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Protein

Carbamoyl-phosphate synthase [ammonia], mitochondrial

Gene

Cps1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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.1 Publication

Catalytic activityi

2 ATP + NH3 + HCO3- = 2 ADP + phosphate + carbamoyl phosphate.By similarity

Enzyme regulationi

Requires N-acetyl-L-glutamate (NAG) as an allosteric activator.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei1391Allosteric activatorBy similarity1
Binding sitei1394Allosteric activatorBy similarity1
Binding sitei1410Allosteric activatorBy similarity1
Binding sitei1437Allosteric activatorBy similarity1
Binding sitei1440Allosteric activatorBy similarity1
Binding sitei1449Allosteric activatorBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Urea cycle

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi6.3.4.16. 3474.
ReactomeiR-MMU-70635. Urea cycle.
SABIO-RKQ8C196.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:891996. Cps1.

Subcellular locationi

  • Mitochondrion By similarity
  • Nucleusnucleolus By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 38MitochondrionBy similarityAdd BLAST38
ChainiPRO_000002989839 – 1500Carbamoyl-phosphate synthase [ammonia], mitochondrialBy similarityAdd BLAST1462

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei44N6-acetyllysine; alternateCombined sources1 Publication1
Modified residuei44N6-succinyllysine; alternateCombined sources1 Publication1
Modified residuei55N6-acetyllysine; alternateCombined sources1
Modified residuei55N6-glutaryllysine; alternateBy similarity1
Modified residuei55N6-succinyllysine; alternateCombined sources1
Modified residuei57N6-acetyllysine; alternateCombined sources1
Modified residuei57N6-succinyllysine; alternateCombined sources1
Modified residuei119N6-acetyllysine; alternateCombined sources1
Modified residuei119N6-succinyllysine; alternateCombined sources1
Modified residuei148PhosphoserineCombined sources1
Modified residuei157N6-acetyllysine; alternateCombined sources1
Modified residuei157N6-succinyllysine; alternateCombined sources1
Modified residuei171N6-acetyllysine; alternateCombined sources1
Modified residuei171N6-glutaryllysine; alternateBy similarity1
Modified residuei176N6-glutaryllysineBy similarity1
Modified residuei182N6-acetyllysineCombined sources1
Modified residuei189PhosphoserineBy similarity1
Modified residuei197N6-acetyllysineCombined sources1
Modified residuei207N6-acetyllysine; alternateCombined sources1
Modified residuei207N6-glutaryllysine; alternateBy similarity1
Modified residuei207N6-succinyllysine; alternateCombined sources1
Modified residuei210N6-acetyllysine; alternateCombined sources1
Modified residuei210N6-glutaryllysine; alternateBy similarity1
Modified residuei214N6-acetyllysine; alternateCombined sources1
Modified residuei214N6-glutaryllysine; alternateBy similarity1
Modified residuei214N6-succinyllysine; alternateCombined sources1
Modified residuei219N6-acetyllysine; alternateCombined sources1
Modified residuei219N6-glutaryllysine; alternateBy similarity1
Modified residuei228N6-acetyllysine; alternateCombined sources1
Modified residuei228N6-glutaryllysine; alternateBy similarity1
Modified residuei237N6-glutaryllysineBy similarity1
Modified residuei279N6-acetyllysineCombined sources1
Modified residuei280N6-acetyllysine; alternateCombined sources1
Modified residuei280N6-glutaryllysine; alternateBy similarity1
Modified residuei287N6-acetyllysine; alternateCombined sources1 Publication1
Modified residuei287N6-succinyllysine; alternateCombined sources1 Publication1
Modified residuei307N6-acetyllysine; alternateCombined sources1
Modified residuei307N6-glutaryllysine; alternateBy similarity1
Modified residuei307N6-succinyllysine; alternateCombined sources1
Modified residuei310N6-acetyllysine; alternateCombined sources1
Modified residuei310N6-glutaryllysine; alternateBy similarity1
Modified residuei400N6-succinyllysineCombined sources1
Modified residuei402N6-glutaryllysine; alternateBy similarity1
Modified residuei402N6-succinyllysine; alternateCombined sources1
Modified residuei412N6-acetyllysine; alternateCombined sources1
Modified residuei412N6-glutaryllysine; alternateBy similarity1
Modified residuei412N6-succinyllysine; alternateCombined sources1
Modified residuei453N6-acetyllysine; alternateCombined sources1
Modified residuei453N6-glutaryllysine; alternateBy similarity1
Modified residuei458N6-acetyllysine; alternateCombined sources1
Modified residuei458N6-glutaryllysine; alternateBy similarity1
Modified residuei458N6-succinyllysine; alternateCombined sources1
Modified residuei522N6-acetyllysine; alternateCombined sources1
Modified residuei522N6-succinyllysine; alternateCombined sources1
Modified residuei527N6-acetyllysine; alternateCombined sources1
Modified residuei527N6-glutaryllysine; alternateBy similarity1
Modified residuei527N6-succinyllysine; alternateCombined sources1
Modified residuei532N6-acetyllysine; alternateCombined sources1
Modified residuei532N6-glutaryllysine; alternateBy similarity1
Modified residuei537Phosphoserine; alternateCombined sources1
Glycosylationi537O-linked (GlcNAc); alternateBy similarity1
Modified residuei540PhosphoserineBy similarity1
Modified residuei553N6-acetyllysine; alternateCombined sources1
Modified residuei553N6-glutaryllysine; alternateBy similarity1
Modified residuei553N6-succinyllysine; alternateCombined sources1
Modified residuei560N6-acetyllysine; alternateCombined sources1
Modified residuei560N6-succinyllysine; alternateCombined sources1
Modified residuei569PhosphoserineBy similarity1
Modified residuei575N6-acetyllysine; alternateCombined sources1
Modified residuei575N6-succinyllysine; alternateCombined sources1
Modified residuei603N6-acetyllysine; alternateCombined sources1
Modified residuei603N6-succinyllysine; alternateCombined sources1
Modified residuei612N6-acetyllysine; alternateCombined sources1
Modified residuei612N6-succinyllysine; alternateCombined sources1
Modified residuei630N6-acetyllysineCombined sources1
Modified residuei728N6-glutaryllysineBy similarity1
Modified residuei751N6-acetyllysine; alternateCombined sources1
Modified residuei751N6-succinyllysine; alternateCombined sources1
Modified residuei757N6-acetyllysine; alternateCombined sources1
Modified residuei757N6-glutaryllysine; alternateBy similarity1
Modified residuei757N6-succinyllysine; alternateCombined sources1
Modified residuei772N6-acetyllysine; alternateCombined sources1
Modified residuei772N6-glutaryllysine; alternateBy similarity1
Modified residuei793N6-acetyllysine; alternateCombined sources1
Modified residuei793N6-glutaryllysine; alternateBy similarity1
Modified residuei793N6-succinyllysine; alternateCombined sources1
Modified residuei811N6-acetyllysine; alternateCombined sources1
Modified residuei811N6-glutaryllysine; alternateBy similarity1
Modified residuei831N6-acetyllysine; alternateCombined sources1
Modified residuei831N6-succinyllysine; alternateCombined sources1
Modified residuei840N6-acetyllysine; alternateCombined sources1
Modified residuei840N6-succinyllysine; alternateCombined sources1
Modified residuei841N6-acetyllysine; alternateCombined sources1
Modified residuei841N6-glutaryllysine; alternateBy similarity1
Modified residuei856N6-acetyllysine; alternateCombined sources1
Modified residuei856N6-glutaryllysine; alternateBy similarity1
Modified residuei875N6-acetyllysine; alternateCombined sources1
Modified residuei875N6-glutaryllysine; alternateBy similarity1
Modified residuei875N6-succinyllysine; alternateCombined sources1
Modified residuei889N6-acetyllysine; alternateCombined sources1
Modified residuei889N6-glutaryllysine; alternateBy similarity1
Modified residuei889N6-succinyllysine; alternateCombined sources1
Modified residuei892N6-acetyllysine; alternateCombined sources1
Modified residuei892N6-glutaryllysine; alternateBy similarity1
Modified residuei892N6-succinyllysine; alternateCombined sources1
Modified residuei896PhosphoserineBy similarity1
Modified residuei898PhosphoserineBy similarity1
Modified residuei908N6-acetyllysine; alternateCombined sources1
Modified residuei908N6-glutaryllysine; alternateBy similarity1
Modified residuei915N6-acetyllysine; alternateCombined sources1
Modified residuei915N6-glutaryllysine; alternateBy similarity1
Modified residuei915N6-succinyllysine; alternateCombined sources1
Modified residuei919N6-acetyllysine; alternateCombined sources1
Modified residuei919N6-glutaryllysine; alternateBy similarity1
Modified residuei919N6-succinyllysine; alternateCombined sources1
Modified residuei935N6-acetyllysineCombined sources1
Modified residuei1036PhosphoserineBy similarity1
Modified residuei1074N6-acetyllysine; alternateCombined sources1
Modified residuei1074N6-glutaryllysine; alternateBy similarity1
Modified residuei1074N6-succinyllysine; alternateCombined sources1
Modified residuei1079PhosphoserineCombined sources1
Modified residuei1090PhosphoserineBy similarity1
Modified residuei1093PhosphoserineBy similarity1
Modified residuei1100N6-acetyllysine; alternateCombined sources1
Modified residuei1100N6-succinyllysine; alternateCombined sources1
Modified residuei1149N6-succinyllysineCombined sources1
Modified residuei1168N6-acetyllysine; alternateCombined sources1
Modified residuei1168N6-glutaryllysine; alternateBy similarity1
Modified residuei1168N6-succinyllysine; alternateCombined sources1
Modified residuei1183N6-acetyllysine; alternateCombined sources1
Modified residuei1183N6-glutaryllysine; alternateBy similarity1
Modified residuei1183N6-succinyllysine; alternateCombined sources1
Modified residuei1203PhosphoserineBy similarity1
Modified residuei1222N6-acetyllysineCombined sources1
Modified residuei1224N6-glutaryllysineBy similarity1
Modified residuei1232N6-acetyllysine; alternateCombined sources1
Modified residuei1232N6-succinyllysine; alternateCombined sources1
Modified residuei1269N6-acetyllysine; alternateCombined sources1
Modified residuei1269N6-succinyllysine; alternateCombined sources1
Modified residuei1291N6-acetyllysine; alternateCombined sources2 Publications1
Modified residuei1291N6-succinyllysine; alternateCombined sources1 Publication1
Glycosylationi1331O-linked (GlcNAc)By similarity1
Glycosylationi1332O-linked (GlcNAc)By similarity1
Modified residuei1356N6-acetyllysine; alternateCombined sources1
Modified residuei1356N6-glutaryllysine; alternateBy similarity1
Modified residuei1356N6-succinyllysine; alternateCombined sources1
Modified residuei1360N6-glutaryllysine; alternateBy similarity1
Modified residuei1360N6-succinyllysine; alternateCombined sources1
Modified residuei1419PhosphoserineBy similarity1
Modified residuei1431PhosphoserineBy similarity1
Modified residuei1444N6-acetyllysine; alternateCombined sources1
Modified residuei1444N6-succinyllysine; alternateCombined sources1
Modified residuei1471N6-acetyllysine; alternateCombined sources1
Modified residuei1471N6-succinyllysine; alternateCombined sources1
Modified residuei1479N6-acetyllysine; alternateCombined sources1
Modified residuei1479N6-glutaryllysine; alternateBy similarity1
Modified residuei1479N6-succinyllysine; alternateCombined sources1
Modified residuei1486N6-acetyllysine; alternateCombined sources1
Modified residuei1486N6-glutaryllysine; alternateBy similarity1
Modified residuei1486N6-succinyllysine; alternateCombined sources1

Post-translational modificationi

Undergoes proteolytic cleavage in the C-terminal region corresponding to the loss of approximately 12 AA residues from the C-terminus.By similarity
Acetylation of Lys-287, Lys-603, Lys-841 and Lys-1291 is observed in liver mitochondria from fasted mice but not from fed mice.2 Publications
Succinylated at Lys-44, Lys-287 and Lys-1291. Desuccinylated at Lys-1291 by SIRT5, leading to activation.1 Publication
Glutarylated. Glutarylation levels increase during fasting. Deglutarylated by SIRT5 at Lys-55, Lys-219, Lys-412, Lys-889, Lys-892, Lys-915, Lys-1360 and Lys-1486, leading to activation.By similarity1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ8C196.
PaxDbiQ8C196.
PeptideAtlasiQ8C196.
PRIDEiQ8C196.

PTM databases

iPTMnetiQ8C196.
PhosphoSitePlusiQ8C196.
SwissPalmiQ8C196.

Expressioni

Gene expression databases

BgeeiENSMUSG00000025991.
CleanExiMM_CPS1.
GenevisibleiQ8C196. MM.

Interactioni

Subunit structurei

Can form homooligomers (monomers as predominant form and dimers).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Sirt5Q8K2C62EBI-2348828,EBI-2348809

Protein-protein interaction databases

BioGridi230602. 1 interactor.
IntActiQ8C196. 5 interactors.
MINTiMINT-1856511.
STRINGi10090.ENSMUSP00000027144.

Structurei

3D structure databases

ProteinModelPortaliQ8C196.
SMRiQ8C196.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini219 – 404Glutamine amidotransferase type-1Add BLAST186
Domaini551 – 743ATP-grasp 1Add BLAST193
Domaini1093 – 1284ATP-grasp 2Add BLAST192

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni39 – 218Anthranilate phosphoribosyltransferase homologAdd BLAST180

Domaini

The type-1 glutamine amidotransferase domain is defective.By similarity

Sequence similaritiesi

Contains 2 ATP-grasp domains.Curated

Keywords - Domaini

Repeat, Transit peptide

Phylogenomic databases

eggNOGiKOG0370. Eukaryota.
COG0458. LUCA.
COG0505. LUCA.
GeneTreeiENSGT00390000015604.
HOGENOMiHOG000234583.
HOVERGENiHBG000279.
InParanoidiQ8C196.
KOiK01948.
OMAiMPWSRFR.
OrthoDBiEOG091G00DC.
PhylomeDBiQ8C196.
TreeFamiTF331485.

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. 1 hit.
InterProiIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006275. CarbamoylP_synth_lsu.
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]
PfamiPF02786. 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.

Q8C196-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRILTACKV VKTLKSGFGF ANVTTKRQWD FSRPGIRLLS VKAKTAHIVL
60 70 80 90 100
EDGTKMKGYS FGHPSSVAGE VVFNTGLGGY PEALTDPAYK GQILTMANPI
110 120 130 140 150
IGNGGAPDTT ARDELGLNKY MESDGIKVAG LLVLNYSNDY NHWLATKSLG
160 170 180 190 200
QWLQEEKVPA IYGVDTRMLT KIIRDKGTML GKIEFEGQSV DFVDPNKQNL
210 220 230 240 250
IAEVSTKDVK VFGKGNPTKV VAVDCGIKNN VIRLLVKRGA EVHLVPWNHD
260 270 280 290 300
FTQMEYDGLL IAGGPGNPAL AQPLIQNVKK ILESDRKEPL FGISTGNIIT
310 320 330 340 350
GLAAGAKSYK MSMANRGQNQ PVLNITNRQA FITAQNHGYA LDNTLPAGWK
360 370 380 390 400
PLFVNVNDQT NEGIMHESKP FFAVQFHPEV SPGPTDTEYL FDSFFSLIKK
410 420 430 440 450
GKGTTITSVL PKPALVASRV EVSKVLILGS GGLSIGQAGE FDYSGSQAVK
460 470 480 490 500
AMKEENVKTV LMNPNIASVQ TNEVGLKQAD AVYFLPITPQ FVTEVIKAER
510 520 530 540 550
PDGLILGMGG QTALNCGVEL FKRGVLKEYG VKVLGTSVES IMATEDRQLF
560 570 580 590 600
SDKLNEINEK IAPSFAVESM EDALKAADTI GYPVMIRSAY ALGGLGSGIC
610 620 630 640 650
PNKETLIDLG TKAFAMTNQI LVERSVTGWK EIEYEVVRDA DDNCVTVCNM
660 670 680 690 700
ENVDAMGVHT GDSVVVAPAQ TLSNAEFQML RRTSVNVVRH LGIVGECNIQ
710 720 730 740 750
FALHPTSMEY CIIEVNARLS RSSALASKAT GYPLAFIAAK IALGIPLPEI
760 770 780 790 800
KNVVSGKTSA CFEPSLDYMV TKIPRWDLDR FHGTSSRIGS SMKSVGEVMA
810 820 830 840 850
IGRTFEESFQ KALRMCHPSV DGFTPRLPMN KEWPANLDLK KELSEPSSTR
860 870 880 890 900
IYAIAKALEN NMSLDEIVRL TSIDKWFLYK MRDILNMDKT LKGLNSDSVT
910 920 930 940 950
EETLRKAKEI GFSDKQISKC LGLTEAQTRE LRLKKNIHPW VKQIDTLAAE
960 970 980 990 1000
YPSVTNYLYV TYNGQEHDIK FDEHGIMVLG CGPYHIGSSV EFDWCAVSSI
1010 1020 1030 1040 1050
RTLRQLGKKT VVVNCNPETV STDFDECDKL YFEELSLERI LDIYHQEACN
1060 1070 1080 1090 1100
GCIISVGGQI PNNLAVPLYK NGVKIMGTSP LQIDRAEDRS IFSAVLDELK
1110 1120 1130 1140 1150
VAQAPWKAVN TLNEALEFAN SVGYPCLLRP SYVLSGSAMN VVFSEDEMKR
1160 1170 1180 1190 1200
FLEEATRVSQ EHPVVLTKFV EGAREVEMDA VGKEGRVISH AISEHVEDAG
1210 1220 1230 1240 1250
VHSGDATLML PTQTISQGAI EKVKDATRKI AKAFAISGPF NVQFLVKGND
1260 1270 1280 1290 1300
VLVIECNLRA SRSFPFVSKT LGVDFIDVAT KVMIGESIDE KRLPTLEQPI
1310 1320 1330 1340 1350
IPSDYVAIKA PMFSWPRLRD ADPILRCEMA STGEVACFGE GIHTAFLKAM
1360 1370 1380 1390 1400
LSTGFKIPQK GILIGIQQSF RPRFLGVAEQ LHNEGFKLFA TEATSDWLNA
1410 1420 1430 1440 1450
NNVPATPVAW PSQEGQNPSL SSIRKLIRDG SIDLVINLPN NNTKFVHDNY
1460 1470 1480 1490 1500
VIRRTAVDSG IALLTNFQVT KLFAEAVQKS RTVDSKSLFH YRQYSAGKAA
Length:1,500
Mass (Da):164,618
Last modified:August 30, 2005 - v2
Checksum:i84A7268C1D7E8101
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti931 – 934LRLK → HASE in AAH67211 (PubMed:15489334).Curated4

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC101854 Genomic DNA. No translation available.
AC133187 Genomic DNA. No translation available.
BC067211 mRNA. Translation: AAH67211.1.
BC126969 mRNA. Translation: AAI26970.1.
AK028683 mRNA. Translation: BAC26064.1.
CCDSiCCDS35605.1.
RefSeqiNP_001074278.1. NM_001080809.2.
XP_011236802.1. XM_011238500.1.
UniGeneiMm.343942.

Genome annotation databases

EnsembliENSMUST00000027144; ENSMUSP00000027144; ENSMUSG00000025991.
GeneIDi227231.
KEGGimmu:227231.
UCSCiuc007biy.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC101854 Genomic DNA. No translation available.
AC133187 Genomic DNA. No translation available.
BC067211 mRNA. Translation: AAH67211.1.
BC126969 mRNA. Translation: AAI26970.1.
AK028683 mRNA. Translation: BAC26064.1.
CCDSiCCDS35605.1.
RefSeqiNP_001074278.1. NM_001080809.2.
XP_011236802.1. XM_011238500.1.
UniGeneiMm.343942.

3D structure databases

ProteinModelPortaliQ8C196.
SMRiQ8C196.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230602. 1 interactor.
IntActiQ8C196. 5 interactors.
MINTiMINT-1856511.
STRINGi10090.ENSMUSP00000027144.

PTM databases

iPTMnetiQ8C196.
PhosphoSitePlusiQ8C196.
SwissPalmiQ8C196.

Proteomic databases

MaxQBiQ8C196.
PaxDbiQ8C196.
PeptideAtlasiQ8C196.
PRIDEiQ8C196.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027144; ENSMUSP00000027144; ENSMUSG00000025991.
GeneIDi227231.
KEGGimmu:227231.
UCSCiuc007biy.2. mouse.

Organism-specific databases

CTDi1373.
MGIiMGI:891996. Cps1.

Phylogenomic databases

eggNOGiKOG0370. Eukaryota.
COG0458. LUCA.
COG0505. LUCA.
GeneTreeiENSGT00390000015604.
HOGENOMiHOG000234583.
HOVERGENiHBG000279.
InParanoidiQ8C196.
KOiK01948.
OMAiMPWSRFR.
OrthoDBiEOG091G00DC.
PhylomeDBiQ8C196.
TreeFamiTF331485.

Enzyme and pathway databases

BRENDAi6.3.4.16. 3474.
ReactomeiR-MMU-70635. Urea cycle.
SABIO-RKQ8C196.

Miscellaneous databases

PROiQ8C196.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000025991.
CleanExiMM_CPS1.
GenevisibleiQ8C196. MM.

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. 1 hit.
InterProiIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006275. CarbamoylP_synth_lsu.
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]
PfamiPF02786. 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]
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Entry informationi

Entry nameiCPSM_MOUSE
AccessioniPrimary (citable) accession number: Q8C196
Secondary accession number(s): A0JNU4, Q6NX75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: August 30, 2005
Last modified: November 2, 2016
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Was initially reported to be deacetylated by Sirt5 (PubMed:19410549). However, it was later shown that Sirt5 has poor deacetylase activity and mediates desuccinylation of Cps1 instead (PubMed:22076378).2 Publications

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.