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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1391 – 13911Allosteric activatorBy similarity
Binding sitei1394 – 13941Allosteric activatorBy similarity
Binding sitei1410 – 14101Allosteric activatorBy similarity
Binding sitei1437 – 14371Allosteric activatorBy similarity
Binding sitei1440 – 14401Allosteric activatorBy similarity
Binding sitei1449 – 14491Allosteric activatorBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3838MitochondrionBy similarityAdd
BLAST
Chaini39 – 15001462Carbamoyl-phosphate synthase [ammonia], mitochondrialBy similarityPRO_0000029898Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441N6-acetyllysine; alternateCombined sources1 Publication
Modified residuei44 – 441N6-succinyllysine; alternateCombined sources1 Publication
Modified residuei55 – 551N6-acetyllysine; alternateCombined sources
Modified residuei55 – 551N6-glutaryllysine; alternateBy similarity
Modified residuei55 – 551N6-succinyllysine; alternateCombined sources
Modified residuei57 – 571N6-acetyllysine; alternateCombined sources
Modified residuei57 – 571N6-succinyllysine; alternateCombined sources
Modified residuei119 – 1191N6-acetyllysine; alternateCombined sources
Modified residuei119 – 1191N6-succinyllysine; alternateCombined sources
Modified residuei148 – 1481PhosphoserineCombined sources
Modified residuei157 – 1571N6-acetyllysine; alternateCombined sources
Modified residuei157 – 1571N6-succinyllysine; alternateCombined sources
Modified residuei171 – 1711N6-acetyllysine; alternateCombined sources
Modified residuei171 – 1711N6-glutaryllysine; alternateBy similarity
Modified residuei176 – 1761N6-glutaryllysineBy similarity
Modified residuei182 – 1821N6-acetyllysineCombined sources
Modified residuei189 – 1891PhosphoserineBy similarity
Modified residuei197 – 1971N6-acetyllysineCombined sources
Modified residuei207 – 2071N6-acetyllysine; alternateCombined sources
Modified residuei207 – 2071N6-glutaryllysine; alternateBy similarity
Modified residuei207 – 2071N6-succinyllysine; alternateCombined sources
Modified residuei210 – 2101N6-acetyllysine; alternateCombined sources
Modified residuei210 – 2101N6-glutaryllysine; alternateBy similarity
Modified residuei214 – 2141N6-acetyllysine; alternateCombined sources
Modified residuei214 – 2141N6-glutaryllysine; alternateBy similarity
Modified residuei214 – 2141N6-succinyllysine; alternateCombined sources
Modified residuei219 – 2191N6-acetyllysine; alternateCombined sources
Modified residuei219 – 2191N6-glutaryllysine; alternateBy similarity
Modified residuei228 – 2281N6-acetyllysine; alternateCombined sources
Modified residuei228 – 2281N6-glutaryllysine; alternateBy similarity
Modified residuei237 – 2371N6-glutaryllysineBy similarity
Modified residuei279 – 2791N6-acetyllysineCombined sources
Modified residuei280 – 2801N6-acetyllysine; alternateCombined sources
Modified residuei280 – 2801N6-glutaryllysine; alternateBy similarity
Modified residuei287 – 2871N6-acetyllysine; alternateCombined sources1 Publication
Modified residuei287 – 2871N6-succinyllysine; alternateCombined sources1 Publication
Modified residuei307 – 3071N6-acetyllysine; alternateCombined sources
Modified residuei307 – 3071N6-glutaryllysine; alternateBy similarity
Modified residuei307 – 3071N6-succinyllysine; alternateCombined sources
Modified residuei310 – 3101N6-acetyllysine; alternateCombined sources
Modified residuei310 – 3101N6-glutaryllysine; alternateBy similarity
Modified residuei400 – 4001N6-succinyllysineCombined sources
Modified residuei402 – 4021N6-glutaryllysine; alternateBy similarity
Modified residuei402 – 4021N6-succinyllysine; alternateCombined sources
Modified residuei412 – 4121N6-acetyllysine; alternateCombined sources
Modified residuei412 – 4121N6-glutaryllysine; alternateBy similarity
Modified residuei412 – 4121N6-succinyllysine; alternateCombined sources
Modified residuei453 – 4531N6-acetyllysine; alternateCombined sources
Modified residuei453 – 4531N6-glutaryllysine; alternateBy similarity
Modified residuei458 – 4581N6-acetyllysine; alternateCombined sources
Modified residuei458 – 4581N6-glutaryllysine; alternateBy similarity
Modified residuei458 – 4581N6-succinyllysine; alternateCombined sources
Modified residuei522 – 5221N6-acetyllysine; alternateCombined sources
Modified residuei522 – 5221N6-succinyllysine; alternateCombined sources
Modified residuei527 – 5271N6-acetyllysine; alternateCombined sources
Modified residuei527 – 5271N6-glutaryllysine; alternateBy similarity
Modified residuei527 – 5271N6-succinyllysine; alternateCombined sources
Modified residuei532 – 5321N6-acetyllysine; alternateCombined sources
Modified residuei532 – 5321N6-glutaryllysine; alternateBy similarity
Modified residuei537 – 5371Phosphoserine; alternateCombined sources
Glycosylationi537 – 5371O-linked (GlcNAc); alternateBy similarity
Modified residuei540 – 5401PhosphoserineBy similarity
Modified residuei553 – 5531N6-acetyllysine; alternateCombined sources
Modified residuei553 – 5531N6-glutaryllysine; alternateBy similarity
Modified residuei553 – 5531N6-succinyllysine; alternateCombined sources
Modified residuei560 – 5601N6-acetyllysine; alternateCombined sources
Modified residuei560 – 5601N6-succinyllysine; alternateCombined sources
Modified residuei569 – 5691PhosphoserineBy similarity
Modified residuei575 – 5751N6-acetyllysine; alternateCombined sources
Modified residuei575 – 5751N6-succinyllysine; alternateCombined sources
Modified residuei603 – 6031N6-acetyllysine; alternateCombined sources
Modified residuei603 – 6031N6-succinyllysine; alternateCombined sources
Modified residuei612 – 6121N6-acetyllysine; alternateCombined sources
Modified residuei612 – 6121N6-succinyllysine; alternateCombined sources
Modified residuei630 – 6301N6-acetyllysineCombined sources
Modified residuei728 – 7281N6-glutaryllysineBy similarity
Modified residuei751 – 7511N6-acetyllysine; alternateCombined sources
Modified residuei751 – 7511N6-succinyllysine; alternateCombined sources
Modified residuei757 – 7571N6-acetyllysine; alternateCombined sources
Modified residuei757 – 7571N6-glutaryllysine; alternateBy similarity
Modified residuei757 – 7571N6-succinyllysine; alternateCombined sources
Modified residuei772 – 7721N6-acetyllysine; alternateCombined sources
Modified residuei772 – 7721N6-glutaryllysine; alternateBy similarity
Modified residuei793 – 7931N6-acetyllysine; alternateCombined sources
Modified residuei793 – 7931N6-glutaryllysine; alternateBy similarity
Modified residuei793 – 7931N6-succinyllysine; alternateCombined sources
Modified residuei811 – 8111N6-acetyllysine; alternateCombined sources
Modified residuei811 – 8111N6-glutaryllysine; alternateBy similarity
Modified residuei831 – 8311N6-acetyllysine; alternateCombined sources
Modified residuei831 – 8311N6-succinyllysine; alternateCombined sources
Modified residuei840 – 8401N6-acetyllysine; alternateCombined sources
Modified residuei840 – 8401N6-succinyllysine; alternateCombined sources
Modified residuei841 – 8411N6-acetyllysine; alternateCombined sources
Modified residuei841 – 8411N6-glutaryllysine; alternateBy similarity
Modified residuei856 – 8561N6-acetyllysine; alternateCombined sources
Modified residuei856 – 8561N6-glutaryllysine; alternateBy similarity
Modified residuei875 – 8751N6-acetyllysine; alternateCombined sources
Modified residuei875 – 8751N6-glutaryllysine; alternateBy similarity
Modified residuei875 – 8751N6-succinyllysine; alternateCombined sources
Modified residuei889 – 8891N6-acetyllysine; alternateCombined sources
Modified residuei889 – 8891N6-glutaryllysine; alternateBy similarity
Modified residuei889 – 8891N6-succinyllysine; alternateCombined sources
Modified residuei892 – 8921N6-acetyllysine; alternateCombined sources
Modified residuei892 – 8921N6-glutaryllysine; alternateBy similarity
Modified residuei892 – 8921N6-succinyllysine; alternateCombined sources
Modified residuei896 – 8961PhosphoserineBy similarity
Modified residuei898 – 8981PhosphoserineBy similarity
Modified residuei908 – 9081N6-acetyllysine; alternateCombined sources
Modified residuei908 – 9081N6-glutaryllysine; alternateBy similarity
Modified residuei915 – 9151N6-acetyllysine; alternateCombined sources
Modified residuei915 – 9151N6-glutaryllysine; alternateBy similarity
Modified residuei915 – 9151N6-succinyllysine; alternateCombined sources
Modified residuei919 – 9191N6-acetyllysine; alternateCombined sources
Modified residuei919 – 9191N6-glutaryllysine; alternateBy similarity
Modified residuei919 – 9191N6-succinyllysine; alternateCombined sources
Modified residuei935 – 9351N6-acetyllysineCombined sources
Modified residuei1036 – 10361PhosphoserineBy similarity
Modified residuei1074 – 10741N6-acetyllysine; alternateCombined sources
Modified residuei1074 – 10741N6-glutaryllysine; alternateBy similarity
Modified residuei1074 – 10741N6-succinyllysine; alternateCombined sources
Modified residuei1079 – 10791PhosphoserineCombined sources
Modified residuei1090 – 10901PhosphoserineBy similarity
Modified residuei1093 – 10931PhosphoserineBy similarity
Modified residuei1100 – 11001N6-acetyllysine; alternateCombined sources
Modified residuei1100 – 11001N6-succinyllysine; alternateCombined sources
Modified residuei1149 – 11491N6-succinyllysineCombined sources
Modified residuei1168 – 11681N6-acetyllysine; alternateCombined sources
Modified residuei1168 – 11681N6-glutaryllysine; alternateBy similarity
Modified residuei1168 – 11681N6-succinyllysine; alternateCombined sources
Modified residuei1183 – 11831N6-acetyllysine; alternateCombined sources
Modified residuei1183 – 11831N6-glutaryllysine; alternateBy similarity
Modified residuei1183 – 11831N6-succinyllysine; alternateCombined sources
Modified residuei1203 – 12031PhosphoserineBy similarity
Modified residuei1222 – 12221N6-acetyllysineCombined sources
Modified residuei1224 – 12241N6-glutaryllysineBy similarity
Modified residuei1232 – 12321N6-acetyllysine; alternateCombined sources
Modified residuei1232 – 12321N6-succinyllysine; alternateCombined sources
Modified residuei1269 – 12691N6-acetyllysine; alternateCombined sources
Modified residuei1269 – 12691N6-succinyllysine; alternateCombined sources
Modified residuei1291 – 12911N6-acetyllysine; alternateCombined sources2 Publications
Modified residuei1291 – 12911N6-succinyllysine; alternateCombined sources1 Publication
Glycosylationi1331 – 13311O-linked (GlcNAc)By similarity
Glycosylationi1332 – 13321O-linked (GlcNAc)By similarity
Modified residuei1356 – 13561N6-acetyllysine; alternateCombined sources
Modified residuei1356 – 13561N6-glutaryllysine; alternateBy similarity
Modified residuei1356 – 13561N6-succinyllysine; alternateCombined sources
Modified residuei1360 – 13601N6-glutaryllysine; alternateBy similarity
Modified residuei1360 – 13601N6-succinyllysine; alternateCombined sources
Modified residuei1419 – 14191PhosphoserineBy similarity
Modified residuei1431 – 14311PhosphoserineBy similarity
Modified residuei1444 – 14441N6-acetyllysine; alternateCombined sources
Modified residuei1444 – 14441N6-succinyllysine; alternateCombined sources
Modified residuei1471 – 14711N6-acetyllysine; alternateCombined sources
Modified residuei1471 – 14711N6-succinyllysine; alternateCombined sources
Modified residuei1479 – 14791N6-acetyllysine; alternateCombined sources
Modified residuei1479 – 14791N6-glutaryllysine; alternateBy similarity
Modified residuei1479 – 14791N6-succinyllysine; alternateCombined sources
Modified residuei1486 – 14861N6-acetyllysine; alternateCombined sources
Modified residuei1486 – 14861N6-glutaryllysine; alternateBy similarity
Modified residuei1486 – 14861N6-succinyllysine; alternateCombined sources

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.
PhosphoSiteiQ8C196.
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

IntActiQ8C196. 5 interactions.
MINTiMINT-1856511.
STRINGi10090.ENSMUSP00000027144.

Structurei

3D structure databases

ProteinModelPortaliQ8C196.
SMRiQ8C196. Positions 1343-1478.
ModBaseiSearch...
MobiDBiSearch...

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 homologAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti931 – 9344LRLK → HASE in AAH67211 (PubMed:15489334).Curated

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. Positions 1343-1478.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8C196. 5 interactions.
MINTiMINT-1856511.
STRINGi10090.ENSMUSP00000027144.

PTM databases

iPTMnetiQ8C196.
PhosphoSiteiQ8C196.
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]
ProtoNetiSearch...

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: September 7, 2016
This is version 125 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.