical course. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078419 | 356 | G → V in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078420 | 357 – 412 | Missing in CTLN1. 1 Publication Manual assertion based on experiment ini
| 56 | |
Natural variantiVAR_058360 | 359 | Y → D in CTLN1; mild clinical course. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015904 | 362 | G → V in CTLN1; mild; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity. 4 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_016010 | 363 | R → G in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_000692 | 363 | R → L in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_016011 | 363 | R → Q in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_000693 | 363 | R → W in CTLN1. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078421 | 380 – 412 | Missing in CTLN1. 1 Publication Manual assertion based on experiment ini
| 33 | |
Natural variantiVAR_016012 | 389 | T → I in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078422 | 389 | T → P in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_000694 | 390 | G → R in CTLN1; loss of argininosuccinate synthase activity. 7 Publications Manual assertion based on experiment ini
| 1 |
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 165 | K → Q or R: Significant loss of acetylation but no decrease in enzyme activity; when associated with Q-176 or R-176. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 176 | K → Q or R: Significant loss of acetylation but no decrease in enzyme activity; when associated with Q-165 or R-165. 1 Publication Manual assertion based on experiment ini
| 1 |
Keywords - Diseasei
Disease mutationOrganism-specific databases
DisGeNET More...DisGeNETi | 445 |
GeneReviews a resource of expert-authored, peer-reviewed disease descriptions. More...GeneReviewsi | ASS1 |
MalaCards human disease database More...MalaCardsi | ASS1 |
MIMi | 215700, phenotype |
Open Targets More...OpenTargetsi | ENSG00000130707 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 247546, Acute neonatal citrullinemia type I 247573, Adult-onset citrullinemia type I |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA162376926 |
Miscellaneous databases
Pharos NIH Druggable Genome Knowledgebase More...Pharosi | P00966, Tbio |
Chemistry databases
Drug and drug target database More...DrugBanki | DB00125, Arginine DB00128, Aspartic acid DB00171, ATP DB00155, Citrulline |
DrugCentral More...DrugCentrali | P00966 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | ASS1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 20141195 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000148554 | 1 – 412 | Argininosuccinate synthaseAdd BLAST | 412 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 87 | PhosphotyrosineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
Modified residuei | 112 | N6-acetyllysineBy similarity Manual assertion inferred from sequence similarity toi | 1 | |
Modified residuei | 113 | PhosphotyrosineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 165 | N6-acetyllysine; by CLOCK1 Publication Manual assertion based on experiment ini
| 1 | |
Modified residuei | 176 | N6-acetyllysine; by CLOCK1 Publication Manual assertion based on experiment ini
| 1 | |
Modified residuei | 180 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 219 | PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
Manual assertion based on experiment ini
- Ref.14"CLOCK acetylates ASS1 to drive circadian rhythm of ureagenesis."
Lin R., Mo Y., Zha H., Qu Z., Xie P., Zhu Z.J., Xu Y., Xiong Y., Guan K.L.
Mol. Cell 68:198-209(2017) [PubMed] [Europe PMC] [Abstract]Cited for: ACETYLATION AT LYS-165 AND LYS-176, MUTAGENESIS OF LYS-165 AND LYS-176, INTERACTION WITH CLOCK, SUBCELLULAR LOCATION.
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
The CPTAC Assay portal More...CPTACi | CPTAC-169 CPTAC-170 |
Encyclopedia of Proteome Dynamics More...EPDi | P00966 |
jPOST - Japan Proteome Standard Repository/Database More...jPOSTi | P00966 |
MassIVE - Mass Spectrometry Interactive Virtual Environment More...MassIVEi | P00966 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P00966 |
PeptideAtlas More...PeptideAtlasi | P00966 |
PRoteomics IDEntifications database More...PRIDEi | P00966 |
ProteomicsDB: a multi-organism proteome resource More...ProteomicsDBi | 51293 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P00966 |
MetOSite database of methionine sulfoxide sites More...MetOSitei | P00966 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P00966 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
Manual assertion based on experiment ini
- Ref.9"Molecular characterization of the murine argininosuccinate synthetase locus."
Surh L.C., Beaudet A.L., O'Brien W.E.
Gene 99:181-189(1991) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei
Manual assertion based on experiment ini
- Ref.9"Molecular characterization of the murine argininosuccinate synthetase locus."
Surh L.C., Beaudet A.L., O'Brien W.E.
Gene 99:181-189(1991) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000130707, Expressed in nephron tubule and 242 other tissues |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P00966, baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P00966, HS |
Organism-specific databases
Human Protein Atlas More...HPAi | ENSG00000130707, Group enriched (kidney, liver) |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Homotetramer (PubMed:18323623).
Interacts with NMRAL1 (PubMed:17496144).
Interacts with CLOCK; in a circadian manner (PubMed:28985504).
3 PublicationsManual assertion based on experiment ini
- Ref.14"CLOCK acetylates ASS1 to drive circadian rhythm of ureagenesis."
Lin R., Mo Y., Zha H., Qu Z., Xie P., Zhu Z.J., Xu Y., Xiong Y., Guan K.L.
Mol. Cell 68:198-209(2017) [PubMed] [Europe PMC] [Abstract]Cited for: ACETYLATION AT LYS-165 AND LYS-176, MUTAGENESIS OF LYS-165 AND LYS-176, INTERACTION WITH CLOCK, SUBCELLULAR LOCATION. - Ref.17"Structure of human argininosuccinate synthetase."
Karlberg T., Collins R., van den Berg S., Flores A., Hammarstrom M., Hogbom M., Holmberg Schiavone L., Uppenberg J.
Acta Crystallogr. D 64:279-286(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH CITRULLINE AND ASPARTATE, SUBUNIT.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
Show more detailsHide detailsP00966
With | #Exp. | IntAct |
---|---|---|
ARAF [P10398] | 4 | EBI-536842,EBI-365961 |
itself | 3 | EBI-536842,EBI-536842 |
NMRAL1 [Q9HBL8] | 3 | EBI-536842,EBI-2862643 |
PRMT7 [Q9NVM4] | 9 | EBI-536842,EBI-3215577 |
GO - Molecular functioni
- identical protein binding Source: IntActInferred from physical interactioni
- "Towards a proteome-scale map of the human protein-protein interaction network."
Rual J.F., Venkatesan K., Hao T., Hirozane-Kishikawa T., Dricot A., Li N., Berriz G.F., Gibbons F.D., Dreze M., Ayivi-Guedehoussou N., Klitgord N., Simon C., Boxem M., Milstein S., Rosenberg J., Goldberg D.S., Zhang L.V., Wong S.L. , Franklin G., Li S., Albala J.S., Lim J., Fraughton C., Llamosas E., Cevik S., Bex C., Lamesch P., Sikorski R.S., Vandenhaute J., Zoghbi H.Y., Smolyar A., Bosak S., Sequerra R., Doucette-Stamm L., Cusick M.E., Hill D.E., Roth F.P., Vidal M.
Nature 437:1173-1178(2005) [PubMed] [Europe PMC] [Abstract] - "Toward an understanding of the protein interaction network of the human liver."
Wang J., Huo K., Ma L., Tang L., Li D., Huang X., Yuan Y., Li C., Wang W., Guan W., Chen H., Jin C., Wei J., Zhang W., Yang Y., Liu Q., Zhou Y., Zhang C. , Wu Z., Xu W., Zhang Y., Liu T., Yu D., Zhang Y., Chen L., Zhu D., Zhong X., Kang L., Gan X., Yu X., Ma Q., Yan J., Zhou L., Liu Z., Zhu Y., Zhou T., He F., Yang X.
Mol Syst Biol 7:536-536(2011) [PubMed] [Europe PMC] [Abstract] - "A proteome-scale map of the human interactome network."
Rolland T., Tasan M., Charloteaux B., Pevzner S.J., Zhong Q., Sahni N., Yi S., Lemmens I., Fontanillo C., Mosca R., Kamburov A., Ghiassian S.D., Yang X., Ghamsari L., Balcha D., Begg B.E., Braun P., Brehme M. , Broly M.P., Carvunis A.R., Convery-Zupan D., Corominas R., Coulombe-Huntington J., Dann E., Dreze M., Dricot A., Fan C., Franzosa E., Gebreab F., Gutierrez B.J., Hardy M.F., Jin M., Kang S., Kiros R., Lin G.N., Luck K., MacWilliams A., Menche J., Murray R.R., Palagi A., Poulin M.M., Rambout X., Rasla J., Reichert P., Romero V., Ruyssinck E., Sahalie J.M., Scholz A., Shah A.A., Sharma A., Shen Y., Spirohn K., Tam S., Tejeda A.O., Trigg S.A., Twizere J.C., Vega K., Walsh J., Cusick M.E., Xia Y., Barabasi A.L., Iakoucheva L.M., Aloy P., De Las Rivas J., Tavernier J., Calderwood M.A., Hill D.E., Hao T., Roth F.P., Vidal M.
Cell 159:1212-1226(2014) [PubMed] [Europe PMC] [Abstract]
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGRID) More...BioGRIDi | 106937, 105 interactors |
Database of interacting proteins More...DIPi | DIP-34055N |
Protein interaction database and analysis system More...IntActi | P00966, 31 interactors |
Molecular INTeraction database More...MINTi | P00966 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000361471 |
Miscellaneous databases
RNAct, Protein-RNA interaction predictions for model organisms. More...RNActi | P00966, protein |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 5 – 10 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 15 – 26 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
Beta strandi | 29 – 39 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
Helixi | 44 – 54 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
Beta strandi | 57 – 63 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
Helixi | 65 – 71 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
Helixi | 73 – 78 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 84 – 86 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Turni | 90 – 93 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 94 – 109 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 16 | |
Beta strandi | 112 – 115 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 124 – 135 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
Beta strandi | 140 – 142 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 144 – 146 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 148 – 151 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 158 – 166 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
Beta strandi | 181 – 183 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 188 – 190 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 193 – 196 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 204 – 206 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Turni | 213 – 215 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 221 – 228 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
Beta strandi | 231 – 237 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
Turni | 238 – 240 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 247 – 261 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
Beta strandi | 265 – 271 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
Beta strandi | 277 – 283 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
Helixi | 285 – 301 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 17 | |
Helixi | 304 – 323 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 20 | |
Beta strandi | 326 – 328 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 329 – 341 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
Turni | 342 – 344 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 347 – 354 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
Beta strandi | 357 – 364 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
Helixi | 372 – 375 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 385 – 404 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 20 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P00966 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P00966 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1706, Eukaryota |
Ensembl GeneTree More...GeneTreei | ENSGT00390000004524 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | CLU_032784_4_2_1 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P00966 |
Identification of Orthologs from Complete Genome Data More...OMAi | FHIRSGG |
Database of Orthologous Groups More...OrthoDBi | 1459745at2759 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P00966 |
TreeFam database of animal gene trees More...TreeFami | TF300736 |
Family and domain databases
Conserved Domains Database More...CDDi | cd01999, Argininosuccinate_Synthase, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.40.50.620, 1 hit 3.90.1260.10, 1 hit |
HAMAP database of protein families More...HAMAPi | MF_00005, Arg_succ_synth_type1, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001518, Arginosuc_synth IPR018223, Arginosuc_synth_CS IPR023434, Arginosuc_synth_type_1_subfam IPR024074, AS_cat/multimer_dom_body IPR014729, Rossmann-like_a/b/a_fold |
The PANTHER Classification System More...PANTHERi | PTHR11587, PTHR11587, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00764, Arginosuc_synth, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF69864, SSF69864, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR00032, argG, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00564, ARGININOSUCCIN_SYN_1, 1 hit PS00565, ARGININOSUCCIN_SYN_2, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All
10 20 30 40 50
MSSKGSVVLA YSGGLDTSCI LVWLKEQGYD VIAYLANIGQ KEDFEEARKK
60 70 80 90 100
ALKLGAKKVF IEDVSREFVE EFIWPAIQSS ALYEDRYLLG TSLARPCIAR
110 120 130 140 150
KQVEIAQREG AKYVSHGATG KGNDQVRFEL SCYSLAPQIK VIAPWRMPEF
160 170 180 190 200
YNRFKGRNDL MEYAKQHGIP IPVTPKNPWS MDENLMHISY EAGILENPKN
210 220 230 240 250
QAPPGLYTKT QDPAKAPNTP DILEIEFKKG VPVKVTNVKD GTTHQTSLEL
260 270 280 290 300
FMYLNEVAGK HGVGRIDIVE NRFIGMKSRG IYETPAGTIL YHAHLDIEAF
310 320 330 340 350
TMDREVRKIK QGLGLKFAEL VYTGFWHSPE CEFVRHCIAK SQERVEGKVQ
360 370 380 390 400
VSVLKGQVYI LGRESPLSLY NEELVSMNVQ GDYEPTDATG FININSLRLK
410
EYHRLQSKVT AK
<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketEntry | Entry name | Protein names | Gene names | Length | Annotation | ||
---|---|---|---|---|---|---|---|
Q5T6L5 | Q5T6L5_HUMAN | Citrulline--aspartate ligase Citrulline--aspartate ligase, EC 6.3.4.5 | ASS1 | 179 | Annotation score: Annotation score:2 out of 5 <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p> | ||
Q5T6L6 | Q5T6L6_HUMAN | Citrulline--aspartate ligase Citrulline--aspartate ligase, EC 6.3.4.5 | ASS1 | 198 | Annotation score: Annotation score:2 out of 5 <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p> |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 325 – 327 | FWH → LRP in CAA25771 (PubMed:6194510).Curated | 3 | |
Sequence conflicti | 325 – 327 | FWH → LRP in AAA51783 (PubMed:6321498).Curated | 3 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_000681 | 14 | G → S in CTLN1. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_000682 | 18 | S → L in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015891 | 19 | C → R in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078387 | 27 – 412 | Missing in CTLN1. 1 Publication Manual assertion based on experiment ini
| 386 | |
Natural variantiVAR_058337 | 40 | Q → L in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078388 | 64 | V → I in CTLN1; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_016013 | 69 | V → A in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_058338 | 79 | S → P in CTLN1. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_000683 | 86 | R → C in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015892 | 86 | R → H in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078389 | 91 | T → P in CTLN1; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015893 | 95 | R → S in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_058339 | 96 | P → H in CTLN1; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078390 | 96 | P → L in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; loss of argininosuccinate synthase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015894 | 96 | P → S in CTLN1; no effect on thermal stability; decreased argininosuccinate synthase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078391 | 97 – 412 | Missing in CTLN1. 1 Publication Manual assertion based on experiment ini
| 316 | |
Natural variantiVAR_078392 | 100 | R → C in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078393 | 100 | R → H in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_016014 | 108 | R → L in CTLN1. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078394 | 111 | A → D in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078395 | 117 | G → C in CTLN1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015896 | 117 | G → D in CTLN1. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_015895 | 117 | G → S in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_000684 | 118 | A → T in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_016015 | 119 | T → I in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_058340 | 124 | D → N in CTLN1; loss of argininosuccinate synthase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_078396 | 127 | R → L Increased thermal stability; loss of argininosuccinate synthase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_058341 | 127 | R → Q in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_058342 | 127 | R → W in CTLN1; severe clinical course; loss of argininosuccinate synthase activity. 2 Publications Manual assertion based on experiment ini
|