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P31327 (CPSM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 167. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carbamoyl-phosphate synthase [ammonia], mitochondrial

EC=6.3.4.16
Alternative name(s):
Carbamoyl-phosphate synthetase I
Short name=CPSase I
Gene names
Name:CPS1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1500 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell. HAMAP-Rule MF_01209

Catalytic activity

2 ATP + NH3 + CO2 + H2O = 2 ADP + phosphate + carbamoyl phosphate. HAMAP-Rule MF_01209

Enzyme regulation

Requires N-acetyl-L-glutamate (NAG) as an allosteric activator. HAMAP-Rule MF_01209

Subcellular location

Mitochondrion. Nucleusnucleolus Ref.15.

Tissue specificity

Primarily in the liver and small intestine.

Domain

The type-1 glutamine amidotransferase domain is defective. HAMAP-Rule MF_01209

Post-translational modification

Succinylated at Lys-287 and Lys-1291. Desuccinylated at Lys-1291 by SIRT5, leading to activation By similarity. HAMAP-Rule MF_01209

Involvement in disease

Carbamoyl phosphate synthetase 1 deficiency (CPS1D) [MIM:237300]: An autosomal recessive disorder of the urea cycle causing hyperammonemia. It can present as a devastating metabolic disease dominated by severe hyperammonemia in neonates or as a more insidious late-onset condition, generally manifesting as life-threatening hyperammonemic crises under catabolic situations. Clinical features include protein intolerance, intermittent ataxia, seizures, lethargy, developmental delay and mental retardation.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.5 Ref.6 Ref.17 Ref.18 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.26

Pulmonary hypertension, neonatal (PHN) [MIM:615371]: A disease characterized by elevated pulmonary artery pressure. Pulmonary hypertension in the neonate is associated with multiple underlying problems such as respiratory distress syndrome, meconium aspiration syndrome, congenital diaphragmatic hernia, bronchopulmonary dysplasia, sepsis, or congenital heart disease.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. CPS1 variants influence the availability of precursors for nitric oxide (NO) synthesis and play a role in clinical situations where endogenous NO production is critically important, such as neonatal pulmonary hypertension, increased pulmonary artery pressure following surgical repair of congenital heart defects or hepatovenocclusive disease following bone marrow transplantation. Infants with neonatal pulmonary hypertension homozygous for Thr-1406 have lower L-arginine concentrations than neonates homozygous for Asn-1406 (Ref.19). Ref.19

Sequence similarities

Contains 2 ATP-grasp domains.

Contains 1 glutamine amidotransferase type-1 domain.

Sequence caution

The sequence BAD92037.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processUrea cycle
   Cellular componentMitochondrion
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainRepeat
Transit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Allosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanion homeostasis

Inferred from electronic annotation. Source: Ensembl

carbamoyl phosphate biosynthetic process

Inferred from mutant phenotype PubMed 7416778. Source: UniProtKB

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

cellular response to cAMP

Inferred from electronic annotation. Source: Ensembl

cellular response to fibroblast growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to glucagon stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to oleic acid

Inferred from electronic annotation. Source: Ensembl

citrulline biosynthetic process

Non-traceable author statement PubMed 14718356. Source: BHF-UCL

glutamine catabolic process

Inferred from electronic annotation. Source: InterPro

glycogen catabolic process

Inferred from mutant phenotype Ref.2. Source: BHF-UCL

hepatocyte differentiation

Inferred from electronic annotation. Source: Ensembl

homocysteine metabolic process

Inferred from direct assay PubMed 20031578. Source: UniProtKB

midgut development

Inferred from electronic annotation. Source: Ensembl

nitric oxide metabolic process

Inferred from mutant phenotype PubMed 14718356. Source: BHF-UCL

positive regulation of vasodilation

Inferred from mutant phenotype PubMed 14718356. Source: BHF-UCL

response to amine

Inferred from electronic annotation. Source: Ensembl

response to amino acid

Inferred from electronic annotation. Source: Ensembl

response to dexamethasone

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to food

Inferred from electronic annotation. Source: Ensembl

response to growth hormone

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from direct assay PubMed 15897806. Source: UniProtKB

response to starvation

Inferred from electronic annotation. Source: Ensembl

response to toxic substance

Inferred from electronic annotation. Source: Ensembl

response to zinc ion

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

triglyceride catabolic process

Inferred from mutant phenotype Ref.2. Source: BHF-UCL

urea cycle

Non-traceable author statement Ref.1. Source: BHF-UCL

   Cellular_componentmitochondrial inner membrane

Inferred from electronic annotation. Source: Ensembl

mitochondrial matrix

Traceable author statement. Source: Reactome

mitochondrial nucleoid

Inferred from direct assay PubMed 18063578. Source: BHF-UCL

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

calcium ion binding

Inferred from electronic annotation. Source: Ensembl

carbamoyl-phosphate synthase (ammonia) activity

Inferred from mutant phenotype PubMed 8486760Ref.2. Source: BHF-UCL

endopeptidase activity

Inferred from electronic annotation. Source: Ensembl

glutamate binding

Inferred from electronic annotation. Source: Ensembl

modified amino acid binding

Inferred from direct assay PubMed 20031578. Source: UniProtKB

phospholipid binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P31327-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P31327-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-451: Missing.
Isoform 3 (identifier: P31327-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPQIIKM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3838Mitochondrion By similarity
Chain39 – 15001462Carbamoyl-phosphate synthase [ammonia], mitochondrial HAMAP-Rule MF_01209
PRO_0000029897

Regions

Domain219 – 404186Glutamine amidotransferase type-1
Domain551 – 743193ATP-grasp 1
Domain1093 – 1284192ATP-grasp 2
Region39 – 218180Anthranilate phosphoribosyltransferase homolog HAMAP-Rule MF_01209

Sites

Binding site13911Allosteric activator Probable
Binding site13941Allosteric activator Probable
Binding site14101Allosteric activator Probable
Binding site14371Allosteric activator Probable
Binding site14401Allosteric activator Probable
Binding site14491Allosteric activator Probable

Amino acid modifications

Modified residue551N6-acetyllysine; alternate By similarity
Modified residue551N6-succinyllysine; alternate By similarity
Modified residue571N6-acetyllysine; alternate By similarity
Modified residue571N6-succinyllysine; alternate By similarity
Modified residue1191N6-acetyllysine; alternate By similarity
Modified residue1191N6-succinyllysine; alternate By similarity
Modified residue1571N6-acetyllysine; alternate By similarity
Modified residue1571N6-succinyllysine; alternate By similarity
Modified residue1711N6-acetyllysine By similarity
Modified residue1821N6-acetyllysine By similarity
Modified residue1971N6-acetyllysine By similarity
Modified residue2071N6-acetyllysine; alternate By similarity
Modified residue2071N6-succinyllysine; alternate By similarity
Modified residue2101N6-acetyllysine By similarity
Modified residue2141N6-acetyllysine; alternate By similarity
Modified residue2141N6-succinyllysine; alternate By similarity
Modified residue2191N6-acetyllysine By similarity
Modified residue2281N6-acetyllysine By similarity
Modified residue2801N6-acetyllysine By similarity
Modified residue2871N6-acetyllysine; alternate By similarity
Modified residue2871N6-succinyllysine; alternate By similarity
Modified residue3071N6-acetyllysine; alternate By similarity
Modified residue3071N6-succinyllysine; alternate By similarity
Modified residue3101N6-acetyllysine By similarity
Modified residue4001N6-succinyllysine By similarity
Modified residue4021N6-succinyllysine By similarity
Modified residue4121N6-acetyllysine; alternate By similarity
Modified residue4121N6-succinyllysine; alternate By similarity
Modified residue4531N6-acetyllysine By similarity
Modified residue4581N6-acetyllysine; alternate By similarity
Modified residue4581N6-succinyllysine; alternate By similarity
Modified residue5221N6-acetyllysine; alternate By similarity
Modified residue5221N6-succinyllysine; alternate By similarity
Modified residue5271N6-acetyllysine; alternate By similarity
Modified residue5271N6-succinyllysine; alternate By similarity
Modified residue5321N6-acetyllysine By similarity
Modified residue5371Phosphoserine By similarity
Modified residue5531N6-acetyllysine; alternate By similarity
Modified residue5531N6-succinyllysine; alternate By similarity
Modified residue5601N6-acetyllysine; alternate By similarity
Modified residue5601N6-succinyllysine; alternate By similarity
Modified residue5751N6-acetyllysine; alternate By similarity
Modified residue5751N6-succinyllysine; alternate By similarity
Modified residue6121N6-acetyllysine; alternate By similarity
Modified residue6121N6-succinyllysine; alternate By similarity
Modified residue6301N6-acetyllysine By similarity
Modified residue7511N6-acetyllysine; alternate By similarity
Modified residue7511N6-succinyllysine; alternate By similarity
Modified residue7571N6-acetyllysine; alternate By similarity
Modified residue7571N6-succinyllysine; alternate By similarity
Modified residue7721N6-acetyllysine By similarity
Modified residue7931N6-acetyllysine; alternate By similarity
Modified residue7931N6-succinyllysine; alternate By similarity
Modified residue8111N6-acetyllysine By similarity
Modified residue8311N6-acetyllysine; alternate By similarity
Modified residue8311N6-succinyllysine; alternate By similarity
Modified residue8411N6-acetyllysine By similarity
Modified residue8561N6-acetyllysine By similarity
Modified residue8751N6-acetyllysine; alternate By similarity
Modified residue8751N6-succinyllysine; alternate By similarity
Modified residue8891N6-acetyllysine; alternate By similarity
Modified residue8891N6-succinyllysine; alternate By similarity
Modified residue8921N6-acetyllysine; alternate By similarity
Modified residue8921N6-succinyllysine; alternate By similarity
Modified residue9081N6-acetyllysine By similarity
Modified residue9151N6-acetyllysine; alternate By similarity
Modified residue9151N6-succinyllysine; alternate By similarity
Modified residue9191N6-acetyllysine; alternate By similarity
Modified residue9191N6-succinyllysine; alternate By similarity
Modified residue9351N6-acetyllysine By similarity
Modified residue10741N6-acetyllysine; alternate By similarity
Modified residue10741N6-succinyllysine; alternate By similarity
Modified residue10791Phosphoserine By similarity
Modified residue11001N6-acetyllysine; alternate By similarity
Modified residue11001N6-succinyllysine; alternate By similarity
Modified residue11491N6-succinyllysine By similarity
Modified residue11681N6-acetyllysine; alternate By similarity
Modified residue11681N6-succinyllysine; alternate By similarity
Modified residue11831N6-acetyllysine; alternate By similarity
Modified residue11831N6-succinyllysine; alternate By similarity
Modified residue12221N6-acetyllysine By similarity
Modified residue12321N6-acetyllysine; alternate By similarity
Modified residue12321N6-succinyllysine; alternate By similarity
Modified residue12691N6-acetyllysine; alternate By similarity
Modified residue12691N6-succinyllysine; alternate By similarity
Modified residue12911N6-acetyllysine; alternate By similarity
Modified residue12911N6-succinyllysine; alternate By similarity
Modified residue13561N6-acetyllysine; alternate By similarity
Modified residue13561N6-succinyllysine; alternate By similarity
Modified residue13601N6-succinyllysine By similarity
Modified residue14441N6-acetyllysine; alternate By similarity
Modified residue14441N6-succinyllysine; alternate By similarity
Modified residue14711N6-acetyllysine; alternate By similarity
Modified residue14711N6-succinyllysine; alternate By similarity
Modified residue14791N6-acetyllysine; alternate By similarity
Modified residue14791N6-succinyllysine; alternate By similarity
Modified residue14861N6-acetyllysine; alternate By similarity
Modified residue14861N6-succinyllysine; alternate By similarity

Natural variations

Alternative sequence1 – 451451Missing in isoform 2.
VSP_009332
Alternative sequence11M → MPQIIKM in isoform 3.
VSP_046685
Natural variant431A → V in CPS1D. Ref.26
VAR_066171
Natural variant581G → D in CPS1D. Ref.26
VAR_066172
Natural variant651S → F in CPS1D. Ref.26
VAR_066173
Natural variant711V → G in CPS1D. Ref.26
VAR_066174
Natural variant791G → E in CPS1D. Ref.23
VAR_063560
Natural variant871P → S in CPS1D. Ref.26
VAR_066175
Natural variant891Y → D in CPS1D. Ref.26
VAR_066176
Natural variant1231S → F in CPS1D; modestly decreases enzyme activity. Ref.24
VAR_064062
Natural variant1651D → G in CPS1D. Ref.26
VAR_066177
Natural variant2121Y → N in CPS1D. Ref.23
VAR_063561
Natural variant2241D → V in CPS1D. Ref.26
VAR_066178
Natural variant2331R → C in CPS1D. Ref.26
VAR_066179
Natural variant2431H → P in CPS1D. Ref.26
VAR_066180
Natural variant2581G → E in CPS1D. Ref.26
VAR_066181
Natural variant2631G → E in CPS1D. Ref.26
VAR_066182
Natural variant2801K → N in CPS1D. Ref.23
VAR_063562
Natural variant3011G → E in CPS1D. Ref.22
VAR_066104
Natural variant3041A → V in CPS1D; associated with T-986. Ref.26
VAR_066183
Natural variant3171G → E in CPS1D. Ref.26
VAR_066184
Natural variant3371H → R in CPS1D; modestly decreases enzyme activity. Ref.18 Ref.24
Corresponds to variant rs28940283 [ dbSNP | Ensembl ].
VAR_014077
Natural variant3441T → A. Ref.2 Ref.3 Ref.11
Corresponds to variant rs1047883 [ dbSNP | Ensembl ].
VAR_006834
Natural variant3441T → S.
Corresponds to variant rs1047883 [ dbSNP | Ensembl ].
VAR_061752
Natural variant3581D → H in CPS1D. Ref.26
VAR_066185
Natural variant3821P → L in CPS1D. Ref.26
VAR_066186
Natural variant3891Y → C in CPS1D. Ref.22
VAR_066105
Natural variant3901L → R in CPS1D. Ref.22
VAR_066106
Natural variant4011G → R in CPS1D. Ref.26
VAR_066187
Natural variant4311G → R in CPS1D. Ref.26
VAR_066188
Natural variant4321G → V in CPS1D. Ref.26
VAR_066189
Natural variant4381A → P in CPS1D. Ref.23
VAR_063563
Natural variant4381A → T in CPS1D. Ref.26
VAR_066190
Natural variant4501K → E in CPS1D. Ref.26
VAR_066191
Natural variant4571V → G in CPS1D. Ref.5
VAR_017562
Natural variant4711T → N in CPS1D. Ref.24
VAR_064063
Natural variant4981A → P in CPS1D. Ref.26
VAR_066192
Natural variant5301G → V Found in a patient with VACTERL syndrome and postsurgical PHN; variant of unknown pathological significance. Ref.27
VAR_070211
Natural variant5311V → E in CPS1D. Ref.26
VAR_066193
Natural variant5311V → G in CPS1D. Ref.26
VAR_066194
Natural variant5441T → M in CPS1D. Ref.2 Ref.26
VAR_006835
Natural variant5871R → C in CPS1D. Ref.26
VAR_066195
Natural variant5871R → H in CPS1D. Ref.23 Ref.26
VAR_063564
Natural variant5871R → L in CPS1D. Ref.26
VAR_066196
Natural variant5891A → T in CPS1D. Ref.22
VAR_066142
Natural variant5931G → R in CPS1D. Ref.23
VAR_063565
Natural variant5971S → L in CPS1D. Ref.26
VAR_066197
Natural variant6221V → M in CPS1D. Ref.26
VAR_066198
Natural variant6281G → D in CPS1D. Ref.26
VAR_066199
Natural variant6321I → R in CPS1D. Ref.26
VAR_066200
Natural variant6381R → P in CPS1D. Ref.26
VAR_066201
Natural variant6401A → S in CPS1D. Ref.22
Corresponds to variant rs142693704 [ dbSNP | Ensembl ].
VAR_066143
Natural variant6481C → Y in CPS1D. Ref.26
VAR_066202
Natural variant6511E → K in CPS1D. Ref.23
VAR_063566
Natural variant6541D → V in CPS1D. Ref.26
VAR_066203
Natural variant6741N → I in CPS1D. Ref.23
VAR_063567
Natural variant6741N → K in CPS1D. Ref.26
VAR_066204
Natural variant6781Q → P in CPS1D; results in a poor enzyme expression and solubility; hampers correct enzyme folding. Ref.24
VAR_064064
Natural variant6981N → S in CPS1D. Ref.26
VAR_066205
Natural variant7161N → K in CPS1D. Ref.22
VAR_066144
Natural variant7181R → K in CPS1D. Ref.26
VAR_066107
Natural variant7211R → Q in CPS1D. Ref.26
VAR_066108
Natural variant7241A → P in CPS1D. Ref.26
VAR_066109
Natural variant7261A → T in CPS1D. Ref.26
VAR_066110
Natural variant7671D → V in CPS1D. Ref.26
VAR_066111
Natural variant7741P → L in CPS1D; the enzyme is inactive. Ref.24
VAR_064065
Natural variant7801R → H in CPS1D. Ref.23 Ref.26
VAR_063568
Natural variant7921M → I in CPS1D. Ref.26
VAR_066112
Natural variant8031R → C in CPS1D. Ref.26
VAR_066145
Natural variant8031R → G in CPS1D. Ref.26
VAR_066146
Natural variant8031R → S in CPS1D. Ref.26
VAR_066147
Natural variant8051F → L in CPS1D. Ref.22
VAR_066148
Natural variant8051F → S in CPS1D. Ref.26
VAR_066149
Natural variant8101Q → R in CPS1D. Ref.5
VAR_017563
Natural variant8141R → W in CPS1D. Ref.26
VAR_066150
Natural variant8161C → R in CPS1D. Ref.26
VAR_066151
Natural variant8431L → S in CPS1D. Ref.6 Ref.21
VAR_017564
Natural variant8501R → C in CPS1D. Ref.23
VAR_063569
Natural variant8501R → H in CPS1D. Ref.20 Ref.26
VAR_030675
Natural variant8751K → E in CPS1D. Ref.6 Ref.21
Corresponds to variant rs147062907 [ dbSNP | Ensembl ].
VAR_017565
Natural variant9111G → E in CPS1D. Ref.26
VAR_066152
Natural variant9111G → V in CPS1D. Ref.22
VAR_066153
Natural variant9131S → L in CPS1D. Ref.26
VAR_066154
Natural variant9141D → G in CPS1D. Ref.26
VAR_066155
Natural variant9141D → H in CPS1D. Ref.26
VAR_066156
Natural variant9181S → P in CPS1D. Ref.20
VAR_030676
Natural variant9321R → T in CPS1D. Ref.26
VAR_066157
Natural variant9491A → T in CPS1D. Ref.26
VAR_066158
Natural variant9581L → P in CPS1D. Ref.22
VAR_066159
Natural variant9591Y → C in CPS1D. Ref.26
VAR_066160
Natural variant9621Y → C in CPS1D. Ref.26
VAR_066161
Natural variant9781V → E in CPS1D. Ref.26
VAR_066113
Natural variant9821G → D in CPS1D. Ref.23
VAR_063570
Natural variant9821G → S in CPS1D. Ref.22
VAR_066162
Natural variant9821G → V in CPS1D. Ref.26
VAR_066114
Natural variant9841Y → H in CPS1D. Ref.26
VAR_066115
Natural variant9861I → T in CPS1D; associated with V-304. Ref.26
VAR_066116
Natural variant9871G → C in CPS1D; may affect splicing. Ref.26
VAR_066117
Natural variant9921F → S in CPS1D. Ref.26
VAR_066118
Natural variant9981S → F in CPS1D. Ref.22
VAR_066163
Natural variant10161N → S in CPS1D. Ref.26
VAR_066119
Natural variant10171P → L in CPS1D. Ref.26
VAR_066120
Natural variant10221T → I in CPS1D. Ref.26
VAR_066121
Natural variant10341E → G in CPS1D. Ref.26
VAR_066122
Natural variant10451H → R in CPS1D. Ref.26
VAR_066123
Natural variant10541I → R in CPS1D. Ref.17
VAR_066164
Natural variant10591Q → R in CPS1D. Ref.26
VAR_066124
Natural variant10651A → E in CPS1D. Ref.26
VAR_066125
Natural variant10891R → C in CPS1D. Ref.26
VAR_066126
Natural variant10891R → L in CPS1D. Ref.22
VAR_066165
Natural variant11031Q → R in CPS1D. Ref.23
VAR_063571
Natural variant11411V → G in CPS1D. Ref.23
VAR_063572
Natural variant11551A → E in CPS1D. Ref.26
VAR_066127
Natural variant11551A → V in CPS1D. Ref.26
VAR_066128
Natural variant11951H → P in CPS1D. Ref.23
VAR_063573
Natural variant12031S → L in CPS1D. Ref.26
VAR_066129
Natural variant12031S → P in CPS1D. Ref.22
VAR_066166
Natural variant12051D → N in CPS1D. Ref.22
VAR_066167
Natural variant12151I → V in CPS1D. Ref.23
Corresponds to variant rs141373204 [ dbSNP | Ensembl ].
VAR_063574
Natural variant12281R → Q in CPS1D. Ref.26
VAR_066130
Natural variant12411N → K in CPS1D. Ref.23
VAR_063575
Natural variant12551E → D in CPS1D. Ref.26
VAR_066131
Natural variant12621R → P in CPS1D. Ref.26
VAR_066132
Natural variant12621R → Q in CPS1D. Ref.26
VAR_066133
Natural variant12661F → S. Ref.1
Corresponds to variant rs1047886 [ dbSNP | Ensembl ].
VAR_017566
Natural variant12741D → H in CPS1D. Ref.26
VAR_066134
Natural variant12831M → L. Ref.1
Corresponds to variant rs1047887 [ dbSNP | Ensembl ].
VAR_017567
Natural variant13271C → R in CPS1D. Ref.26
VAR_066135
Natural variant13311S → P in CPS1D. Ref.22
VAR_066168
Natural variant13331G → E in CPS1D. Ref.26
VAR_066136
Natural variant13711R → L in CPS1D. Ref.26
VAR_066137
Natural variant13761G → S Polymorphism with no functional consequences. Ref.3 Ref.24
Corresponds to variant rs140578009 [ dbSNP | Ensembl ].
VAR_017568
Natural variant13781A → T in CPS1D. Ref.22
VAR_066169
Natural variant13911T → M in CPS1D. Ref.26
VAR_066138
Natural variant13981L → V in CPS1D. Ref.26
VAR_066139
Natural variant14061T → N Associated with PHN susceptibility; 30-40% higher activity; also highly associated with hepatocellular carcinoma (HCC) progression. Ref.1 Ref.3 Ref.5 Ref.19 Ref.25 Ref.27 Ref.28
Corresponds to variant rs1047891 [ dbSNP | Ensembl ].
VAR_017569
Natural variant14111P → L in CPS1D; modestly decreases enzyme activity. Ref.22 Ref.24
VAR_064066
Natural variant14391P → L in CPS1D. Ref.26
VAR_066140
Natural variant14431T → A in CPS1D. Ref.22
VAR_066170
Natural variant14531R → Q in CPS1D; the enzyme is inactive. Ref.24
VAR_064067
Natural variant14531R → W in CPS1D; the enzyme is inactive. Ref.24 Ref.26
VAR_064068
Natural variant14621P → R in CPS1D. Ref.26
VAR_066141
Natural variant14911Y → H in CPS1D; triggers a large decrease in the apparent affinity for N-acetyl-L-glutamate (NAG). Ref.24
VAR_064069

Experimental info

Sequence conflict1111A → S in BAA14328. Ref.1
Sequence conflict2791R → Q in BAA14328. Ref.1
Sequence conflict3381G → C in BAA14328. Ref.1
Sequence conflict718 – 7225RLSRS → KMSPN in BAA14328. Ref.1
Sequence conflict7291A → T in BAA14328. Ref.1
Sequence conflict7491E → G in BAA14328. Ref.1
Sequence conflict9121F → L in CAE45707. Ref.6
Sequence conflict1161 – 11622EH → AT in BAA14328. Ref.1
Sequence conflict1204 – 12052GD → EN in BAA14328. Ref.1
Sequence conflict12541I → N in BAA14328. Ref.1
Sequence conflict13031A → V in BAA14328. Ref.1
Isoform 3:
Sequence conflict51I → IF in BAD92037. Ref.11

Secondary structure

......................... 1500
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: E53A22D77563961D

FASTA1,500164,939
        10         20         30         40         50         60 
MTRILTAFKV VRTLKTGFGF TNVTAHQKWK FSRPGIRLLS VKAQTAHIVL EDGTKMKGYS 

        70         80         90        100        110        120 
FGHPSSVAGE VVFNTGLGGY PEAITDPAYK GQILTMANPI IGNGGAPDTT ALDELGLSKY 

       130        140        150        160        170        180 
LESNGIKVSG LLVLDYSKDY NHWLATKSLG QWLQEEKVPA IYGVDTRMLT KIIRDKGTML 

       190        200        210        220        230        240 
GKIEFEGQPV DFVDPNKQNL IAEVSTKDVK VYGKGNPTKV VAVDCGIKNN VIRLLVKRGA 

       250        260        270        280        290        300 
EVHLVPWNHD FTKMEYDGIL IAGGPGNPAL AEPLIQNVRK ILESDRKEPL FGISTGNLIT 

       310        320        330        340        350        360 
GLAAGAKTYK MSMANRGQNQ PVLNITNKQA FITAQNHGYA LDNTLPAGWK PLFVNVNDQT 

       370        380        390        400        410        420 
NEGIMHESKP FFAVQFHPEV TPGPIDTEYL FDSFFSLIKK GKATTITSVL PKPALVASRV 

       430        440        450        460        470        480 
EVSKVLILGS GGLSIGQAGE FDYSGSQAVK AMKEENVKTV LMNPNIASVQ TNEVGLKQAD 

       490        500        510        520        530        540 
TVYFLPITPQ FVTEVIKAEQ PDGLILGMGG QTALNCGVEL FKRGVLKEYG VKVLGTSVES 

       550        560        570        580        590        600 
IMATEDRQLF SDKLNEINEK IAPSFAVESI EDALKAADTI GYPVMIRSAY ALGGLGSGIC 

       610        620        630        640        650        660 
PNRETLMDLS TKAFAMTNQI LVEKSVTGWK EIEYEVVRDA DDNCVTVCNM ENVDAMGVHT 

       670        680        690        700        710        720 
GDSVVVAPAQ TLSNAEFQML RRTSINVVRH LGIVGECNIQ FALHPTSMEY CIIEVNARLS 

       730        740        750        760        770        780 
RSSALASKAT GYPLAFIAAK IALGIPLPEI KNVVSGKTSA CFEPSLDYMV TKIPRWDLDR 

       790        800        810        820        830        840 
FHGTSSRIGS SMKSVGEVMA IGRTFEESFQ KALRMCHPSI EGFTPRLPMN KEWPSNLDLR 

       850        860        870        880        890        900 
KELSEPSSTR IYAIAKAIDD NMSLDEIEKL TYIDKWFLYK MRDILNMEKT LKGLNSESMT 

       910        920        930        940        950        960 
EETLKRAKEI GFSDKQISKC LGLTEAQTRE LRLKKNIHPW VKQIDTLAAE YPSVTNYLYV 

       970        980        990       1000       1010       1020 
TYNGQEHDVN FDDHGMMVLG CGPYHIGSSV EFDWCAVSSI RTLRQLGKKT VVVNCNPETV 

      1030       1040       1050       1060       1070       1080 
STDFDECDKL YFEELSLERI LDIYHQEACG GCIISVGGQI PNNLAVPLYK NGVKIMGTSP 

      1090       1100       1110       1120       1130       1140 
LQIDRAEDRS IFSAVLDELK VAQAPWKAVN TLNEALEFAK SVDYPCLLRP SYVLSGSAMN 

      1150       1160       1170       1180       1190       1200 
VVFSEDEMKK FLEEATRVSQ EHPVVLTKFV EGAREVEMDA VGKDGRVISH AISEHVEDAG 

      1210       1220       1230       1240       1250       1260 
VHSGDATLML PTQTISQGAI EKVKDATRKI AKAFAISGPF NVQFLVKGND VLVIECNLRA 

      1270       1280       1290       1300       1310       1320 
SRSFPFVSKT LGVDFIDVAT KVMIGENVDE KHLPTLDHPI IPADYVAIKA PMFSWPRLRD 

      1330       1340       1350       1360       1370       1380 
ADPILRCEMA STGEVACFGE GIHTAFLKAM LSTGFKIPQK GILIGIQQSF RPRFLGVAEQ 

      1390       1400       1410       1420       1430       1440 
LHNEGFKLFA TEATSDWLNA NNVPATPVAW PSQEGQNPSL SSIRKLIRDG SIDLVINLPN 

      1450       1460       1470       1480       1490       1500 
NNTKFVHDNY VIRRTAVDSG IPLLTNFQVT KLFAEAVQKS RKVDSKSLFH YRQYSAGKAA 

« Hide

Isoform 2 [UniParc].

Checksum: 74C9ABBFABAD2AD2
Show »

FASTA1,049116,038
Isoform 3 [UniParc].

Checksum: 35B58EDD104A9503
Show »

FASTA1,506165,650

References

« Hide 'large scale' references
[1]"Cloning and sequence of a cDNA encoding human carbamyl phosphate synthetase I: molecular analysis of hyperammonemia."
Haraguchi Y., Uchino T., Takiguchi M., Endo F., Mori M., Matsuda I.
Gene 107:335-340(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS SER-1266; LEU-1283 AND ASN-1406.
Tissue: Liver.
[2]"Prenatal diagnosis of carbamoyl phosphate synthetase I deficiency by identification of a missense mutation in CPS1."
Finckh U., Kohlschuetter A., Schaefer H., Sperhake K., Colombo J.-P., Gal A.
Hum. Mutat. 12:206-211(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT CPS1D MET-544, VARIANT ALA-344.
Tissue: Liver.
[3]"Characterization of genomic structure and polymorphisms in the human carbamyl phosphate synthetase I gene."
Summar M.L., Hall L.D., Eeds A.M., Hutcheson H.B., Kuo A.N., Willis A.S., Rubio V., Arvin M.K., Schofield J.P., Dawson E.P.
Gene 311:51-57(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ALA-344; SER-1376 AND ASN-1406.
[4]"Cloning of an isoform of CPS1 gene related to spermatogenesis."
Huo R., Zhu H., Huang X.Y., Xu Z.Y., Lu L., Xu M., Yin L.L., Li J.M., Zhou Z.M., Sha J.H.
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Testis.
[5]"Structural organization of the human carbamyl phosphate synthetase I gene (CPS1) and identification of two novel genetic lesions."
Funghini S., Donati M.A., Pasquini E., Zammarchi E., Morrone A.
Hum. Mutat. 22:340-341(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS CPS1D GLY-457 AND ARG-810, VARIANT ASN-1406.
[6]"Gene structure of human carbamylphosphate synthetase 1 and novel mutations in patients with neonatal onset."
Haeberle J., Schmidt E., Pauli S., Rapp B., Christensen E., Wermuth B., Koch H.G.
Hum. Mutat. 21:444-444(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS CPS1D SER-843 AND GLU-875.
[7]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Testis.
[8]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[11]"Homo sapiens protein coding cDNA."
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT ALA-344.
Tissue: Brain.
[12]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 795-1500.
Tissue: Small intestine.
[13]"Structural insight on the control of urea synthesis: identification of the binding site for N-acetyl-L-glutamate, the essential allosteric activator of mitochondrial carbamoyl phosphate synthetase."
Pekkala S., Martinez A.I., Barcelona B., Gallego J., Bendala E., Yefimenko I., Rubio V., Cervera J.
Biochem. J. 424:211-220(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ALLOSTERIC ACTIVATOR NAG BINDING SITE.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Systematic analysis of protein pools, isoforms, and modifications affecting turnover and subcellular localization."
Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.
Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[16]"Crystal structure of MGS domain of carbamoyl-phosphate synthetase from Homo sapiens."
RIKEN structural genomics initiative (RSGI)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 1343-1478.
[17]"Genetic analysis of carbamoylphosphate synthetase I and ornithine transcarbamylase deficiency using fibroblasts."
Rapp B., Haberle J., Linnebank M., Wermuth B., Marquardt T., Harms E., Koch H.G.
Eur. J. Pediatr. 160:283-287(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CPS1D ARG-1054.
[18]"Novel mutations (H337R and 238-362del) in the CPS1 gene cause carbamoyl phosphate synthetase I deficiency."
Aoshima T., Kajita M., Sekido Y., Kikuchi S., Yasuda I., Saheki T., Watanabe K., Shimokata K., Niwa T.
Hum. Hered. 52:99-101(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CPS1D ARG-337.
[19]"Neonatal pulmonary hypertension -- urea-cycle intermediates, nitric oxide production, and carbamoyl-phosphate synthetase function."
Pearson D.L., Dawling S., Walsh W.F., Haines J.L., Christman B.W., Bazyk A., Scott N., Summar M.L.
N. Engl. J. Med. 344:1832-1838(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ASN-1406, INVOLVEMENT IN PHN.
[20]"Mutational analysis of carbamoylphosphate synthetase I deficiency in three Japanese patients."
Wakutani Y., Nakayasu H., Takeshima T., Adachi M., Kawataki M., Kihira K., Sawada H., Bonno M., Yamamoto H., Nakashima K.
J. Inherit. Metab. Dis. 27:787-788(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CPS1D HIS-850 AND PRO-918.
[21]"Genetic approach to prenatal diagnosis in urea cycle defects."
Haeberle J., Koch H.G.
Prenat. Diagn. 24:378-383(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CPS1D SER-843 AND GLU-875.
[22]"The frequent observation of evidence for nonsense-mediated decay in RNA from patients with carbamyl phosphate synthetase I deficiency."
Eeds A.M., Hall L.D., Yadav M., Willis A., Summar S., Putnam A., Barr F., Summar M.L.
Mol. Genet. Metab. 89:80-86(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CPS1D GLU-301; CYS-389; ARG-390; THR-589; SER-640; LYS-716; LEU-805; VAL-911; PRO-958; SER-982; PHE-998; LEU-1089; PRO-1203; ASN-1205; PRO-1331; THR-1378; LEU-1411 AND ALA-1443.
[23]"Molecular and clinical analyses of Japanese patients with carbamoylphosphate synthetase 1 (CPS1) deficiency."
Kurokawa K., Yorifuji T., Kawai M., Momoi T., Nagasaka H., Takayanagi M., Kobayashi K., Yoshino M., Kosho T., Adachi M., Otsuka H., Yamamoto S., Murata T., Suenaga A., Ishii T., Terada K., Shimura N., Kiwaki K. expand/collapse author list , Shintaku H., Yamakawa M., Nakabayashi H., Wakutani Y., Nakahata T.
J. Hum. Genet. 52:349-354(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CPS1D GLU-79; ASN-212; ASN-280; PRO-438; HIS-587; ARG-593; LYS-651; ILE-674; HIS-780; CYS-850; ASP-982; ARG-1103; GLY-1141; PRO-1195; VAL-1215 AND LYS-1241.
[24]"Understanding carbamoyl-phosphate synthetase I (CPS1) deficiency by using expression studies and structure-based analysis."
Pekkala S., Martinez A.I., Barcelona B., Yefimenko I., Finckh U., Rubio V., Cervera J.
Hum. Mutat. 31:801-808(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CPS1D PHE-123; ARG-337; ASN-471; PRO-678; LEU-774; LEU-1411; GLN-1453; TRP-1453 AND HIS-1491, VARIANT SER-1376, CHARACTERIZATION OF VARIANTS CPS1D PHE-123; ARG-337; ASN-471; PRO-678; LEU-774; LEU-1411; GLN-1453; TRP-1453 AND HIS-1491, CHARACTERIZATION OF VARIANT SER-1376.
[25]"The T1405N carbamoyl phosphate synthetase polymorphism does not affect plasma arginine concentrations in preterm infants."
Moonen R.M., Reyes I., Cavallaro G., Gonzalez-Luis G., Bakker J.A., Villamor E.
PLoS ONE 5:E10792-E10792(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ASN-1406.
[26]"Molecular defects in human carbamoyl phosphate synthetase I: mutational spectrum, diagnostic and protein structure considerations."
Haberle J., Shchelochkov O.A., Wang J., Katsonis P., Hall L., Reiss S., Eeds A., Willis A., Yadav M., Summar S., Lichtarge O., Rubio V., Wong L.J., Summar M.
Hum. Mutat. 32:579-589(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CPS1D VAL-43; ASP-58; PHE-65; GLY-71; SER-87; ASP-89; GLY-165; VAL-224; CYS-233; PRO-243; GLU-258; GLU-263; VAL-304; GLU-317; HIS-358; LEU-382; ARG-401; ARG-431; VAL-432; THR-438; GLU-450; PRO-498; GLU-531; GLY-531; MET-544; CYS-587; HIS-587; LEU-587; LEU-597; MET-622; ASP-628; ARG-632; PRO-638; TYR-648; VAL-654; LYS-674; SER-698; LYS-718; GLN-721; PRO-724; THR-726; VAL-767; HIS-780; ILE-792; SER-803; GLY-803; CYS-803; SER-805; TRP-814; ARG-816; HIS-850; GLU-911; LEU-913; HIS-914; GLY-914; THR-932; THR-949; CYS-959; CYS-962; GLU-978; VAL-982; HIS-984; THR-986; CYS-987; SER-992; SER-1016; LEU-1017; ILE-1022; GLY-1034; ARG-1045; ARG-1059; GLU-1065; CYS-1089; GLU-1155; VAL-1155; LEU-1203; GLN-1228; ASP-1255; GLN-1262; PRO-1262; HIS-1274; ARG-1327; GLU-1333; LEU-1371; MET-1391; VAL-1398; LEU-1439; TRP-1453 AND ARG-1462.
[27]"Personalized genomic medicine: lessons from the exome."
NISC Comparative Sequencing Program
Solomon B.D., Pineda-Alvarez D.E., Hadley D.W., Teer J.K., Cherukuri P.F., Hansen N.F., Cruz P., Young A.C., Blakesley R.W., Lanpher B., Mayfield Gibson S., Sincan M., Chandrasekharappa S.C., Mullikin J.C.
Mol. Genet. Metab. 104:189-191(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VAL-530 AND ASN-1406.
[28]"Large-scale quantification of single amino-acid variations by a variation-associated database search strategy."
Song C., Wang F., Cheng K., Wei X., Bian Y., Wang K., Tan Y., Wang H., Ye M., Zou H.
J. Proteome Res. 13:241-248(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ASN-1406.
+Additional computationally mapped references.

Web resources

GeneReviews
LOVD-Leiden Open Variation Database

Carbamoyl-Phosphate Synthetase 1 (CPS1)

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D90282 mRNA. Translation: BAA14328.1.
Y15793 mRNA. Translation: CAA75785.1.
AF154830 mRNA. Translation: AAD38072.1.
AY317138 mRNA. Translation: AAP84318.1.
AY167007 expand/collapse EMBL AC list , AY166970, AY166971, AY166972, AY166973, AY166974, AY166975, AY166976, AY166977, AY166978, AY166979, AY166980, AY166981, AY166982, AY166983, AY166984, AY166985, AY166986, AY166987, AY166988, AY166989, AY166990, AY166991, AY166992, AY166993, AY166994, AY166995, AY166996, AY166997, AY166998, AY166999, AY167000, AY167001, AY167002, AY167003, AY167004, AY167005, AY167006 Genomic DNA. Translation: AAO31763.1.
AF536523 Genomic DNA. Translation: AAN77181.1.
AK302778 mRNA. Translation: BAH13804.1.
AC007970 Genomic DNA. No translation available.
AC008172 Genomic DNA. Translation: AAY14960.1.
CH471063 Genomic DNA. Translation: EAW70492.1.
BC140943 mRNA. Translation: AAI40944.1.
AB208800 mRNA. Translation: BAD92037.1. Different initiation.
BX640601 mRNA. Translation: CAE45707.1.
PIRJQ1348.
RefSeqNP_001116105.1. NM_001122633.2.
NP_001116106.1. NM_001122634.2.
NP_001866.2. NM_001875.4.
UniGeneHs.149252.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YVQX-ray1.98A1343-1478[»]
ProteinModelPortalP31327.
SMRP31327. Positions 44-404, 416-820, 971-1478.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107764. 21 interactions.
IntActP31327. 7 interactions.
MINTMINT-4991575.
STRING9606.ENSP00000402608.

Chemistry

ChEMBLCHEMBL2362990.

Protein family/group databases

MEROPSC26.951.

PTM databases

PhosphoSiteP31327.

Polymorphism databases

DMDM4033707.

Proteomic databases

PaxDbP31327.
PRIDEP31327.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000233072; ENSP00000233072; ENSG00000021826. [P31327-1]
ENST00000430249; ENSP00000402608; ENSG00000021826. [P31327-3]
ENST00000451903; ENSP00000406136; ENSG00000021826. [P31327-2]
GeneID1373.
KEGGhsa:1373.
UCSCuc002vee.4. human. [P31327-1]

Organism-specific databases

CTD1373.
GeneCardsGC02P211342.
HGNCHGNC:2323. CPS1.
HPACAB003781.
HPA021400.
MIM237300. phenotype.
608307. gene.
615371. phenotype.
neXtProtNX_P31327.
Orphanet147. Carbamoylphosphate synthetase deficiency.
PharmGKBPA26840.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0458.
HOGENOMHOG000234583.
HOVERGENHBG000279.
InParanoidP31327.
KOK01948.
OMARLVVIEM.
OrthoDBEOG7M6D6F.
PhylomeDBP31327.
TreeFamTF331485.

Enzyme and pathway databases

BioCycMetaCyc:HS00415-MONOMER.
BRENDA6.3.4.16. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKP31327.

Gene expression databases

ArrayExpressP31327.
BgeeP31327.
CleanExHS_CPS1.
GenevestigatorP31327.

Family and domain databases

Gene3D1.10.1030.10. 1 hit.
3.30.1490.20. 2 hits.
3.30.470.20. 2 hits.
3.40.50.1380. 1 hit.
3.40.50.20. 2 hits.
3.50.30.20. 1 hit.
HAMAPMF_01209. CPSase_S_chain.
InterProIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006275. CarbamoylP_synth_lsu.
IPR005481. CarbamoylP_synth_lsu_N.
IPR005480. CarbamoylP_synth_lsu_oligo.
IPR006274. CarbamoylP_synth_ssu.
IPR002474. CarbamoylP_synth_ssu_N.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR005483. CbamoylP_synth_lsu_CPSase_dom.
IPR017926. GATASE.
IPR011607. MGS-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamPF00289. CPSase_L_chain. 2 hits.
PF02786. CPSase_L_D2. 2 hits.
PF02787. CPSase_L_D3. 1 hit.
PF00988. CPSase_sm_chain. 1 hit.
PF00117. GATase. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PRINTSPR00098. CPSASE.
SMARTSM01096. CPSase_L_D3. 1 hit.
SM01097. CPSase_sm_chain. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMSSF48108. SSF48108. 1 hit.
SSF52021. SSF52021. 1 hit.
SSF52335. SSF52335. 1 hit.
SSF52440. SSF52440. 2 hits.
TIGRFAMsTIGR01369. CPSaseII_lrg. 1 hit.
TIGR01368. CPSaseIIsmall. 1 hit.
PROSITEPS50975. ATP_GRASP. 2 hits.
PS00866. CPSASE_1. 2 hits.
PS00867. CPSASE_2. 2 hits.
PS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCPS1. human.
EvolutionaryTraceP31327.
GenomeRNAi1373.
NextBio35535364.
PROP31327.
SOURCESearch...

Entry information

Entry nameCPSM_HUMAN
AccessionPrimary (citable) accession number: P31327
Secondary accession number(s): B7Z818 expand/collapse secondary AC list , J3KQL0, O43774, Q53TL5, Q59HF8, Q7Z5I5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: December 15, 1998
Last modified: April 16, 2014
This is version 167 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM