P05089 (ARGI1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Arginase-1
EC=3.5.3.1

Alternative name(s):
Liver-type arginase
Type I arginase

Gene names

Name:

ARG1

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	322 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	L-arginine + H2O = L-ornithine + urea.
Cofactor	Binds 2 manganese ions per subunit.
Pathway	Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1.
Subunit structure	Homotrimer. Ref.7 Ref.9 Ref.11
Subcellular location	Cytoplasm Ref.9.
Induction	By arginine or homoarginine.
Involvement in disease	Argininemia (ARGIN) [MIM:207800]: A rare autosomal recessive disorder of the urea cycle. Arginine is elevated in the blood and cerebrospinal fluid, and periodic hyperammonemia occurs. Clinical manifestations include developmental delay, seizures, mental retardation, hypotonia, ataxia and progressive spastic quadriplegia. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13 Ref.15
Sequence similarities	Belongs to the arginase family.

Ontologies

Keywords
Biological process	Arginine metabolism Urea cycle
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Ligand	Manganese Metal-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	arginine catabolic process Traceable author statement Ref.1. Source: ProtInc cellular response to dexamethasone stimulus Inferred from electronic annotation. Source: Compara cellular response to glucagon stimulus Inferred from electronic annotation. Source: Compara cellular response to hydrogen peroxide Inferred from electronic annotation. Source: Compara cellular response to lipopolysaccharide Inferred from electronic annotation. Source: Compara cellular response to transforming growth factor beta stimulus Inferred from electronic annotation. Source: Compara collagen biosynthetic process Inferred from electronic annotation. Source: Compara liver development Inferred from electronic annotation. Source: Compara lung development Inferred from electronic annotation. Source: Compara mammary gland involution Inferred from electronic annotation. Source: Compara maternal process involved in female pregnancy Inferred from electronic annotation. Source: Compara positive regulation of endothelial cell proliferation Inferred from electronic annotation. Source: Compara protein homotrimerization Inferred from electronic annotation. Source: Compara regulation of L-arginine import Inferred from electronic annotation. Source: Compara response to amine stimulus Inferred from electronic annotation. Source: Compara response to amino acid stimulus Inferred from electronic annotation. Source: Compara response to axon injury Inferred from electronic annotation. Source: Compara response to cadmium ion Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to herbicide Inferred from electronic annotation. Source: Compara response to manganese ion Inferred from electronic annotation. Source: Compara response to methylmercury Inferred from electronic annotation. Source: Compara response to selenium ion Inferred from electronic annotation. Source: Compara response to vitamin A Inferred from electronic annotation. Source: Compara response to vitamin E Inferred from electronic annotation. Source: Compara response to zinc ion Inferred from electronic annotation. Source: Compara urea cycle Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome extracellular space Inferred from electronic annotation. Source: Compara neuron projection Inferred from electronic annotation. Source: Compara neuronal cell body Inferred from electronic annotation. Source: Compara
Molecular_function	arginase activity Inferred from experiment. Source: Reactome manganese ion binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P05089-1)

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: P05089-2)

Also known as: Erythroid variant;

The sequence of this isoform differs from the canonical sequence as follows:
     43-43: Q → QVTQNFLIL

Note: May be due to a competing acceptor splice site. No experimental confirmation available.

Isoform 3 (identifier: P05089-3)

The sequence of this isoform differs from the canonical sequence as follows:
     204-289: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 322

322

Arginase-1

PRO_0000173693

Regions

Region

126 – 130

5

Substrate binding

Region

137 – 139

3

Substrate binding

Sites

Metal binding

101

1

Manganese 1

Metal binding

124

1

Manganese 1

Metal binding

124

1

Manganese 2

Metal binding

126

1

Manganese 2

Metal binding

128

1

Manganese 1

Metal binding

232

1

Manganese 1

Metal binding

232

1

Manganese 2

Metal binding

234

1

Manganese 2

Binding site

183

1

Substrate

Amino acid modifications

Modified residue

230

1

Phosphoserine By similarity

Natural variations

Alternative sequence

43

1

Q → QVTQNFLIL in isoform 2.

VSP_009330

Alternative sequence

204 – 289

86

Missing in isoform 3.

VSP_009331

Natural variant

11

1

I → T in ARGIN; 12% of wild-type activity. Ref.15
Corresponds to variant rs28941474 [ dbSNP | Ensembl ].

VAR_015594

Natural variant

138

1

G → V in ARGIN. Ref.15

VAR_015595

Natural variant

235

1

G → R in ARGIN. Ref.13

VAR_000674

Natural variant

290

1

T → S. Ref.14

VAR_000675

Experimental info

Sequence conflict

48

1

K → E in AAL71547. Ref.3

Sequence conflict

86

1

E → Q in AAA51776. Ref.1

Sequence conflict

202

1

E → K in AAL71547. Ref.3

Secondary structure

1

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322

Helix Strand Turn

Details...

Beta strand

7 – 13

7

Helix

22 – 26

5

Helix

27 – 33

7

Helix

36 – 42

7

Beta strand

46 – 52

7

Beta strand

67 – 69

3

Helix

70 – 89

20

Beta strand

93 – 99

7

Helix

101 – 103

3

Helix

104 – 114

11

Beta strand

119 – 126

8

Turn

132 – 134

3

Helix

140 – 142

3

Helix

144 – 148

5

Helix

150 – 152

3

Turn

153 – 155

3

Helix

171 – 173

3

Beta strand

174 – 179

6

Helix

184 – 193

10

Beta strand

196 – 199

4

Helix

200 – 206

7

Helix

208 – 220

13

Beta strand

221 – 223

3

Beta strand

227 – 232

6

Helix

233 – 235

3

Turn

238 – 240

3

Beta strand

243 – 246

4

Helix

254 – 267

14

Beta strand

270 – 276

7

Helix

280 – 282

3

Helix

286 – 303

18

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 11, 2001. Version 2. Checksum: 8F3BE2652243F622	FASTA	322	34,735
	10 20 30 40 50 60 MSAKSRTIGI IGAPFSKGQP RGGVEEGPTV LRKAGLLEKL KEQECDVKDY GDLPFADIPN 70 80 90 100 110 120 DSPFQIVKNP RSVGKASEQL AGKVAEVKKN GRISLVLGGD HSLAIGSISG HARVHPDLGV 130 140 150 160 170 180 IWVDAHTDIN TPLTTTSGNL HGQPVSFLLK ELKGKIPDVP GFSWVTPCIS AKDIVYIGLR 190 200 210 220 230 240 DVDPGEHYIL KTLGIKYFSM TEVDRLGIGK VMEETLSYLL GRKKRPIHLS FDVDGLDPSF 250 260 270 280 290 300 TPATGTPVVG GLTYREGLYI TEEIYKTGLL SGLDIMEVNP SLGKTPEEVT RTVNTAVAIT 310 320 LACFGLAREG NHKPIDYLNP PK
	Isoform 2 (Erythroid variant) [UniParc]. Checksum: 3547D8B6C254179B	FASTA	330	35,664
	10 20 30 40 50 60 MSAKSRTIGI IGAPFSKGQP RGGVEEGPTV LRKAGLLEKL KEQVTQNFLI LECDVKDYGD 70 80 90 100 110 120 LPFADIPNDS PFQIVKNPRS VGKASEQLAG KVAEVKKNGR ISLVLGGDHS LAIGSISGHA 130 140 150 160 170 180 RVHPDLGVIW VDAHTDINTP LTTTSGNLHG QPVSFLLKEL KGKIPDVPGF SWVTPCISAK 190 200 210 220 230 240 DIVYIGLRDV DPGEHYILKT LGIKYFSMTE VDRLGIGKVM EETLSYLLGR KKRPIHLSFD 250 260 270 280 290 300 VDGLDPSFTP ATGTPVVGGL TYREGLYITE EIYKTGLLSG LDIMEVNPSL GKTPEEVTRT 310 320 330 VNTAVAITLA CFGLAREGNH KPIDYLNPPK
	Isoform 3 [UniParc]. Checksum: 79F02C69B700AB67	FASTA	236	25,356
	10 20 30 40 50 60 MSAKSRTIGI IGAPFSKGQP RGGVEEGPTV LRKAGLLEKL KEQECDVKDY GDLPFADIPN 70 80 90 100 110 120 DSPFQIVKNP RSVGKASEQL AGKVAEVKKN GRISLVLGGD HSLAIGSISG HARVHPDLGV 130 140 150 160 170 180 IWVDAHTDIN TPLTTTSGNL HGQPVSFLLK ELKGKIPDVP GFSWVTPCIS AKDIVYIGLR 190 200 210 220 230 DVDPGEHYIL KTLGIKYFSM TEVTRTVNTA VAITLACFGL AREGNHKPID YLNPPK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and nucleotide sequence of cDNA for human liver arginase." Haraguchi Y., Takiguchi M., Amaya Y., Kawamoto S., Matsuda I., Mori M. Proc. Natl. Acad. Sci. U.S.A. 84:412-415(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Liver.
[2]	"Human liver-type arginase gene: structure of the gene and analysis of the promoter region." Takiguchi M., Haraguchi Y., Mori M. Nucleic Acids Res. 16:8789-8802(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Blood.
[3]	Lee Y.T., Miller J.L. Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Erythroblast.
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[5]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] (ISOFORMS 1 AND 3). Tissue: Liver and Skeletal muscle.
[7]	"Expression of human liver arginase in Escherichia coli. Purification and properties of the product." Ikemoto M., Tabata M., Miyake T., Kono T., Mori M., Totani M., Murachi T. Biochem. J. 270:697-703(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-13, SUBUNIT. Tissue: Liver.
[8]	"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].
[9]	"Crystal structure of human arginase I at 1.29-A resolution and exploration of inhibition in the immune response." Di Costanzo L., Sabio G., Mora A., Rodriguez P.C., Ochoa A.C., Centeno F., Christianson D.W. Proc. Natl. Acad. Sci. U.S.A. 102:13058-13063(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.29 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS AND THE SYNTHETIC INHIBITOR 2(S)-AMINO-6-BORONOHEXANOIC ACID, SUBCELLULAR LOCATION, SUBUNIT.
[10]	"Expression, purification, assay, and crystal structure of perdeuterated human arginase I." Di Costanzo L., Moulin M., Haertlein M., Meilleur F., Christianson D.W. Arch. Biochem. Biophys. 465:82-89(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS AND THE SYNTHETIC INHIBITOR 2(S)-AMINO-6-BORONOHEXANOIC ACID, MASS SPECTROMETRY.
[11]	"Crystal structure of human arginase I complexed with thiosemicarbazide reveals an unusual thiocarbonyl mu-sulfide ligand in the binuclear manganese cluster." Di Costanzo L., Pique M.E., Christianson D.W. J. Am. Chem. Soc. 129:6388-6389(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS AND THIOSEMICARBAZIDE, SUBUNIT.
[12]	"Synthesis of (2S)-2-amino-7,8-epoxyoctanoic acid and structure of its metal-bridging complex with human arginase I." Zakharian T.Y., Di Costanzo L., Christianson D.W. Org. Biomol. Chem. 6:3240-3243(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.51 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS AND THE SYNTHETIC INHIBITOR (2S)-2-AMINO-7,8-EPOXYOCTANOIC ACID.
[13]	"Three novel mutations in the liver-type arginase gene in three unrelated Japanese patients with argininemia." Uchino T., Haraguchi Y., Aparicio J.M., Mizutani N., Higashikawa M., Naitoh H., Mori M., Matsuda I. Am. J. Hum. Genet. 51:1406-1412(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ARGIN ARG-235.
[14]	"Molecular genetic study of human arginase deficiency." Grody W.W., Klein D., Dodson A.E., Kern R.M., Wissmann P.B., Goodman B.K., Bassand P., Marescau B., Kang S.-S., Leonard J.V., Cederbaum S.D. Am. J. Hum. Genet. 50:1281-1290(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SER-290.
[15]	"Molecular basis of phenotypic variation in patients with argininemia." Uchino T., Snyderman S.E., Lambert M., Qureshi I.A., Shapira S.K., Sansaricq C., Smit L.M.E., Jakobs C., Matsuda I. Hum. Genet. 96:255-260(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ARGIN THR-11 AND VAL-138.
+	Additional computationally mapped references.

Web resources

GeneReviews

Wikipedia

Arginase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M14502 mRNA. Translation: AAA51776.1.
X12662 , X12663, X12664, X12665, X12666, X12667, X12668, X12669 Genomic DNA. Translation: CAA31188.1.
AY074488 mRNA. Translation: AAL71547.1.
BT006741 mRNA. Translation: AAP35387.1.
AL121575 Genomic DNA. Translation: CAB92071.1.
AL121575 Genomic DNA. Translation: CAI23317.1.
AL121575 Genomic DNA. Translation: CAI23318.1.
BC005321 mRNA. Translation: AAH05321.1.
BC020653 mRNA. Translation: AAH20653.1.

IPI

IPI00038356.
IPI00291560.
IPI00398768.

PIR

A26370. S02132.

RefSeq

NP_000036.2. NM_000045.3.
NP_001231367.1. NM_001244438.1.

UniGene

Hs.440934.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WVA	X-ray	1.94	A/B	1-322	[»]
1WVB	X-ray	2.30	A/B	1-322	[»]
2AEB	X-ray	1.29	A/B	1-322	[»]
2PHA	X-ray	1.90	A/B	1-322	[»]
2PHO	X-ray	1.95	A/B	1-322	[»]
2PLL	X-ray	1.90	A/B	1-322	[»]
2ZAV	X-ray	1.70	A/B	1-322	[»]
3DJ8	X-ray	1.51	A/B	1-322	[»]
3E6K	X-ray	2.10	A/B	1-322	[»]
3E6V	X-ray	1.72	A/B	1-322	[»]
3F80	X-ray	1.60	A/B	1-322	[»]
3GMZ	X-ray	1.43	A/B	1-322	[»]
3GN0	X-ray	1.70	A/B	1-322	[»]
3KV2	X-ray	1.55	A/B	1-322	[»]
3LP4	X-ray	1.90	A/B	1-322	[»]
3LP7	X-ray	2.04	A/B	1-322	[»]
3MFV	X-ray	1.90	A/B	1-322	[»]
3MFW	X-ray	1.47	A/B	1-322	[»]
3MJL	X-ray	1.90	A/B	1-322	[»]
3SJT	X-ray	1.60	A/B	1-322	[»]
3SKK	X-ray	1.70	A/B	1-322	[»]
3TF3	X-ray	1.64	A/B	1-322	[»]
3TH7	X-ray	2.10	A/B	1-322	[»]
3THE	X-ray	1.97	A/B	1-322	[»]
3THH	X-ray	1.85	A/B	1-322	[»]
3THJ	X-ray	1.50	A/B	1-322	[»]
4FCI	X-ray	1.82	A/B	1-322	[»]
4FCK	X-ray	1.90	A/B	1-322	[»]
4GSM	X-ray	1.70	A/B	1-322	[»]
4GSV	X-ray	1.48	A/B	1-322	[»]
4GSZ	X-ray	2.20	A/B	1-322	[»]
4GWC	X-ray	1.90	A/B	1-322	[»]
4GWD	X-ray	1.53	A/B	1-322	[»]
4HWW	X-ray	1.30	A/B	5-318	[»]
4HXQ	X-ray	1.45	A/B	5-318	[»]
4IE1	X-ray	2.00	A/B	5-318	[»]

ProteinModelPortal

P05089.

ModBase

Search...

Protein-protein interaction databases

IntAct

P05089. 7 interactions.

MINT

MINT-3974693.

STRING

9606.ENSP00000357066.

PTM databases

PhosphoSite

P05089.

Polymorphism databases

DMDM

12230985.

Proteomic databases

PaxDb

P05089.

PRIDE

P05089.

Protocols and materials databases

DNASU

383.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000356962; ENSP00000349446; ENSG00000118520.
ENST00000368087; ENSP00000357066; ENSG00000118520.
ENST00000476845; ENSP00000417694; ENSG00000118520.

GeneID

383.

KEGG

hsa:383.

UCSC

uc003qco.2. human.
uc010kfm.2. human.

Organism-specific databases

CTD

383.

GeneCards

GC06P131936.

HGNC

HGNC:663. ARG1.

HPA

CAB009434.
CAB056159.
HPA003595.
HPA024006.

MIM

207800. phenotype.
608313. gene.

neXtProt

NX_P05089.

Orphanet

90. Argininemia.

PharmGKB

PA24947.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0010.

HOGENOM

HOG000204319.

HOVERGEN

HBG003030.

KO

K01476.

OMA

GVEEGPT.

OrthoDB

EOG4D26QJ.

Enzyme and pathway databases

BioCyc

MetaCyc:HS04231-MONOMER.

Pathway_Interaction_DB

il4_2pathway. IL4-mediated signaling events.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P05089.

UniPathway

UPA00158; UER00270.

Gene expression databases

Bgee

P05089.

CleanEx

HS_ARG1.

Genevestigator

P05089.

GermOnline

ENSG00000118520. Homo sapiens.

Family and domain databases

Gene3D

3.40.800.10. 1 hit.

InterPro

IPR014033. Arginase.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]

PANTHER

PTHR11358. PTHR11358. 1 hit.

Pfam

PF00491. Arginase. 1 hit.
[Graphical view]

PIRSF

PIRSF036979. Arginase. 1 hit.

PRINTS

PR00116. ARGINASE.

TIGRFAMs

TIGR01229. rocF_arginase. 1 hit.

PROSITE

PS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]

ProtoNet

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Other

BindingDB

P05089.

ChEMBL

CHEMBL1075097.

DrugBank

DB00129. L-Ornithine.

EvolutionaryTrace

P05089.

GenomeRNAi

383.

NextBio

1603.

SOURCE

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Entry information

Entry name

ARGI1_HUMAN

Accession

Primary (citable) accession number: P05089
Secondary accession number(s): A6NEA0 , Q5JWT5, Q5JWT6, Q8TE72, Q9BS50

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	January 11, 2001
Last modified:	May 29, 2013
This is version 164 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.