UniProtKB - P27708 (PYR1_HUMAN)

BLAST

>sp|P27708|PYR1_HUMAN CAD protein OS=Homo sapiens OX=9606 GN=CAD PE=1 SV=3
MAALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNY
GIPPDEMDEFGLCKWFESSGIHVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVD
TRELTKKLREQGSLLGKLVQNGTEPSSLPFLDPNARPLVPEVSIKTPRVFNTGGAPRILA
LDCGLKYNQIRCLCQRGAEVTVVPWDHALDSQEYEGLFLSNGPGDPASYPSVVSTLSRVL
SEPNPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVE
TDSLPADWAPLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLETVKEA
TAGNPGGQTVRERLTERLCPPGIPTPGSGLPPPRKVLILGSGGLSIGQAGEFDYSGSQAI
KALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGVLLTFGGQT
ALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQ
AQAAAERLGYPVLVRAAFALGGLGSGFASNREELSALVAPAFAHTSQVLVDKSLKGWKEI
EYEVVRDAYGNCVTVCNMENLDPLGIHTGESIVVAPSQTLNDREYQLLRQTAIKVTQHLG
IVGECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPELRN
SVTGGTAAFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKAL
RMVDENCVGFDHTVKPVSDMELETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRM
KRIIAHAQLLEQHRGQPLPPDLLQQAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAV
KQIDTVAAEWPAQTNYLYLTYWGTTHDLTFRTPHVLVLGSGVYRIGSSVEFDWCAVGCIQ
QLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLP
NNMAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQT
VGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAV
ASDGVVAAIAISEHVENAGVHSGDATLVTPPQDITAKTLERIKAIVHAVGQELQVTGPFN
LQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGEEVEPVGLMTGSGVVG
VKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNILLTIG
SYKNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEAVDGECPPQRSI
LEQLAEKNFELVINLSMRGAGGRRLSSFVTKGYRTRRLAADFSVPLIIDIKCTKLFVEAL
GQIGPAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMV
CAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASSENAGTLGTVAGSAAGLKLYLN
ETFSELRLDSVVQWMEHFETWPSHLPIVAHAEQQTVAAVLMVAQLTQRSVHICHVARKEE
ILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPGKGEVRPELGSRQDVEALWENMAVI
DCFASDHAPHTLEEKCGSRPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIF
HLPPQEDTYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVL
VPPGYGQDVRKWPQGAVPQLPPSAPATSEMTTTPERPRRGIPGLPDGRFHLPPRIHRASD
PGLPAEEPKEKSSRKVAEPELMGTPDGTCYPPPPVPRQASPQNLGTPGLLHPQTSPLLHS
LVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSF
AAAMARLGGAVLSFSEATSSVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRR
PVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKHGRTVHSLACLLTQYRVS
LRYVAPPSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSTQEYEA
CFGQFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLAT
VLGRF

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History
Entry version 216 (07 Nov 2018)
Sequence version 3 (19 Jul 2004)
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Protein

CAD protein

Gene

CAD

Organism

Homo sapiens (Human)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

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 + L-glutamine + HCO₃^- + H₂O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate.1 Publication

Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate.1 Publication

(S)-dihydroorotate + H₂O = N-carbamoyl-L-aspartate.1 Publication

Cofactorⁱ

Protein has several cofactor binding sites:

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

Pathwayⁱ: UMP biosynthesis via de novo pathway

This protein is involved in step 1, 2 and 3 of the subpathway that synthesizes (S)-dihydroorotate from bicarbonate.1 Publication
Proteins known to be involved in the 3 steps of the subpathway in this organism are:

CAD protein (CAD)
CAD protein (CAD)
CAD protein (CAD)

This subpathway is part of the pathway UMP biosynthesis via de novo pathway, which is itself part of Pyrimidine metabolism.
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	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 (ammonia) activity
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Source: BHF-UCL
dihydroorotase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 24332717
enzyme binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 15326225
identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 24332717
protein kinase activity Source: BHF-UCL
zinc ion binding
Source: UniProtKB
Inferred from direct assayⁱ
- 24332717

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

'de novo' pyrimidine nucleobase biosynthetic process
Source: UniProtKB
Inferred from direct assayⁱ
- 24332717
'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
animal organ regeneration Source: Ensembl
arginine biosynthetic process
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
carbamoyl phosphate biosynthetic process
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
cellular response to drug Source: Ensembl
cellular response to epidermal growth factor stimulus Source: Ensembl
citrulline biosynthetic process
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
drug metabolic process Source: BHF-UCL
female pregnancy Source: Ensembl
glutamine metabolic process Source: BHF-UCL
heart development Source: Ensembl
lactation
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
liver development Source: Ensembl
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: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
response to insulin Source: Ensembl
response to starvation Source: Ensembl
response to testosterone
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
urea cycle
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
UTP biosynthetic process
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635

View the complete GO annotation on QuickGO ...

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
Reactomeⁱ	R-HSA-500753 Pyrimidine biosynthesis
SIGNORⁱ	P27708
UniPathwayⁱ	UPA00070;UER00115 UPA00070;UER00116 UPA00070;UER00117

Protein family/group databases

MEROPS protease database More...MEROPSⁱ	M38.972

MEROPSⁱ

M38.972

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: CAD protein Including the following 3 domains: Glutamine-dependent carbamoyl-phosphate synthase (EC:6.3.5.51 Publication) Aspartate carbamoyltransferase (EC:2.1.3.21 Publication) Dihydroorotase (EC:3.5.2.31 Publication)
Gene namesⁱ	Name:CADImported
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
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
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 2

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000084774.13
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:1424 CAD
MIMⁱ	114010 gene
neXtProtⁱ	NX_P27708

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

Pathology & 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.

Mutagenesis

Feature key	Position(s)	DescriptionActions	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, Epilepsy

Organism-specific databases

DisGeNET More...DisGeNETⁱ	790
MalaCards human disease database More...MalaCardsⁱ	CAD
MIMⁱ	616457 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000084774
Orphanetⁱ	448010 CAD-CDG
PharmGKBⁱ	PA26023

Chemistry databases

ChEMBLⁱ	CHEMBL3093
Drug and drug target database More...DrugBankⁱ	DB00128 L-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	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 sensitivy to feedback inhibition by UTP.3 Publications

Keywords - PTMⁱ

Acetylation, Phosphoprotein

Proteomic databases

EPDⁱ	P27708
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P27708
PaxDbⁱ	P27708
PeptideAtlas More...PeptideAtlasⁱ	P27708
PRIDEⁱ	P27708
ProteomicsDBⁱ	54409

PTM databases

iPTMnetⁱ	P27708
PhosphoSitePlusⁱ	P27708
SwissPalmⁱ	P27708

Miscellaneous databases

PMAP-CutDBⁱ	P27708

PMAP-CutDBⁱ

P27708

Expressionⁱ

Inductionⁱ

Transcriptionally repressed following hypoxia by HIF1A.1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000084774 Expressed in 170 organ(s), highest expression level in right lobe of liver
CleanExⁱ	HS_CAD
ExpressionAtlasⁱ	P27708 baseline and differential
Genevisibleⁱ	P27708 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB007781 HPA057266 HPA069341

HPAⁱ

CAB007781
HPA057266
HPA069341

Interactionⁱ

Subunit structureⁱ

Homohexamer (PubMed:24332717). Interacts with CIPC (PubMed:26657846).2 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-355504,EBI-355504

With

Entry

#Exp.

IntAct

Notes

itself

EBI-355504,EBI-355504

GO - Molecular functionⁱ

enzyme binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 15326225
identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 24332717

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	107243, 119 interactors
Database of interacting proteins More...DIPⁱ	DIP-39484N
IntActⁱ	P27708, 52 interactors
Molecular INTeraction database More...MINTⁱ	P27708
STRINGⁱ	9606.ENSP00000264705

Chemistry databases

BindingDBⁱ

P27708

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	1462 – 1465	Combined sources	4
Beta strandⁱ	1467 – 1472	Combined sources	6
Turnⁱ	1476 – 1478	Combined sources	3
Turnⁱ	1480 – 1482	Combined sources	3
Helixⁱ	1485 – 1494	Combined sources	10
Beta strandⁱ	1497 – 1502	Combined sources	6
Beta strandⁱ	1506 – 1508	Combined sources	3
Helixⁱ	1513 – 1526	Combined sources	14
Beta strandⁱ	1528 – 1533	Combined sources	6
Turnⁱ	1546 – 1548	Combined sources	3
Helixⁱ	1549 – 1551	Combined sources	3
Beta strandⁱ	1555 – 1558	Combined sources	4
Beta strandⁱ	1560 – 1563	Combined sources	4
Turnⁱ	1564 – 1566	Combined sources	3
Helixⁱ	1571 – 1580	Combined sources	10
Beta strandⁱ	1587 – 1590	Combined sources	4
Helixⁱ	1594 – 1605	Combined sources	12
Beta strandⁱ	1610 – 1612	Combined sources	3
Helixⁱ	1618 – 1629	Combined sources	12
Beta strandⁱ	1634 – 1638	Combined sources	5
Helixⁱ	1640 – 1644	Combined sources	5
Helixⁱ	1647 – 1649	Combined sources	3
Helixⁱ	1650 – 1657	Combined sources	8
Helixⁱ	1667 – 1675	Combined sources	9
Helixⁱ	1677 – 1679	Combined sources	3
Helixⁱ	1692 – 1695	Combined sources	4
Beta strandⁱ	1697 – 1699	Combined sources	3
Helixⁱ	1707 – 1719	Combined sources	13
Helixⁱ	1725 – 1732	Combined sources	8
Helixⁱ	1734 – 1740	Combined sources	7
Beta strandⁱ	1749 – 1759	Combined sources	11
Turnⁱ	1773 – 1776	Combined sources	4
Beta strandⁱ	1778 – 1788	Combined sources	11
Beta strandⁱ	1791 – 1795	Combined sources	5
Helixⁱ	1809 – 1811	Combined sources	3
Helixⁱ	1813 – 1815	Combined sources	3
Helixⁱ	1929 – 1931	Combined sources	3
Helixⁱ	1934 – 1952	Combined sources	19
Turnⁱ	1959 – 1962	Combined sources	4
Beta strandⁱ	1964 – 1971	Combined sources	8
Helixⁱ	1975 – 1986	Combined sources	12
Beta strandⁱ	1990 – 1995	Combined sources	6
Helixⁱ	1996 – 1998	Combined sources	3
Helixⁱ	2000 – 2003	Combined sources	4
Helixⁱ	2007 – 2014	Combined sources	8
Turnⁱ	2015 – 2017	Combined sources	3
Beta strandⁱ	2019 – 2027	Combined sources	9
Helixⁱ	2030 – 2035	Combined sources	6
Beta strandⁱ	2042 – 2047	Combined sources	6
Helixⁱ	2053 – 2067	Combined sources	15
Beta strandⁱ	2074 – 2079	Combined sources	6
Turnⁱ	2081 – 2083	Combined sources	3
Helixⁱ	2085 – 2094	Combined sources	10
Beta strandⁱ	2100 – 2104	Combined sources	5
Beta strandⁱ	2107 – 2109	Combined sources	3
Helixⁱ	2113 – 2121	Combined sources	9
Beta strandⁱ	2126 – 2131	Combined sources	6
Helixⁱ	2132 – 2135	Combined sources	4
Helixⁱ	2136 – 2138	Combined sources	3
Beta strandⁱ	2140 – 2144	Combined sources	5
Helixⁱ	2149 – 2151	Combined sources	3
Helixⁱ	2155 – 2160	Combined sources	6
Helixⁱ	2169 – 2172	Combined sources	4
Beta strandⁱ	2180 – 2182	Combined sources	3
Beta strandⁱ	2188 – 2191	Combined sources	4
Helixⁱ	2193 – 2195	Combined sources	3
Helixⁱ	2203 – 2221	Combined sources	19

Show more details

3D structure databases

Database of protein disorder More...DisProtⁱ	DP01024
ProteinModelPortalⁱ	P27708
SMRⁱ	P27708
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	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	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

Repeat

Phylogenomic databases

eggNOGⁱ	KOG0370 Eukaryota COG0458 LUCA COG0505 LUCA COG0540 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00910000144175
HOGENOMⁱ	HOG000234584
HOVERGENⁱ	HBG000279
InParanoidⁱ	P27708
KEGG Orthology (KO) More...KOⁱ	K11540
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G00DC
PhylomeDBⁱ	P27708
TreeFamⁱ	TF105604

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd01744 GATase1_CPSase, 1 hit
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
Pfam protein domain database More...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 PR00101 ATCASE 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

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 4 potential isoforms that are computationally mapped.Show all Align All

P27708-1 [UniParc]FASTA Add to basket

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        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

Length:2,225

Mass (Da):242,984

Last modified:July 19, 2004 - v3

Checksum:ⁱ2AB8E8413E825A8F

Computationally mapped potential isoform sequencesⁱ

There are 4 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

F8VPD4	F8VPD4_HUMAN	CAD protein CAD protein	CAD	2,162	Annotation score:
H7C2E4	H7C2E4_HUMAN	CAD protein CAD protein	CAD	293	Annotation score:
H7BZB3	H7BZB3_HUMAN	CAD protein CAD protein	CAD	279	Annotation score:
H7C3Z5	H7C3Z5_HUMAN	CAD protein CAD protein	CAD	269	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	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	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:rs763410987Ensembl.	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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS1742.1
PIRⁱ	A36240
NCBI Reference Sequences More...RefSeqⁱ	NP_001293008.1, NM_001306079.1 NP_004332.2, NM_004341.4
UniGeneⁱ	Hs.377010

Genome annotation databases

Ensemblⁱ	ENST00000264705; ENSP00000264705; ENSG00000084774
GeneIDⁱ	790
KEGGⁱ	hsa:790
UCSC genome browser More...UCSCⁱ	uc002rji.4 human

Keywords - Coding sequence diversityⁱ

Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P27708	Uncharacterized protein CAD (Fragment)		HUMAN		2151	UniRef100_P27708

Protein	Similar proteins		Species	Score	Length	Source
P27708	CAD protein		MESAU		2225	UniRef90_P27708
CAD protein		MOUSE		2225
Uncharacterized protein CAD (Fragment)		HUMAN		2151
Uncharacterized protein		MACMU		2401
Carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase (Fragment)		MUSPF		67
+250

Protein	Similar proteins		Species	Score	Length	Source
P27708	CAD protein		MESAU		2225	UniRef50_P27708
CAD protein		MOUSE		2225
Uncharacterized protein CAD (Fragment)		HUMAN		2151
Uncharacterized protein		MACMU		2401
Carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase (Fragment)		MUSPF		67
+324

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
UniGeneⁱ	Hs.377010

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...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	[»]
DisProtⁱ	DP01024
ProteinModelPortalⁱ	P27708
SMRⁱ	P27708
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	107243, 119 interactors
DIPⁱ	DIP-39484N
IntActⁱ	P27708, 52 interactors
MINTⁱ	P27708
STRINGⁱ	9606.ENSP00000264705

Chemistry databases

BindingDBⁱ	P27708
ChEMBLⁱ	CHEMBL3093
DrugBankⁱ	DB00128 L-Aspartic Acid DB00130 L-Glutamine DB03459 Sparfosic acid

Protein family/group databases

MEROPSⁱ	M38.972

MEROPSⁱ

M38.972

PTM databases

iPTMnetⁱ	P27708
PhosphoSitePlusⁱ	P27708
SwissPalmⁱ	P27708

Polymorphism and mutation databases

BioMutaⁱ	CAD
DMDMⁱ	50403731

Proteomic databases

EPDⁱ	P27708
MaxQBⁱ	P27708
PaxDbⁱ	P27708
PeptideAtlasⁱ	P27708
PRIDEⁱ	P27708
ProteomicsDBⁱ	54409

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

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	CAB007781 HPA057266 HPA069341
MalaCardsⁱ	CAD
MIMⁱ	114010 gene 616457 phenotype
neXtProtⁱ	NX_P27708
OpenTargetsⁱ	ENSG00000084774
Orphanetⁱ	448010 CAD-CDG
PharmGKBⁱ	PA26023
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0370 Eukaryota COG0458 LUCA COG0505 LUCA COG0540 LUCA
GeneTreeⁱ	ENSGT00910000144175
HOGENOMⁱ	HOG000234584
HOVERGENⁱ	HBG000279
InParanoidⁱ	P27708
KOⁱ	K11540
OrthoDBⁱ	EOG091G00DC
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
Reactomeⁱ	R-HSA-500753 Pyrimidine biosynthesis
SIGNORⁱ	P27708

Miscellaneous databases

ChiTaRSⁱ	CAD human
GenomeRNAiⁱ	790
PMAP-CutDBⁱ	P27708
Protein Ontology More...PROⁱ	PR:P27708
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000084774 Expressed in 170 organ(s), highest expression level in right lobe of liver
CleanExⁱ	HS_CAD
ExpressionAtlasⁱ	P27708 baseline and differential
Genevisibleⁱ	P27708 HS

Family and domain databases

CDDⁱ	cd01744 GATase1_CPSase, 1 hit
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 PR00101 ATCASE 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...

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:	November 7, 2018
	This is version 216 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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
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

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P27708 (PYR1_HUMAN)

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CAD protein

CAD

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

Miscellaneous

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: UMP biosynthesis via de novo pathway

Sites

Regions

<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

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<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

Organism-specific databases

<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

Nucleus

Other locations

Cytosol

Extracellular region or secreted

Nucleus

Other locations

Keywords - Cellular componenti

<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

Mutagenesis

Keywords - Diseasei

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<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

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

Miscellaneous databases

<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

Gene expression databases

Organism-specific databases

<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

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<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

3D structure databases

<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

Domains and Repeats

Region

<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

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

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Functionⁱ

Kineticsⁱ

Pathwayⁱ: UMP biosynthesis via de novo pathway

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ