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Q8C196 (CPSM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carbamoyl-phosphate synthase [ammonia], mitochondrial

EC=6.3.4.16
Alternative name(s):
Carbamoyl-phosphate synthetase I
Short name=CPSase I
Gene names
Name:Cps1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1500 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell. HAMAP-Rule MF_01209

Catalytic activity

2 ATP + NH3 + CO2 + H2O = 2 ADP + phosphate + carbamoyl phosphate. HAMAP-Rule MF_01209

Enzyme regulation

Requires N-acetyl-L-glutamate (NAG) as an allosteric activator By similarity. HAMAP-Rule MF_01209

Subcellular location

Mitochondrion By similarity. Nucleusnucleolus By similarity HAMAP-Rule MF_01209.

Domain

The type-1 glutamine amidotransferase domain is defective By similarity. HAMAP-Rule MF_01209

Post-translational modification

Acetylation of Lys-287, Lys-603, Lys-841 and Lys-1291 is observed in liver mitochondria from fasted mice but not from fed mice. Ref.6 Ref.7

Succinylated at Lys-44, Lys-287 and Lys-1291. Desuccinylated at Lys-1291 by SIRT5, leading to activation. Ref.7

Sequence similarities

Contains 2 ATP-grasp domains.

Contains 1 glutamine amidotransferase type-1 domain.

Caution

Was initially reported to be deacetylated by Sirt5 (Ref.6). However, it was later shown that Sirt5 has poor deacetylase activity and mediates desuccinylation of Cps1 instead (Ref.7).

Ontologies

Keywords
   Biological processUrea cycle
   Cellular componentMitochondrion
Nucleus
   DomainRepeat
Transit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
Phosphoprotein
   Technical termAllosteric enzyme
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processanion homeostasis

Inferred from electronic annotation. Source: Ensembl

carbamoyl phosphate biosynthetic process

Inferred from electronic annotation. Source: Ensembl

cellular response to cAMP

Inferred from electronic annotation. Source: Ensembl

cellular response to fibroblast growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to glucagon stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to oleic acid

Inferred from electronic annotation. Source: Ensembl

glutamine catabolic process

Inferred from electronic annotation. Source: InterPro

glycogen catabolic process

Inferred from electronic annotation. Source: Ensembl

hepatocyte differentiation

Inferred from electronic annotation. Source: Ensembl

homocysteine metabolic process

Inferred from electronic annotation. Source: Ensembl

midgut development

Inferred from electronic annotation. Source: Ensembl

nitric oxide metabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of vasodilation

Inferred from electronic annotation. Source: Ensembl

response to amine

Inferred from electronic annotation. Source: Ensembl

response to amino acid

Inferred from electronic annotation. Source: Ensembl

response to dexamethasone

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to food

Inferred from electronic annotation. Source: Ensembl

response to growth hormone

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to starvation

Inferred from electronic annotation. Source: Ensembl

response to toxic substance

Inferred from electronic annotation. Source: Ensembl

response to zinc ion

Inferred from electronic annotation. Source: Ensembl

triglyceride catabolic process

Inferred from electronic annotation. Source: Ensembl

urea cycle

Inferred by curator PubMed 9862865. Source: MGI

   Cellular_componentmitochondrial inner membrane

Inferred from electronic annotation. Source: Ensembl

mitochondrial nucleoid

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from direct assay PubMed 22402285PubMed 6200105. Source: MGI

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

calcium ion binding

Inferred from electronic annotation. Source: Ensembl

carbamoyl-phosphate synthase (ammonia) activity

Inferred from mutant phenotype PubMed 9862865. Source: MGI

endopeptidase activity

Inferred from electronic annotation. Source: Ensembl

glutamate binding

Inferred from electronic annotation. Source: Ensembl

modified amino acid binding

Inferred from electronic annotation. Source: Ensembl

phospholipid binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sirt5Q8K2C62EBI-2348828,EBI-2348809

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3838Mitochondrion By similarity
Chain39 – 15001462Carbamoyl-phosphate synthase [ammonia], mitochondrial By similarity
PRO_0000029898

Regions

Domain219 – 404186Glutamine amidotransferase type-1
Domain551 – 743193ATP-grasp 1
Domain1093 – 1284192ATP-grasp 2
Region39 – 218180Anthranilate phosphoribosyltransferase homolog HAMAP-Rule MF_01209

Sites

Binding site13911Allosteric activator By similarity
Binding site13941Allosteric activator By similarity
Binding site14101Allosteric activator By similarity
Binding site14371Allosteric activator By similarity
Binding site14401Allosteric activator By similarity
Binding site14491Allosteric activator By similarity

Amino acid modifications

Modified residue441N6-acetyllysine; alternate Ref.7 Ref.9
Modified residue441N6-succinyllysine; alternate Ref.7 Ref.8
Modified residue551N6-acetyllysine; alternate Ref.9
Modified residue551N6-succinyllysine; alternate Ref.8
Modified residue571N6-acetyllysine; alternate Ref.9
Modified residue571N6-succinyllysine; alternate Ref.8
Modified residue1191N6-acetyllysine; alternate Ref.9
Modified residue1191N6-succinyllysine; alternate Ref.8
Modified residue1571N6-acetyllysine; alternate Ref.9
Modified residue1571N6-succinyllysine; alternate Ref.8
Modified residue1711N6-acetyllysine Ref.9
Modified residue1821N6-acetyllysine Ref.9
Modified residue1971N6-acetyllysine Ref.9
Modified residue2071N6-acetyllysine; alternate Ref.9
Modified residue2071N6-succinyllysine; alternate Ref.8
Modified residue2101N6-acetyllysine Ref.9
Modified residue2141N6-acetyllysine; alternate Ref.9
Modified residue2141N6-succinyllysine; alternate Ref.8
Modified residue2191N6-acetyllysine Ref.9
Modified residue2281N6-acetyllysine Ref.9
Modified residue2791N6-acetyllysine Ref.9
Modified residue2801N6-acetyllysine Ref.9
Modified residue2871N6-acetyllysine; alternate Ref.7 Ref.9
Modified residue2871N6-succinyllysine; alternate Ref.7 Ref.8
Modified residue3071N6-acetyllysine; alternate Ref.9
Modified residue3071N6-succinyllysine; alternate Ref.8
Modified residue3101N6-acetyllysine Ref.9
Modified residue4001N6-succinyllysine Ref.8
Modified residue4021N6-succinyllysine Ref.8
Modified residue4121N6-acetyllysine; alternate Ref.9
Modified residue4121N6-succinyllysine; alternate Ref.8
Modified residue4531N6-acetyllysine Ref.9
Modified residue4581N6-acetyllysine; alternate Ref.9
Modified residue4581N6-succinyllysine; alternate Ref.8
Modified residue5221N6-acetyllysine; alternate Ref.9
Modified residue5221N6-succinyllysine; alternate Ref.8
Modified residue5271N6-acetyllysine; alternate Ref.9
Modified residue5271N6-succinyllysine; alternate Ref.8
Modified residue5321N6-acetyllysine Ref.9
Modified residue5371Phosphoserine Ref.5
Modified residue5531N6-acetyllysine; alternate Ref.9
Modified residue5531N6-succinyllysine; alternate Ref.8
Modified residue5601N6-acetyllysine; alternate Ref.9
Modified residue5601N6-succinyllysine; alternate Ref.8
Modified residue5751N6-acetyllysine; alternate Ref.9
Modified residue5751N6-succinyllysine; alternate Ref.8
Modified residue6031N6-acetyllysine; alternate Ref.9
Modified residue6031N6-succinyllysine; alternate Ref.8
Modified residue6121N6-acetyllysine; alternate Ref.9
Modified residue6121N6-succinyllysine; alternate Ref.8
Modified residue6301N6-acetyllysine Ref.9
Modified residue7511N6-acetyllysine; alternate Ref.9
Modified residue7511N6-succinyllysine; alternate Ref.8
Modified residue7571N6-acetyllysine; alternate Ref.9
Modified residue7571N6-succinyllysine; alternate Ref.8
Modified residue7721N6-acetyllysine Ref.9
Modified residue7931N6-acetyllysine; alternate Ref.9
Modified residue7931N6-succinyllysine; alternate Ref.8
Modified residue8111N6-acetyllysine Ref.9
Modified residue8311N6-acetyllysine; alternate Ref.9
Modified residue8311N6-succinyllysine; alternate Ref.8
Modified residue8401N6-acetyllysine; alternate Ref.9
Modified residue8401N6-succinyllysine; alternate Ref.8
Modified residue8411N6-acetyllysine Ref.9
Modified residue8561N6-acetyllysine Ref.9
Modified residue8751N6-acetyllysine; alternate Ref.9
Modified residue8751N6-succinyllysine; alternate Ref.8
Modified residue8891N6-acetyllysine; alternate Ref.9
Modified residue8891N6-succinyllysine; alternate Ref.8
Modified residue8921N6-acetyllysine; alternate Ref.9
Modified residue8921N6-succinyllysine; alternate Ref.8
Modified residue9081N6-acetyllysine Ref.9
Modified residue9151N6-acetyllysine; alternate Ref.9
Modified residue9151N6-succinyllysine; alternate Ref.8
Modified residue9191N6-acetyllysine; alternate Ref.9
Modified residue9191N6-succinyllysine; alternate Ref.8
Modified residue9351N6-acetyllysine Ref.9
Modified residue10741N6-acetyllysine; alternate Ref.9
Modified residue10741N6-succinyllysine; alternate Ref.8
Modified residue10791Phosphoserine Ref.5
Modified residue11001N6-acetyllysine; alternate Ref.9
Modified residue11001N6-succinyllysine; alternate Ref.8
Modified residue11491N6-succinyllysine Ref.8
Modified residue11681N6-acetyllysine; alternate Ref.9
Modified residue11681N6-succinyllysine; alternate Ref.8
Modified residue11831N6-acetyllysine; alternate Ref.9
Modified residue11831N6-succinyllysine; alternate Ref.8
Modified residue12221N6-acetyllysine Ref.9
Modified residue12321N6-acetyllysine; alternate Ref.9
Modified residue12321N6-succinyllysine; alternate Ref.8
Modified residue12691N6-acetyllysine; alternate Ref.9
Modified residue12691N6-succinyllysine; alternate Ref.8
Modified residue12911N6-acetyllysine; alternate Ref.6 Ref.7 Ref.9
Modified residue12911N6-succinyllysine; alternate Ref.7 Ref.8
Modified residue13561N6-acetyllysine; alternate Ref.9
Modified residue13561N6-succinyllysine; alternate Ref.8
Modified residue13601N6-succinyllysine Ref.8
Modified residue14441N6-acetyllysine; alternate Ref.9
Modified residue14441N6-succinyllysine; alternate Ref.8
Modified residue14711N6-acetyllysine; alternate Ref.9
Modified residue14711N6-succinyllysine; alternate Ref.8
Modified residue14791N6-acetyllysine; alternate Ref.9
Modified residue14791N6-succinyllysine; alternate Ref.8
Modified residue14861N6-acetyllysine; alternate Ref.9
Modified residue14861N6-succinyllysine; alternate Ref.8

Experimental info

Sequence conflict931 – 9344LRLK → HASE in AAH67211. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8C196 [UniParc].

Last modified August 30, 2005. Version 2.
Checksum: 84A7268C1D7E8101

FASTA1,500164,618
        10         20         30         40         50         60 
MTRILTACKV VKTLKSGFGF ANVTTKRQWD FSRPGIRLLS VKAKTAHIVL EDGTKMKGYS 

        70         80         90        100        110        120 
FGHPSSVAGE VVFNTGLGGY PEALTDPAYK GQILTMANPI IGNGGAPDTT ARDELGLNKY 

       130        140        150        160        170        180 
MESDGIKVAG LLVLNYSNDY NHWLATKSLG QWLQEEKVPA IYGVDTRMLT KIIRDKGTML 

       190        200        210        220        230        240 
GKIEFEGQSV DFVDPNKQNL IAEVSTKDVK VFGKGNPTKV VAVDCGIKNN VIRLLVKRGA 

       250        260        270        280        290        300 
EVHLVPWNHD FTQMEYDGLL IAGGPGNPAL AQPLIQNVKK ILESDRKEPL FGISTGNIIT 

       310        320        330        340        350        360 
GLAAGAKSYK MSMANRGQNQ PVLNITNRQA FITAQNHGYA LDNTLPAGWK PLFVNVNDQT 

       370        380        390        400        410        420 
NEGIMHESKP FFAVQFHPEV SPGPTDTEYL FDSFFSLIKK GKGTTITSVL PKPALVASRV 

       430        440        450        460        470        480 
EVSKVLILGS GGLSIGQAGE FDYSGSQAVK AMKEENVKTV LMNPNIASVQ TNEVGLKQAD 

       490        500        510        520        530        540 
AVYFLPITPQ FVTEVIKAER PDGLILGMGG QTALNCGVEL FKRGVLKEYG VKVLGTSVES 

       550        560        570        580        590        600 
IMATEDRQLF SDKLNEINEK IAPSFAVESM EDALKAADTI GYPVMIRSAY ALGGLGSGIC 

       610        620        630        640        650        660 
PNKETLIDLG TKAFAMTNQI LVERSVTGWK EIEYEVVRDA DDNCVTVCNM ENVDAMGVHT 

       670        680        690        700        710        720 
GDSVVVAPAQ TLSNAEFQML RRTSVNVVRH LGIVGECNIQ FALHPTSMEY CIIEVNARLS 

       730        740        750        760        770        780 
RSSALASKAT GYPLAFIAAK IALGIPLPEI KNVVSGKTSA CFEPSLDYMV TKIPRWDLDR 

       790        800        810        820        830        840 
FHGTSSRIGS SMKSVGEVMA IGRTFEESFQ KALRMCHPSV DGFTPRLPMN KEWPANLDLK 

       850        860        870        880        890        900 
KELSEPSSTR IYAIAKALEN NMSLDEIVRL TSIDKWFLYK MRDILNMDKT LKGLNSDSVT 

       910        920        930        940        950        960 
EETLRKAKEI GFSDKQISKC LGLTEAQTRE LRLKKNIHPW VKQIDTLAAE YPSVTNYLYV 

       970        980        990       1000       1010       1020 
TYNGQEHDIK FDEHGIMVLG CGPYHIGSSV EFDWCAVSSI RTLRQLGKKT VVVNCNPETV 

      1030       1040       1050       1060       1070       1080 
STDFDECDKL YFEELSLERI LDIYHQEACN GCIISVGGQI PNNLAVPLYK NGVKIMGTSP 

      1090       1100       1110       1120       1130       1140 
LQIDRAEDRS IFSAVLDELK VAQAPWKAVN TLNEALEFAN SVGYPCLLRP SYVLSGSAMN 

      1150       1160       1170       1180       1190       1200 
VVFSEDEMKR FLEEATRVSQ EHPVVLTKFV EGAREVEMDA VGKEGRVISH AISEHVEDAG 

      1210       1220       1230       1240       1250       1260 
VHSGDATLML PTQTISQGAI EKVKDATRKI AKAFAISGPF NVQFLVKGND VLVIECNLRA 

      1270       1280       1290       1300       1310       1320 
SRSFPFVSKT LGVDFIDVAT KVMIGESIDE KRLPTLEQPI IPSDYVAIKA PMFSWPRLRD 

      1330       1340       1350       1360       1370       1380 
ADPILRCEMA STGEVACFGE GIHTAFLKAM LSTGFKIPQK GILIGIQQSF RPRFLGVAEQ 

      1390       1400       1410       1420       1430       1440 
LHNEGFKLFA TEATSDWLNA NNVPATPVAW PSQEGQNPSL SSIRKLIRDG SIDLVINLPN 

      1450       1460       1470       1480       1490       1500 
NNTKFVHDNY VIRRTAVDSG IALLTNFQVT KLFAEAVQKS RTVDSKSLFH YRQYSAGKAA 

« Hide

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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
Cited for: PROTEIN SEQUENCE OF 113-167; 183-207; 287-307; 317-328; 403-419; 459-522; 533-624; 631-638; 683-689; 729-740; 794-811; 815-826; 842-850; 857-880; 883-889; 893-905; 1030-1039; 1075-1085; 1090-1100; 1158-1168; 1175-1183; 1233-1259; 1270-1317; 1320-1326; 1349-1356; 1361-1387; 1429-1444 AND 1455-1479, IDENTIFICATION BY MASS SPECTROMETRY.
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. expand/collapse author list , 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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001074278.1. NM_001080809.2.
UniGeneMm.343942.

3D structure databases

ProteinModelPortalQ8C196.
SMRQ8C196. Positions 44-404, 416-819, 971-1478.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8C196. 5 interactions.
MINTMINT-1856511.

PTM databases

PhosphoSiteQ8C196.

Proteomic databases

PaxDbQ8C196.
PRIDEQ8C196.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027144; ENSMUSP00000027144; ENSMUSG00000025991.
GeneID227231.
KEGGmmu:227231.
UCSCuc007biy.1. mouse.

Organism-specific databases

CTD1373.
MGIMGI:891996. Cps1.

Phylogenomic databases

eggNOGCOG0458.
GeneTreeENSGT00390000015604.
HOGENOMHOG000234583.
HOVERGENHBG000279.
InParanoidA0JNU4.
KOK01948.
OMAFDKFQGA.
OrthoDBEOG7M6D6F.
PhylomeDBQ8C196.
TreeFamTF331485.

Enzyme and pathway databases

SABIO-RKQ8C196.

Gene expression databases

BgeeQ8C196.
CleanExMM_CPS1.
GenevestigatorQ8C196.

Family and domain databases

Gene3D1.10.1030.10. 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.
3.50.30.20. 1 hit.
HAMAPMF_01209. CPSase_S_chain.
InterProIPR011761. 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.
IPR017926. GATASE.
IPR011607. MGS-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamPF00289. 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]
PRINTSPR00098. CPSASE.
SMARTSM01096. CPSase_L_D3. 1 hit.
SM01097. CPSase_sm_chain. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMSSF48108. SSF48108. 1 hit.
SSF52021. SSF52021. 1 hit.
SSF52335. SSF52335. 1 hit.
SSF52440. SSF52440. 2 hits.
TIGRFAMsTIGR01369. CPSaseII_lrg. 1 hit.
TIGR01368. CPSaseIIsmall. 1 hit.
PROSITEPS50975. ATP_GRASP. 2 hits.
PS00866. CPSASE_1. 2 hits.
PS00867. CPSASE_2. 2 hits.
PS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio378522.
PROQ8C196.
SOURCESearch...

Entry information

Entry nameCPSM_MOUSE
AccessionPrimary (citable) accession number: Q8C196
Secondary accession number(s): A0JNU4, Q6NX75
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: August 30, 2005
Last modified: April 16, 2014
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot