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B2RQC6

- PYR1_MOUSE

UniProt

B2RQC6 - PYR1_MOUSE

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Protein

CAD protein

Gene
Cad
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase) By similarity.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 By similarity.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. amino acid binding Source: InterPro
  2. aspartate carbamoyltransferase activity Source: UniProtKB-EC
  3. ATP binding Source: UniProtKB-KW
  4. carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Source: UniProtKB-EC
  5. dihydroorotase activity Source: UniProtKB
  6. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. 'de novo' pyrimidine nucleobase biosynthetic process Source: UniProtKB
  2. 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
  3. carbamoyl phosphate biosynthetic process Source: InterPro
  4. cellular response to drug Source: Ensembl
  5. cellular response to epidermal growth factor stimulus Source: Ensembl
  6. drug metabolic process Source: Ensembl
  7. embryo development Source: Ensembl
  8. female pregnancy Source: Ensembl
  9. glutamine catabolic process Source: InterPro
  10. lactation Source: Ensembl
  11. organ regeneration Source: Ensembl
  12. response to amine Source: Ensembl
  13. response to caffeine Source: Ensembl
  14. response to cortisol Source: Ensembl
  15. response to testosterone Source: Ensembl
  16. UTP biosynthetic process Source: Ensembl
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

UniPathwayiUPA00070; UER00115.
UPA00070; UER00116.
UPA00070; UER00117.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1916969. Cad.

Subcellular locationi

Cytoplasm By similarity. 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. cytosol Source: Ensembl
  2. neuronal cell body Source: Ensembl
  3. nuclear matrix Source: Ensembl
  4. protein complex Source: Ensembl
  5. terminal bouton Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 22252224CAD proteinUniRule annotationPRO_0000425955Add
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 PKA By similarity
Modified residuei1411 – 14111N6-acetyllysine By similarity
Modified residuei1556 – 15561N6-carboxylysine By similarity
Modified residuei1859 – 18591Phosphoserine; by RPS6KB1 and PKA 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. Phosphorylation at Ser-1406 reduces sensitivy to feedback inhibition by UTP By similarity.UniRule annotation

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiB2RQC6.

Expressioni

Gene expression databases

ArrayExpressiB2RQC6.
GenevestigatoriB2RQC6.

Interactioni

Subunit structurei

Homohexamer By similarity.UniRule annotation

Protein-protein interaction databases

IntActiB2RQC6. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliB2RQC6.
SMRiB2RQC6. Positions 1460-1823.

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

eggNOGiCOG0458.
GeneTreeiENSGT00390000015604.
HOGENOMiHOG000234584.
HOVERGENiHBG000279.
InParanoidiB2RQC6.
KOiK11540.
OMAiKRIVTHA.
OrthoDBiEOG7M6D6F.
PhylomeDBiB2RQC6.
TreeFamiTF105604.

Family and domain databases

Gene3Di1.10.1030.10. 1 hit.
3.30.1490.20. 2 hits.
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: B2RQC6-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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MAALVLEDGS VLQGRPFGAA VSTAGEVVFQ TGMVGYPEAL TDPSYKAQIL     50
VLTYPLIGNY GIPSDEEDEF GLSKWFESSE IHVAGLVVGE CCPTPSHWSA 100
NCTLHEWLQQ RGIPGLQGVD TRELTKKLRE QGSLLGKLVQ KGTEPSALPF 150
VDPNARPLAP EVSIKTPRVF NAGGAPRICA LDCGLKYNQI RCLCQLGAEV 200
TVVPWDHELD SQKYDGLFLS NGPGDPASYP GVVSTLSRVL SEPNPRPVFG 250
ICLGHQLLAL AIGAKTYKMR YGNRGHNQPC LLVGTGRCFL TSQNHGFAVD 300
ADSLPAGWAP LFTNANDCSN EGIVHDSLPF FSVQFHPEHR AGPSDMELLF 350
DVFLETVREA AAGNIGGQTV RERLAQRLCP PELPIPGSGL PPPRKVLILG 400
SGGLSIGQAG EFDYSGSQAI KALKEENIQT LLINPNIATV QTSQGLADKV 450
YFLPITLHYV 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 DHTVKPVSDM 800
ELETPTDKRI FVVAAALWAG YSVERLYELT RIDCWFLHRM KRIVTHAQLL 850
EQHRGQALPQ DLLHQAKCLG FSDKQIALAV LSTELAVRKL RQELGICPAV 900
KQIDTVAAEW PAQTNYLYLT YWGNTHDLDF RAPHVLVLGS GVYRIGSSVE 950
FDWCAVGCIQ QLRKMGYKTI MVNYNPETVS TDYDMCDRLY FDEISFEVVM 1000
DIYELENPEG VILSMGGQLP NNMAMALHRQ QCRVLGTSPE AIDSAENRFK 1050
FSRLLDTIGI SQPQWRELSD LESARQFCHT VGYPCVVRPS YVLSGAAMNV 1100
AYTDGDLERF LSSAAAVSKE HPVVISKFIQ EAKEIDVDAV ACDGIVSAIA 1150
ISEHVENAGV HSGDATLVTP PQDITPKTLE RIKAIVHAVG QELQVTGPFN 1200
LQLIAKDDQL KVIECNVRVS RSFPFVSKTL GVDLVALATR IIMGEKVEPV 1250
GLMTGSGVVG VKVPQFSFSR LAGADVVLGV EMTSTGEVAG FGESRCEAYL 1300
KAMLSTGFKI PEKNILLTIG 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 FTLFLGASSE NAGTLGAVAG 1550
SAAGLKLYLN ETFSELRLDS VAQWMEHFET WPAHLPIVAH AERQSVAAVL 1600
MVAQLTQRPV HICHVARKEE ILLIKTAKAQ GLPVTCEVAP HHLFLNREDL 1650
ERLGPGKGEV RPELGSREDM EALWENMAVI DCFASDHAPH TLEEKCGPKP 1700
PPGFPGLETM LPLLLTAVSE GRLSLDDLLQ RLHHNPRRIF HLPLQEDTYV 1750
EVDLEHEWTV PSHMPFSKAR WTPFEGQKVK GTVRRVVLRG EVAYIDGQVL 1800
VPPGYGQDVR KWPQGVVPQP PPSTPATTEI TTTPERPRRV IPGLPDGRFH 1850
LPPRIHRASD PGLPAEEPKE KPPRKVVEPE LMGTPDGPCY PAPPVPRQAS 1900
PQNLGSSGLL HPQMSPLLHS LVGQHILSVK QFTKDQMSHL FNVAHTLRMM 1950
VQKERSLDIL KGKVMASMFY EVSTRTSSSF AAAMARLGGA VLSFSEATSS 2000
VQKGESLADS VQTMSCYADV IVLRHPQPGA VELAAKHCRR PVINAGDGVG 2050
EHPTQALLDI FTIREELGTV NGMTITMVGD LKHGRTVHSL ACLLTQYRVS 2100
LRYVAPPSLR MPPSVRDFVA SRGTKQEEFE SIEEALPDTD VLYMTRIQKE 2150
RFGSVQEYEA CFGQFILTPH IMTRAKKKMV VMHPMPRVNE ISVEVDSDPR 2200
AAYFRQAENG MYIRMALLAT VLGRF 2225
Length:2,225
Mass (Da):243,238
Last modified:July 1, 2008 - v1
Checksum:iE7E606A0F650ABB4
GO
Isoform 2 (identifier: B2RQC6-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1962-2032: Missing.

Show »
Length:2,154
Mass (Da):235,851
Checksum:iA83FA6E22929070C
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1962 – 203271Missing in isoform 2. VSP_053912Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC109608 Genomic DNA. No translation available.
CH466524 Genomic DNA. Translation: EDL37329.1.
BC137856 mRNA. Translation: AAI37857.1.
BC144972 mRNA. Translation: AAI44973.1.
CCDSiCCDS19171.1. [B2RQC6-1]
RefSeqiNP_001276451.1. NM_001289522.1. [B2RQC6-2]
NP_076014.1. NM_023525.2. [B2RQC6-1]
UniGeneiMm.305535.

Genome annotation databases

EnsembliENSMUST00000013773; ENSMUSP00000013773; ENSMUSG00000013629. [B2RQC6-1]
ENSMUST00000170329; ENSMUSP00000130789; ENSMUSG00000013629. [B2RQC6-2]
GeneIDi69719.
KEGGimmu:69719.
UCSCiuc008wwz.1. mouse. [B2RQC6-1]
uc012duk.1. mouse.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC109608 Genomic DNA. No translation available.
CH466524 Genomic DNA. Translation: EDL37329.1 .
BC137856 mRNA. Translation: AAI37857.1 .
BC144972 mRNA. Translation: AAI44973.1 .
CCDSi CCDS19171.1. [B2RQC6-1 ]
RefSeqi NP_001276451.1. NM_001289522.1. [B2RQC6-2 ]
NP_076014.1. NM_023525.2. [B2RQC6-1 ]
UniGenei Mm.305535.

3D structure databases

ProteinModelPortali B2RQC6.
SMRi B2RQC6. Positions 1460-1823.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi B2RQC6. 3 interactions.

Chemistry

ChEMBLi CHEMBL2774.

Proteomic databases

MaxQBi B2RQC6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000013773 ; ENSMUSP00000013773 ; ENSMUSG00000013629 . [B2RQC6-1 ]
ENSMUST00000170329 ; ENSMUSP00000130789 ; ENSMUSG00000013629 . [B2RQC6-2 ]
GeneIDi 69719.
KEGGi mmu:69719.
UCSCi uc008wwz.1. mouse. [B2RQC6-1 ]
uc012duk.1. mouse.

Organism-specific databases

CTDi 790.
MGIi MGI:1916969. Cad.

Phylogenomic databases

eggNOGi COG0458.
GeneTreei ENSGT00390000015604.
HOGENOMi HOG000234584.
HOVERGENi HBG000279.
InParanoidi B2RQC6.
KOi K11540.
OMAi KRIVTHA.
OrthoDBi EOG7M6D6F.
PhylomeDBi B2RQC6.
TreeFami TF105604.

Enzyme and pathway databases

UniPathwayi UPA00070 ; UER00115 .
UPA00070 ; UER00116 .
UPA00070 ; UER00117 .

Miscellaneous databases

ChiTaRSi cad. mouse.
NextBioi 330178.
SOURCEi Search...

Gene expression databases

ArrayExpressi B2RQC6.
Genevestigatori B2RQC6.

Family and domain databases

Gene3Di 1.10.1030.10. 1 hit.
3.30.1490.20. 2 hits.
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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-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] (ISOFORMS 1 AND 2).
    Tissue: Brain.

Entry informationi

Entry nameiPYR1_MOUSE
AccessioniPrimary (citable) accession number: B2RQC6
Secondary accession number(s): B7ZN27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 19, 2014
Last sequence update: July 1, 2008
Last modified: September 3, 2014
This is version 66 of the entry and version 1 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, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi