P31327 (CPSM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1500 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Catalytic activity	2 ATP + NH3 + CO2 + H2O = 2 ADP + phosphate + carbamoyl phosphate.
Enzyme regulation	Requires N-acetyl-L-glutamate (NAG) as an allosteric activator.
Subcellular location	Mitochondrion.
Tissue specificity	Primarily in the liver and small intestine.
Domain	The type-1 glutamine amidotransferase domain is defective.
Involvement in disease	Defects in CPS1 are the cause of carbamoyl phosphate synthetase 1 deficiency (CPS1D) [MIM:237300]. CPS1D is an autosomal recessive disorder of the urea cycle causing hyperammonemia. Clinical features include protein intolerance, intermittent ataxia, seizures, lethargy, developmental delay and mental retardation. Ref.2 Ref.5 Ref.6 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Note=Genetic variations in CPS1 influence the availability of precursors for nitric oxide (NO) synthesis and play a role in clinical situations where endogenous NO production is critically important, such as neonatal pulmonary hypertension, increased pulmonary artery pressure following surgical repair of congenital heart defects or hepatovenocclusive disease following bone marrow transplantation. Infants with neonatal pulmonary hypertension homozygous for Thr-1406 have lower L-arginine concentrations than neonates homozygous for Asn-1406. Ref.21
Sequence similarities	Contains 2 ATP-grasp domains. Contains 1 glutamine amidotransferase type-1 domain.

Ontologies

Keywords
Biological process	Urea cycle
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Repeat Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	carbamoyl phosphate biosynthetic process Inferred from mutant phenotype. Source: UniProtKB citrulline biosynthetic process Non-traceable author statement. Source: BHF-UCL glutamine metabolic process Inferred from electronic annotation. Source: InterPro glycogen catabolic process Inferred from mutant phenotype Ref.2. Source: BHF-UCL nitric oxide metabolic process Inferred from mutant phenotype. Source: BHF-UCL positive regulation of vasodilation Inferred from mutant phenotype. Source: BHF-UCL response to lipopolysaccharide Inferred from direct assay. Source: UniProtKB triglyceride catabolic process Inferred from mutant phenotype Ref.2. Source: BHF-UCL urea cycle Non-traceable author statement Ref.1. Source: BHF-UCL
Cellular component	mitochondrial nucleoid Inferred from direct assay. Source: BHF-UCL
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW carbamoyl-phosphate synthase (ammonia) activity Inferred from mutant phenotype Ref.2. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARAF	P10398	3	EBI-536811,EBI-365961
RAF1	P04049	4	EBI-536811,EBI-365996

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P31327-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P31327-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-451: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 38

38

Mitochondrion By similarity

Chain

39 – 1500

1462

Carbamoyl-phosphate synthase [ammonia], mitochondrial

PRO_0000029897

Regions

Domain

219 – 404

186

Glutamine amidotransferase type-1

Domain

551 – 743

193

ATP-grasp 1

Domain

1093 – 1284

192

ATP-grasp 2

Region

39 – 218

180

Anthranilate phosphoribosyltransferase homolog

Sites

Binding site

1391

1

Allosteric activator Probable

Binding site

1394

1

Allosteric activator Probable

Binding site

1410

1

Allosteric activator Probable

Binding site

1437

1

Allosteric activator Probable

Binding site

1440

1

Allosteric activator Probable

Binding site

1449

1

Allosteric activator Probable

Amino acid modifications

Modified residue

55

1

N6-acetyllysine By similarity

Modified residue

119

1

N6-acetyllysine By similarity

Modified residue

287

1

N6-acetyllysine By similarity

Modified residue

527

1

N6-acetyllysine By similarity

Modified residue

841

1

N6-acetyllysine By similarity

Modified residue

892

1

N6-acetyllysine By similarity

Modified residue

898

1

Phosphoserine By similarity

Modified residue

1291

1

N6-acetyllysine By similarity

Natural variations

Alternative sequence

1 – 451

451

Missing in isoform 2.

VSP_009332

Natural variant

43

1

A → V in CPS1D. Ref.22

VAR_066171

Natural variant

58

1

G → D in CPS1D. Ref.22

VAR_066172

Natural variant

65

1

S → F in CPS1D. Ref.22

VAR_066173

Natural variant

71

1

V → G in CPS1D. Ref.22

VAR_066174

Natural variant

79

1

G → E in CPS1D. Ref.19

VAR_063560

Natural variant

87

1

P → S in CPS1D. Ref.22

VAR_066175

Natural variant

89

1

Y → D in CPS1D. Ref.22

VAR_066176

Natural variant

123

1

S → F in CPS1D; modestly decreases enzyme activity. Ref.20

VAR_064062

Natural variant

165

1

D → G in CPS1D. Ref.22

VAR_066177

Natural variant

212

1

Y → N in CPS1D. Ref.19

VAR_063561

Natural variant

224

1

D → V in CPS1D. Ref.22

VAR_066178

Natural variant

233

1

R → C in CPS1D. Ref.22

VAR_066179

Natural variant

243

1

H → P in CPS1D. Ref.22

VAR_066180

Natural variant

258

1

G → E in CPS1D. Ref.22

VAR_066181

Natural variant

263

1

G → E in CPS1D. Ref.22

VAR_066182

Natural variant

280

1

K → N in CPS1D. Ref.19

VAR_063562

Natural variant

301

1

G → E in CPS1D. Ref.18

VAR_066104

Natural variant

304

1

A → V in CPS1D; associated with T-986. Ref.22

VAR_066183

Natural variant

317

1

G → E in CPS1D. Ref.22

VAR_066184

Natural variant

337

1

H → R in CPS1D; modestly decreases enzyme activity. Ref.14 Ref.20
Corresponds to variant rs28940283 [ dbSNP | Ensembl ].

VAR_014077

Natural variant

344

1

T → A. Ref.2 Ref.3
Corresponds to variant rs1047883 [ dbSNP | Ensembl ].

VAR_006834

Natural variant

344

1

T → S.
Corresponds to variant rs1047883 [ dbSNP | Ensembl ].

VAR_061752

Natural variant

358

1

D → H in CPS1D. Ref.22

VAR_066185

Natural variant

382

1

P → L in CPS1D. Ref.22

VAR_066186

Natural variant

389

1

Y → C in CPS1D. Ref.18

VAR_066105

Natural variant

390

1

L → R in CPS1D. Ref.18

VAR_066106

Natural variant

401

1

G → R in CPS1D. Ref.22

VAR_066187

Natural variant

431

1

G → R in CPS1D. Ref.22

VAR_066188

Natural variant

432

1

G → V in CPS1D. Ref.22

VAR_066189

Natural variant

438

1

A → P in CPS1D. Ref.19

VAR_063563

Natural variant

438

1

A → T in CPS1D. Ref.22

VAR_066190

Natural variant

450

1

K → E in CPS1D. Ref.22

VAR_066191

Natural variant

457

1

V → G in CPS1D. Ref.5

VAR_017562

Natural variant

471

1

T → N in CPS1D. Ref.20

VAR_064063

Natural variant

498

1

A → P in CPS1D. Ref.22

VAR_066192

Natural variant

531

1

V → E in CPS1D. Ref.22

VAR_066193

Natural variant

531

1

V → G in CPS1D. Ref.22

VAR_066194

Natural variant

544

1

T → M in CPS1D. Ref.2 Ref.22

VAR_006835

Natural variant

587

1

R → C in CPS1D. Ref.22

VAR_066195

Natural variant

587

1

R → H in CPS1D. Ref.19 Ref.22

VAR_063564

Natural variant

587

1

R → L in CPS1D. Ref.22

VAR_066196

Natural variant

589

1

A → T in CPS1D. Ref.18

VAR_066142

Natural variant

593

1

G → R in CPS1D. Ref.19

VAR_063565

Natural variant

597

1

S → L in CPS1D. Ref.22

VAR_066197

Natural variant

622

1

V → M in CPS1D. Ref.22

VAR_066198

Natural variant

628

1

G → D in CPS1D. Ref.22

VAR_066199

Natural variant

632

1

I → R in CPS1D. Ref.22

VAR_066200

Natural variant

638

1

R → P in CPS1D. Ref.22

VAR_066201

Natural variant

640

1

A → S in CPS1D. Ref.18

VAR_066143

Natural variant

648

1

C → Y in CPS1D. Ref.22

VAR_066202

Natural variant

651

1

E → K in CPS1D. Ref.19

VAR_063566

Natural variant

654

1

D → V in CPS1D. Ref.22

VAR_066203

Natural variant

674

1

N → I in CPS1D. Ref.19

VAR_063567

Natural variant

674

1

N → K in CPS1D. Ref.22

VAR_066204

Natural variant

678

1

Q → P in CPS1D; results in a poor enzyme expression and solubility; hampers correct enzyme folding. Ref.20

VAR_064064

Natural variant

698

1

N → S in CPS1D. Ref.22

VAR_066205

Natural variant

716

1

N → K in CPS1D. Ref.18

VAR_066144

Natural variant

718

1

R → K in CPS1D. Ref.22

VAR_066107

Natural variant

721

1

R → Q in CPS1D. Ref.22

VAR_066108

Natural variant

724

1

A → P in CPS1D. Ref.22

VAR_066109

Natural variant

726

1

A → T in CPS1D. Ref.22

VAR_066110

Natural variant

767

1

D → V in CPS1D. Ref.22

VAR_066111

Natural variant

774

1

P → L in CPS1D; the enzyme is inactive. Ref.20

VAR_064065

Natural variant

780

1

R → H in CPS1D. Ref.19 Ref.22

VAR_063568

Natural variant

792

1

M → I in CPS1D. Ref.22

VAR_066112

Natural variant

803

1

R → C in CPS1D. Ref.22

VAR_066145

Natural variant

803

1

R → G in CPS1D. Ref.22

VAR_066146

Natural variant

803

1

R → S in CPS1D. Ref.22

VAR_066147

Natural variant

805

1

F → L in CPS1D. Ref.18

VAR_066148

Natural variant

805

1

F → S in CPS1D. Ref.22

VAR_066149

Natural variant

810

1

Q → R in CPS1D. Ref.5

VAR_017563

Natural variant

814

1

R → W in CPS1D. Ref.22

VAR_066150

Natural variant

816

1

C → R in CPS1D. Ref.22

VAR_066151

Natural variant

843

1

L → S in CPS1D. Ref.6 Ref.17

VAR_017564

Natural variant

850

1

R → C in CPS1D. Ref.19

VAR_063569

Natural variant

850

1

R → H in CPS1D. Ref.16 Ref.22

VAR_030675

Natural variant

875

1

K → E in CPS1D. Ref.6 Ref.17

VAR_017565

Natural variant

911

1

G → E in CPS1D. Ref.22

VAR_066152

Natural variant

911

1

G → V in CPS1D. Ref.18

VAR_066153

Natural variant

913

1

S → L in CPS1D. Ref.22

VAR_066154

Natural variant

914

1

D → G in CPS1D. Ref.22

VAR_066155

Natural variant

914

1

D → H in CPS1D. Ref.22

VAR_066156

Natural variant

918

1

S → P in CPS1D. Ref.16

VAR_030676

Natural variant

932

1

R → T in CPS1D. Ref.22

VAR_066157

Natural variant

949

1

A → T in CPS1D. Ref.22

VAR_066158

Natural variant

958

1

L → P in CPS1D. Ref.18

VAR_066159

Natural variant

959

1

Y → C in CPS1D. Ref.22

VAR_066160

Natural variant

962

1

Y → C in CPS1D. Ref.22

VAR_066161

Natural variant

978

1

V → E in CPS1D. Ref.22

VAR_066113

Natural variant

982

1

G → D in CPS1D. Ref.19

VAR_063570

Natural variant

982

1

G → S in CPS1D. Ref.18

VAR_066162

Natural variant

982

1

G → V in CPS1D. Ref.22

VAR_066114

Natural variant

984

1

Y → H in CPS1D. Ref.22

VAR_066115

Natural variant

986

1

I → T in CPS1D; associated with V-304. Ref.22

VAR_066116

Natural variant

987

1

G → C in CPS1D; may affect splicing. Ref.22

VAR_066117

Natural variant

992

1

F → S in CPS1D. Ref.22

VAR_066118

Natural variant

998

1

S → F in CPS1D. Ref.18

VAR_066163

Natural variant

1016

1

N → S in CPS1D. Ref.22

VAR_066119

Natural variant

1017

1

P → L in CPS1D. Ref.22

VAR_066120

Natural variant

1022

1

T → I in CPS1D. Ref.22

VAR_066121

Natural variant

1034

1

E → G in CPS1D. Ref.22

VAR_066122

Natural variant

1045

1

H → R in CPS1D. Ref.22

VAR_066123

Natural variant

1054

1

I → R in CPS1D. Ref.13

VAR_066164

Natural variant

1059

1

Q → R in CPS1D. Ref.22

VAR_066124

Natural variant

1065

1

A → E in CPS1D. Ref.22

VAR_066125

Natural variant

1089

1

R → C in CPS1D. Ref.22

VAR_066126

Natural variant

1089

1

R → L in CPS1D. Ref.18

VAR_066165

Natural variant

1103

1

Q → R in CPS1D. Ref.19

VAR_063571

Natural variant

1141

1

V → G in CPS1D. Ref.19

VAR_063572

Natural variant

1155

1

A → E in CPS1D. Ref.22

VAR_066127

Natural variant

1155

1

A → V in CPS1D. Ref.22

VAR_066128

Natural variant

1195

1

H → P in CPS1D. Ref.19

VAR_063573

Natural variant

1203

1

S → L in CPS1D. Ref.22

VAR_066129

Natural variant

1203

1

S → P in CPS1D. Ref.18

VAR_066166

Natural variant

1205

1

D → N in CPS1D. Ref.18

VAR_066167

Natural variant

1215

1

I → V in CPS1D. Ref.19

VAR_063574

Natural variant

1228

1

R → Q in CPS1D. Ref.22

VAR_066130

Natural variant

1241

1

N → K in CPS1D. Ref.19

VAR_063575

Natural variant

1255

1

E → D in CPS1D. Ref.22

VAR_066131

Natural variant

1262

1

R → P in CPS1D. Ref.22

VAR_066132

Natural variant

1262

1

R → Q in CPS1D. Ref.22

VAR_066133

Natural variant

1266

1

F → S. Ref.1
Corresponds to variant rs1047886 [ dbSNP | Ensembl ].

VAR_017566

Natural variant

1274

1

D → H in CPS1D. Ref.22

VAR_066134

Natural variant

1283

1

M → L. Ref.1
Corresponds to variant rs1047887 [ dbSNP | Ensembl ].

VAR_017567

Natural variant

1327

1

C → R in CPS1D. Ref.22

VAR_066135

Natural variant

1331

1

S → P in CPS1D. Ref.18

VAR_066168

Natural variant

1333

1

G → E in CPS1D. Ref.22

VAR_066136

Natural variant

1371

1

R → L in CPS1D. Ref.22

VAR_066137

Natural variant

1376

1

G → S Polymorphism with no functional consequences. Ref.3 Ref.20

VAR_017568

Natural variant

1378

1

A → T in CPS1D. Ref.18

VAR_066169

Natural variant

1391

1

T → M in CPS1D. Ref.22

VAR_066138

Natural variant

1398

1

L → V in CPS1D. Ref.22

VAR_066139

Natural variant

1406

1

T → N 30-40% higher activity. Ref.1 Ref.3 Ref.5 Ref.15 Ref.21
Corresponds to variant rs1047891 [ dbSNP | Ensembl ].

VAR_017569

Natural variant

1411

1

P → L in CPS1D; modestly decreases enzyme activity. Ref.18 Ref.20

VAR_064066

Natural variant

1439

1

P → L in CPS1D. Ref.22

VAR_066140

Natural variant

1443

1

T → A in CPS1D. Ref.18

VAR_066170

Natural variant

1453

1

R → Q in CPS1D; the enzyme is inactive. Ref.20

VAR_064067

Natural variant

1453

1

R → W in CPS1D; the enzyme is inactive. Ref.20 Ref.22

VAR_064068

Natural variant

1462

1

P → R in CPS1D. Ref.22

VAR_066141

Natural variant

1491

1

Y → H in CPS1D; triggers a large decrease in the apparent affinity for N-acetyl-L-glutamate (NAG). Ref.20

VAR_064069

Experimental info

Sequence conflict

111

1

A → S in BAA14328. Ref.1

Sequence conflict

279

1

R → Q in BAA14328. Ref.1

Sequence conflict

338

1

G → C in BAA14328. Ref.1

Sequence conflict

718 – 722

5

RLSRS → KMSPN in BAA14328. Ref.1

Sequence conflict

729

1

A → T in BAA14328. Ref.1

Sequence conflict

749

1

E → G in BAA14328. Ref.1

Sequence conflict

912

1

F → L in CAE45707. Ref.6

Sequence conflict

1161 – 1162

2

EH → AT in BAA14328. Ref.1

Sequence conflict

1204 – 1205

2

GD → EN in BAA14328. Ref.1

Sequence conflict

1254

1

I → N in BAA14328. Ref.1

Sequence conflict

1303

1

A → V in BAA14328. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1500

Helix Strand Turn

Details...

Helix

1344 – 1350

7

Beta strand

1360 – 1365

6

Helix

1368 – 1370

3

Helix

1371 – 1382

12

Turn

1383 – 1385

3

Beta strand

1387 – 1391

5

Helix

1392 – 1400

9

Beta strand

1406 – 1408

3

Helix

1411 – 1413

3

Helix

1423 – 1428

6

Beta strand

1434 – 1437

4

Helix

1443 – 1445

3

Helix

1446 – 1458

13

Helix

1467 – 1475

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 15, 1998. Version 2. Checksum: E53A22D77563961D	FASTA	1,500	164,939
	10 20 30 40 50 60 MTRILTAFKV VRTLKTGFGF TNVTAHQKWK FSRPGIRLLS VKAQTAHIVL EDGTKMKGYS 70 80 90 100 110 120 FGHPSSVAGE VVFNTGLGGY PEAITDPAYK GQILTMANPI IGNGGAPDTT ALDELGLSKY 130 140 150 160 170 180 LESNGIKVSG LLVLDYSKDY NHWLATKSLG QWLQEEKVPA IYGVDTRMLT KIIRDKGTML 190 200 210 220 230 240 GKIEFEGQPV DFVDPNKQNL IAEVSTKDVK VYGKGNPTKV VAVDCGIKNN VIRLLVKRGA 250 260 270 280 290 300 EVHLVPWNHD FTKMEYDGIL IAGGPGNPAL AEPLIQNVRK ILESDRKEPL FGISTGNLIT 310 320 330 340 350 360 GLAAGAKTYK MSMANRGQNQ PVLNITNKQA FITAQNHGYA LDNTLPAGWK PLFVNVNDQT 370 380 390 400 410 420 NEGIMHESKP FFAVQFHPEV TPGPIDTEYL FDSFFSLIKK GKATTITSVL PKPALVASRV 430 440 450 460 470 480 EVSKVLILGS GGLSIGQAGE FDYSGSQAVK AMKEENVKTV LMNPNIASVQ TNEVGLKQAD 490 500 510 520 530 540 TVYFLPITPQ FVTEVIKAEQ PDGLILGMGG QTALNCGVEL FKRGVLKEYG VKVLGTSVES 550 560 570 580 590 600 IMATEDRQLF SDKLNEINEK IAPSFAVESI EDALKAADTI GYPVMIRSAY ALGGLGSGIC 610 620 630 640 650 660 PNRETLMDLS TKAFAMTNQI LVEKSVTGWK EIEYEVVRDA DDNCVTVCNM ENVDAMGVHT 670 680 690 700 710 720 GDSVVVAPAQ TLSNAEFQML RRTSINVVRH LGIVGECNIQ FALHPTSMEY CIIEVNARLS 730 740 750 760 770 780 RSSALASKAT GYPLAFIAAK IALGIPLPEI KNVVSGKTSA CFEPSLDYMV TKIPRWDLDR 790 800 810 820 830 840 FHGTSSRIGS SMKSVGEVMA IGRTFEESFQ KALRMCHPSI EGFTPRLPMN KEWPSNLDLR 850 860 870 880 890 900 KELSEPSSTR IYAIAKAIDD NMSLDEIEKL TYIDKWFLYK MRDILNMEKT LKGLNSESMT 910 920 930 940 950 960 EETLKRAKEI GFSDKQISKC LGLTEAQTRE LRLKKNIHPW VKQIDTLAAE YPSVTNYLYV 970 980 990 1000 1010 1020 TYNGQEHDVN FDDHGMMVLG CGPYHIGSSV EFDWCAVSSI RTLRQLGKKT VVVNCNPETV 1030 1040 1050 1060 1070 1080 STDFDECDKL YFEELSLERI LDIYHQEACG GCIISVGGQI PNNLAVPLYK NGVKIMGTSP 1090 1100 1110 1120 1130 1140 LQIDRAEDRS IFSAVLDELK VAQAPWKAVN TLNEALEFAK SVDYPCLLRP SYVLSGSAMN 1150 1160 1170 1180 1190 1200 VVFSEDEMKK FLEEATRVSQ EHPVVLTKFV EGAREVEMDA VGKDGRVISH AISEHVEDAG 1210 1220 1230 1240 1250 1260 VHSGDATLML PTQTISQGAI EKVKDATRKI AKAFAISGPF NVQFLVKGND VLVIECNLRA 1270 1280 1290 1300 1310 1320 SRSFPFVSKT LGVDFIDVAT KVMIGENVDE KHLPTLDHPI IPADYVAIKA 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 IPLLTNFQVT KLFAEAVQKS RKVDSKSLFH YRQYSAGKAA
	Isoform 2 [UniParc]. Checksum: 74C9ABBFABAD2AD2	FASTA	1,049	116,038
	10 20 30 40 50 60 MKEENVKTVL MNPNIASVQT NEVGLKQADT VYFLPITPQF VTEVIKAEQP DGLILGMGGQ 70 80 90 100 110 120 TALNCGVELF KRGVLKEYGV KVLGTSVESI MATEDRQLFS DKLNEINEKI APSFAVESIE 130 140 150 160 170 180 DALKAADTIG YPVMIRSAYA LGGLGSGICP NRETLMDLST KAFAMTNQIL VEKSVTGWKE 190 200 210 220 230 240 IEYEVVRDAD DNCVTVCNME NVDAMGVHTG DSVVVAPAQT LSNAEFQMLR RTSINVVRHL 250 260 270 280 290 300 GIVGECNIQF ALHPTSMEYC IIEVNARLSR SSALASKATG YPLAFIAAKI ALGIPLPEIK 310 320 330 340 350 360 NVVSGKTSAC FEPSLDYMVT KIPRWDLDRF HGTSSRIGSS MKSVGEVMAI GRTFEESFQK 370 380 390 400 410 420 ALRMCHPSIE GFTPRLPMNK EWPSNLDLRK ELSEPSSTRI YAIAKAIDDN MSLDEIEKLT 430 440 450 460 470 480 YIDKWFLYKM RDILNMEKTL KGLNSESMTE ETLKRAKEIG FSDKQISKCL GLTEAQTREL 490 500 510 520 530 540 RLKKNIHPWV KQIDTLAAEY PSVTNYLYVT YNGQEHDVNF DDHGMMVLGC GPYHIGSSVE 550 560 570 580 590 600 FDWCAVSSIR TLRQLGKKTV VVNCNPETVS TDFDECDKLY FEELSLERIL DIYHQEACGG 610 620 630 640 650 660 CIISVGGQIP NNLAVPLYKN GVKIMGTSPL QIDRAEDRSI FSAVLDELKV AQAPWKAVNT 670 680 690 700 710 720 LNEALEFAKS VDYPCLLRPS YVLSGSAMNV VFSEDEMKKF LEEATRVSQE HPVVLTKFVE 730 740 750 760 770 780 GAREVEMDAV GKDGRVISHA ISEHVEDAGV HSGDATLMLP TQTISQGAIE KVKDATRKIA 790 800 810 820 830 840 KAFAISGPFN VQFLVKGNDV LVIECNLRAS RSFPFVSKTL GVDFIDVATK VMIGENVDEK 850 860 870 880 890 900 HLPTLDHPII PADYVAIKAP MFSWPRLRDA DPILRCEMAS TGEVACFGEG IHTAFLKAML 910 920 930 940 950 960 STGFKIPQKG ILIGIQQSFR PRFLGVAEQL HNEGFKLFAT EATSDWLNAN NVPATPVAWP 970 980 990 1000 1010 1020 SQEGQNPSLS SIRKLIRDGS IDLVINLPNN NTKFVHDNYV IRRTAVDSGI PLLTNFQVTK 1030 1040 LFAEAVQKSR KVDSKSLFHY RQYSAGKAA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequence of a cDNA encoding human carbamyl phosphate synthetase I: molecular analysis of hyperammonemia." Haraguchi Y., Uchino T., Takiguchi M., Endo F., Mori M., Matsuda I. Gene 107:335-340(1991) [PubMed: 1840546] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS SER-1266; LEU-1283 AND ASN-1406. Tissue: Liver.
[2]	"Prenatal diagnosis of carbamoyl phosphate synthetase I deficiency by identification of a missense mutation in CPS1." Finckh U., Kohlschuetter A., Schaefer H., Sperhake K., Colombo J.-P., Gal A. Hum. Mutat. 12:206-211(1998) [PubMed: 9711878] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT CPS1D MET-544, VARIANT ALA-344. Tissue: Liver.
[3]	"Characterization of genomic structure and polymorphisms in the human carbamyl phosphate synthetase I gene." Summar M.L., Hall L.D., Eeds A.M., Hutcheson H.B., Kuo A.N., Willis A.S., Rubio V., Arvin M.K., Schofield J.P., Dawson E.P. Gene 311:51-57(2003) [PubMed: 12853138] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ALA-344; SER-1376 AND ASN-1406.
[4]	"Cloning of an isoform of CPS1 gene related to spermatogenesis." Huo R., Zhu H., Huang X.Y., Xu Z.Y., Lu L., Xu M., Yin L.L., Li J.M., Zhou Z.M., Sha J.H. Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Testis.
[5]	"Structural organization of the human carbamyl phosphate synthetase I gene (CPS1) and identification of two novel genetic lesions." Funghini S., Donati M.A., Pasquini E., Zammarchi E., Morrone A. Hum. Mutat. 22:340-341(2003) [PubMed: 12955727] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS CPS1D GLY-457 AND ARG-810, VARIANT ASN-1406.
[6]	"Gene structure of human carbamylphosphate synthetase 1 and novel mutations in patients with neonatal onset." Haeberle J., Schmidt E., Pauli S., Rapp B., Christensen E., Wermuth B., Koch H.G. Hum. Mutat. 21:444-444(2003) [PubMed: 12655559] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS CPS1D SER-843 AND GLU-875.
[7]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Testis.
[8]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 795-1500. Tissue: Small intestine.
[10]	"Structural insight on the control of urea synthesis: identification of the binding site for N-acetyl-L-glutamate, the essential allosteric activator of mitochondrial carbamoyl phosphate synthetase." Pekkala S., Martinez A.I., Barcelona B., Gallego J., Bendala E., Yefimenko I., Rubio V., Cervera J. Biochem. J. 424:211-220(2009) [PubMed: 19754428] [Abstract] Cited for: ALLOSTERIC ACTIVATOR NAG BINDING SITE.
[11]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"Crystal structure of MGS domain of carbamoyl-phosphate synthetase from Homo sapiens." RIKEN structural genomics initiative (RSGI) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 1343-1478.
[13]	"Genetic analysis of carbamoylphosphate synthetase I and ornithine transcarbamylase deficiency using fibroblasts." Rapp B., Haberle J., Linnebank M., Wermuth B., Marquardt T., Harms E., Koch H.G. Eur. J. Pediatr. 160:283-287(2001) [PubMed: 11388595] [Abstract] Cited for: VARIANT CPS1D ARG-1054.
[14]	"Novel mutations (H337R and 238-362del) in the CPS1 gene cause carbamoyl phosphate synthetase I deficiency." Aoshima T., Kajita M., Sekido Y., Kikuchi S., Yasuda I., Saheki T., Watanabe K., Shimokata K., Niwa T. Hum. Hered. 52:99-101(2001) [PubMed: 11474210] [Abstract] Cited for: VARIANT CPS1D ARG-337.
[15]	"Neonatal pulmonary hypertension -- urea-cycle intermediates, nitric oxide production, and carbamoyl-phosphate synthetase function." Pearson D.L., Dawling S., Walsh W.F., Haines J.L., Christman B.W., Bazyk A., Scott N., Summar M.L. N. Engl. J. Med. 344:1832-1838(2001) [PubMed: 11407344] [Abstract] Cited for: VARIANT ASN-1406, ASSOCIATION WITH ARGININE LEVELS.
[16]	"Mutational analysis of carbamoylphosphate synthetase I deficiency in three Japanese patients." Wakutani Y., Nakayasu H., Takeshima T., Adachi M., Kawataki M., Kihira K., Sawada H., Bonno M., Yamamoto H., Nakashima K. J. Inherit. Metab. Dis. 27:787-788(2004) [PubMed: 15617192] [Abstract] Cited for: VARIANTS CPS1D HIS-850 AND PRO-918.
[17]	"Genetic approach to prenatal diagnosis in urea cycle defects." Haeberle J., Koch H.G. Prenat. Diagn. 24:378-383(2004) [PubMed: 15164414] [Abstract] Cited for: VARIANTS CPS1D SER-843 AND GLU-875.
[18]	"The frequent observation of evidence for nonsense-mediated decay in RNA from patients with carbamyl phosphate synthetase I deficiency." Eeds A.M., Hall L.D., Yadav M., Willis A., Summar S., Putnam A., Barr F., Summar M.L. Mol. Genet. Metab. 89:80-86(2006) [PubMed: 16737834] [Abstract] Cited for: VARIANTS CPS1D GLU-301; CYS-389; ARG-390; THR-589; SER-640; LYS-716; LEU-805; VAL-911; PRO-958; SER-982; PHE-998; LEU-1089; PRO-1203; ASN-1205; PRO-1331; THR-1378; LEU-1411 AND ALA-1443.
[19]	"Molecular and clinical analyses of Japanese patients with carbamoylphosphate synthetase 1 (CPS1) deficiency." Kurokawa K., Yorifuji T., Kawai M., Momoi T., Nagasaka H., Takayanagi M., Kobayashi K., Yoshino M., Kosho T., Adachi M., Otsuka H., Yamamoto S., Murata T., Suenaga A., Ishii T., Terada K., Shimura N., Kiwaki K. , Shintaku H., Yamakawa M., Nakabayashi H., Wakutani Y., Nakahata T. J. Hum. Genet. 52:349-354(2007) [PubMed: 17310273] [Abstract] Cited for: VARIANTS CPS1D GLU-79; ASN-212; ASN-280; PRO-438; HIS-587; ARG-593; LYS-651; ILE-674; HIS-780; CYS-850; ASP-982; ARG-1103; GLY-1141; PRO-1195; VAL-1215 AND LYS-1241.
[20]	"Understanding carbamoyl-phosphate synthetase I (CPS1) deficiency by using expression studies and structure-based analysis." Pekkala S., Martinez A.I., Barcelona B., Yefimenko I., Finckh U., Rubio V., Cervera J. Hum. Mutat. 31:801-808(2010) [PubMed: 20578160] [Abstract] Cited for: VARIANTS CPS1D PHE-123; ARG-337; ASN-471; PRO-678; LEU-774; LEU-1411; GLN-1453; TRP-1453 AND HIS-1491, VARIANT SER-1376, CHARACTERIZATION OF VARIANTS CPS1D PHE-123; ARG-337; ASN-471; PRO-678; LEU-774; LEU-1411; GLN-1453; TRP-1453 AND HIS-1491, CHARACTERIZATION OF VARIANT SER-1376.
[21]	"The T1405N carbamoyl phosphate synthetase polymorphism does not affect plasma arginine concentrations in preterm infants." Moonen R.M., Reyes I., Cavallaro G., Gonzalez-Luis G., Bakker J.A., Villamor E. PLoS ONE 5:E10792-E10792(2010) [PubMed: 20520828] [Abstract] Cited for: VARIANT ASN-1406, DISEASE.
[22]	"Molecular defects in human carbamoy phosphate synthetase I: mutational spectrum, diagnostic and protein structure considerations." Haberle J., Shchelochkov O.A., Wang J., Katsonis P., Hall L., Reiss S., Eeds A., Willis A., Yadav M., Summar S., Lichtarge O., Rubio V., Wong L.J., Summar M. Hum. Mutat. 32:579-589(2011) [PubMed: 21120950] [Abstract] Cited for: VARIANTS CPS1D VAL-43; ASP-58; PHE-65; GLY-71; SER-87; ASP-89; GLY-165; VAL-224; CYS-233; PRO-243; GLU-258; GLU-263; VAL-304; GLU-317; HIS-358; LEU-382; ARG-401; ARG-431; VAL-432; THR-438; GLU-450; PRO-498; GLU-531; GLY-531; MET-544; CYS-587; HIS-587; LEU-587; LEU-597; MET-622; ASP-628; ARG-632; PRO-638; TYR-648; VAL-654; LYS-674; SER-698; LYS-718; GLN-721; PRO-724; THR-726; VAL-767; HIS-780; ILE-792; SER-803; GLY-803; CYS-803; SER-805; TRP-814; ARG-816; HIS-850; GLU-911; LEU-913; HIS-914; GLY-914; THR-932; THR-949; CYS-959; CYS-962; GLU-978; VAL-982; HIS-984; THR-986; CYS-987; SER-992; SER-1016; LEU-1017; ILE-1022; GLY-1034; ARG-1045; ARG-1059; GLU-1065; CYS-1089; GLU-1155; VAL-1155; LEU-1203; GLN-1228; ASP-1255; GLN-1262; PRO-1262; HIS-1274; ARG-1327; GLU-1333; LEU-1371; MET-1391; VAL-1398; LEU-1439; TRP-1453 AND ARG-1462.
+	Additional computationally mapped references.

Web resources

GeneReviews

LOVD-Leiden Open Variation Database

Carbamoyl-Phosphate Synthetase 1 (CPS1)

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D90282 mRNA. Translation: BAA14328.1.
Y15793 mRNA. Translation: CAA75785.1.
AF154830 mRNA. Translation: AAD38072.1.
AY317138 mRNA. Translation: AAP84318.1.
AY167007 , AY166970, AY166971, AY166972, AY166973, AY166974, AY166975, AY166976, AY166977, AY166978, AY166979, AY166980, AY166981, AY166982, AY166983, AY166984, AY166985, AY166986, AY166987, AY166988, AY166989, AY166990, AY166991, AY166992, AY166993, AY166994, AY166995, AY166996, AY166997, AY166998, AY166999, AY167000, AY167001, AY167002, AY167003, AY167004, AY167005, AY167006 Genomic DNA. Translation: AAO31763.1.
AF536523 Genomic DNA. Translation: AAN77181.1.
AK302778 mRNA. Translation: BAH13804.1.
AC008172 Genomic DNA. No translation available.
BX640601 mRNA. Translation: CAE45707.1.

IPI

IPI00011062.
IPI00397498.

PIR

JQ1348.

RefSeq

NP_001116105.1. NM_001122633.2.
NP_001116106.1. NM_001122634.2.
NP_001866.2. NM_001875.4.

UniGene

Hs.149252.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2YVQ	X-ray	1.98	A	1343-1478	[»]

ProteinModelPortal

P31327.

SMR

P31327. Positions 44-404, 416-820, 971-1478.

ModBase

Search...

Protein-protein interaction databases

IntAct

P31327. 6 interactions.

MINT

MINT-4991575.

STRING

P31327.

Protein family/group databases

MEROPS

C26.951.

PTM databases

PhosphoSite

P31327.

Polymorphism databases

DMDM

4033707.

Proteomic databases

PRIDE

P31327.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000233072; ENSP00000233072; ENSG00000021826.
ENST00000430249; ENSP00000402608; ENSG00000021826.
ENST00000451903; ENSP00000406136; ENSG00000021826.

GeneID

1373.

KEGG

hsa:1373.

UCSC

uc002vee.2. human.
uc010fus.1. human.

Organism-specific databases

CTD

1373.

GeneCards

GC02P211342.

HGNC

HGNC:2323. CPS1.

HPA

CAB003781.
HPA021400.

MIM

237300. phenotype.
608307. gene.

neXtProt

NX_P31327.

Orphanet

147. Carbamoylphosphate synthetase deficiency.

PharmGKB

PA26840.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG04683.

GeneTree

ENSGT00390000015604.

HOVERGEN

HBG000279.

InParanoid

P31327.

OrthoDB

EOG45MN4G.

PhylomeDB

P31327.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-11364.

BRENDA

6.3.4.16. 2681.

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

P31327.

Bgee

P31327.

CleanEx

HS_CPS1.

Genevestigator

P31327.

GermOnline

ENSG00000021826. Homo sapiens.

Family and domain databases

InterPro

IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006275. CarbamoylP_synth_lsu.
IPR005479. CarbamoylP_synth_lsu_ATP-bd.
IPR005483. CarbamoylP_synth_lsu_CPS-dom.
IPR005481. CarbamoylP_synth_lsu_N.
IPR005480. CarbamoylP_synth_lsu_oligo.
IPR006274. CarbamoylP_synth_ssu.
IPR002474. CarbamoylP_synth_ssu_N.
IPR017926. GATASE_1.
IPR011607. MGS-like_dom.
IPR013817. Pre-ATP_grasp.
IPR016185. PreATP-grasp-like.
[Graphical view]

Gene3D

G3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 2 hits.
G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 2 hits.
G3DSA:1.10.1030.10. CarbamoylP_synth_lsu_oligo. 1 hit.
G3DSA:3.50.30.20. G3DSA:3.50.30.20. 1 hit.
G3DSA:3.40.50.1380. MGS-like_dom. 1 hit.
G3DSA:3.40.50.20. Pre-ATP_grasp. 2 hits.

KO

K01948.

Pfam

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]

PRINTS

PR00098. CPSASE.

SMART

SM01096. CPSase_L_D3. 1 hit.
SM01097. CPSase_sm_chain. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]

SUPFAM

SSF48108. CarbamoylP_synth_lsu_oligo. 1 hit.
SSF52021. CP_synthsmall. 1 hit.
SSF52335. MGS-like_dom. 1 hit.
SSF52440. PreATP-grasp-like. 2 hits.

TIGRFAMs

TIGR01369. CPSaseII_lrg. 1 hit.
TIGR01368. CPSaseIIsmall. 1 hit.

PROSITE

PS50975. ATP_GRASP. 2 hits.
PS00866. CPSASE_1. 2 hits.
PS00867. CPSASE_2. 2 hits.
PS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]

ProtoNet

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Other

NextBio

5565.

SOURCE

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Entry information

Entry name

CPSM_HUMAN

Accession

Primary (citable) accession number: P31327
Secondary accession number(s): B7Z818, O43774, Q7Z5I5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	December 15, 1998
Last modified:	January 25, 2012
This is version 143 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.