P27708 (PYR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
CAD protein

Including the following 3 domains:

1. Glutamine-dependent carbamoyl-phosphate synthase
   EC=6.3.5.5
2. Aspartate carbamoyltransferase
   EC=2.1.3.2
3. Dihydroorotase
   EC=3.5.2.3

Gene names

Name:

CAD

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2225 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase).
Catalytic activity	2 ATP + L-glutamine + HCO3- + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate. Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate. (S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate.
Cofactor	Binds 1 zinc ion per subunit (for dihydroorotase activity) Potential.
Enzyme regulation	Allosterically regulated and controlled by phosphorylation. 5-phosphoribose 1-diphosphate is an activator while UMP is an inhibitor of the CPSase reaction.
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3. Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
Subunit structure	Homohexamer.
Subcellular location	Cytoplasm.
Miscellaneous	GATase (glutamine amidotransferase) and CPSase (carbamoyl phosphate synthase) form together the glutamine-dependent CPSase (GD-CPSase) (EC 6.3.5.5).
Sequence similarities	In the central section; belongs to the DHOase family. Contains 2 ATP-grasp domains. Contains 1 glutamine amidotransferase type-1 domain.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Domain	Repeat
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Hydrolase Ligase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Allosteric enzyme Complete proteome Direct protein sequencing Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	'de novo' UMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway 'de novo' pyrimidine nucleobase biosynthetic process Inferred from sequence or structural similarity. Source: BHF-UCL UTP biosynthetic process Inferred from electronic annotation. Source: Compara carbamoyl phosphate biosynthetic process Inferred from electronic annotation. Source: InterPro cellular response to drug Inferred from electronic annotation. Source: Compara cellular response to epidermal growth factor stimulus Inferred from electronic annotation. Source: Compara drug metabolic process Inferred from sequence or structural similarity. Source: BHF-UCL embryo development Inferred from electronic annotation. Source: Compara female pregnancy Inferred from electronic annotation. Source: Compara glutamine catabolic process Inferred from electronic annotation. Source: InterPro glutamine metabolic process Inferred from sequence or structural similarity. Source: BHF-UCL lactation Inferred from electronic annotation. Source: Compara organ regeneration Inferred from electronic annotation. Source: Compara peptidyl-threonine phosphorylation Inferred from sequence or structural similarity. Source: BHF-UCL protein autophosphorylation Inferred from sequence or structural similarity. Source: BHF-UCL pyrimidine nucleoside biosynthetic process Traceable author statement. Source: Reactome response to amine stimulus Inferred from electronic annotation. Source: Compara response to caffeine Inferred from electronic annotation. Source: Compara response to cortisol stimulus Inferred from electronic annotation. Source: Compara response to testosterone stimulus Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Inferred from direct assay PubMed 15890648. Source: BHF-UCL neuronal cell body Inferred from sequence or structural similarity. Source: BHF-UCL nuclear matrix Inferred from direct assay PubMed 9525610. Source: BHF-UCL protein complex Inferred from electronic annotation. Source: Compara terminal bouton Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular_function	ATP binding Inferred from sequence or structural similarity. Source: BHF-UCL aspartate binding Inferred from sequence or structural similarity. Source: BHF-UCL aspartate carbamoyltransferase activity Inferred from sequence or structural similarity. Source: BHF-UCL carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Inferred from sequence or structural similarity. Source: BHF-UCL dihydroorotase activity Inferred from sequence or structural similarity. Source: BHF-UCL identical protein binding Inferred from sequence or structural similarity. Source: BHF-UCL metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein kinase activity Inferred from sequence or structural similarity. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.4
	Chain	2 – 2225	2224	CAD protein		PRO_0000199506
Regions
	Domain	177 – 363	187	Glutamine amidotransferase type-1
	Domain	519 – 711	193	ATP-grasp 1
	Domain	1052 – 1243	192	ATP-grasp 2
	Region	2 – 365	364	GATase (Glutamine amidotransferase)
	Region	366 – 394	29	Linker
	Region	395 – 1455	1061	CPSase (Carbamoyl-phosphate synthase)
	Region	395 – 933	539	CPSase A
	Region	934 – 1455	522	CPSase B
	Region	1456 – 1788	333	DHOase (dihydroorotase)
	Region	1789 – 1917	129	Linker
	Region	1918 – 2225	308	ATCase (Aspartate transcarbamylase)
Sites
	Active site	252	1	For GATase activity By similarity
	Active site	336	1	For GATase activity By similarity
	Active site	338	1	For GATase activity By similarity
	Metal binding	1471	1	Zinc Potential
	Metal binding	1473	1	Zinc Potential
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.4
	Modified residue	747	1	N6-acetyllysine Ref.11
	Modified residue	1406	1	Phosphoserine Ref.14
	Modified residue	1411	1	N6-acetyllysine Ref.11
	Modified residue	1859	1	Phosphoserine Ref.6 Ref.7 Ref.8 Ref.12 Ref.14
	Modified residue	1884	1	Phosphothreonine Ref.8 Ref.9
	Modified residue	1900	1	Phosphoserine Ref.12
	Modified residue	1906	1	Phosphothreonine Ref.12
Natural variations
	Natural variant	177	1	R → Q in a colorectal cancer sample; somatic mutation. Ref.15		VAR_035897
	Natural variant	735	1	Y → C in a colorectal cancer sample; somatic mutation. Ref.15		VAR_035898
Experimental info
	Sequence conflict	505	1	P → T in BAA11423. Ref.1
	Sequence conflict	535	1	A → G in BAA11423. Ref.1
	Sequence conflict	560	1	L → V in BAA11423. Ref.1
	Sequence conflict	1103	1	T → A in BAA11423. Ref.1
	Sequence conflict	1513	1	A → G in BAA11423. Ref.1
	Sequence conflict	1676	1	N → D in BAA11423. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P27708 [UniParc]. Last modified July 19, 2004. Version 3. Checksum: 2AB8E8413E825A8F	FASTA	2,225	242,984
	10 20 30 40 50 60 MAALVLEDGS VLRGQPFGAA VSTAGEVVFQ TGMVGYPEAL TDPSYKAQIL VLTYPLIGNY 70 80 90 100 110 120 GIPPDEMDEF GLCKWFESSG IHVAALVVGE CCPTPSHWSA TRTLHEWLQQ HGIPGLQGVD 130 140 150 160 170 180 TRELTKKLRE QGSLLGKLVQ NGTEPSSLPF LDPNARPLVP EVSIKTPRVF NTGGAPRILA 190 200 210 220 230 240 LDCGLKYNQI RCLCQRGAEV TVVPWDHALD SQEYEGLFLS NGPGDPASYP SVVSTLSRVL 250 260 270 280 290 300 SEPNPRPVFG ICLGHQLLAL AIGAKTYKMR YGNRGHNQPC LLVGSGRCFL TSQNHGFAVE 310 320 330 340 350 360 TDSLPADWAP LFTNANDGSN EGIVHNSLPF FSVQFHPEHQ AGPSDMELLF DIFLETVKEA 370 380 390 400 410 420 TAGNPGGQTV RERLTERLCP PGIPTPGSGL PPPRKVLILG SGGLSIGQAG EFDYSGSQAI 430 440 450 460 470 480 KALKEENIQT LLINPNIATV QTSQGLADKV YFLPITPHYV TQVIRNERPD GVLLTFGGQT 490 500 510 520 530 540 ALNCGVELTK AGVLARYGVR VLGTPVETIE LTEDRRAFAA RMAEIGEHVA PSEAANSLEQ 550 560 570 580 590 600 AQAAAERLGY PVLVRAAFAL GGLGSGFASN REELSALVAP AFAHTSQVLV DKSLKGWKEI 610 620 630 640 650 660 EYEVVRDAYG NCVTVCNMEN LDPLGIHTGE SIVVAPSQTL NDREYQLLRQ TAIKVTQHLG 670 680 690 700 710 720 IVGECNVQYA LNPESEQYYI IEVNARLSRS SALASKATGY PLAYVAAKLA LGIPLPELRN 730 740 750 760 770 780 SVTGGTAAFE PSVDYCVVKI PRWDLSKFLR VSTKIGSCMK SVGEVMGIGR SFEEAFQKAL 790 800 810 820 830 840 RMVDENCVGF DHTVKPVSDM ELETPTDKRI FVVAAALWAG YSVDRLYELT RIDRWFLHRM 850 860 870 880 890 900 KRIIAHAQLL EQHRGQPLPP DLLQQAKCLG FSDKQIALAV LSTELAVRKL RQELGICPAV 910 920 930 940 950 960 KQIDTVAAEW PAQTNYLYLT YWGTTHDLTF RTPHVLVLGS GVYRIGSSVE FDWCAVGCIQ 970 980 990 1000 1010 1020 QLRKMGYKTI MVNYNPETVS TDYDMCDRLY FDEISFEVVM DIYELENPEG VILSMGGQLP 1030 1040 1050 1060 1070 1080 NNMAMALHRQ QCRVLGTSPE AIDSAENRFK FSRLLDTIGI SQPQWRELSD LESARQFCQT 1090 1100 1110 1120 1130 1140 VGYPCVVRPS YVLSGAAMNV AYTDGDLERF LSSAAAVSKE HPVVISKFIQ EAKEIDVDAV 1150 1160 1170 1180 1190 1200 ASDGVVAAIA ISEHVENAGV HSGDATLVTP PQDITAKTLE RIKAIVHAVG QELQVTGPFN 1210 1220 1230 1240 1250 1260 LQLIAKDDQL KVIECNVRVS RSFPFVSKTL GVDLVALATR VIMGEEVEPV GLMTGSGVVG 1270 1280 1290 1300 1310 1320 VKVPQFSFSR LAGADVVLGV EMTSTGEVAG FGESRCEAYL KAMLSTGFKI PKKNILLTIG 1330 1340 1350 1360 1370 1380 SYKNKSELLP TVRLLESLGY SLYASLGTAD FYTEHGVKVT AVDWHFEEAV DGECPPQRSI 1390 1400 1410 1420 1430 1440 LEQLAEKNFE LVINLSMRGA GGRRLSSFVT KGYRTRRLAA DFSVPLIIDI KCTKLFVEAL 1450 1460 1470 1480 1490 1500 GQIGPAPPLK VHVDCMTSQK LVRLPGLIDV HVHLREPGGT HKEDFASGTA AALAGGITMV 1510 1520 1530 1540 1550 1560 CAMPNTRPPI IDAPALALAQ KLAEAGARCD FALFLGASSE NAGTLGTVAG SAAGLKLYLN 1570 1580 1590 1600 1610 1620 ETFSELRLDS VVQWMEHFET WPSHLPIVAH AEQQTVAAVL MVAQLTQRSV HICHVARKEE 1630 1640 1650 1660 1670 1680 ILLIKAAKAR GLPVTCEVAP HHLFLSHDDL ERLGPGKGEV RPELGSRQDV EALWENMAVI 1690 1700 1710 1720 1730 1740 DCFASDHAPH TLEEKCGSRP PPGFPGLETM LPLLLTAVSE GRLSLDDLLQ RLHHNPRRIF 1750 1760 1770 1780 1790 1800 HLPPQEDTYV EVDLEHEWTI PSHMPFSKAH WTPFEGQKVK GTVRRVVLRG EVAYIDGQVL 1810 1820 1830 1840 1850 1860 VPPGYGQDVR KWPQGAVPQL PPSAPATSEM TTTPERPRRG IPGLPDGRFH LPPRIHRASD 1870 1880 1890 1900 1910 1920 PGLPAEEPKE KSSRKVAEPE LMGTPDGTCY PPPPVPRQAS PQNLGTPGLL HPQTSPLLHS 1930 1940 1950 1960 1970 1980 LVGQHILSVQ QFTKDQMSHL FNVAHTLRMM VQKERSLDIL KGKVMASMFY EVSTRTSSSF 1990 2000 2010 2020 2030 2040 AAAMARLGGA VLSFSEATSS VQKGESLADS VQTMSCYADV VVLRHPQPGA VELAAKHCRR 2050 2060 2070 2080 2090 2100 PVINAGDGVG EHPTQALLDI FTIREELGTV NGMTITMVGD LKHGRTVHSL ACLLTQYRVS 2110 2120 2130 2140 2150 2160 LRYVAPPSLR MPPTVRAFVA SRGTKQEEFE SIEEALPDTD VLYMTRIQKE RFGSTQEYEA 2170 2180 2190 2200 2210 2220 CFGQFILTPH IMTRAKKKMV VMHPMPRVNE ISVEVDSDPR AAYFRQAENG MYIRMALLAT VLGRF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of a human cDNA encoding a trifunctional enzyme of carbamoyl-phosphate synthetase-aspartate transcarbamoylase-dihydroorotase in de Novo pyrimidine synthesis." Iwahana H., Fujimura M., Ii S., Kondo M., Moritani M., Takahashi Y., Yamaoka T., Yoshimoto K., Itakura M. Biochem. Biophys. Res. Commun. 219:249-255(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetal lung fibroblast.
[2]	Mural R.J., Istrail S., Sutton G.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. , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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]. Tissue: Eye.
[4]	Bienvenut W.V., Dhillon A.S., Matallanas D., Murray L., Brunton V.G., Cooper W.N., Boldt K., von Kriegsheim A.F., Kolch W., Frame M.C. Submitted (FEB-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-13; 157-165; 169-177; 359-371; 501-516; 548-555; 599-606; 697-719; 761-778; 843-854; 932-944; 1034-1048; 1067-1075; 1110-1127; 1229-1240; 1263-1270; 1313-1323; 1326-1333; 1658-1667; 1723-1731; 1840-1848; 1976-1986; 2025-2036; 2103-2110; 2179-2187 AND 2215-2225, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Colon adenocarcinoma and Hepatoma.
[5]	"Organization and nucleotide sequence of the 3' end of the human CAD gene." Davidson J.N., Rao G.N., Niswander L., Andreano C., Tamer C., Chen K.C. DNA Cell Biol. 9:667-676(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1752-2225.
[6]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1859, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1859, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1859 AND THR-1884, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1884, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[11]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-747 AND LYS-1411, MASS SPECTROMETRY.
[12]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1859; SER-1900 AND THR-1906, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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].
[14]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1406 AND SER-1859, MASS SPECTROMETRY.
[15]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-177 AND CYS-735.
+	Additional computationally mapped references.

Web resources

Wikipedia

Aspartate carbamoyltransferase entry

Cross-references

Sequence databases
EMBL GenBank DDBJ	D78586 mRNA. Translation: BAA11423.1. CH471053 Genomic DNA. Translation: EAX00612.1. CH471053 Genomic DNA. Translation: EAX00613.1. CH471053 Genomic DNA. Translation: EAX00614.1. BC065510 mRNA. Translation: AAH65510.1. M38561 Genomic DNA. Translation: AAA51907.1.
IPI	IPI00301263.
PIR	A36240.
RefSeq	NP_004332.2. NM_004341.3.
UniGene	Hs.377010.
3D structure databases
ProteinModelPortal	P27708.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-39484N.
IntAct	P27708. 16 interactions.
MINT	MINT-5000537.
STRING	9606.ENSP00000264705.
Protein family/group databases
MEROPS	C26.952.
PTM databases
PhosphoSite	P27708.
Polymorphism databases
DMDM	50403731.
Proteomic databases
PaxDb	P27708.
PeptideAtlas	P27708.
PRIDE	P27708.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000264705; ENSP00000264705; ENSG00000084774.
GeneID	790.
KEGG	hsa:790.
UCSC	uc002rji.3. human.
Organism-specific databases
CTD	790.
GeneCards	GC02P027440.
HGNC	HGNC:1424. CAD.
HPA	CAB007781.
MIM	114010. gene.
neXtProt	NX_P27708.
PharmGKB	PA26023.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0458.
HOGENOM	HOG000234584.
HOVERGEN	HBG000279.
InParanoid	P27708.
KO	K11540.
OrthoDB	EOG46WZ7G.
PhylomeDB	P27708.
Enzyme and pathway databases
BioCyc	MetaCyc:ENSG00000084774-MONOMER.
BRENDA	3.5.2.3. 2681.
Reactome	REACT_111217. Metabolism.
UniPathway	UPA00070; UER00115. UPA00070; UER00116. UPA00070; UER00117.
Gene expression databases
ArrayExpress	P27708.
Bgee	P27708.
CleanEx	HS_CAD.
Genevestigator	P27708.
GermOnline	ENSG00000084774. Homo sapiens.
Family and domain databases
Gene3D	1.10.1030.10. 1 hit. 3.30.1490.20. 1 hit. 3.30.470.20. 2 hits. 3.40.50.1380. 1 hit. 3.40.50.20. 2 hits. 3.50.30.20. 1 hit.
InterPro	IPR006132. Asp/Orn_carbamoyltranf_P-bd. IPR006130. Asp/Orn_carbamoylTrfase. IPR002082. Asp_carbamoyltransf. IPR006131. Asp_carbamoyltransf_Asp/Orn-bd. IPR011761. 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. IPR002195. Dihydroorotase_CS. IPR017926. GATASE_1. IPR011059. Metal-dep_hydrolase_composite. IPR011607. MGS-like_dom. IPR016185. PreATP-grasp_dom. [Graphical view]
Pfam	PF00289. 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. PF00185. OTCace. 1 hit. PF02729. OTCace_N. 1 hit. [Graphical view]
PRINTS	PR00100. AOTCASE. PR00101. ATCASE. PR00098. CPSASE.
SMART	SM01096. CPSase_L_D3. 1 hit. SM01097. CPSase_sm_chain. 1 hit. SM00851. MGS. 1 hit. [Graphical view]
SUPFAM	SSF53671. Asp/Orn_carbamoyltranf. 1 hit. SSF48108. CarbamoylP_synth_lsu_oligo. 1 hit. SSF52021. CP_synthsmall. 1 hit. SSF51338. Metalo_hydrolase. 1 hit. SSF52335. MGS-like_dom. 1 hit. SSF52440. PreATP-grasp-like. 2 hits.
TIGRFAMs	TIGR00670. asp_carb_tr. 1 hit. TIGR01369. CPSaseII_lrg. 1 hit. TIGR01368. CPSaseIIsmall. 1 hit.
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. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P27708.
ChEMBL	CHEMBL3093.
ChiTaRS	cad. human.
DrugBank	DB00128. L-Aspartic Acid. DB00130. L-Glutamine.
GenomeRNAi	790.
NextBio	3214.
PMAP-CutDB	P27708.
SOURCE	Search...

Entry information

Entry name

PYR1_HUMAN

Accession

Primary (citable) accession number: P27708
Secondary accession number(s): D6W552, Q6P0Q0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	July 19, 2004
Last modified:	May 1, 2013
This is version 156 of the entry and version 3 of the sequence. [Complete history]

Entry status

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.