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Q8C196

- CPSM_MOUSE

UniProt

Q8C196 - CPSM_MOUSE

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Protein

Carbamoyl-phosphate synthase [ammonia], mitochondrial

Gene

Cps1

Organism
Mus musculus (Mouse)
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.

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

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

GO - Biological processi

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

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Urea cycle

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

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: Chromosome 1

Organism-specific databases

MGIiMGI:891996. Cps1.

Subcellular locationi

Mitochondrion By similarity. Nucleusnucleolus By similarity

GO - Cellular componenti

  1. mitochondrial inner membrane Source: Ensembl
  2. mitochondrial nucleoid Source: Ensembl
  3. mitochondrion Source: MGI
  4. nucleus Source: UniProtKB-KW
  5. protein complex Source: Ensembl
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-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 residuei157 – 1571N6-acetyllysine; alternate1 Publication
Modified residuei157 – 1571N6-succinyllysine; alternate1 Publication
Modified residuei171 – 1711N6-acetyllysine1 Publication
Modified residuei182 – 1821N6-acetyllysine1 Publication
Modified residuei197 – 1971N6-acetyllysine1 Publication
Modified residuei207 – 2071N6-acetyllysine; alternate1 Publication
Modified residuei207 – 2071N6-succinyllysine; alternate1 Publication
Modified residuei210 – 2101N6-acetyllysine1 Publication
Modified residuei214 – 2141N6-acetyllysine; alternate1 Publication
Modified residuei214 – 2141N6-succinyllysine; alternate1 Publication
Modified residuei219 – 2191N6-acetyllysine1 Publication
Modified residuei228 – 2281N6-acetyllysine1 Publication
Modified residuei279 – 2791N6-acetyllysine1 Publication
Modified residuei280 – 2801N6-acetyllysine1 Publication
Modified residuei287 – 2871N6-acetyllysine; alternate2 Publications
Modified residuei287 – 2871N6-succinyllysine; alternate2 Publications
Modified residuei307 – 3071N6-acetyllysine; alternate1 Publication
Modified residuei307 – 3071N6-succinyllysine; alternate1 Publication
Modified residuei310 – 3101N6-acetyllysine1 Publication
Modified residuei400 – 4001N6-succinyllysine1 Publication
Modified residuei402 – 4021N6-succinyllysine1 Publication
Modified residuei412 – 4121N6-acetyllysine; alternate1 Publication
Modified residuei412 – 4121N6-succinyllysine; alternate1 Publication
Modified residuei453 – 4531N6-acetyllysine1 Publication
Modified residuei458 – 4581N6-acetyllysine; alternate1 Publication
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-succinyllysine; alternate1 Publication
Modified residuei532 – 5321N6-acetyllysine1 Publication
Modified residuei537 – 5371Phosphoserine1 Publication
Glycosylationi537 – 5371O-linked (GlcNAc)By similarity
Modified residuei553 – 5531N6-acetyllysine; alternate1 Publication
Modified residuei553 – 5531N6-succinyllysine; alternate1 Publication
Modified residuei560 – 5601N6-acetyllysine; alternate1 Publication
Modified residuei560 – 5601N6-succinyllysine; alternate1 Publication
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 residuei751 – 7511N6-acetyllysine; alternate1 Publication
Modified residuei751 – 7511N6-succinyllysine; alternate1 Publication
Modified residuei757 – 7571N6-acetyllysine; alternate1 Publication
Modified residuei757 – 7571N6-succinyllysine; alternate1 Publication
Modified residuei772 – 7721N6-acetyllysine1 Publication
Modified residuei793 – 7931N6-acetyllysine; alternate1 Publication
Modified residuei793 – 7931N6-succinyllysine; alternate1 Publication
Modified residuei811 – 8111N6-acetyllysine1 Publication
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 residuei856 – 8561N6-acetyllysine1 Publication
Modified residuei875 – 8751N6-acetyllysine; alternate1 Publication
Modified residuei875 – 8751N6-succinyllysine; alternate1 Publication
Modified residuei889 – 8891N6-acetyllysine; alternate1 Publication
Modified residuei889 – 8891N6-succinyllysine; alternate1 Publication
Modified residuei892 – 8921N6-acetyllysine; alternate1 Publication
Modified residuei892 – 8921N6-succinyllysine; alternate1 Publication
Modified residuei908 – 9081N6-acetyllysine1 Publication
Modified residuei915 – 9151N6-acetyllysine; alternate1 Publication
Modified residuei915 – 9151N6-succinyllysine; alternate1 Publication
Modified residuei919 – 9191N6-acetyllysine; alternate1 Publication
Modified residuei919 – 9191N6-succinyllysine; alternate1 Publication
Modified residuei935 – 9351N6-acetyllysine1 Publication
Modified residuei1074 – 10741N6-acetyllysine; alternate1 Publication
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-succinyllysine; alternate1 Publication
Modified residuei1183 – 11831N6-acetyllysine; alternate1 Publication
Modified residuei1183 – 11831N6-succinyllysine; alternate1 Publication
Modified residuei1222 – 12221N6-acetyllysine1 Publication
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-succinyllysine; alternate1 Publication
Modified residuei1360 – 13601N6-succinyllysine1 Publication
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-succinyllysine; alternate1 Publication
Modified residuei1486 – 14861N6-acetyllysine; alternate1 Publication
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.3 Publications
Succinylated at Lys-44, Lys-287 and Lys-1291. Desuccinylated at Lys-1291 by SIRT5, leading to activation.2 Publications

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ8C196.
PaxDbiQ8C196.
PRIDEiQ8C196.

PTM databases

PhosphoSiteiQ8C196.

Expressioni

Gene expression databases

BgeeiQ8C196.
CleanExiMM_CPS1.
ExpressionAtlasiQ8C196. baseline and differential.
GenevestigatoriQ8C196.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

IntActiQ8C196. 5 interactions.
MINTiMINT-1856511.

Structurei

3D structure databases

ProteinModelPortaliQ8C196.
SMRiQ8C196. Positions 44-404, 535-812, 996-1338, 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.
OMAiMDLGTKA.
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 [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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS35605.1.
RefSeqi NP_001074278.1. NM_001080809.2.
UniGenei Mm.343942.

3D structure databases

ProteinModelPortali Q8C196.
SMRi Q8C196. Positions 44-404, 535-812, 996-1338, 1343-1478.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8C196. 5 interactions.
MINTi MINT-1856511.

PTM databases

PhosphoSitei Q8C196.

Proteomic databases

MaxQBi Q8C196.
PaxDbi Q8C196.
PRIDEi Q8C196.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000027144 ; ENSMUSP00000027144 ; ENSMUSG00000025991 .
GeneIDi 227231.
KEGGi mmu:227231.
UCSCi uc007biy.1. mouse.

Organism-specific databases

CTDi 1373.
MGIi MGI:891996. Cps1.

Phylogenomic databases

eggNOGi COG0458.
GeneTreei ENSGT00390000015604.
HOGENOMi HOG000234583.
HOVERGENi HBG000279.
InParanoidi Q8C196.
KOi K01948.
OMAi MDLGTKA.
OrthoDBi EOG7M6D6F.
PhylomeDBi Q8C196.
TreeFami TF331485.

Enzyme and pathway databases

SABIO-RK Q8C196.

Miscellaneous databases

NextBioi 378522.
PROi Q8C196.
SOURCEi Search...

Gene expression databases

Bgeei Q8C196.
CleanExi MM_CPS1.
ExpressionAtlasi Q8C196. baseline and differential.
Genevestigatori Q8C196.

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

« 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.

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: October 29, 2014
This is version 107 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