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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 + CO2 + H2O = 2 ADP + phosphate + carbamoyl phosphate.

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.
ReactomeiREACT_315699. 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
ProteomesiUP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:891996. Cps1.

Subcellular locationi

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; alternate2 Publications
Modified residuei44 – 441N6-succinyllysine; alternate2 Publications
Modified residuei55 – 551N6-acetyllysine; alternate1 Publication
Modified residuei55 – 551N6-glutaryllysineBy similarity
Modified residuei55 – 551N6-succinyllysine; alternate1 Publication
Modified residuei57 – 571N6-acetyllysine; alternate1 Publication
Modified residuei57 – 571N6-succinyllysine; alternate1 Publication
Modified residuei119 – 1191N6-acetyllysine; alternate1 Publication
Modified residuei119 – 1191N6-succinyllysine; alternate1 Publication
Modified residuei148 – 1481PhosphoserineBy similarity
Modified residuei157 – 1571N6-acetyllysine; alternate1 Publication
Modified residuei157 – 1571N6-succinyllysine; alternate1 Publication
Modified residuei171 – 1711N6-acetyllysine1 Publication
Modified residuei171 – 1711N6-glutaryllysineBy similarity
Modified residuei176 – 1761N6-glutaryllysineBy similarity
Modified residuei182 – 1821N6-acetyllysine1 Publication
Modified residuei197 – 1971N6-acetyllysine1 Publication
Modified residuei207 – 2071N6-acetyllysine; alternate1 Publication
Modified residuei207 – 2071N6-glutaryllysineBy similarity
Modified residuei207 – 2071N6-succinyllysine; alternate1 Publication
Modified residuei210 – 2101N6-acetyllysine1 Publication
Modified residuei210 – 2101N6-glutaryllysineBy similarity
Modified residuei214 – 2141N6-acetyllysine; alternate1 Publication
Modified residuei214 – 2141N6-glutaryllysineBy similarity
Modified residuei214 – 2141N6-succinyllysine; alternate1 Publication
Modified residuei219 – 2191N6-acetyllysine1 Publication
Modified residuei219 – 2191N6-glutaryllysineBy similarity
Modified residuei228 – 2281N6-acetyllysine1 Publication
Modified residuei228 – 2281N6-glutaryllysineBy similarity
Modified residuei237 – 2371N6-glutaryllysineBy similarity
Modified residuei279 – 2791N6-acetyllysine1 Publication
Modified residuei280 – 2801N6-acetyllysine1 Publication
Modified residuei280 – 2801N6-glutaryllysineBy similarity
Modified residuei287 – 2871N6-acetyllysine; alternate2 Publications
Modified residuei287 – 2871N6-succinyllysine; alternate2 Publications
Modified residuei307 – 3071N6-acetyllysine; alternate1 Publication
Modified residuei307 – 3071N6-glutaryllysineBy similarity
Modified residuei307 – 3071N6-succinyllysine; alternate1 Publication
Modified residuei310 – 3101N6-acetyllysine1 Publication
Modified residuei310 – 3101N6-glutaryllysineBy similarity
Modified residuei400 – 4001N6-succinyllysine1 Publication
Modified residuei402 – 4021N6-glutaryllysineBy similarity
Modified residuei402 – 4021N6-succinyllysine1 Publication
Modified residuei412 – 4121N6-acetyllysine; alternate1 Publication
Modified residuei412 – 4121N6-glutaryllysineBy similarity
Modified residuei412 – 4121N6-succinyllysine; alternate1 Publication
Modified residuei453 – 4531N6-acetyllysine1 Publication
Modified residuei453 – 4531N6-glutaryllysineBy similarity
Modified residuei458 – 4581N6-acetyllysine; alternate1 Publication
Modified residuei458 – 4581N6-glutaryllysineBy similarity
Modified residuei458 – 4581N6-succinyllysine; alternate1 Publication
Modified residuei522 – 5221N6-acetyllysine; alternate1 Publication
Modified residuei522 – 5221N6-succinyllysine; alternate1 Publication
Modified residuei527 – 5271N6-acetyllysine; alternate1 Publication
Modified residuei527 – 5271N6-glutaryllysineBy similarity
Modified residuei527 – 5271N6-succinyllysine; alternate1 Publication
Modified residuei532 – 5321N6-acetyllysine1 Publication
Modified residuei532 – 5321N6-glutaryllysineBy similarity
Modified residuei537 – 5371Phosphoserine; alternate1 Publication
Glycosylationi537 – 5371O-linked (GlcNAc); alternateBy similarity
Modified residuei553 – 5531N6-acetyllysine; alternate1 Publication
Modified residuei553 – 5531N6-glutaryllysineBy similarity
Modified residuei553 – 5531N6-succinyllysine; alternate1 Publication
Modified residuei560 – 5601N6-acetyllysine; alternate1 Publication
Modified residuei560 – 5601N6-succinyllysine; alternate1 Publication
Modified residuei569 – 5691PhosphoserineBy similarity
Modified residuei575 – 5751N6-acetyllysine; alternate1 Publication
Modified residuei575 – 5751N6-succinyllysine; alternate1 Publication
Modified residuei603 – 6031N6-acetyllysine; alternate1 Publication
Modified residuei603 – 6031N6-succinyllysine; alternate1 Publication
Modified residuei612 – 6121N6-acetyllysine; alternate1 Publication
Modified residuei612 – 6121N6-succinyllysine; alternate1 Publication
Modified residuei630 – 6301N6-acetyllysine1 Publication
Modified residuei728 – 7281N6-glutaryllysineBy similarity
Modified residuei751 – 7511N6-acetyllysine; alternate1 Publication
Modified residuei751 – 7511N6-succinyllysine; alternate1 Publication
Modified residuei757 – 7571N6-acetyllysine; alternate1 Publication
Modified residuei757 – 7571N6-glutaryllysineBy similarity
Modified residuei757 – 7571N6-succinyllysine; alternate1 Publication
Modified residuei772 – 7721N6-acetyllysine1 Publication
Modified residuei772 – 7721N6-glutaryllysineBy similarity
Modified residuei793 – 7931N6-acetyllysine; alternate1 Publication
Modified residuei793 – 7931N6-glutaryllysineBy similarity
Modified residuei793 – 7931N6-succinyllysine; alternate1 Publication
Modified residuei811 – 8111N6-acetyllysine1 Publication
Modified residuei811 – 8111N6-glutaryllysineBy similarity
Modified residuei831 – 8311N6-acetyllysine; alternate1 Publication
Modified residuei831 – 8311N6-succinyllysine; alternate1 Publication
Modified residuei840 – 8401N6-acetyllysine; alternate1 Publication
Modified residuei840 – 8401N6-succinyllysine; alternate1 Publication
Modified residuei841 – 8411N6-acetyllysine1 Publication
Modified residuei841 – 8411N6-glutaryllysineBy similarity
Modified residuei856 – 8561N6-acetyllysine1 Publication
Modified residuei856 – 8561N6-glutaryllysineBy similarity
Modified residuei875 – 8751N6-acetyllysine; alternate1 Publication
Modified residuei875 – 8751N6-glutaryllysineBy similarity
Modified residuei875 – 8751N6-succinyllysine; alternate1 Publication
Modified residuei889 – 8891N6-acetyllysine; alternate1 Publication
Modified residuei889 – 8891N6-glutaryllysineBy similarity
Modified residuei889 – 8891N6-succinyllysine; alternate1 Publication
Modified residuei892 – 8921N6-acetyllysine; alternate1 Publication
Modified residuei892 – 8921N6-glutaryllysineBy similarity
Modified residuei892 – 8921N6-succinyllysine; alternate1 Publication
Modified residuei908 – 9081N6-acetyllysine1 Publication
Modified residuei908 – 9081N6-glutaryllysineBy similarity
Modified residuei915 – 9151N6-acetyllysine; alternate1 Publication
Modified residuei915 – 9151N6-glutaryllysineBy similarity
Modified residuei915 – 9151N6-succinyllysine; alternate1 Publication
Modified residuei919 – 9191N6-acetyllysine; alternate1 Publication
Modified residuei919 – 9191N6-glutaryllysineBy similarity
Modified residuei919 – 9191N6-succinyllysine; alternate1 Publication
Modified residuei935 – 9351N6-acetyllysine1 Publication
Modified residuei1074 – 10741N6-acetyllysine; alternate1 Publication
Modified residuei1074 – 10741N6-glutaryllysineBy similarity
Modified residuei1074 – 10741N6-succinyllysine; alternate1 Publication
Modified residuei1079 – 10791Phosphoserine1 Publication
Modified residuei1100 – 11001N6-acetyllysine; alternate1 Publication
Modified residuei1100 – 11001N6-succinyllysine; alternate1 Publication
Modified residuei1149 – 11491N6-succinyllysine1 Publication
Modified residuei1168 – 11681N6-acetyllysine; alternate1 Publication
Modified residuei1168 – 11681N6-glutaryllysineBy similarity
Modified residuei1168 – 11681N6-succinyllysine; alternate1 Publication
Modified residuei1183 – 11831N6-acetyllysine; alternate1 Publication
Modified residuei1183 – 11831N6-glutaryllysineBy similarity
Modified residuei1183 – 11831N6-succinyllysine; alternate1 Publication
Modified residuei1203 – 12031PhosphoserineBy similarity
Modified residuei1222 – 12221N6-acetyllysine1 Publication
Modified residuei1224 – 12241N6-glutaryllysineBy similarity
Modified residuei1232 – 12321N6-acetyllysine; alternate1 Publication
Modified residuei1232 – 12321N6-succinyllysine; alternate1 Publication
Modified residuei1269 – 12691N6-acetyllysine; alternate1 Publication
Modified residuei1269 – 12691N6-succinyllysine; alternate1 Publication
Modified residuei1291 – 12911N6-acetyllysine; alternate3 Publications
Modified residuei1291 – 12911N6-succinyllysine; alternate2 Publications
Glycosylationi1331 – 13311O-linked (GlcNAc)By similarity
Glycosylationi1332 – 13321O-linked (GlcNAc)By similarity
Modified residuei1356 – 13561N6-acetyllysine; alternate1 Publication
Modified residuei1356 – 13561N6-glutaryllysineBy similarity
Modified residuei1356 – 13561N6-succinyllysine; alternate1 Publication
Modified residuei1360 – 13601N6-glutaryllysineBy similarity
Modified residuei1360 – 13601N6-succinyllysine1 Publication
Modified residuei1419 – 14191PhosphoserineBy similarity
Modified residuei1431 – 14311PhosphoserineBy similarity
Modified residuei1444 – 14441N6-acetyllysine; alternate1 Publication
Modified residuei1444 – 14441N6-succinyllysine; alternate1 Publication
Modified residuei1471 – 14711N6-acetyllysine; alternate1 Publication
Modified residuei1471 – 14711N6-succinyllysine; alternate1 Publication
Modified residuei1479 – 14791N6-acetyllysine; alternate1 Publication
Modified residuei1479 – 14791N6-glutaryllysineBy similarity
Modified residuei1479 – 14791N6-succinyllysine; alternate1 Publication
Modified residuei1486 – 14861N6-acetyllysine; alternate1 Publication
Modified residuei1486 – 14861N6-glutaryllysineBy similarity
Modified residuei1486 – 14861N6-succinyllysine; alternate1 Publication

Post-translational modificationi

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.
PRIDEiQ8C196.

PTM databases

PhosphoSiteiQ8C196.

Expressioni

Gene expression databases

BgeeiQ8C196.
CleanExiMM_CPS1.
ExpressionAtlasiQ8C196. baseline and differential.
GenevisibleiQ8C196. MM.

Interactioni

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

eggNOGiCOG0458.
GeneTreeiENSGT00390000015604.
HOGENOMiHOG000234583.
HOVERGENiHBG000279.
InParanoidiQ8C196.
KOiK01948.
OMAiQFIEFEG.
OrthoDBiEOG7M6D6F.
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.
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.

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.
UniGeneiMm.343942.

Genome annotation databases

EnsembliENSMUST00000027144; ENSMUSP00000027144; ENSMUSG00000025991.
GeneIDi227231.
KEGGimmu:227231.
UCSCiuc007biy.1. 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.
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

PhosphoSiteiQ8C196.

Proteomic databases

MaxQBiQ8C196.
PaxDbiQ8C196.
PRIDEiQ8C196.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027144; ENSMUSP00000027144; ENSMUSG00000025991.
GeneIDi227231.
KEGGimmu:227231.
UCSCiuc007biy.1. mouse.

Organism-specific databases

CTDi1373.
MGIiMGI:891996. Cps1.

Phylogenomic databases

eggNOGiCOG0458.
GeneTreeiENSGT00390000015604.
HOGENOMiHOG000234583.
HOVERGENiHBG000279.
InParanoidiQ8C196.
KOiK01948.
OMAiQFIEFEG.
OrthoDBiEOG7M6D6F.
PhylomeDBiQ8C196.
TreeFamiTF331485.

Enzyme and pathway databases

BRENDAi6.3.4.16. 3474.
ReactomeiREACT_315699. Urea cycle.
SABIO-RKQ8C196.

Miscellaneous databases

NextBioi378522.
PROiQ8C196.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C196.
CleanExiMM_CPS1.
ExpressionAtlasiQ8C196. baseline and differential.
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.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "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].
    Strain: FVB/N.
    Tissue: Liver.
  3. Bienvenut W.V.
    Submitted (JUL-2005) to UniProtKB
    Strain: C57BL/6.
    Tissue: Liver.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 753-1500.
    Strain: C57BL/6J.
    Tissue: Skin.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537 AND SER-1079, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "SIRT5 Deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle."
    Nakagawa T., Lomb D.J., Haigis M.C., Guarente L.
    Cell 137:560-570(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-1291, DEACETYLATION.
  7. "Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase."
    Du J., Zhou Y., Su X., Yu J.J., Khan S., Jiang H., Kim J., Woo J., Kim J.H., Choi B.H., He B., Chen W., Zhang S., Cerione R.A., Auwerx J., Hao Q., Lin H.
    Science 334:806-809(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-44; LYS-287 AND LYS-1291, SUCCINYLATION AT LYS-44; LYS-287 AND LYS-1291, DESUCCINYLATION BY SIRT5.
  8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-44; LYS-55; LYS-57; LYS-119; LYS-157; LYS-207; LYS-214; LYS-287; LYS-307; LYS-400; LYS-402; LYS-412; LYS-458; LYS-522; LYS-527; LYS-553; LYS-560; LYS-575; LYS-603; LYS-612; LYS-751; LYS-757; LYS-793; LYS-831; LYS-840; LYS-875; LYS-889; LYS-892; LYS-915; LYS-919; LYS-1074; LYS-1100; LYS-1149; LYS-1168; LYS-1183; LYS-1232; LYS-1269; LYS-1291; LYS-1356; LYS-1360; LYS-1444; LYS-1471; LYS-1479 AND LYS-1486, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-44; LYS-55; LYS-57; LYS-119; LYS-157; LYS-171; LYS-182; LYS-197; LYS-207; LYS-210; LYS-214; LYS-219; LYS-228; LYS-279; LYS-280; LYS-287; LYS-307; LYS-310; LYS-412; LYS-453; LYS-458; LYS-522; LYS-527; LYS-532; LYS-553; LYS-560; LYS-575; LYS-603; LYS-612; LYS-630; LYS-751; LYS-757; LYS-772; LYS-793; LYS-811; LYS-831; LYS-840; LYS-841; LYS-856; LYS-875; LYS-889; LYS-892; LYS-908; LYS-915; LYS-919; LYS-935; LYS-1074; LYS-1100; LYS-1168; LYS-1183; LYS-1222; LYS-1232; LYS-1269; LYS-1291; LYS-1356; LYS-1444; LYS-1471; LYS-1479 AND LYS-1486, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. Cited for: FUNCTION, GLUTARYLATION.

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: June 24, 2015
This is version 114 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

External Data

Dasty 3

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 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.