Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q8C196

- CPSM_MOUSE

UniProt

Q8C196 - CPSM_MOUSE

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 2 (30 Aug 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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
    8. protein binding Source: IntAct

    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

    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. nucleolus Source: UniProtKB-SubCell
    5. protein complex Source: Ensembl

    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.
    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.
    InParanoidiA0JNU4.
    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.

    Q8C196-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTRILTACKV VKTLKSGFGF ANVTTKRQWD FSRPGIRLLS VKAKTAHIVL     50
    EDGTKMKGYS FGHPSSVAGE VVFNTGLGGY PEALTDPAYK GQILTMANPI 100
    IGNGGAPDTT ARDELGLNKY MESDGIKVAG LLVLNYSNDY NHWLATKSLG 150
    QWLQEEKVPA IYGVDTRMLT KIIRDKGTML GKIEFEGQSV DFVDPNKQNL 200
    IAEVSTKDVK VFGKGNPTKV VAVDCGIKNN VIRLLVKRGA EVHLVPWNHD 250
    FTQMEYDGLL IAGGPGNPAL AQPLIQNVKK ILESDRKEPL FGISTGNIIT 300
    GLAAGAKSYK MSMANRGQNQ PVLNITNRQA FITAQNHGYA LDNTLPAGWK 350
    PLFVNVNDQT NEGIMHESKP FFAVQFHPEV SPGPTDTEYL FDSFFSLIKK 400
    GKGTTITSVL PKPALVASRV EVSKVLILGS GGLSIGQAGE FDYSGSQAVK 450
    AMKEENVKTV LMNPNIASVQ TNEVGLKQAD AVYFLPITPQ FVTEVIKAER 500
    PDGLILGMGG QTALNCGVEL FKRGVLKEYG VKVLGTSVES IMATEDRQLF 550
    SDKLNEINEK IAPSFAVESM EDALKAADTI GYPVMIRSAY ALGGLGSGIC 600
    PNKETLIDLG TKAFAMTNQI LVERSVTGWK EIEYEVVRDA DDNCVTVCNM 650
    ENVDAMGVHT GDSVVVAPAQ TLSNAEFQML RRTSVNVVRH LGIVGECNIQ 700
    FALHPTSMEY CIIEVNARLS RSSALASKAT GYPLAFIAAK IALGIPLPEI 750
    KNVVSGKTSA CFEPSLDYMV TKIPRWDLDR FHGTSSRIGS SMKSVGEVMA 800
    IGRTFEESFQ KALRMCHPSV DGFTPRLPMN KEWPANLDLK KELSEPSSTR 850
    IYAIAKALEN NMSLDEIVRL TSIDKWFLYK MRDILNMDKT LKGLNSDSVT 900
    EETLRKAKEI GFSDKQISKC LGLTEAQTRE LRLKKNIHPW VKQIDTLAAE 950
    YPSVTNYLYV TYNGQEHDIK FDEHGIMVLG CGPYHIGSSV EFDWCAVSSI 1000
    RTLRQLGKKT VVVNCNPETV STDFDECDKL YFEELSLERI LDIYHQEACN 1050
    GCIISVGGQI PNNLAVPLYK NGVKIMGTSP LQIDRAEDRS IFSAVLDELK 1100
    VAQAPWKAVN TLNEALEFAN SVGYPCLLRP SYVLSGSAMN VVFSEDEMKR 1150
    FLEEATRVSQ EHPVVLTKFV EGAREVEMDA VGKEGRVISH AISEHVEDAG 1200
    VHSGDATLML PTQTISQGAI EKVKDATRKI AKAFAISGPF NVQFLVKGND 1250
    VLVIECNLRA SRSFPFVSKT LGVDFIDVAT KVMIGESIDE KRLPTLEQPI 1300
    IPSDYVAIKA PMFSWPRLRD ADPILRCEMA STGEVACFGE GIHTAFLKAM 1350
    LSTGFKIPQK GILIGIQQSF RPRFLGVAEQ LHNEGFKLFA TEATSDWLNA 1400
    NNVPATPVAW PSQEGQNPSL SSIRKLIRDG SIDLVINLPN NNTKFVHDNY 1450
    VIRRTAVDSG IALLTNFQVT KLFAEAVQKS RTVDSKSLFH YRQYSAGKAA 1500
    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 A0JNU4.
    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.
    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

    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 1, 2014
    This is version 106 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