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Protein

Arginase-1

Gene

ARG1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-arginine + H2O = L-ornithine + urea.

Cofactori

Mn2+Note: Binds 2 manganese ions per subunit.

Pathway:iurea cycle

This protein is involved in step 1 of the subpathway that synthesizes L-ornithine and urea from L-arginine.
Proteins known to be involved in this subpathway in this organism are:
  1. Arginase (ARG2), Arginase-2, mitochondrial (ARG2), Arginase-1 (ARG1)
This subpathway is part of the pathway urea cycle, which is itself part of Nitrogen metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-ornithine and urea from L-arginine, the pathway urea cycle and in Nitrogen metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi101 – 1011Manganese 1
Metal bindingi124 – 1241Manganese 1
Metal bindingi124 – 1241Manganese 2
Metal bindingi126 – 1261Manganese 2
Metal bindingi128 – 1281Manganese 1
Binding sitei183 – 1831Substrate
Metal bindingi232 – 2321Manganese 1
Metal bindingi232 – 2321Manganese 2
Metal bindingi234 – 2341Manganese 2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Arginine metabolism, Urea cycle

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS04231-MONOMER.
BRENDAi3.5.3.1. 2681.
ReactomeiREACT_847. Urea cycle.
SABIO-RKP05089.
UniPathwayiUPA00158; UER00270.

Names & Taxonomyi

Protein namesi
Recommended name:
Arginase-1 (EC:3.5.3.1)
Alternative name(s):
Liver-type arginase
Type I arginase
Gene namesi
Name:ARG1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:663. ARG1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: ProtInc
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: Ensembl
  • mitochondrial outer membrane Source: Ensembl
  • neuronal cell body Source: Ensembl
  • neuron projection Source: Ensembl
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Argininemia (ARGIN)4 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:207800
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111I → T in ARGIN; 12% of wild-type activity. 2 Publications
Corresponds to variant rs28941474 [ dbSNP | Ensembl ].
VAR_015594
Natural varianti27 – 271G → D in ARGIN; 5.2% of wild-type activity. 1 Publication
VAR_072164
Natural varianti74 – 741G → V in ARGIN; 9.3% of wild-type activity. 1 Publication
VAR_072165
Natural varianti125 – 1251A → V in ARGIN; decreases erythrocyte arginase activity. 1 Publication
VAR_072166
Natural varianti134 – 1341T → I in ARGIN; 9.3% of wild-type activity. 1 Publication
VAR_072167
Natural varianti138 – 1381G → V in ARGIN. 1 Publication
VAR_015595
Natural varianti180 – 1801R → T in ARGIN; decreases erythrocyte arginase activity. 1 Publication
VAR_072168
Natural varianti235 – 2351G → R in ARGIN; decreases erythrocyte arginase activity. 2 Publications
VAR_000674
Natural varianti308 – 3081R → Q in ARGIN; 20.8% of wild-type activity. 1 Publication
VAR_072169

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi207800. phenotype.
Orphaneti90. Argininemia.
PharmGKBiPA24947.

Chemistry

DrugBankiDB00129. L-Ornithine.

Polymorphism and mutation databases

BioMutaiARG1.
DMDMi12230985.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 322322Arginase-1PRO_0000173693Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171N6-succinyllysineBy similarity
Modified residuei62 – 621Phosphoserine1 Publication
Modified residuei72 – 721PhosphoserineBy similarity
Modified residuei75 – 751N6-succinyllysineBy similarity
Modified residuei163 – 1631Phosphoserine1 Publication
Modified residuei217 – 2171Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP05089.
PaxDbiP05089.
PRIDEiP05089.

PTM databases

PhosphoSiteiP05089.

Expressioni

Inductioni

By arginine or homoarginine.

Gene expression databases

BgeeiP05089.
CleanExiHS_ARG1.
GenevisibleiP05089. HS.

Organism-specific databases

HPAiCAB009434.
CAB056159.
HPA003595.
HPA024006.

Interactioni

Subunit structurei

Homotrimer.5 Publications

Protein-protein interaction databases

BioGridi106878. 14 interactions.
IntActiP05089. 8 interactions.
MINTiMINT-3974693.
STRINGi9606.ENSP00000357066.

Structurei

Secondary structure

1
322
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 137Combined sources
Helixi22 – 265Combined sources
Helixi27 – 337Combined sources
Helixi36 – 427Combined sources
Beta strandi46 – 527Combined sources
Beta strandi67 – 693Combined sources
Helixi70 – 8920Combined sources
Beta strandi93 – 997Combined sources
Helixi101 – 1033Combined sources
Helixi104 – 11411Combined sources
Beta strandi119 – 1268Combined sources
Turni132 – 1343Combined sources
Helixi140 – 1423Combined sources
Helixi144 – 1485Combined sources
Helixi150 – 1523Combined sources
Turni153 – 1553Combined sources
Helixi171 – 1733Combined sources
Beta strandi174 – 1796Combined sources
Helixi184 – 19310Combined sources
Beta strandi196 – 1994Combined sources
Helixi200 – 2067Combined sources
Helixi208 – 22013Combined sources
Beta strandi221 – 2233Combined sources
Beta strandi227 – 2326Combined sources
Helixi233 – 2353Combined sources
Turni238 – 2403Combined sources
Beta strandi243 – 2464Combined sources
Helixi254 – 26714Combined sources
Beta strandi270 – 2767Combined sources
Helixi280 – 2823Combined sources
Helixi286 – 30318Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WVAX-ray1.94A/B1-322[»]
1WVBX-ray2.30A/B1-322[»]
2AEBX-ray1.29A/B1-322[»]
2PHAX-ray1.90A/B1-322[»]
2PHOX-ray1.95A/B1-322[»]
2PLLX-ray1.90A/B1-322[»]
2ZAVX-ray1.70A/B1-322[»]
3DJ8X-ray1.51A/B1-322[»]
3E6KX-ray2.10A/B1-322[»]
3E6VX-ray1.72A/B1-322[»]
3F80X-ray1.60A/B1-322[»]
3GMZX-ray1.43A/B1-322[»]
3GN0X-ray1.70A/B1-322[»]
3KV2X-ray1.55A/B1-322[»]
3LP4X-ray1.90A/B1-322[»]
3LP7X-ray2.04A/B1-322[»]
3MFVX-ray1.90A/B1-322[»]
3MFWX-ray1.47A/B1-322[»]
3MJLX-ray1.90A/B1-322[»]
3SJTX-ray1.60A/B1-322[»]
3SKKX-ray1.70A/B1-322[»]
3TF3X-ray1.64A/B1-322[»]
3TH7X-ray2.10A/B1-322[»]
3THEX-ray1.97A/B1-322[»]
3THHX-ray1.85A/B1-322[»]
3THJX-ray1.50A/B1-322[»]
4FCIX-ray1.82A/B1-322[»]
4FCKX-ray1.90A/B1-322[»]
4GSMX-ray1.70A/B1-322[»]
4GSVX-ray1.48A/B1-322[»]
4GSZX-ray2.20A/B1-322[»]
4GWCX-ray1.90A/B1-322[»]
4GWDX-ray1.53A/B1-322[»]
4HWWX-ray1.30A/B5-318[»]
4HXQX-ray1.45A/B5-318[»]
4IE1X-ray2.00A/B5-318[»]
ProteinModelPortaliP05089.
SMRiP05089. Positions 5-318.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05089.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni126 – 1305Substrate binding
Regioni137 – 1393Substrate binding

Sequence similaritiesi

Belongs to the arginase family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0010.
GeneTreeiENSGT00530000063082.
HOGENOMiHOG000204319.
HOVERGENiHBG003030.
InParanoidiP05089.
KOiK01476.
OMAiEQECDVK.
OrthoDBiEOG747PJ5.
PhylomeDBiP05089.
TreeFamiTF300034.

Family and domain databases

Gene3Di3.40.800.10. 1 hit.
InterProiIPR014033. Arginase.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERiPTHR11358. PTHR11358. 1 hit.
PfamiPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFiPIRSF036979. Arginase. 1 hit.
PRINTSiPR00116. ARGINASE.
TIGRFAMsiTIGR01229. rocF_arginase. 1 hit.
PROSITEiPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P05089-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSAKSRTIGI IGAPFSKGQP RGGVEEGPTV LRKAGLLEKL KEQECDVKDY
60 70 80 90 100
GDLPFADIPN DSPFQIVKNP RSVGKASEQL AGKVAEVKKN GRISLVLGGD
110 120 130 140 150
HSLAIGSISG HARVHPDLGV IWVDAHTDIN TPLTTTSGNL HGQPVSFLLK
160 170 180 190 200
ELKGKIPDVP GFSWVTPCIS AKDIVYIGLR DVDPGEHYIL KTLGIKYFSM
210 220 230 240 250
TEVDRLGIGK VMEETLSYLL GRKKRPIHLS FDVDGLDPSF TPATGTPVVG
260 270 280 290 300
GLTYREGLYI TEEIYKTGLL SGLDIMEVNP SLGKTPEEVT RTVNTAVAIT
310 320
LACFGLAREG NHKPIDYLNP PK
Length:322
Mass (Da):34,735
Last modified:January 11, 2001 - v2
Checksum:i8F3BE2652243F622
GO
Isoform 2 (identifier: P05089-2) [UniParc]FASTAAdd to basket

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.
Show »
Length:330
Mass (Da):35,664
Checksum:i3547D8B6C254179B
GO
Isoform 3 (identifier: P05089-3) [UniParc]FASTAAdd to basket

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

Show »
Length:236
Mass (Da):25,356
Checksum:i79F02C69B700AB67
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481K → E in AAL71547 (Ref. 3) Curated
Sequence conflicti86 – 861E → Q in AAA51776 (PubMed:3540966).Curated
Sequence conflicti202 – 2021E → K in AAL71547 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111I → T in ARGIN; 12% of wild-type activity. 2 Publications
Corresponds to variant rs28941474 [ dbSNP | Ensembl ].
VAR_015594
Natural varianti27 – 271G → D in ARGIN; 5.2% of wild-type activity. 1 Publication
VAR_072164
Natural varianti74 – 741G → V in ARGIN; 9.3% of wild-type activity. 1 Publication
VAR_072165
Natural varianti125 – 1251A → V in ARGIN; decreases erythrocyte arginase activity. 1 Publication
VAR_072166
Natural varianti134 – 1341T → I in ARGIN; 9.3% of wild-type activity. 1 Publication
VAR_072167
Natural varianti138 – 1381G → V in ARGIN. 1 Publication
VAR_015595
Natural varianti180 – 1801R → T in ARGIN; decreases erythrocyte arginase activity. 1 Publication
VAR_072168
Natural varianti235 – 2351G → R in ARGIN; decreases erythrocyte arginase activity. 2 Publications
VAR_000674
Natural varianti290 – 2901T → S.1 Publication
VAR_000675
Natural varianti308 – 3081R → Q in ARGIN; 20.8% of wild-type activity. 1 Publication
VAR_072169

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei43 – 431Q → QVTQNFLIL in isoform 2. 1 PublicationVSP_009330
Alternative sequencei204 – 28986Missing in isoform 3. 2 PublicationsVSP_009331Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS5145.1. [P05089-1]
CCDS59038.1. [P05089-2]
PIRiS02132. A26370.
RefSeqiNP_000036.2. NM_000045.3. [P05089-1]
NP_001231367.1. NM_001244438.1. [P05089-2]
UniGeneiHs.440934.

Genome annotation databases

EnsembliENST00000356962; ENSP00000349446; ENSG00000118520. [P05089-2]
ENST00000368087; ENSP00000357066; ENSG00000118520.
GeneIDi383.
KEGGihsa:383.
UCSCiuc003qco.2. human. [P05089-1]
uc010kfm.2. human. [P05089-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Arginase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS5145.1. [P05089-1]
CCDS59038.1. [P05089-2]
PIRiS02132. A26370.
RefSeqiNP_000036.2. NM_000045.3. [P05089-1]
NP_001231367.1. NM_001244438.1. [P05089-2]
UniGeneiHs.440934.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WVAX-ray1.94A/B1-322[»]
1WVBX-ray2.30A/B1-322[»]
2AEBX-ray1.29A/B1-322[»]
2PHAX-ray1.90A/B1-322[»]
2PHOX-ray1.95A/B1-322[»]
2PLLX-ray1.90A/B1-322[»]
2ZAVX-ray1.70A/B1-322[»]
3DJ8X-ray1.51A/B1-322[»]
3E6KX-ray2.10A/B1-322[»]
3E6VX-ray1.72A/B1-322[»]
3F80X-ray1.60A/B1-322[»]
3GMZX-ray1.43A/B1-322[»]
3GN0X-ray1.70A/B1-322[»]
3KV2X-ray1.55A/B1-322[»]
3LP4X-ray1.90A/B1-322[»]
3LP7X-ray2.04A/B1-322[»]
3MFVX-ray1.90A/B1-322[»]
3MFWX-ray1.47A/B1-322[»]
3MJLX-ray1.90A/B1-322[»]
3SJTX-ray1.60A/B1-322[»]
3SKKX-ray1.70A/B1-322[»]
3TF3X-ray1.64A/B1-322[»]
3TH7X-ray2.10A/B1-322[»]
3THEX-ray1.97A/B1-322[»]
3THHX-ray1.85A/B1-322[»]
3THJX-ray1.50A/B1-322[»]
4FCIX-ray1.82A/B1-322[»]
4FCKX-ray1.90A/B1-322[»]
4GSMX-ray1.70A/B1-322[»]
4GSVX-ray1.48A/B1-322[»]
4GSZX-ray2.20A/B1-322[»]
4GWCX-ray1.90A/B1-322[»]
4GWDX-ray1.53A/B1-322[»]
4HWWX-ray1.30A/B5-318[»]
4HXQX-ray1.45A/B5-318[»]
4IE1X-ray2.00A/B5-318[»]
ProteinModelPortaliP05089.
SMRiP05089. Positions 5-318.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106878. 14 interactions.
IntActiP05089. 8 interactions.
MINTiMINT-3974693.
STRINGi9606.ENSP00000357066.

Chemistry

BindingDBiP05089.
ChEMBLiCHEMBL1075097.
DrugBankiDB00129. L-Ornithine.

PTM databases

PhosphoSiteiP05089.

Polymorphism and mutation databases

BioMutaiARG1.
DMDMi12230985.

Proteomic databases

MaxQBiP05089.
PaxDbiP05089.
PRIDEiP05089.

Protocols and materials databases

DNASUi383.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000356962; ENSP00000349446; ENSG00000118520. [P05089-2]
ENST00000368087; ENSP00000357066; ENSG00000118520.
GeneIDi383.
KEGGihsa:383.
UCSCiuc003qco.2. human. [P05089-1]
uc010kfm.2. human. [P05089-2]

Organism-specific databases

CTDi383.
GeneCardsiGC06P131936.
GeneReviewsiARG1.
HGNCiHGNC:663. ARG1.
HPAiCAB009434.
CAB056159.
HPA003595.
HPA024006.
MIMi207800. phenotype.
608313. gene.
neXtProtiNX_P05089.
Orphaneti90. Argininemia.
PharmGKBiPA24947.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0010.
GeneTreeiENSGT00530000063082.
HOGENOMiHOG000204319.
HOVERGENiHBG003030.
InParanoidiP05089.
KOiK01476.
OMAiEQECDVK.
OrthoDBiEOG747PJ5.
PhylomeDBiP05089.
TreeFamiTF300034.

Enzyme and pathway databases

UniPathwayiUPA00158; UER00270.
BioCyciMetaCyc:HS04231-MONOMER.
BRENDAi3.5.3.1. 2681.
ReactomeiREACT_847. Urea cycle.
SABIO-RKP05089.

Miscellaneous databases

EvolutionaryTraceiP05089.
GenomeRNAii383.
NextBioi1603.
PROiP05089.
SOURCEiSearch...

Gene expression databases

BgeeiP05089.
CleanExiHS_ARG1.
GenevisibleiP05089. HS.

Family and domain databases

Gene3Di3.40.800.10. 1 hit.
InterProiIPR014033. Arginase.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERiPTHR11358. PTHR11358. 1 hit.
PfamiPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFiPIRSF036979. Arginase. 1 hit.
PRINTSiPR00116. ARGINASE.
TIGRFAMsiTIGR01229. rocF_arginase. 1 hit.
PROSITEiPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-163 AND SER-217, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "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.
  11. "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, IDENTIFICATION BY MASS SPECTROMETRY.
  12. "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.
  13. "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.
  14. "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.
  15. "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.
  16. Cited for: VARIANTS ARGIN THR-11 AND VAL-138.
  17. "Analysis of novel ARG1 mutations causing hyperargininemia and correlation with arginase I activity in erythrocytes."
    Carvalho D.R., Brand G.D., Brum J.M., Takata R.I., Speck-Martins C.E., Pratesi R.
    Gene 509:124-130(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ARGIN THR-11; ASP-27; VAL-74; ILE-134 AND GLN-308.
  18. "Five novel mutations in ARG1 gene in Chinese patients of argininemia."
    Wu T.F., Liu Y.P., Li X.Y., Wang Q., Ding Y., Ma Y.Y., Song J.Q., Yang Y.L.
    Pediatr. Neurol. 49:119-123(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ARGIN VAL-125; THR-180 AND ARG-235.

Entry informationi

Entry nameiARGI1_HUMAN
AccessioniPrimary (citable) accession number: P05089
Secondary accession number(s): A6NEA0
, Q5JWT5, Q5JWT6, Q8TE72, Q9BS50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 11, 2001
Last modified: July 22, 2015
This is version 188 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.