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P07756

- CPSM_RAT

UniProt

P07756 - CPSM_RAT

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Protein

Carbamoyl-phosphate synthase [ammonia], mitochondrial

Gene
Cps1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell.UniRule annotation

Catalytic activityi

2 ATP + NH3 + CO2 + H2O = 2 ADP + phosphate + carbamoyl phosphate.1 Publication

Enzyme regulationi

Requires N-acetyl-L-glutamate (NAG) as an allosteric activator. N-acetyl-L-beta-phenylglutamate (Phe-NAG) can also activate CPSase I, but with an activation constant that is 2-fold higher than that for NAG.1 Publication

Kineticsi

The activation constant Ka of N-acetyl-L-glutamate for the reaction is 0.11 mM.

  1. KM=1.06 mM for ATP1 Publication
  2. KM=6.43 mM for HCO3-
  3. KM=1.07 mM for NH4+

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1391 – 13911Allosteric activator
Binding sitei1394 – 13941Allosteric activator
Binding sitei1410 – 14101Allosteric activator
Binding sitei1437 – 14371Allosteric activator
Binding sitei1440 – 14401Allosteric activator
Binding sitei1449 – 14491Allosteric activator

GO - Molecular functioni

  1. ATP binding Source: RGD
  2. calcium ion binding Source: RGD
  3. carbamoyl-phosphate synthase (ammonia) activity Source: RGD
  4. endopeptidase activity Source: RGD
  5. glutamate binding Source: RGD
  6. modified amino acid binding Source: Ensembl
  7. phospholipid binding Source: RGD
  8. protein complex binding Source: RGD

GO - Biological processi

  1. anion homeostasis Source: RGD
  2. carbamoyl phosphate biosynthetic process Source: Ensembl
  3. cellular response to cAMP Source: RGD
  4. cellular response to fibroblast growth factor stimulus Source: RGD
  5. cellular response to glucagon stimulus Source: RGD
  6. cellular response to oleic acid Source: RGD
  7. glutamine catabolic process Source: InterPro
  8. glycogen catabolic process Source: Ensembl
  9. hepatocyte differentiation Source: RGD
  10. homocysteine metabolic process Source: Ensembl
  11. liver development Source: RGD
  12. midgut development Source: RGD
  13. nitric oxide metabolic process Source: Ensembl
  14. positive regulation of vasodilation Source: Ensembl
  15. proteolysis Source: GOC
  16. response to acid Source: RGD
  17. response to amine Source: RGD
  18. response to amino acid Source: RGD
  19. response to cAMP Source: RGD
  20. response to dexamethasone Source: RGD
  21. response to drug Source: RGD
  22. response to food Source: RGD
  23. response to glucagon Source: RGD
  24. response to glucocorticoid Source: RGD
  25. response to growth hormone Source: RGD
  26. response to lipopolysaccharide Source: RGD
  27. response to oleic acid Source: RGD
  28. response to starvation Source: RGD
  29. response to steroid hormone Source: RGD
  30. response to toxic substance Source: RGD
  31. response to zinc ion Source: RGD
  32. triglyceride catabolic process Source: Ensembl
  33. urea cycle Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Urea cycle

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_216480. Urea cycle.
SABIO-RKP07756.

Protein family/group databases

MEROPSiC26.951.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbamoyl-phosphate synthase [ammonia], mitochondrial (EC:6.3.4.16)
Alternative name(s):
Carbamoyl-phosphate synthetase I
Short name:
CPSase I
Gene namesi
Name:Cps1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 9

Organism-specific databases

RGDi2395. Cps1.

Subcellular locationi

Mitochondrion. Nucleusnucleolus By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: RGD
  2. mitochondrial inner membrane Source: RGD
  3. mitochondrial nucleoid Source: Ensembl
  4. mitochondrion Source: HGNC
  5. nucleolus Source: UniProtKB-SubCell
  6. protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1391 – 13911T → V: 400-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG. 1 Publication
Mutagenesisi1394 – 13941T → A: 900-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG. 1 Publication
Mutagenesisi1410 – 14101W → K: 60-fold increase in the activation constant of NAG. 1 Publication
Mutagenesisi1437 – 14371N → D: 70-fold increase in the activation constant of NAG. 1 Publication
Mutagenesisi1440 – 14401N → D: 110-fold increase in the activation constant of NAG. Modifies the specificity for the activator: Binds Phe-NAG considerably better than NAG. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3838MitochondrionUniRule annotationAdd
BLAST
Chaini39 – 15001462Carbamoyl-phosphate synthase [ammonia], mitochondrialUniRule annotationPRO_0000029899Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei55 – 551N6-acetyllysine; alternate By similarity
Modified residuei55 – 551N6-succinyllysine; alternate By similarity
Modified residuei57 – 571N6-acetyllysine; alternate By similarity
Modified residuei57 – 571N6-succinyllysine; alternate By similarity
Modified residuei119 – 1191N6-acetyllysine; alternate By similarity
Modified residuei119 – 1191N6-succinyllysine; alternate By similarity
Modified residuei157 – 1571N6-acetyllysine; alternate By similarity
Modified residuei157 – 1571N6-succinyllysine; alternate By similarity
Modified residuei171 – 1711N6-acetyllysine By similarity
Modified residuei182 – 1821N6-acetyllysine By similarity
Modified residuei197 – 1971N6-acetyllysine By similarity
Modified residuei207 – 2071N6-acetyllysine; alternate By similarity
Modified residuei207 – 2071N6-succinyllysine; alternate By similarity
Modified residuei210 – 2101N6-acetyllysine By similarity
Modified residuei214 – 2141N6-acetyllysine; alternate By similarity
Modified residuei214 – 2141N6-succinyllysine; alternate By similarity
Modified residuei219 – 2191N6-acetyllysine By similarity
Modified residuei228 – 2281N6-acetyllysine By similarity
Modified residuei279 – 2791N6-acetyllysine By similarity
Modified residuei280 – 2801N6-acetyllysine By similarity
Modified residuei287 – 2871N6-acetyllysine; alternate By similarity
Modified residuei287 – 2871N6-succinyllysine; alternate By similarity
Modified residuei307 – 3071N6-acetyllysine; alternate By similarity
Modified residuei307 – 3071N6-succinyllysine; alternate By similarity
Modified residuei310 – 3101N6-acetyllysine By similarity
Modified residuei400 – 4001N6-succinyllysine By similarity
Modified residuei402 – 4021N6-succinyllysine By similarity
Modified residuei412 – 4121N6-acetyllysine; alternate By similarity
Modified residuei412 – 4121N6-succinyllysine; alternate By similarity
Modified residuei453 – 4531N6-acetyllysine By similarity
Modified residuei458 – 4581N6-acetyllysine; alternate By similarity
Modified residuei458 – 4581N6-succinyllysine; alternate By similarity
Modified residuei522 – 5221N6-acetyllysine; alternate By similarity
Modified residuei522 – 5221N6-succinyllysine; alternate By similarity
Modified residuei527 – 5271N6-acetyllysine; alternate By similarity
Modified residuei527 – 5271N6-succinyllysine; alternate By similarity
Modified residuei532 – 5321N6-acetyllysine By similarity
Modified residuei537 – 5371Phosphoserine By similarity
Glycosylationi537 – 5371O-linked (GlcNAc)
Modified residuei553 – 5531N6-acetyllysine; alternate By similarity
Modified residuei553 – 5531N6-succinyllysine; alternate By similarity
Modified residuei560 – 5601N6-acetyllysine; alternate By similarity
Modified residuei560 – 5601N6-succinyllysine; alternate By similarity
Modified residuei575 – 5751N6-acetyllysine; alternate By similarity
Modified residuei575 – 5751N6-succinyllysine; alternate By similarity
Modified residuei603 – 6031N6-acetyllysine; alternate By similarity
Modified residuei603 – 6031N6-succinyllysine; alternate By similarity
Modified residuei612 – 6121N6-acetyllysine; alternate By similarity
Modified residuei612 – 6121N6-succinyllysine; alternate By similarity
Modified residuei630 – 6301N6-acetyllysine By similarity
Modified residuei751 – 7511N6-acetyllysine; alternate By similarity
Modified residuei751 – 7511N6-succinyllysine; alternate By similarity
Modified residuei757 – 7571N6-acetyllysine; alternate By similarity
Modified residuei757 – 7571N6-succinyllysine; alternate By similarity
Modified residuei772 – 7721N6-acetyllysine By similarity
Modified residuei793 – 7931N6-acetyllysine; alternate By similarity
Modified residuei793 – 7931N6-succinyllysine; alternate By similarity
Modified residuei811 – 8111N6-acetyllysine By similarity
Modified residuei831 – 8311N6-acetyllysine; alternate By similarity
Modified residuei831 – 8311N6-succinyllysine; alternate By similarity
Modified residuei841 – 8411N6-acetyllysine By similarity
Modified residuei856 – 8561N6-acetyllysine By similarity
Modified residuei875 – 8751N6-acetyllysine; alternate By similarity
Modified residuei875 – 8751N6-succinyllysine; alternate By similarity
Modified residuei889 – 8891N6-acetyllysine; alternate By similarity
Modified residuei889 – 8891N6-succinyllysine; alternate By similarity
Modified residuei892 – 8921N6-acetyllysine; alternate By similarity
Modified residuei892 – 8921N6-succinyllysine; alternate By similarity
Modified residuei908 – 9081N6-acetyllysine By similarity
Modified residuei915 – 9151N6-acetyllysine; alternate By similarity
Modified residuei915 – 9151N6-succinyllysine; alternate By similarity
Modified residuei919 – 9191N6-acetyllysine; alternate By similarity
Modified residuei919 – 9191N6-succinyllysine; alternate By similarity
Modified residuei935 – 9351N6-acetyllysine By similarity
Modified residuei1074 – 10741N6-acetyllysine; alternate By similarity
Modified residuei1074 – 10741N6-succinyllysine; alternate By similarity
Modified residuei1079 – 10791Phosphoserine By similarity
Modified residuei1100 – 11001N6-acetyllysine; alternate By similarity
Modified residuei1100 – 11001N6-succinyllysine; alternate By similarity
Modified residuei1149 – 11491N6-succinyllysine By similarity
Modified residuei1168 – 11681N6-acetyllysine; alternate By similarity
Modified residuei1168 – 11681N6-succinyllysine; alternate By similarity
Modified residuei1183 – 11831N6-acetyllysine; alternate By similarity
Modified residuei1183 – 11831N6-succinyllysine; alternate By similarity
Modified residuei1222 – 12221N6-acetyllysine By similarity
Modified residuei1232 – 12321N6-acetyllysine; alternate By similarity
Modified residuei1232 – 12321N6-succinyllysine; alternate By similarity
Modified residuei1269 – 12691N6-acetyllysine; alternate By similarity
Modified residuei1269 – 12691N6-succinyllysine; alternate By similarity
Modified residuei1291 – 12911N6-acetyllysine; alternate By similarity
Modified residuei1291 – 12911N6-succinyllysine; alternate By similarity
Glycosylationi1331 – 13311O-linked (GlcNAc)
Glycosylationi1332 – 13321O-linked (GlcNAc)
Modified residuei1356 – 13561N6-acetyllysine; alternate By similarity
Modified residuei1356 – 13561N6-succinyllysine; alternate By similarity
Modified residuei1360 – 13601N6-succinyllysine By similarity
Modified residuei1444 – 14441N6-acetyllysine; alternate By similarity
Modified residuei1444 – 14441N6-succinyllysine; alternate By similarity
Modified residuei1471 – 14711N6-acetyllysine; alternate By similarity
Modified residuei1471 – 14711N6-succinyllysine; alternate By similarity
Modified residuei1479 – 14791N6-acetyllysine; alternate By similarity
Modified residuei1479 – 14791N6-succinyllysine; alternate By similarity
Modified residuei1486 – 14861N6-acetyllysine; alternate By similarity
Modified residuei1486 – 14861N6-succinyllysine; alternate By similarity

Post-translational modificationi

50% of the mature protein that was isolated had Leu-39 as its N-terminal residue and 50% had Ser-40 suggesting two adjacent processing sites. However, the possibility of proteolytic removal of Leu-39 during the isolation of the enzyme cannot be excluded.UniRule annotation
Succinylated at Lys-287 and Lys-1291. Desuccinylated at Lys-1291 by SIRT5, leading to activation By similarity.UniRule annotation

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP07756.
PRIDEiP07756.

PTM databases

PhosphoSiteiP07756.

Expressioni

Tissue specificityi

Primarily in the liver and small intestine.

Gene expression databases

GenevestigatoriP07756.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000019021.

Structurei

3D structure databases

ProteinModelPortaliP07756.
SMRiP07756. Positions 1343-1478.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini219 – 404186Glutamine amidotransferase type-1Add
BLAST
Domaini551 – 743193ATP-grasp 1Add
BLAST
Domaini1093 – 1284192ATP-grasp 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni39 – 218180Anthranilate phosphoribosyltransferase homologUniRule annotationAdd
BLAST

Domaini

The type-1 glutamine amidotransferase domain is defective.UniRule annotation

Sequence similaritiesi

Contains 2 ATP-grasp domains.

Keywords - Domaini

Repeat, Transit peptide

Phylogenomic databases

eggNOGiCOG0458.
GeneTreeiENSGT00390000015604.
HOGENOMiHOG000234583.
HOVERGENiHBG000279.
InParanoidiP07756.
KOiK01948.
OMAiMDLGTKA.
OrthoDBiEOG7M6D6F.
PhylomeDBiP07756.

Family and domain databases

Gene3Di1.10.1030.10. 1 hit.
3.30.1490.20. 2 hits.
3.30.470.20. 2 hits.
3.40.50.1380. 1 hit.
3.40.50.20. 2 hits.
3.40.50.880. 1 hit.
3.50.30.20. 1 hit.
HAMAPiMF_01209. CPSase_S_chain.
InterProiIPR011761. 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.
IPR017926. GATASE.
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.
[Graphical view]
PRINTSiPR00098. CPSASE.
SMARTiSM01096. CPSase_L_D3. 1 hit.
SM01097. CPSase_sm_chain. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMiSSF48108. SSF48108. 1 hit.
SSF52021. SSF52021. 1 hit.
SSF52317. SSF52317. 1 hit.
SSF52335. SSF52335. 1 hit.
SSF52440. SSF52440. 2 hits.
TIGRFAMsiTIGR01369. CPSaseII_lrg. 1 hit.
TIGR01368. CPSaseIIsmall. 1 hit.
PROSITEiPS50975. ATP_GRASP. 2 hits.
PS00866. CPSASE_1. 2 hits.
PS00867. CPSASE_2. 2 hits.
PS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P07756-1 [UniParc]FASTAAdd to Basket

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MTRILTACKV VKTLKSGFGL ANVTSKRQWD FSRPGIRLLS VKAQTAHIVL     50
EDGTKMKGYS FGHPSSVAGE VVFNTGLGGY SEALTDPAYK GQILTMANPI 100
IGNGGAPDTT ARDELGLNKY MESDGIKVAG LLVLNYSHDY NHWLATKSLG 150
QWLQEEKVPA IYGVDTRMLT KIIRDKGTML GKIEFEGQSV DFVDPNKQNL 200
IAEVSTKDVK VFGKGNPTKV VAVDCGIKNN VIRLLVKRGA EVHLVPWNHD 250
FTQMDYDGLL IAGGPGNPAL AQPLIQNVKK ILESDRKEPL FGISTGNIIT 300
GLAAGAKSYK MSMANRGQNQ PVLNITNRQA FITAQNHGYA LDNTLPAGWK 350
PLFVNVNDQT NEGIMHESKP FFAVQFHPEV SPGPTDTEYL FDSFFSLIKK 400
GKGTTITSVL PKPALVASRV EVSKVLILGS GGLSIGQAGE FDYSGSQAVK 450
AMKEENVKTV LMNPNIASVQ TNEVGLKQAD AVYFLPITPQ FVTEVIKAER 500
PDGLILGMGG QTALNCGVEL FKRGVLKEYG VKVLGTSVES IMATEDRQLF 550
SDKLNEINEK IAPSFAVESM EDALKAADTI GYPVMIRSAY ALGGLGSGIC 600
PNKETLMDLG TKAFAMTNQI LVERSVTGWK EIEYEVVRDA DDNCVTVCNM 650
ENVDAMGVHT GDSVVVAPAQ TLSNAEFQML RRTSINVVRH LGIVGECNIQ 700
FALHPTSMEY CIIEVNARLS RSSALASKAT GYPLAFIAAK IALGIPLPEI 750
KNVVSGKTSA CFEPSLDYMV TKIPRWDLDR FHGTSSRIGS SMKSVGEVMA 800
IGRTFEESFQ KALRMCHPSV DGFTPRLPMN KEWPANLDLR KELSEPSSTR 850
IYAIAKALEN NMSLDEIVKL TSIDKWFLYK MRDILNMDKT LKGLNSESVT 900
EETLRQAKEI GFSDKQISKC LGLTEAQTRE LRLKKNIHPW VKQIDTLAAE 950
YPSVTNYLYV TYNGQEHDIK FDEHGIMVLG CGPYHIGSSV EFDWCAVSSI 1000
RTLRQLGKKT VVVNCNPETV STDFDECDKL YFEELSLERI LDIYHQEACN 1050
GCIISVGGQI PNNLAVPLYK NGVKIMGTSP LQIDRAEDRS IFSAVLDELK 1100
VAQAPWKAVN TLNEALEFAN SVGYPCLLRP SYVLSGSAMN VVFSEDEMKR 1150
FLEEATRVSQ EHPVVLTKFI EGAREVEMDA VGKEGRVISH AISEHVEDAG 1200
VHSGDATLML PTQTISQGAI EKVKDATRKI AKAFAISGPF NVQFLVKGND 1250
VLVIECNLRA SRSFPFVSKT LGVDFIDVAT KVMIGESVDE KHLPTLEQPI 1300
IPSDYVAIKA PMFSWPRLRD ADPILRCEMA STGEVACFGE GIHTAFLKAM 1350
LSTGFKIPQK GILIGIQQSF RPRFLGVAEQ LHNEGFKLFA TEATSDWLNA 1400
NNVPATPVAW PSQEGQNPSL SSIRKLIRDG SIDLVINLPN NNTKFVHDNY 1450
VIRRTAVDSG IALLTNFQVT KLFAEAVQKA RTVDSKSLFH YRQYSAGKAA 1500
Length:1,500
Mass (Da):164,580
Last modified:August 1, 1988 - v1
Checksum:i038E8F893DE1C34D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M12335
, M11710, M12318, M12319, M12320, M12321, M12322, M12323, M12324, M12325, M12326, M12327, M12328 Genomic DNA. Translation: AAB59717.1.
J02805 Genomic DNA. Translation: AAA40959.1.
PIRiA28481. SYRTCA.
RefSeqiNP_058768.1. NM_017072.1.
UniGeneiRn.53968.

Genome annotation databases

EnsembliENSRNOT00000019023; ENSRNOP00000019021; ENSRNOG00000013704.
GeneIDi497840.
KEGGirno:497840.
UCSCiRGD:2395. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M12335
, M11710 , M12318 , M12319 , M12320 , M12321 , M12322 , M12323 , M12324 , M12325 , M12326 , M12327 , M12328 Genomic DNA. Translation: AAB59717.1 .
J02805 Genomic DNA. Translation: AAA40959.1 .
PIRi A28481. SYRTCA.
RefSeqi NP_058768.1. NM_017072.1.
UniGenei Rn.53968.

3D structure databases

ProteinModelPortali P07756.
SMRi P07756. Positions 1343-1478.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000019021.

Protein family/group databases

MEROPSi C26.951.

PTM databases

PhosphoSitei P07756.

Proteomic databases

PaxDbi P07756.
PRIDEi P07756.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000019023 ; ENSRNOP00000019021 ; ENSRNOG00000013704 .
GeneIDi 497840.
KEGGi rno:497840.
UCSCi RGD:2395. rat.

Organism-specific databases

CTDi 1373.
RGDi 2395. Cps1.

Phylogenomic databases

eggNOGi COG0458.
GeneTreei ENSGT00390000015604.
HOGENOMi HOG000234583.
HOVERGENi HBG000279.
InParanoidi P07756.
KOi K01948.
OMAi MDLGTKA.
OrthoDBi EOG7M6D6F.
PhylomeDBi P07756.

Enzyme and pathway databases

Reactomei REACT_216480. Urea cycle.
SABIO-RK P07756.

Miscellaneous databases

NextBioi 697797.
PROi P07756.

Gene expression databases

Genevestigatori P07756.

Family and domain databases

Gene3Di 1.10.1030.10. 1 hit.
3.30.1490.20. 2 hits.
3.30.470.20. 2 hits.
3.40.50.1380. 1 hit.
3.40.50.20. 2 hits.
3.40.50.880. 1 hit.
3.50.30.20. 1 hit.
HAMAPi MF_01209. CPSase_S_chain.
InterProi 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.
IPR017926. GATASE.
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.
[Graphical view ]
PRINTSi 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.
SSF52021. SSF52021. 1 hit.
SSF52317. SSF52317. 1 hit.
SSF52335. SSF52335. 1 hit.
SSF52440. SSF52440. 2 hits.
TIGRFAMsi TIGR01369. CPSaseII_lrg. 1 hit.
TIGR01368. CPSaseIIsmall. 1 hit.
PROSITEi PS50975. ATP_GRASP. 2 hits.
PS00866. CPSASE_1. 2 hits.
PS00867. CPSASE_2. 2 hits.
PS51273. GATASE_TYPE_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Characterization and derivation of the gene coding for mitochondrial carbamyl phosphate synthetase I of rat."
    Nyunoya H., Broglie K.E., Widgren E.E., Lusty C.J.
    J. Biol. Chem. 260:9346-9356(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  2. "Rat carbamyl-phosphate synthetase I gene. Promoter sequence and tissue-specific transcriptional regulation in vitro."
    Lagace M., Howell B.W., Burak R., Lusty C.J., Shore G.C.
    J. Biol. Chem. 262:10415-10418(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42.
  3. "Structural insight on the control of urea synthesis: identification of the binding site for N-acetyl-L-glutamate, the essential allosteric activator of mitochondrial carbamoyl phosphate synthetase."
    Pekkala S., Martinez A.I., Barcelona B., Gallego J., Bendala E., Yefimenko I., Rubio V., Cervera J.
    Biochem. J. 424:211-220(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, ALLOSTERIC ACTIVATOR NAG BINDING SITE, KINETIC PARAMETERS, MUTAGENESIS OF THR-1391; THR-1394; TRP-1410; ASN-1437 AND ASN-1440.
  4. "Discovery and confirmation of O-GlcNAcylated proteins in rat liver mitochondria by combination of mass spectrometry and immunological methods."
    Cao W., Cao J., Huang J., Yao J., Yan G., Xu H., Yang P.
    PLoS ONE 8:E76399-E76399(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT SER-537; SER-1331 AND THR-1332.

Entry informationi

Entry nameiCPSM_RAT
AccessioniPrimary (citable) accession number: P07756
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: September 3, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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