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P08955

- PYR1_MESAU

UniProt

P08955 - PYR1_MESAU

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Protein

CAD protein

Gene
CAD
Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed - Annotation score: 5 out of 5 - 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).UniRule annotation

Catalytic activityi

2 ATP + L-glutamine + HCO3- + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate.UniRule annotation
Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate.UniRule annotation
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate.UniRule annotation

Cofactori

Binds 3 zinc ions per subunit (for dihydroorotase activity) By similarity.

Enzyme 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.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei252 – 2521For GATase activity By similarity
Active sitei336 – 3361For GATase activity By similarity
Active sitei338 – 3381For GATase activity By similarity
Metal bindingi1471 – 14711Zinc 1; via tele nitrogen By similarity
Metal bindingi1471 – 14711Zinc 2; via pros nitrogen By similarity
Metal bindingi1473 – 14731Zinc 1; via tele nitrogen By similarity
Binding sitei1475 – 14751N-carbamoyl-L-aspartate By similarity
Binding sitei1505 – 15051N-carbamoyl-L-aspartate By similarity
Metal bindingi1556 – 15561Zinc 1; via carbamate group By similarity
Metal bindingi1556 – 15561Zinc 3; via carbamate group By similarity
Metal bindingi1590 – 15901Zinc 3; via pros nitrogen By similarity
Metal bindingi1613 – 16131Zinc 2 By similarity
Metal bindingi1614 – 16141Zinc 3; via tele nitrogen By similarity
Metal bindingi1637 – 16371Zinc 2 By similarity
Binding sitei1661 – 16611N-carbamoyl-L-aspartate; via amide nitrogen and carbonyl oxygen By similarity
Metal bindingi1686 – 16861Zinc 1 By similarity
Binding sitei1686 – 16861N-carbamoyl-L-aspartate By similarity
Binding sitei1690 – 16901N-carbamoyl-L-aspartate By similarity

GO - Molecular functioni

  1. aspartate binding Source: BHF-UCL
  2. aspartate carbamoyltransferase activity Source: BHF-UCL
  3. ATP binding Source: BHF-UCL
  4. carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Source: BHF-UCL
  5. dihydroorotase activity Source: BHF-UCL
  6. protein kinase activity Source: BHF-UCL
  7. UTP binding Source: MGI
  8. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. 'de novo' pyrimidine nucleobase biosynthetic process Source: BHF-UCL
  2. 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
  3. carbamoyl phosphate biosynthetic process Source: InterPro
  4. glutamine catabolic process Source: InterPro
  5. glutamine metabolic process Source: BHF-UCL
  6. peptidyl-threonine phosphorylation Source: BHF-UCL
  7. protein autophosphorylation Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Ligase, Transferase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.2.3. 3239.
SABIO-RKP08955.
UniPathwayiUPA00070; UER00115.
UPA00070; UER00116.
UPA00070; UER00117.

Protein family/group databases

MEROPSiM38.972.

Names & Taxonomyi

Protein namesi
Recommended name:
CAD protein
Including the following 3 domains:
Glutamine-dependent carbamoyl-phosphate synthase (EC:6.3.5.5)
Aspartate carbamoyltransferase (EC:2.1.3.2)
Dihydroorotase (EC:3.5.2.3)
Gene namesi
Name:CAD
OrganismiMesocricetus auratus (Golden hamster)
Taxonomic identifieri10036 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Subcellular locationi

Cytoplasm. Nucleus By similarity
Note: Cytosolic and unphosphorylated in resting cells, translocates to the nucleus in response to EGF stimulation, nuclear import promotes optimal cell growth By similarity.UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: BHF-UCL
  3. mitochondrion Source: BHF-UCL
  4. nuclear matrix Source: BHF-UCL
  5. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1406 – 14061S → A: No effect on enzyme kinetics. 1 Publication
Mutagenesisi1406 – 14061S → D: Increases CPSase activity and reduces sensitivy to feedback inhibition by UTP. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 22252224CAD proteinUniRule annotationPRO_0000199507Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei456 – 4561Phosphothreonine; by MAPK1 By similarity
Modified residuei747 – 7471N6-acetyllysine By similarity
Modified residuei1406 – 14061Phosphoserine; by PKA1 Publication
Modified residuei1411 – 14111N6-acetyllysine By similarity
Modified residuei1556 – 15561N6-carboxylysine By similarity
Modified residuei1859 – 18591Phosphoserine; by RPS6KB1 and PKA By similarity
Modified residuei1873 – 18731Phosphoserine; by PKC; in vitro By similarity
Modified residuei1884 – 18841Phosphothreonine By similarity
Modified residuei1900 – 19001Phosphoserine By similarity

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 By similarity. Phosphorylation at Ser-1406 reduces sensitivy to feedback inhibition by UTP.UniRule annotation

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP08955.

Interactioni

Subunit structurei

Homohexamer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP08955.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini177 – 363187Glutamine amidotransferase type-1Add
BLAST
Domaini519 – 711193ATP-grasp 1Add
BLAST
Domaini1052 – 1243192ATP-grasp 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 365364GATase (Glutamine amidotransferase)UniRule annotationAdd
BLAST
Regioni366 – 39429LinkerUniRule annotationAdd
BLAST
Regioni395 – 14551061CPSase (Carbamoyl-phosphate synthase)UniRule annotationAdd
BLAST
Regioni395 – 933539CPSase AUniRule annotationAdd
BLAST
Regioni934 – 1455522CPSase BUniRule annotationAdd
BLAST
Regioni1456 – 1788333DHOase (dihydroorotase)UniRule annotationAdd
BLAST
Regioni1789 – 1917129LinkerUniRule annotationAdd
BLAST
Regioni1918 – 2225308ATCase (Aspartate transcarbamylase)UniRule annotationAdd
BLAST

Sequence similaritiesi

In the central section; belongs to the DHOase family.
Contains 2 ATP-grasp domains.

Keywords - Domaini

Repeat

Phylogenomic databases

HOVERGENiHBG000279.

Family and domain databases

Gene3Di1.10.1030.10. 1 hit.
3.30.1490.20. 1 hit.
3.30.470.20. 2 hits.
3.40.50.1370. 2 hits.
3.40.50.1380. 1 hit.
3.40.50.20. 2 hits.
3.40.50.880. 1 hit.
3.50.30.20. 1 hit.
HAMAPiMF_00001. Asp_carb_tr.
MF_01209. CPSase_S_chain.
InterProiIPR006132. 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.
IPR029062. Class_I_gatase-like.
IPR002195. Dihydroorotase_CS.
IPR017926. GATASE.
IPR011059. Metal-dep_hydrolase_composite.
IPR011607. MGS-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamiPF00289. 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]
PRINTSiPR00100. AOTCASE.
PR00101. ATCASE.
PR00098. CPSASE.
SMARTiSM01096. CPSase_L_D3. 1 hit.
SM01097. CPSase_sm_chain. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMiSSF48108. SSF48108. 1 hit.
SSF51338. SSF51338. 1 hit.
SSF52021. SSF52021. 1 hit.
SSF52317. SSF52317. 1 hit.
SSF52335. SSF52335. 1 hit.
SSF52440. SSF52440. 2 hits.
SSF53671. SSF53671. 1 hit.
TIGRFAMsiTIGR00670. asp_carb_tr. 1 hit.
TIGR01369. CPSaseII_lrg. 1 hit.
TIGR01368. CPSaseIIsmall. 1 hit.
PROSITEiPS50975. 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]

Sequencei

Sequence statusi: Complete.

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

P08955-1 [UniParc]FASTAAdd to Basket

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MAALVLEDGS VLQGRPFGAA VSTAGEVVFQ TGMVGYPEAL TDPSYKAQIL     50
VLTYPLIGNY GIPSDEEDEF GLSKWFESSE NHVAGLVVGE CCPTPSHWSA 100
TCTLHEWLQQ HGIPGLQGVD TRELTKKLRE QGSLLGKLVQ SGTEPSTLPF 150
VDPNARPLAP EVSIKTPRVF NAGGAPRICA LDCGLKYNQI RCLCQLGAEV 200
TVVPWNHELD SQKYDGLFLS NGPGDPASYP GVVATLNRVL SEPNPRPVFG 250
ICLGHQLLAL AIGAKTYKMR YGNRGHNQPC LLVGTGRCFL TSQNHGFAVD 300
ADSLPAGWTP LFTNANDCSN EGIVHDSLPF FSVQFHPEHR AGPSDMELLF 350
DVFLETVREA VAGNPGGQTV KERLVQRLCP PGLLIPGSGL PPPRKVLILG 400
SGGLSIGQAG EFDYSGSQAI KALKEENIQT LLINPNIATV QTSQGLADKV 450
YFLPITPHYV TQVIRNERPD GVLLTFGGQT ALNCGVELTK AGVLARYGVR 500
VLGTPVETIE LTEDRRAFAA RMAEIGEHVA PSEAANSLEQ AQAAAERLGY 550
PVLVRAAFAL GGLGSGFAST KEELSALVAP AFAHTSQVLI DKSLKGWKEI 600
EYEVVRDAYG NCVTVCNMEN LDPLGIHTGE SIVVAPSQTL NDREYQLLRR 650
TAIKVTQHLG IVGECNVQYA LNPESEQYYI IEVNARLSRS SALASKATGY 700
PLAYVAAKLA LGIPLPELRN SVTGGTAAFE PSLDYCVVKI PRWDLSKFLR 750
VSTKIGSCMK SVGEVMGIGR SFEEAFQKAL RMVDENCVGF DHTVKPVSDV 800
ELETPTDKRI FVVAAALWAG YSVERLYELT RIDCWFLHRM KRIVTHAQLL 850
EQHRGQPLSQ DLLHQAKCLG FSDKQIALAV LSTELAVRKL RQELGICPAV 900
KQIDTVAAEW PAQTNYLYLT YWGNTHDLDF RTPHVLVLGS GVYRIGSSVE 950
FDWCAVGCIQ QLRKMGYKTI MVNYNPETVS TDYDMCDRLY FDEISFEVVM 1000
DIYELENPDG VILSMGGQLP NNMAMALHRQ QCRVLGTSPE AIDSAENRFK 1050
FSRLLDTIGI SQPQWRELSD LESARQFCQT VGYPCVVRPS YVLSGAAMNV 1100
AYTDGDLERF LSSAAAVSKE HPVVISKFIQ EAKEIDVDAV ACDGVVSAIA 1150
ISEHVENAGV HSGDATLVTP PQDITPKTLE RIKAIVHAVG QELQVTGPFN 1200
LQLIAKDDQL KVIECNVRVS RSFPFVSKTL GVDLVALATR IIMGEKVEPI 1250
GLMTGSGVVG VKVPQFSFSR LAGADVVLGV EMTSTGEVAG FGESRCEAYL 1300
KAMLSTGFKI PKKNILLTIG SYKNKSELLP TVRLLESLGY SLYASLGTAD 1350
FYTEHGVKVT AVDWHFEEAV DGECPPQRSI LDQLAENHFE LVINLSMRGA 1400
GGRRLSSFVT KGYRTRRLAA DFSVPLIIDI KCTKLFVEAL GQIGPAPPLK 1450
VHVDCMTSQK LVRLPGLIDV HVHLREPGGT HKEDFASGTA AALAGGVTMV 1500
CAMPNTRPPI IDAPALALAQ KLAEAGARCD FALFLGASSE NAGTLGAVAG 1550
SAAGLKLYLN ETFSELRLDS VAQWMEHFET WPSHLPIVAH AERQSVAAVL 1600
MVAQLTQRPV HICHVARKEE ILLIKTAKAQ GLPVTCEVAP HHLFLNREDL 1650
ERLGPGRGEV RPELGSREDM EALWENMAVI DCFASDHAPH TLEEKCGPKP 1700
PPGFPGLETM LPLLLTAVSE GRLSLDDLLQ RLHHNPRRIF HLPLQEDTYV 1750
EVDLEHEWTI PSHMPFSKAR WTPFEGQKVK GTIRRVVLRG EVAYIDGQVL 1800
VPPGYGQDVR KWPQGAVPQP PPSAPATTEI TTTPERPRRV IPGLPDGRFH 1850
LPPRIHRASD PGLPAEEPKE KPSRKVVEPE LMGTPDGPCY PAPPVPRQAS 1900
PQNLGSSGLL HPQTSPLLHS LVGQHILSVK QFTKDQMSHL FNVAHTLRMM 1950
VQKERSLDIL KGKVMASMFY EVSTRTSSSF AAAMARLGGA VLSFSEATSS 2000
VQKGESLADS VQTMSCYADV VVLRHPQPGA VELAAKHCRR PVINAGDGVG 2050
EHPTQALLDI FTIREELGTV NGMTITMVGD LKHGRTVHSL ACLLTQYRVS 2100
LRYVAPPSLR MPPSVWDFVA SRGTKQEEFE SIEEALPDTD VLYMTRIQKE 2150
RFGSTQEYEA CFGQFILTPH IMTRAKKKMV VMHPMPRVNE ISVEVDSDPR 2200
AAYFRQAENG MYIRMALLAT VLGRF 2225
Length:2,225
Mass (Da):243,128
Last modified:August 1, 1992 - v4
Checksum:i9F6EBA9BD4C6EC5A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05503 mRNA. Translation: AAA37062.1.
M28866 mRNA. Translation: AAA37073.1.
M60078 mRNA. Translation: AAA63617.1.
M11242 mRNA. Translation: AAA37061.1.
M23652 mRNA. Translation: AAA37064.1.
M21927 mRNA. Translation: AAA37063.1.
PIRiA38653. A23443.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05503 mRNA. Translation: AAA37062.1 .
M28866 mRNA. Translation: AAA37073.1 .
M60078 mRNA. Translation: AAA63617.1 .
M11242 mRNA. Translation: AAA37061.1 .
M23652 mRNA. Translation: AAA37064.1 .
M21927 mRNA. Translation: AAA37063.1 .
PIRi A38653. A23443.

3D structure databases

ProteinModelPortali P08955.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M38.972.

Proteomic databases

PRIDEi P08955.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG000279.

Enzyme and pathway databases

UniPathwayi UPA00070 ; UER00115 .
UPA00070 ; UER00116 .
UPA00070 ; UER00117 .
BRENDAi 3.5.2.3. 3239.
SABIO-RK P08955.

Family and domain databases

Gene3Di 1.10.1030.10. 1 hit.
3.30.1490.20. 1 hit.
3.30.470.20. 2 hits.
3.40.50.1370. 2 hits.
3.40.50.1380. 1 hit.
3.40.50.20. 2 hits.
3.40.50.880. 1 hit.
3.50.30.20. 1 hit.
HAMAPi MF_00001. Asp_carb_tr.
MF_01209. CPSase_S_chain.
InterProi 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.
IPR029062. Class_I_gatase-like.
IPR002195. Dihydroorotase_CS.
IPR017926. GATASE.
IPR011059. Metal-dep_hydrolase_composite.
IPR011607. MGS-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view ]
Pfami 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 ]
PRINTSi PR00100. AOTCASE.
PR00101. ATCASE.
PR00098. CPSASE.
SMARTi SM01096. CPSase_L_D3. 1 hit.
SM01097. CPSase_sm_chain. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view ]
SUPFAMi SSF48108. SSF48108. 1 hit.
SSF51338. SSF51338. 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 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 ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning of a cDNA encoding the amino end of the mammalian multifunctional protein CAD and analysis of the 5'-flanking region of the CAD gene."
    Bein K., Simmer J.P., Evans D.R.
    J. Biol. Chem. 266:3791-3799(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-169.
  2. "Characterization of the 5' end of the growth-regulated Syrian hamster CAD gene."
    Farnham P.J., Kollmar R.
    Cell Growth Differ. 1:179-189(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-73.
  3. "Mammalian carbamyl phosphate synthetase (CPS). DNA sequence and evolution of the CPS domain of the Syrian hamster multifunctional protein CAD."
    Simmer J.P., Kelly R.E., Rinker A.G. Jr., Scully J.L., Evans D.R.
    J. Biol. Chem. 265:10395-10402(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 156-1455.
  4. "Identification of the junction between the glutamine amidotransferase and carbamyl phosphate synthetase domains of the mammalian CAD protein."
    Maley J.A., Davidson J.N.
    Biochem. Biophys. Res. Commun. 154:1047-1053(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 246-513.
  5. "Mammalian dihydroorotase: nucleotide sequence, peptide sequences, and evolution of the dihydroorotase domain of the multifunctional protein CAD."
    Simmer J.P., Kelly R.E., Rinker A.G. Jr., Zimmermann B.H., Scully J.L., Kim H., Evans D.R.
    Proc. Natl. Acad. Sci. U.S.A. 87:174-178(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1391-1870.
  6. "Location of the dihydroorotase domain within trifunctional hamster dihydroorotate synthetase."
    Williams N.K., Simpson R.J., Moritz R.L., Peide Y., Crofts L., Minasian E., Leach S.J., Wake R.G., Christopherson R.I.
    Gene 94:283-288(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1403-2110.
  7. "Mammalian aspartate transcarbamylase (ATCase): sequence of the ATCase domain and interdomain linker in the CAD multifunctional polypeptide and properties of the isolated domain."
    Simmer J.P., Kelly R.E., Scully J.L., Grayson D.R., Rinker A.G. Jr., Bergh S.T., Evans D.R.
    Proc. Natl. Acad. Sci. U.S.A. 86:4382-4386(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1774-2225.
  8. "Construction of a cDNA to the hamster CAD gene and its application toward defining the domain for aspartate transcarbamylase."
    Shigesada K., Stark G.R., Maley J.A., Niswander L.A., Davidson J.N.
    Mol. Cell. Biol. 5:1735-1742(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2074-2225.
  9. "Oligomeric structure of the multifunctional protein CAD that initiates pyrimidine biosynthesis in mammalian cells."
    Lee L., Kelly R.E., Pastra-Landis S.C., Evans D.R.
    Proc. Natl. Acad. Sci. U.S.A. 82:6802-6806(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  10. "The structural organization of the hamster multifunctional protein CAD. Controlled proteolysis, domains, and linkers."
    Kim H., Kelly R.E., Evans D.R.
    J. Biol. Chem. 267:7177-7184(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAINS, PARTIAL PROTEIN SEQUENCE.
  11. "Site-directed substitution of Ser1406 of hamster CAD with glutamic acid alters allosteric regulation of carbamyl phosphate synthetase II."
    Banerjei L.C., Davidson J.N.
    Somat. Cell Mol. Genet. 23:37-49(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-1406, MUTAGENESIS OF SER-1406.
  12. "Comparative modeling of mammalian aspartate transcarbamylase."
    Scully J.L., Evans D.R.
    Proteins 9:191-206(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF ATCASE DOMAIN.

Entry informationi

Entry nameiPYR1_MESAU
AccessioniPrimary (citable) accession number: P08955
Secondary accession number(s): P70108
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: August 1, 1992
Last modified: June 11, 2014
This is version 138 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

GATase (glutamine amidotransferase) and CPSase (carbamoyl phosphate synthase) form together the glutamine-dependent CPSase (GD-CPSase) (EC 6.3.5.5).

Keywords - Technical termi

Allosteric enzyme, Direct protein sequencing, Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi