UniProtKB - P27708 (PYR1_HUMAN)
Protein
CAD protein
Gene
CAD
Organism
Homo sapiens (Human)
Status
Functioni
This protein is a 'fusion' protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase).1 Publication
Miscellaneous
GATase (glutamine amidotransferase) and CPSase (carbamoyl phosphate synthase) form together the glutamine-dependent CPSase (GD-CPSase) (EC 6.3.5.5).Curated
Catalytic activityi
- 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H+ + L-glutamate + phosphate1 PublicationEC:6.3.5.51 Publication
- EC:2.1.3.21 Publication
- EC:3.5.2.31 Publication
Cofactori
Protein has several cofactor binding sites:- Zn2+2 PublicationsNote: Binds 3 Zn2+ ions per subunit (for dihydroorotase activity).2 Publications
- Mg2+PROSITE-ProRule annotation, Mn2+PROSITE-ProRule annotationNote: Binds 4 magnesium or manganese ions per subunit.PROSITE-ProRule annotation
Activity regulationi
Allosterically regulated and controlled by phosphorylation. 5-phosphoribose 1-diphosphate (PRPP) is an activator while UMP and UTP are inhibitors of the CPSase reaction.1 Publication
Kineticsi
- KM=28 µM for dihydroorotate1 Publication
- KM=241 µM for N-carbamoyl-L-aspartate1 Publication
: UMP biosynthesis via de novo pathway Pathwayi
This protein is involved in step 1, 2 and 3 of the subpathway that synthesizes (S)-dihydroorotate from bicarbonate.1 PublicationProteins known to be involved in the 3 steps of the subpathway in this organism are:
- CAD protein (CAD)
- CAD protein (CAD), Aspartate carbamoyltransferase (CAD)
- CAD protein (CAD), Aspartate carbamoyltransferase (CAD), Aspartate carbamoyltransferase (CAD)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-dihydroorotate from bicarbonate, the pathway UMP biosynthesis via de novo pathway and in Pyrimidine metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 252 | Nucleophile; for GATase activityPROSITE-ProRule annotation | 1 | |
Active sitei | 336 | For GATase activityPROSITE-ProRule annotation | 1 | |
Active sitei | 338 | For GATase activityPROSITE-ProRule annotation | 1 | |
Metal bindingi | 668 | Magnesium or manganese 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 682 | Magnesium or manganese 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 682 | Magnesium or manganese 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 684 | Magnesium or manganese 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 1202 | Magnesium or manganese 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 1214 | Magnesium or manganese 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 1214 | Magnesium or manganese 4PROSITE-ProRule annotation | 1 | |
Metal bindingi | 1216 | Magnesium or manganese 4PROSITE-ProRule annotation | 1 | |
Metal bindingi | 1471 | Zinc 1; via tele nitrogen1 Publication | 1 | |
Metal bindingi | 1471 | Zinc 2; via pros nitrogen1 Publication | 1 | |
Metal bindingi | 1473 | Zinc 1; via tele nitrogen1 Publication | 1 | |
Binding sitei | 1475 | N-carbamoyl-L-aspartate1 Publication | 1 | |
Binding sitei | 1505 | N-carbamoyl-L-aspartate1 Publication | 1 | |
Metal bindingi | 1556 | Zinc 1; via carbamate group1 Publication | 1 | |
Metal bindingi | 1556 | Zinc 3; via carbamate group1 Publication | 1 | |
Metal bindingi | 1590 | Zinc 3; via pros nitrogen1 Publication | 1 | |
Metal bindingi | 1613 | Zinc 21 Publication | 1 | |
Metal bindingi | 1614 | Zinc 3; via tele nitrogen1 Publication | 1 | |
Metal bindingi | 1637 | Zinc 21 Publication | 1 | |
Binding sitei | 1661 | N-carbamoyl-L-aspartate; via amide nitrogen and carbonyl oxygen1 Publication | 1 | |
Metal bindingi | 1686 | Zinc 11 Publication | 1 | |
Binding sitei | 1686 | N-carbamoyl-L-aspartate1 Publication | 1 | |
Binding sitei | 1690 | N-carbamoyl-L-aspartate1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 545 – 600 | ATPPROSITE-ProRule annotationAdd BLAST | 56 | |
Nucleotide bindingi | 1078 – 1135 | ATPPROSITE-ProRule annotationAdd BLAST | 58 |
GO - Molecular functioni
- aspartate binding Source: BHF-UCL
- aspartate carbamoyltransferase activity Source: BHF-UCL
- ATP binding Source: BHF-UCL
- carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Source: BHF-UCL
- dihydroorotase activity Source: UniProtKB
- enzyme binding Source: UniProtKB
- identical protein binding Source: IntAct
- protein kinase activity Source: BHF-UCL
- zinc ion binding Source: UniProtKB
GO - Biological processi
- 'de novo' pyrimidine nucleobase biosynthetic process Source: UniProtKB
- 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
- animal organ regeneration Source: Ensembl
- cellular response to drug Source: Ensembl
- cellular response to epidermal growth factor stimulus Source: Ensembl
- citrulline biosynthetic process Source: GO_Central
- drug metabolic process Source: BHF-UCL
- female pregnancy Source: Ensembl
- glutamine metabolic process Source: BHF-UCL
- heart development Source: Ensembl
- lactation Source: Ensembl
- liver development Source: Ensembl
- nitrogen compound metabolic process Source: GO_Central
- peptidyl-threonine phosphorylation Source: BHF-UCL
- protein autophosphorylation Source: BHF-UCL
- pyrimidine nucleoside biosynthetic process Source: Reactome
- response to amine Source: Ensembl
- response to caffeine Source: Ensembl
- response to cortisol Source: Ensembl
- response to insulin Source: Ensembl
- response to starvation Source: Ensembl
- response to testosterone Source: Ensembl
- UTP biosynthetic process Source: GO_Central
Keywordsi
Molecular function | Allosteric enzyme, Hydrolase, Ligase, Multifunctional enzyme, Transferase |
Biological process | Pyrimidine biosynthesis |
Ligand | ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding, Zinc |
Enzyme and pathway databases
BioCyci | MetaCyc:ENSG00000084774-MONOMER |
BRENDAi | 3.5.2.3, 2681 |
PathwayCommonsi | P27708 |
Reactomei | R-HSA-500753, Pyrimidine biosynthesis |
SIGNORi | P27708 |
UniPathwayi | UPA00070;UER00115 UPA00070;UER00116 UPA00070;UER00117 |
Protein family/group databases
MEROPSi | M38.972 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:CADImported |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
EuPathDBi | HostDB:ENSG00000084774.13 |
HGNCi | HGNC:1424, CAD |
MIMi | 114010, gene |
neXtProti | NX_P27708 |
Subcellular locationi
Cytosol
- cytosol Source: BHF-UCL
Extracellular region or secreted
- extracellular exosome Source: UniProtKB
Nucleus
- nuclear matrix Source: BHF-UCL
- nucleoplasm Source: HPA
- nucleus Source: BHF-UCL
Other locations
- cell projection Source: BHF-UCL
- cytoplasm Source: GO_Central
- membrane Source: UniProtKB
- neuronal cell body Source: BHF-UCL
- protein-containing complex Source: Ensembl
- terminal bouton Source: BHF-UCL
Keywords - Cellular componenti
Cytoplasm, NucleusPathology & Biotechi
Involvement in diseasei
Epileptic encephalopathy, early infantile, 50 (EIEE50)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of epileptic encephalopathy, a heterogeneous group of severe childhood onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. EIEE50 is an autosomal recessive, progressive disease with onset in infancy and favorable response to treatment with oral uridine.
Related information in OMIMFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_078289 | 33 | M → R in EIEE50; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs751610198EnsemblClinVar. | 1 | |
Natural variantiVAR_078290 | 1789 – 2225 | Missing in EIEE50; unknown pathological significance. 1 PublicationAdd BLAST | 437 | |
Natural variantiVAR_073955 | 2024 | R → Q in EIEE50. 1 PublicationCorresponds to variant dbSNP:rs763410987EnsemblClinVar. | 1 |
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 1471 | H → A: No zinc-binding and no catalytic activity. 2 Publications | 1 | |
Mutagenesisi | 1471 | H → N: Abolishes dihydroorotase activity. 2 Publications | 1 | |
Mutagenesisi | 1473 | H → A: No zinc-binding and no catalytic activity. 1 Publication | 1 | |
Mutagenesisi | 1512 | D → N: No change in catalytic activity. 1 Publication | 1 | |
Mutagenesisi | 1562 | T → A: Abolishes dihydroorotase activity. 1 Publication | 1 | |
Mutagenesisi | 1563 | F → A: Abolishes dihydroorotase activity. 1 Publication | 1 | |
Mutagenesisi | 1590 | H → A: Abolishes dihydroorotase activity. 2 Publications | 1 | |
Mutagenesisi | 1590 | H → N: No catalytic activity. 2 Publications | 1 | |
Mutagenesisi | 1613 | C → S: Reduces dihydroorotase activity. 1 Publication | 1 | |
Mutagenesisi | 1614 | H → A: Abolishes dihydroorotase activity. 1 Publication | 1 | |
Mutagenesisi | 1637 | E → T: Abolishes dihydroorotase activity. 1 Publication | 1 | |
Mutagenesisi | 1642 | H → N: 11.5% of wild-type catalytic activity. 1 Publication | 1 | |
Mutagenesisi | 1686 | D → N: Abolishes dihydroorotase activity. 1 Publication | 1 | |
Mutagenesisi | 1690 | H → N: 3% of wild-type catalytic activity. 1 Publication | 1 | |
Mutagenesisi | 1873 | S → A: Abolishes PMA-induced Thr-456 phosphorylation. 1 Publication | 1 |
Keywords - Diseasei
Congenital disorder of glycosylation, Disease mutation, EpilepsyOrganism-specific databases
DisGeNETi | 790 |
MalaCardsi | CAD |
MIMi | 616457, phenotype |
OpenTargetsi | ENSG00000084774 |
Orphaneti | 448010, CAD-CDG |
PharmGKBi | PA26023 |
Miscellaneous databases
Pharosi | P27708, Tchem |
Chemistry databases
ChEMBLi | CHEMBL3093 |
DrugBanki | DB00128, Aspartic acid DB00130, L-Glutamine DB03459, Sparfosic acid |
Polymorphism and mutation databases
BioMutai | CAD |
DMDMi | 50403731 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedCombined sources1 Publication | |||
ChainiPRO_0000199506 | 2 – 2225 | CAD proteinAdd BLAST | 2224 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylalanineCombined sources1 Publication | 1 | |
Modified residuei | 456 | Phosphothreonine; by MAPK11 Publication | 1 | |
Modified residuei | 747 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 1038 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1406 | Phosphoserine; by PKACombined sources1 Publication | 1 | |
Modified residuei | 1411 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 1556 | N6-carboxylysine1 Publication | 1 | |
Modified residuei | 1859 | Phosphoserine; by RPS6KB1 and PKACombined sources3 Publications | 1 | |
Modified residuei | 1873 | Phosphoserine; by PKC; in vitro1 Publication | 1 | |
Modified residuei | 1884 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 1900 | PhosphoserineCombined sources1 Publication | 1 | |
Modified residuei | 1938 | PhosphoserineCombined sources | 1 |
Post-translational modificationi
Activated by MAP kinase (Erk1/2) phosphorylation just prior to the S phase of the cell cycle, when the demand for pyrimidine nucleotides is greatest, and down-regulated as the cells emerge from S phase by protein kinase A (PKA) phosphorylation. Phosphorylation at Ser-1859 by RPS6KB1 downstream of MTOR promotes oligomerization and stimulates dihydroorotase activity. Phosphorylation at Ser-1406 reduces sensitivity to feedback inhibition by UTP.3 Publications
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
CPTACi | CPTAC-466 CPTAC-467 |
EPDi | P27708 |
jPOSTi | P27708 |
MassIVEi | P27708 |
MaxQBi | P27708 |
PaxDbi | P27708 |
PeptideAtlasi | P27708 |
PRIDEi | P27708 |
ProteomicsDBi | 54409 |
PTM databases
iPTMneti | P27708 |
MetOSitei | P27708 |
PhosphoSitePlusi | P27708 |
SwissPalmi | P27708 |
Expressioni
Inductioni
Transcriptionally repressed following hypoxia by HIF1A.1 Publication
Gene expression databases
Bgeei | ENSG00000084774, Expressed in right lobe of liver and 185 other tissues |
ExpressionAtlasi | P27708, baseline and differential |
Genevisiblei | P27708, HS |
Organism-specific databases
HPAi | ENSG00000084774, Low tissue specificity |
Interactioni
Subunit structurei
Binary interactionsi
P27708
With | #Exp. | IntAct |
---|---|---|
itself | 3 | EBI-355504,EBI-355504 |
GO - Molecular functioni
- enzyme binding Source: UniProtKB
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGRIDi | 107243, 196 interactors |
DIPi | DIP-39484N |
IntActi | P27708, 85 interactors |
MINTi | P27708 |
STRINGi | 9606.ENSP00000264705 |
Chemistry databases
BindingDBi | P27708 |
Miscellaneous databases
RNActi | P27708, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P27708 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 177 – 363 | Glutamine amidotransferase type-1PROSITE-ProRule annotationAdd BLAST | 187 | |
Domaini | 519 – 711 | ATP-grasp 1PROSITE-ProRule annotationAdd BLAST | 193 | |
Domaini | 1052 – 1243 | ATP-grasp 2PROSITE-ProRule annotationAdd BLAST | 192 | |
Domaini | 1308 – 1462 | MGS-likePROSITE-ProRule annotationAdd BLAST | 155 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 2 – 365 | GATase (Glutamine amidotransferase)By similarityAdd BLAST | 364 | |
Regioni | 366 – 394 | LinkerBy similarityAdd BLAST | 29 | |
Regioni | 395 – 1455 | CPSase (Carbamoyl-phosphate synthase)By similarityAdd BLAST | 1061 | |
Regioni | 395 – 933 | CPSase ABy similarityAdd BLAST | 539 | |
Regioni | 934 – 1455 | CPSase BBy similarityAdd BLAST | 522 | |
Regioni | 1456 – 1788 | DHOase (dihydroorotase)By similarityAdd BLAST | 333 | |
Regioni | 1789 – 1917 | LinkerBy similarityAdd BLAST | 129 | |
Regioni | 1918 – 2225 | ATCase (Aspartate transcarbamylase)By similarityAdd BLAST | 308 |
Sequence similaritiesi
In the central section; belongs to the metallo-dependent hydrolases superfamily. DHOase family. CAD subfamily.Curated
Keywords - Domaini
RepeatPhylogenomic databases
eggNOGi | KOG0370, Eukaryota |
GeneTreei | ENSGT00940000157241 |
HOGENOMi | CLU_000513_2_1_1 |
InParanoidi | P27708 |
OrthoDBi | 273358at2759 |
PhylomeDBi | P27708 |
TreeFami | TF105604 |
Family and domain databases
CDDi | cd01744, GATase1_CPSase, 1 hit |
DisProti | DP01024 |
Gene3Di | 1.10.1030.10, 1 hit 3.30.1490.20, 1 hit 3.40.50.1370, 2 hits 3.40.50.1380, 1 hit 3.40.50.880, 1 hit 3.50.30.20, 1 hit |
HAMAPi | MF_00001, Asp_carb_tr, 1 hit MF_01209, CPSase_S_chain, 1 hit |
InterProi | View protein in InterPro IPR006680, Amidohydro-rel IPR006132, Asp/Orn_carbamoyltranf_P-bd IPR006130, Asp/Orn_carbamoylTrfase IPR036901, Asp/Orn_carbamoylTrfase_sf IPR002082, Asp_carbamoyltransf IPR006131, Asp_carbamoyltransf_Asp/Orn-bd IPR011761, ATP-grasp IPR013815, ATP_grasp_subdomain_1 IPR006275, CarbamoylP_synth_lsu IPR005480, CarbamoylP_synth_lsu_oligo IPR036897, CarbamoylP_synth_lsu_oligo_sf IPR006274, CarbamoylP_synth_ssu IPR002474, CarbamoylP_synth_ssu_N IPR036480, CarbP_synth_ssu_N_sf IPR005479, CbamoylP_synth_lsu-like_ATP-bd IPR005483, CbamoylP_synth_lsu_CPSase_dom IPR029062, Class_I_gatase-like IPR035686, CPSase_GATase1 IPR002195, Dihydroorotase_CS IPR017926, GATASE IPR011059, Metal-dep_hydrolase_composite IPR032466, Metal_Hydrolase IPR011607, MGS-like_dom IPR036914, MGS-like_dom_sf IPR016185, PreATP-grasp_dom_sf |
Pfami | View protein in Pfam PF01979, Amidohydro_1, 1 hit 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 PF00185, OTCace, 1 hit PF02729, OTCace_N, 1 hit |
PRINTSi | PR00100, AOTCASE PR00098, CPSASE |
SMARTi | View protein in SMART SM01096, CPSase_L_D3, 1 hit SM01097, CPSase_sm_chain, 1 hit SM00851, MGS, 1 hit |
SUPFAMi | SSF48108, SSF48108, 1 hit SSF51338, SSF51338, 1 hit SSF51556, SSF51556, 1 hit SSF52021, SSF52021, 1 hit SSF52317, SSF52317, 1 hit SSF52335, SSF52335, 1 hit SSF52440, SSF52440, 2 hits SSF53671, SSF53671, 1 hit |
TIGRFAMsi | TIGR00670, asp_carb_tr, 1 hit TIGR01369, CPSaseII_lrg, 1 hit TIGR01368, CPSaseIIsmall, 1 hit |
PROSITEi | View protein in PROSITE PS50975, ATP_GRASP, 2 hits PS00097, CARBAMOYLTRANSFERASE, 1 hit PS00866, CPSASE_1, 2 hits PS00867, CPSASE_2, 2 hits PS00482, DIHYDROOROTASE_1, 1 hit PS00483, DIHYDROOROTASE_2, 1 hit PS51273, GATASE_TYPE_1, 1 hit PS51855, MGS, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All
P27708-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MAALVLEDGS VLRGQPFGAA VSTAGEVVFQ TGMVGYPEAL TDPSYKAQIL
60 70 80 90 100
VLTYPLIGNY GIPPDEMDEF GLCKWFESSG IHVAALVVGE CCPTPSHWSA
110 120 130 140 150
TRTLHEWLQQ HGIPGLQGVD TRELTKKLRE QGSLLGKLVQ NGTEPSSLPF
160 170 180 190 200
LDPNARPLVP EVSIKTPRVF NTGGAPRILA LDCGLKYNQI RCLCQRGAEV
210 220 230 240 250
TVVPWDHALD SQEYEGLFLS NGPGDPASYP SVVSTLSRVL SEPNPRPVFG
260 270 280 290 300
ICLGHQLLAL AIGAKTYKMR YGNRGHNQPC LLVGSGRCFL TSQNHGFAVE
310 320 330 340 350
TDSLPADWAP LFTNANDGSN EGIVHNSLPF FSVQFHPEHQ AGPSDMELLF
360 370 380 390 400
DIFLETVKEA TAGNPGGQTV RERLTERLCP PGIPTPGSGL PPPRKVLILG
410 420 430 440 450
SGGLSIGQAG EFDYSGSQAI KALKEENIQT LLINPNIATV QTSQGLADKV
460 470 480 490 500
YFLPITPHYV TQVIRNERPD GVLLTFGGQT ALNCGVELTK AGVLARYGVR
510 520 530 540 550
VLGTPVETIE LTEDRRAFAA RMAEIGEHVA PSEAANSLEQ AQAAAERLGY
560 570 580 590 600
PVLVRAAFAL GGLGSGFASN REELSALVAP AFAHTSQVLV DKSLKGWKEI
610 620 630 640 650
EYEVVRDAYG NCVTVCNMEN LDPLGIHTGE SIVVAPSQTL NDREYQLLRQ
660 670 680 690 700
TAIKVTQHLG IVGECNVQYA LNPESEQYYI IEVNARLSRS SALASKATGY
710 720 730 740 750
PLAYVAAKLA LGIPLPELRN SVTGGTAAFE PSVDYCVVKI PRWDLSKFLR
760 770 780 790 800
VSTKIGSCMK SVGEVMGIGR SFEEAFQKAL RMVDENCVGF DHTVKPVSDM
810 820 830 840 850
ELETPTDKRI FVVAAALWAG YSVDRLYELT RIDRWFLHRM KRIIAHAQLL
860 870 880 890 900
EQHRGQPLPP DLLQQAKCLG FSDKQIALAV LSTELAVRKL RQELGICPAV
910 920 930 940 950
KQIDTVAAEW PAQTNYLYLT YWGTTHDLTF RTPHVLVLGS GVYRIGSSVE
960 970 980 990 1000
FDWCAVGCIQ QLRKMGYKTI MVNYNPETVS TDYDMCDRLY FDEISFEVVM
1010 1020 1030 1040 1050
DIYELENPEG VILSMGGQLP NNMAMALHRQ QCRVLGTSPE AIDSAENRFK
1060 1070 1080 1090 1100
FSRLLDTIGI SQPQWRELSD LESARQFCQT VGYPCVVRPS YVLSGAAMNV
1110 1120 1130 1140 1150
AYTDGDLERF LSSAAAVSKE HPVVISKFIQ EAKEIDVDAV ASDGVVAAIA
1160 1170 1180 1190 1200
ISEHVENAGV HSGDATLVTP PQDITAKTLE RIKAIVHAVG QELQVTGPFN
1210 1220 1230 1240 1250
LQLIAKDDQL KVIECNVRVS RSFPFVSKTL GVDLVALATR VIMGEEVEPV
1260 1270 1280 1290 1300
GLMTGSGVVG VKVPQFSFSR LAGADVVLGV EMTSTGEVAG FGESRCEAYL
1310 1320 1330 1340 1350
KAMLSTGFKI PKKNILLTIG SYKNKSELLP TVRLLESLGY SLYASLGTAD
1360 1370 1380 1390 1400
FYTEHGVKVT AVDWHFEEAV DGECPPQRSI LEQLAEKNFE LVINLSMRGA
1410 1420 1430 1440 1450
GGRRLSSFVT KGYRTRRLAA DFSVPLIIDI KCTKLFVEAL GQIGPAPPLK
1460 1470 1480 1490 1500
VHVDCMTSQK LVRLPGLIDV HVHLREPGGT HKEDFASGTA AALAGGITMV
1510 1520 1530 1540 1550
CAMPNTRPPI IDAPALALAQ KLAEAGARCD FALFLGASSE NAGTLGTVAG
1560 1570 1580 1590 1600
SAAGLKLYLN ETFSELRLDS VVQWMEHFET WPSHLPIVAH AEQQTVAAVL
1610 1620 1630 1640 1650
MVAQLTQRSV HICHVARKEE ILLIKAAKAR GLPVTCEVAP HHLFLSHDDL
1660 1670 1680 1690 1700
ERLGPGKGEV RPELGSRQDV EALWENMAVI DCFASDHAPH TLEEKCGSRP
1710 1720 1730 1740 1750
PPGFPGLETM LPLLLTAVSE GRLSLDDLLQ RLHHNPRRIF HLPPQEDTYV
1760 1770 1780 1790 1800
EVDLEHEWTI PSHMPFSKAH WTPFEGQKVK GTVRRVVLRG EVAYIDGQVL
1810 1820 1830 1840 1850
VPPGYGQDVR KWPQGAVPQL PPSAPATSEM TTTPERPRRG IPGLPDGRFH
1860 1870 1880 1890 1900
LPPRIHRASD PGLPAEEPKE KSSRKVAEPE LMGTPDGTCY PPPPVPRQAS
1910 1920 1930 1940 1950
PQNLGTPGLL HPQTSPLLHS LVGQHILSVQ QFTKDQMSHL FNVAHTLRMM
1960 1970 1980 1990 2000
VQKERSLDIL KGKVMASMFY EVSTRTSSSF AAAMARLGGA VLSFSEATSS
2010 2020 2030 2040 2050
VQKGESLADS VQTMSCYADV VVLRHPQPGA VELAAKHCRR PVINAGDGVG
2060 2070 2080 2090 2100
EHPTQALLDI FTIREELGTV NGMTITMVGD LKHGRTVHSL ACLLTQYRVS
2110 2120 2130 2140 2150
LRYVAPPSLR MPPTVRAFVA SRGTKQEEFE SIEEALPDTD VLYMTRIQKE
2160 2170 2180 2190 2200
RFGSTQEYEA CFGQFILTPH IMTRAKKKMV VMHPMPRVNE ISVEVDSDPR
2210 2220
AAYFRQAENG MYIRMALLAT VLGRF
Computationally mapped potential isoform sequencesi
There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketF8VPD4 | F8VPD4_HUMAN | Aspartate carbamoyltransferase | CAD | 2,162 | Annotation score: | ||
H7C2E4 | H7C2E4_HUMAN | Aspartate carbamoyltransferase | CAD | 293 | Annotation score: | ||
H7BZB3 | H7BZB3_HUMAN | CAD protein | CAD | 279 | Annotation score: | ||
H7C3Z5 | H7C3Z5_HUMAN | CAD protein | CAD | 269 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 505 | P → T in BAA11423 (PubMed:8619816).Curated | 1 | |
Sequence conflicti | 535 | A → G in BAA11423 (PubMed:8619816).Curated | 1 | |
Sequence conflicti | 560 | L → V in BAA11423 (PubMed:8619816).Curated | 1 | |
Sequence conflicti | 1103 | T → A in BAA11423 (PubMed:8619816).Curated | 1 | |
Sequence conflicti | 1513 | A → G in BAA11423 (PubMed:8619816).Curated | 1 | |
Sequence conflicti | 1676 | N → D in BAA11423 (PubMed:8619816).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_078289 | 33 | M → R in EIEE50; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs751610198EnsemblClinVar. | 1 | |
Natural variantiVAR_035897 | 177 | R → Q in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs374122292Ensembl. | 1 | |
Natural variantiVAR_035898 | 735 | Y → C in a colorectal cancer sample; somatic mutation. 1 Publication | 1 | |
Natural variantiVAR_078290 | 1789 – 2225 | Missing in EIEE50; unknown pathological significance. 1 PublicationAdd BLAST | 437 | |
Natural variantiVAR_073955 | 2024 | R → Q in EIEE50. 1 PublicationCorresponds to variant dbSNP:rs763410987EnsemblClinVar. | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D78586 mRNA Translation: BAA11423.1 CH471053 Genomic DNA Translation: EAX00612.1 CH471053 Genomic DNA Translation: EAX00613.1 CH471053 Genomic DNA Translation: EAX00614.1 BC014178 mRNA Translation: AAH14178.2 BC065510 mRNA Translation: AAH65510.1 M38561 Genomic DNA Translation: AAA51907.1 |
CCDSi | CCDS1742.1 |
PIRi | A36240 |
RefSeqi | NP_001293008.1, NM_001306079.1 NP_004332.2, NM_004341.4 |
Genome annotation databases
Ensembli | ENST00000264705; ENSP00000264705; ENSG00000084774 |
GeneIDi | 790 |
KEGGi | hsa:790 |
UCSCi | uc002rji.4, human |
Keywords - Coding sequence diversityi
PolymorphismSimilar proteinsi
Cross-referencesi
Web resourcesi
Wikipedia Aspartate carbamoyltransferase entry |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D78586 mRNA Translation: BAA11423.1 CH471053 Genomic DNA Translation: EAX00612.1 CH471053 Genomic DNA Translation: EAX00613.1 CH471053 Genomic DNA Translation: EAX00614.1 BC014178 mRNA Translation: AAH14178.2 BC065510 mRNA Translation: AAH65510.1 M38561 Genomic DNA Translation: AAA51907.1 |
CCDSi | CCDS1742.1 |
PIRi | A36240 |
RefSeqi | NP_001293008.1, NM_001306079.1 NP_004332.2, NM_004341.4 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4BY3 | X-ray | 1.73 | A | 1456-1846 | [»] | |
4C6B | X-ray | 1.66 | A | 1456-1846 | [»] | |
4C6C | X-ray | 1.45 | A | 1456-1846 | [»] | |
4C6D | X-ray | 1.30 | A | 1456-1846 | [»] | |
4C6E | X-ray | 1.26 | A | 1456-1846 | [»] | |
4C6F | X-ray | 1.26 | A | 1456-1846 | [»] | |
4C6I | X-ray | 1.35 | A | 1456-1846 | [»] | |
4C6J | X-ray | 1.30 | A | 1456-1846 | [»] | |
4C6K | X-ray | 1.48 | A | 1456-1846 | [»] | |
4C6L | X-ray | 1.55 | A | 1456-1846 | [»] | |
4C6M | X-ray | 1.62 | A | 1456-1846 | [»] | |
4C6N | X-ray | 1.90 | A | 1456-1846 | [»] | |
4C6O | X-ray | 1.65 | A | 1456-1846 | [»] | |
4C6P | X-ray | 1.52 | A | 1456-1846 | [»] | |
4C6Q | X-ray | 1.66 | A | 1456-1846 | [»] | |
5G1N | X-ray | 2.10 | A/B/C/D/E/F | 1915-2225 | [»] | |
5G1O | X-ray | 2.10 | A/B/C/D/E/F | 1915-2225 | [»] | |
5G1P | X-ray | 3.19 | A/B/C/D/E/F | 1915-2225 | [»] | |
5YNZ | X-ray | 2.77 | A | 1456-1846 | [»] | |
6HFD | X-ray | 1.87 | A | 1456-1846 | [»] | |
6HFE | X-ray | 1.48 | A | 1456-1846 | [»] | |
6HFF | X-ray | 1.51 | A | 1456-1846 | [»] | |
6HFH | X-ray | 1.45 | A | 1456-1846 | [»] | |
6HFI | X-ray | 1.46 | A | 1456-1846 | [»] | |
6HFJ | X-ray | 1.20 | A | 1456-1846 | [»] | |
6HFK | X-ray | 1.46 | A | 1456-1846 | [»] | |
6HFL | X-ray | 1.35 | A | 1456-1846 | [»] | |
6HFN | X-ray | 1.45 | A | 1456-1846 | [»] | |
6HFP | X-ray | 1.20 | A | 1456-1846 | [»] | |
6HFQ | X-ray | 1.15 | A | 1456-1846 | [»] | |
6HFR | X-ray | 1.30 | A | 1456-1846 | [»] | |
6HFS | X-ray | 1.35 | A | 1456-1846 | [»] | |
6HFU | X-ray | 1.40 | A | 1456-1846 | [»] | |
6HG1 | X-ray | 2.12 | A | 1460-1559 | [»] | |
A | 1571-1826 | [»] | ||||
SMRi | P27708 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 107243, 196 interactors |
DIPi | DIP-39484N |
IntActi | P27708, 85 interactors |
MINTi | P27708 |
STRINGi | 9606.ENSP00000264705 |
Chemistry databases
BindingDBi | P27708 |
ChEMBLi | CHEMBL3093 |
DrugBanki | DB00128, Aspartic acid DB00130, L-Glutamine DB03459, Sparfosic acid |
Protein family/group databases
MEROPSi | M38.972 |
PTM databases
iPTMneti | P27708 |
MetOSitei | P27708 |
PhosphoSitePlusi | P27708 |
SwissPalmi | P27708 |
Polymorphism and mutation databases
BioMutai | CAD |
DMDMi | 50403731 |
Proteomic databases
CPTACi | CPTAC-466 CPTAC-467 |
EPDi | P27708 |
jPOSTi | P27708 |
MassIVEi | P27708 |
MaxQBi | P27708 |
PaxDbi | P27708 |
PeptideAtlasi | P27708 |
PRIDEi | P27708 |
ProteomicsDBi | 54409 |
Protocols and materials databases
Antibodypediai | 28293, 296 antibodies |
Genome annotation databases
Ensembli | ENST00000264705; ENSP00000264705; ENSG00000084774 |
GeneIDi | 790 |
KEGGi | hsa:790 |
UCSCi | uc002rji.4, human |
Organism-specific databases
CTDi | 790 |
DisGeNETi | 790 |
EuPathDBi | HostDB:ENSG00000084774.13 |
GeneCardsi | CAD |
HGNCi | HGNC:1424, CAD |
HPAi | ENSG00000084774, Low tissue specificity |
MalaCardsi | CAD |
MIMi | 114010, gene 616457, phenotype |
neXtProti | NX_P27708 |
OpenTargetsi | ENSG00000084774 |
Orphaneti | 448010, CAD-CDG |
PharmGKBi | PA26023 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG0370, Eukaryota |
GeneTreei | ENSGT00940000157241 |
HOGENOMi | CLU_000513_2_1_1 |
InParanoidi | P27708 |
OrthoDBi | 273358at2759 |
PhylomeDBi | P27708 |
TreeFami | TF105604 |
Enzyme and pathway databases
UniPathwayi | UPA00070;UER00115 UPA00070;UER00116 UPA00070;UER00117 |
BioCyci | MetaCyc:ENSG00000084774-MONOMER |
BRENDAi | 3.5.2.3, 2681 |
PathwayCommonsi | P27708 |
Reactomei | R-HSA-500753, Pyrimidine biosynthesis |
SIGNORi | P27708 |
Miscellaneous databases
BioGRID-ORCSi | 790, 244 hits in 853 CRISPR screens |
ChiTaRSi | CAD, human |
GenomeRNAii | 790 |
Pharosi | P27708, Tchem |
PROi | PR:P27708 |
RNActi | P27708, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000084774, Expressed in right lobe of liver and 185 other tissues |
ExpressionAtlasi | P27708, baseline and differential |
Genevisiblei | P27708, HS |
Family and domain databases
CDDi | cd01744, GATase1_CPSase, 1 hit |
DisProti | DP01024 |
Gene3Di | 1.10.1030.10, 1 hit 3.30.1490.20, 1 hit 3.40.50.1370, 2 hits 3.40.50.1380, 1 hit 3.40.50.880, 1 hit 3.50.30.20, 1 hit |
HAMAPi | MF_00001, Asp_carb_tr, 1 hit MF_01209, CPSase_S_chain, 1 hit |
InterProi | View protein in InterPro IPR006680, Amidohydro-rel IPR006132, Asp/Orn_carbamoyltranf_P-bd IPR006130, Asp/Orn_carbamoylTrfase IPR036901, Asp/Orn_carbamoylTrfase_sf IPR002082, Asp_carbamoyltransf IPR006131, Asp_carbamoyltransf_Asp/Orn-bd IPR011761, ATP-grasp IPR013815, ATP_grasp_subdomain_1 IPR006275, CarbamoylP_synth_lsu IPR005480, CarbamoylP_synth_lsu_oligo IPR036897, CarbamoylP_synth_lsu_oligo_sf IPR006274, CarbamoylP_synth_ssu IPR002474, CarbamoylP_synth_ssu_N IPR036480, CarbP_synth_ssu_N_sf IPR005479, CbamoylP_synth_lsu-like_ATP-bd IPR005483, CbamoylP_synth_lsu_CPSase_dom IPR029062, Class_I_gatase-like IPR035686, CPSase_GATase1 IPR002195, Dihydroorotase_CS IPR017926, GATASE IPR011059, Metal-dep_hydrolase_composite IPR032466, Metal_Hydrolase IPR011607, MGS-like_dom IPR036914, MGS-like_dom_sf IPR016185, PreATP-grasp_dom_sf |
Pfami | View protein in Pfam PF01979, Amidohydro_1, 1 hit 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 PF00185, OTCace, 1 hit PF02729, OTCace_N, 1 hit |
PRINTSi | PR00100, AOTCASE PR00098, CPSASE |
SMARTi | View protein in SMART SM01096, CPSase_L_D3, 1 hit SM01097, CPSase_sm_chain, 1 hit SM00851, MGS, 1 hit |
SUPFAMi | SSF48108, SSF48108, 1 hit SSF51338, SSF51338, 1 hit SSF51556, SSF51556, 1 hit SSF52021, SSF52021, 1 hit SSF52317, SSF52317, 1 hit SSF52335, SSF52335, 1 hit SSF52440, SSF52440, 2 hits SSF53671, SSF53671, 1 hit |
TIGRFAMsi | TIGR00670, asp_carb_tr, 1 hit TIGR01369, CPSaseII_lrg, 1 hit TIGR01368, CPSaseIIsmall, 1 hit |
PROSITEi | View protein in PROSITE PS50975, ATP_GRASP, 2 hits PS00097, CARBAMOYLTRANSFERASE, 1 hit PS00866, CPSASE_1, 2 hits PS00867, CPSASE_2, 2 hits PS00482, DIHYDROOROTASE_1, 1 hit PS00483, DIHYDROOROTASE_2, 1 hit PS51273, GATASE_TYPE_1, 1 hit PS51855, MGS, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PYR1_HUMAN | |
Accessioni | P27708Primary (citable) accession number: P27708 Secondary accession number(s): D6W552, Q6P0Q0, Q96CK3 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1992 |
Last sequence update: | July 19, 2004 | |
Last modified: | December 2, 2020 | |
This is version 232 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Human chromosome 2
Human chromosome 2: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations