P00966 (ASSY_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Argininosuccinate synthase
EC=6.3.4.5

Alternative name(s):
Citrulline--aspartate ligase

Gene names

Name:	ASS1
Synonyms:	ASS

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	412 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Is indirectly involved in the control of blood pressure By similarity.
Catalytic activity	ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate.
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. Nitrogen metabolism; urea cycle; (N(omega)-L-arginino)succinate from L-aspartate and L-citrulline: step 1/1.
Subunit structure	Homotetramer. Interacts with NMRAL1. Ref.9 Ref.12
Involvement in disease	Citrullinemia 1 (CTLN1) [MIM:215700]: The classic form of citrullinemia, an autosomal recessive disease characterized primarily by elevated serum and urine citrulline levels. Ammonia intoxication is another manifestation. It is a disorder of the urea cycle, usually manifesting in the first few days of life. Affected infants appear normal at birth, but as ammonia builds up in the body they present symptoms such as lethargy, poor feeding, vomiting, seizures and loss of consciousness. Less commonly, a milder form can develop later in childhood or adulthood. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21
Sequence similarities	Belongs to the argininosuccinate synthase family. Type 1 subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis Urea cycle
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	arginine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway urea cycle Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW argininosuccinate synthase activity Inferred from experiment. Source: Reactome
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARAF	P10398	4	EBI-536842,EBI-365961

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 412

412

Argininosuccinate synthase

PRO_0000148554

Regions

Nucleotide binding

10 – 18

9

ATP By similarity

Nucleotide binding

115 – 123

9

ATP By similarity

Sites

Binding site

36

1

ATP; via amide nitrogen and carbonyl oxygen By similarity

Binding site

87

1

Citrulline

Binding site

92

1

Citrulline

Binding site

119

1

Aspartate

Binding site

123

1

Aspartate

Binding site

123

1

Citrulline

Binding site

124

1

Aspartate

Binding site

127

1

Citrulline

Binding site

180

1

Citrulline

Binding site

189

1

Citrulline

Binding site

270

1

Citrulline

Binding site

282

1

Citrulline

Amino acid modifications

Modified residue

180

1

Phosphoserine Ref.10

Modified residue

219

1

Phosphothreonine Ref.10

Natural variations

Natural variant

14

1

G → S in CTLN1. Ref.14 Ref.20

VAR_000681

Natural variant

18

1

S → L in CTLN1. Ref.15

VAR_000682

Natural variant

19

1

C → R in CTLN1. Ref.19

VAR_015891

Natural variant

40

1

Q → L in CTLN1. Ref.20

VAR_058337

Natural variant

65

1

S → I.
Corresponds to variant rs2229556 [ dbSNP | Ensembl ].

VAR_050427

Natural variant

69

1

V → A in CTLN1. Ref.18

VAR_016013

Natural variant

79

1

S → P in CTLN1.

VAR_058338

Natural variant

86

1

R → C in CTLN1. Ref.15

VAR_000683

Natural variant

86

1

R → H in CTLN1. Ref.19

VAR_015892

Natural variant

95

1

R → S in CTLN1. Ref.19

VAR_015893

Natural variant

96

1

P → H in CTLN1.

VAR_058339

Natural variant

96

1

P → S in CTLN1. Ref.19

VAR_015894

Natural variant

108

1

R → L in CTLN1. Ref.3 Ref.18
Corresponds to variant rs35269064 [ dbSNP | Ensembl ].

VAR_016014

Natural variant

117

1

G → D in CTLN1. Ref.18 Ref.19

VAR_015896

Natural variant

117

1

G → S in CTLN1. Ref.19

VAR_015895

Natural variant

118

1

A → T in CTLN1. Ref.16

VAR_000684

Natural variant

119

1

T → I in CTLN1. Ref.18

VAR_016015

Natural variant

124

1

D → N in CTLN1. Ref.21

VAR_058340

Natural variant

127

1

R → Q in CTLN1. Ref.20

VAR_058341

Natural variant

127

1

R → W in CTLN1; severe clinical course.

VAR_058342

Natural variant

157

1

R → C in CTLN1. Ref.19

VAR_015897

Natural variant

157

1

R → H in CTLN1. Ref.14 Ref.21

VAR_000685

Natural variant

160

1

L → P in CTLN1.

VAR_058343

Natural variant

179

1

W → R in CTLN1; mild. Ref.3 Ref.19 Ref.20

VAR_015898

Natural variant

180

1

S → N in CTLN1. Ref.14

VAR_000686

Natural variant

190

1

Y → D in CTLN1. Ref.20

VAR_058344

Natural variant

191

1

E → K in CTLN1. Ref.19

VAR_015899

Natural variant

191

1

E → Q in CTLN1.

VAR_058345

Natural variant

192

1

A → V in CTLN1. Ref.16

VAR_000687

Natural variant

202

1

A → E in CTLN1.

VAR_058346

Natural variant

206

1

L → P in CTLN1.

VAR_058347

Natural variant

263

1

V → M in CTLN1; mild clinical course. Ref.20

VAR_058348

Natural variant

265

1

R → C in CTLN1; severe clinical course.

VAR_058349

Natural variant

265

1

R → H in CTLN1. Ref.19

VAR_015900

Natural variant

269

1

V → M in CTLN1. Ref.19 Ref.20

VAR_015901

Natural variant

270

1

E → Q in CTLN1. Ref.18 Ref.21

VAR_016007

Natural variant

272

1

R → C in CTLN1. Ref.16 Ref.19

VAR_000688

Natural variant

277

1

K → T in CTLN1.

VAR_058350

Natural variant

279

1

R → Q in CTLN1. Ref.21

VAR_016008

Natural variant

280

1

G → R in CTLN1. Ref.16

VAR_000689

Natural variant

283

1

E → K in CTLN1. Ref.19 Ref.21

VAR_015902

Natural variant

284

1

T → I in CTLN1; mild clinical course.

VAR_058351

Natural variant

291

1

Y → S in CTLN1.

VAR_058352

Natural variant

296

1

D → G in CTLN1.

VAR_058353

Natural variant

302

1

M → V in CTLN1.

VAR_058354

Natural variant

304

1

R → W in CTLN1. Ref.14 Ref.16 Ref.19

VAR_000690

Natural variant

307

1

R → C in CTLN1.

VAR_058355

Natural variant

310

1

K → Q in CTLN1. Ref.19

VAR_016009

Natural variant

310

1

K → R in CTLN1.

VAR_015903

Natural variant

324

1

G → S in CTLN1. Ref.14 Ref.19 Ref.20 Ref.21

VAR_000691

Natural variant

324

1

G → V in CTLN1.

VAR_058356

Natural variant

341

1

S → F in CTLN1.

VAR_058357

Natural variant

345

1

V → G in CTLN1.

VAR_058358

Natural variant

347

1

G → R in CTLN1; severe clinical course.

VAR_058359

Natural variant

359

1

Y → D in CTLN1; mild clinical course.

VAR_058360

Natural variant

362

1

G → V in CTLN1; mild. Ref.3 Ref.19 Ref.20

VAR_015904

Natural variant

363

1

R → G in CTLN1. Ref.21

VAR_016010

Natural variant

363

1

R → L in CTLN1. Ref.16

VAR_000692

Natural variant

363

1

R → Q in CTLN1. Ref.19

VAR_016011

Natural variant

363

1

R → W in CTLN1. Ref.14 Ref.19

VAR_000693

Natural variant

389

1

T → I in CTLN1. Ref.19

VAR_016012

Natural variant

390

1

G → R in CTLN1. Ref.3 Ref.14 Ref.18 Ref.19 Ref.21

VAR_000694

Experimental info

Sequence conflict

325 – 327

3

FWH → LRP in CAA25771. Ref.1

Sequence conflict

325 – 327

3

FWH → LRP in AAA51783. Ref.2

Secondary structure

1

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412

Helix Strand Turn

Details...

Beta strand

5 – 10

6

Helix

15 – 26

12

Beta strand

29 – 39

11

Helix

44 – 54

11

Beta strand

57 – 63

7

Helix

65 – 71

7

Helix

73 – 78

6

Turn

84 – 86

3

Turn

90 – 93

4

Helix

94 – 109

16

Beta strand

112 – 115

4

Helix

124 – 135

12

Beta strand

140 – 142

3

Helix

144 – 146

3

Helix

148 – 151

4

Helix

158 – 166

9

Beta strand

181 – 183

3

Beta strand

188 – 190

3

Helix

193 – 196

4

Helix

204 – 206

3

Turn

213 – 215

3

Beta strand

221 – 228

8

Beta strand

231 – 237

7

Turn

238 – 240

3

Helix

247 – 261

15

Beta strand

265 – 271

7

Beta strand

277 – 283

7

Helix

285 – 301

17

Helix

304 – 323

20

Beta strand

326 – 328

3

Helix

329 – 341

13

Turn

342 – 344

3

Beta strand

347 – 354

8

Beta strand

357 – 364

8

Helix

372 – 375

4

Helix

385 – 404

20

Sequences

	Sequence		Length	Mass (Da)
	P00966 [UniParc]. Last modified April 3, 2002. Version 2. Checksum: 47CAD2373AE47E47	FASTA	412	46,530
	10 20 30 40 50 60 MSSKGSVVLA YSGGLDTSCI LVWLKEQGYD VIAYLANIGQ KEDFEEARKK ALKLGAKKVF 70 80 90 100 110 120 IEDVSREFVE EFIWPAIQSS ALYEDRYLLG TSLARPCIAR KQVEIAQREG AKYVSHGATG 130 140 150 160 170 180 KGNDQVRFEL SCYSLAPQIK VIAPWRMPEF YNRFKGRNDL MEYAKQHGIP IPVTPKNPWS 190 200 210 220 230 240 MDENLMHISY EAGILENPKN QAPPGLYTKT QDPAKAPNTP DILEIEFKKG VPVKVTNVKD 250 260 270 280 290 300 GTTHQTSLEL FMYLNEVAGK HGVGRIDIVE NRFIGMKSRG IYETPAGTIL YHAHLDIEAF 310 320 330 340 350 360 TMDREVRKIK QGLGLKFAEL VYTGFWHSPE CEFVRHCIAK SQERVEGKVQ VSVLKGQVYI 370 380 390 400 410 LGRESPLSLY NEELVSMNVQ GDYEPTDATG FININSLRLK EYHRLQSKVT AK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence for human argininosuccinate synthetase cDNA." Bock H.-G.O., Su T.-S., O'Brien W.E., Beaudet A.L. Nucleic Acids Res. 11:6505-6512(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Molecular structures of human argininosuccinate synthetase pseudogenes. Evolutionary and mechanistic implications." Freytag S.O., Bock H.-G.O., Beaudet A.L., O'Brien W.E. J. Biol. Chem. 259:3160-3166(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Structure of the human argininosuccinate synthetase gene and an improved system for molecular diagnostics in patients with classical and mild citrullinemia." Haeberle J., Pauli S., Linnebank M., Kleijer W.J., Bakker H.D., Wanders R.J.A., Harms E., Koch H.G. Hum. Genet. 110:327-333(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CTLN1 LEU-108; ARG-179; VAL-362 AND ARG-390.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Small intestine.
[5]	"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]. Tissue: Kidney and Muscle.
[6]	"Structure of the 5' end region of the human argininosuccinate synthetase gene." Jinno Y., Nomiyama H., Matuo S., Shimada K., Matsuda I., Saheki T. J. Inherit. Metab. Dis. 8:157-159(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
[7]	"Identification of essential arginine residue(s) for Mg-ATP binding of human argininosuccinate synthetase." Isashiki Y., Noda T., Kobayashi K., Sase M., Saheki T., Titani K. Protein Seq. Data Anal. 2:283-287(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 148-161.
[8]	"A two-dimensional gel database of human colon carcinoma proteins." Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J. Electrophoresis 18:605-613(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 200-209. Tissue: Colon carcinoma.
[9]	"Restructuring of the dinucleotide-binding fold in an NADP(H) sensor protein." Zheng X., Dai X., Zhao Y., Chen Q., Lu F., Yao D., Yu Q., Liu X., Zhang C., Gu X., Luo M. Proc. Natl. Acad. Sci. U.S.A. 104:8809-8814(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NMRAL1.
[10]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180 AND THR-219, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"Structure of human argininosuccinate synthetase." Karlberg T., Collins R., van den Berg S., Flores A., Hammarstrom M., Hogbom M., Holmberg Schiavone L., Uppenberg J. Acta Crystallogr. D 64:279-286(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH CITRULLINE AND ASPARTATE, SUBUNIT.
[13]	"Mutations and polymorphisms in the human argininosuccinate synthetase (ASS1) gene." Engel K., Hoehne W., Haeberle J. Hum. Mutat. 30:300-307(2009) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON VARIANTS.
[14]	"Heterogeneity of mutations in argininosuccinate synthetase causing human citrullinemia." Kobayashi K., Jackson M.J., Tick D.B., O'Brien W.E., Beaudet A.L. J. Biol. Chem. 265:11361-11367(1990) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CTLN1 SER-14; HIS-157; ASN-180; TRP-304; SER-324; TRP-363 AND ARG-390.
[15]	"Additional mutations in argininosuccinate synthetase causing citrullinemia." Kobayashi K., Rosenbloom C., Beaudet A.L., O'Brien W.E. Mol. Biol. Med. 8:95-100(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CTLN1 LEU-18 AND CYS-86.
[16]	"Mutations in argininosuccinate synthetase mRNA of Japanese patients, causing classical citrullinemia." Kobayashi K., Shaheen N., Terazono H., Saheki T. Am. J. Hum. Genet. 55:1103-1112(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CTLN1 THR-118; VAL-192; CYS-272; ARG-280; TRP-304 AND LEU-363.
[17]	"Characterization of human wild-type and mutant argininosuccinate synthetase proteins expressed in bacterial cells." Shaheen N., Kobayashi K., Terazono H., Fukushige T., Horiuchi M., Saheki T. Enzyme Protein 48:251-264(1994) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF SOME CTLN1 VARIANTS.
[18]	"Phenotype and genotype heterogeneity in Mediterranean citrullinemia." Vilaseca M.A., Kobayashi K., Briones P., Lambruschini N., Campistol J., Tabata A., Alomar A., Rodes M., Lluch M., Saheki T. Mol. Genet. Metab. 74:396-398(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CTLN1 ALA-69; LEU-108; ASP-117; ILE-119; GLN-270 AND ARG-390.
[19]	"Identification of 16 novel mutations in the argininosuccinate synthetase gene and genotype-phenotype correlation in 38 classical citrullinemia patients." Gao H.-Z., Kobayashi K., Tabata A., Tsuge H., Iijima M., Yasuda T., Kalkanoglu H.S., Dursun A., Tokatli A., Coskun T., Trefz F.K., Skladal D., Mandel H., Seidel J., Kodama S., Shirane S., Ichida T., Makino S. , Yoshino M., Kang J.-H., Mizuguchi M., Barshop B.A., Fuchinoue S., Seneca S., Zeesman S., Knerr I., Rodes M., Wasant P., Yoshida I., De Meirleir L., Abdul-Jalil M., Begum L., Horiuchi M., Katunuma N., Nakagawa S., Saheki T. Hum. Mutat. 22:24-34(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CTLN1 ARG-19; HIS-86; SER-95; SER-96; ASP-117; SER-117; CYS-157; ARG-179; LYS-191; HIS-265; MET-269; CYS-272; LYS-283; TRP-304; GLN-310; SER-324; VAL-362; GLN-363; TRP-363; ILE-389 AND ARG-390.
[20]	"Mild citrullinemia in Caucasians is an allelic variant of argininosuccinate synthetase deficiency (citrullinemia type 1)." Haeberle J., Pauli S., Schmidt E., Schulze-Eilfing B., Berning C., Koch H.G. Mol. Genet. Metab. 80:302-306(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CTLN1 SER-14; LEU-40; GLN-127; ARG-179; ASP-190; MET-263; MET-269; SER-324 AND VAL-362.
[21]	"Prenatal diagnosis of citrullinemia and argininosuccinic aciduria: evidence for a transmission ratio distortion in citrullinemia." Kleijer W.J., Garritsen V.H., van der Sterre M.L., Berning C., Haeberle J., Huijmans J.G.M. Prenat. Diagn. 26:242-247(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CTLN1 ASN-124; HIS-157; GLN-270; GLN-279; LYS-283; SER-324; GLY-363 AND ARG-390.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X01630 mRNA. Translation: CAA25771.1.
L00084 , L00079, L00080, L00081, L00082, L00083 Genomic DNA. Translation: AAA51783.1.
AY034076 Genomic DNA. Translation: AAK67487.1.
AK027126 mRNA. No translation available.
BC009243 mRNA. Translation: AAH09243.1.
BC021676 mRNA. Translation: AAH21676.1.
M34903 Genomic DNA. Translation: AAA51782.1.

IPI

IPI00020632.

PIR

AJHURS. A01195.

RefSeq

NP_000041.2. NM_000050.4.
NP_446464.1. NM_054012.3.

UniGene

Hs.160786.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2NZ2	X-ray	2.40	A	1-412	[»]

ProteinModelPortal

P00966.

ModBase

Search...

Protein-protein interaction databases

IntAct

P00966. 11 interactions.

MINT

MINT-5000467.

STRING

9606.ENSP00000253004.

PTM databases

PhosphoSite

P00966.

Polymorphism databases

DMDM

20141195.

Proteomic databases

PaxDb

P00966.

PRIDE

P00966.

Protocols and materials databases

DNASU

445.

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000334909; ENSP00000361470; ENSG00000130707.
ENST00000352480; ENSP00000253004; ENSG00000130707.
ENST00000372393; ENSP00000361469; ENSG00000130707.
ENST00000372394; ENSP00000361471; ENSG00000130707.

GeneID

445.

KEGG

hsa:445.

UCSC

uc004bzm.3. human.

Organism-specific databases

CTD

445.

GeneCards

GC09P133320.

H-InvDB

HIX0025782.

HGNC

HGNC:758. ASS1.

HPA

HPA020896.
HPA020934.

MIM

215700. phenotype.
603470. gene.

neXtProt

NX_P00966.

Orphanet

247546. Acute neonatal citrullinemia type I.
247573. Adult-onset citrullinemia type I.

PharmGKB

PA162376926.

GenAtlas

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Phylogenomic databases

eggNOG

COG0137.

HOGENOM

HOG000230093.

HOVERGEN

HBG001717.

InParanoid

P00966.

KO

K01940.

OMA

NDQFRFE.

OrthoDB

EOG45B1FK.

PhylomeDB

P00966.

Enzyme and pathway databases

BioCyc

MetaCyc:HS05425-MONOMER.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P00966.

UniPathway

UPA00068; UER00113.
UPA00158; UER00272.

Gene expression databases

ArrayExpress

P00966.

Bgee

P00966.

CleanEx

HS_ASS1.

Genevestigator

P00966.

GermOnline

ENSG00000130707. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.

InterPro

IPR001518. Arginosuc_synth.
IPR018223. Arginosuc_synth_CS.
IPR023434. Arginosuc_synth_type_1_subfam.
IPR024074. AS_cat/multimer_dom_body.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]

PANTHER

PTHR11587. PTHR11587. 1 hit.

Pfam

PF00764. Arginosuc_synth. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00032. argG. 1 hit.

PROSITE

PS00564. ARGININOSUCCIN_SYN_1. 1 hit.
PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
[Graphical view]

ProtoNet

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Other

DrugBank

DB00171. Adenosine triphosphate.
DB00125. L-Arginine.
DB00128. L-Aspartic Acid.
DB00155. L-Citrulline.

EvolutionaryTrace

P00966.

GenomeRNAi

445.

NextBio

1871.

SOURCE

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Entry information

Entry name

ASSY_HUMAN

Accession

Primary (citable) accession number: P00966
Secondary accession number(s): Q6LDL2, Q86UZ0, Q96GT4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	April 3, 2002
Last modified:	May 1, 2013
This is version 155 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.