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P05089

- ARGI1_HUMAN

UniProt

P05089 - ARGI1_HUMAN

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Protein
Arginase-1
Gene
ARG1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Binds 2 manganese ions per subunit.

Pathwayi

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

  1. arginase activity Source: Reactome
  2. manganese ion binding Source: Ensembl

GO - Biological processi

  1. arginine catabolic process Source: ProtInc
  2. cellular nitrogen compound metabolic process Source: Reactome
  3. cellular response to dexamethasone stimulus Source: Ensembl
  4. cellular response to glucagon stimulus Source: Ensembl
  5. cellular response to hydrogen peroxide Source: Ensembl
  6. cellular response to interleukin-4 Source: Ensembl
  7. cellular response to lipopolysaccharide Source: Ensembl
  8. cellular response to transforming growth factor beta stimulus Source: Ensembl
  9. collagen biosynthetic process Source: Ensembl
  10. liver development Source: Ensembl
  11. lung development Source: Ensembl
  12. mammary gland involution Source: Ensembl
  13. maternal process involved in female pregnancy Source: Ensembl
  14. positive regulation of endothelial cell proliferation Source: Ensembl
  15. protein homotrimerization Source: Ensembl
  16. regulation of L-arginine import Source: Ensembl
  17. response to amine Source: Ensembl
  18. response to amino acid Source: Ensembl
  19. response to axon injury Source: Ensembl
  20. response to cadmium ion Source: Ensembl
  21. response to drug Source: Ensembl
  22. response to herbicide Source: Ensembl
  23. response to manganese ion Source: Ensembl
  24. response to methylmercury Source: Ensembl
  25. response to selenium ion Source: Ensembl
  26. response to vitamin A Source: Ensembl
  27. response to vitamin E Source: Ensembl
  28. response to zinc ion Source: Ensembl
  29. small molecule metabolic process Source: Reactome
  30. urea cycle Source: Reactome
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.
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: Chromosome 6

Organism-specific databases

HGNCiHGNC:663. ARG1.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. cytosol Source: Reactome
  3. extracellular space Source: Ensembl
  4. extracellular vesicular exosome Source: UniProt
  5. neuron projection Source: Ensembl
  6. neuronal cell body Source: Ensembl
  7. nucleus Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

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.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111I → T in ARGIN; 12% of wild-type activity. 1 Publication
Corresponds to variant rs28941474 [ dbSNP | Ensembl ].
VAR_015594
Natural varianti138 – 1381G → V in ARGIN. 1 Publication
VAR_015595
Natural varianti235 – 2351G → R in ARGIN. 1 Publication
VAR_000674

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi207800. phenotype.
Orphaneti90. Argininemia.
PharmGKBiPA24947.

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171N6-succinyllysine By similarity
Modified residuei72 – 721Phosphoserine By similarity
Modified residuei75 – 751N6-succinyllysine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP05089.
PaxDbiP05089.
PRIDEiP05089.

PTM databases

PhosphoSiteiP05089.

Expressioni

Inductioni

By arginine or homoarginine.

Gene expression databases

BgeeiP05089.
CleanExiHS_ARG1.
GenevestigatoriP05089.

Organism-specific databases

HPAiCAB009434.
CAB056159.
HPA003595.
HPA024006.

Interactioni

Subunit structurei

Homotrimer.3 Publications

Protein-protein interaction databases

BioGridi106878. 13 interactions.
IntActiP05089. 8 interactions.
MINTiMINT-3974693.
STRINGi9606.ENSP00000357066.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

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.

Phylogenomic databases

eggNOGiCOG0010.
HOGENOMiHOG000204319.
HOVERGENiHBG003030.
KOiK01476.
OMAiKEQECDV.
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. Align

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

MSAKSRTIGI IGAPFSKGQP RGGVEEGPTV LRKAGLLEKL KEQECDVKDY    50
GDLPFADIPN DSPFQIVKNP RSVGKASEQL AGKVAEVKKN GRISLVLGGD 100
HSLAIGSISG HARVHPDLGV IWVDAHTDIN TPLTTTSGNL HGQPVSFLLK 150
ELKGKIPDVP GFSWVTPCIS AKDIVYIGLR DVDPGEHYIL KTLGIKYFSM 200
TEVDRLGIGK VMEETLSYLL GRKKRPIHLS FDVDGLDPSF TPATGTPVVG 250
GLTYREGLYI TEEIYKTGLL SGLDIMEVNP SLGKTPEEVT RTVNTAVAIT 300
LACFGLAREG NHKPIDYLNP PK 322
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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111I → T in ARGIN; 12% of wild-type activity. 1 Publication
Corresponds to variant rs28941474 [ dbSNP | Ensembl ].
VAR_015594
Natural varianti138 – 1381G → V in ARGIN. 1 Publication
VAR_015595
Natural varianti235 – 2351G → R in ARGIN. 1 Publication
VAR_000674
Natural varianti290 – 2901T → S.1 Publication
VAR_000675

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei43 – 431Q → QVTQNFLIL in isoform 2.
VSP_009330
Alternative sequencei204 – 28986Missing in isoform 3.
VSP_009331Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481K → E in AAL71547. 1 Publication
Sequence conflicti86 – 861E → Q in AAA51776. 1 Publication
Sequence conflicti202 – 2021E → K in AAL71547. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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. [P05089-1]
GeneIDi383.
KEGGihsa:383.
UCSCiuc003qco.2. human. [P05089-1]
uc010kfm.2. human. [P05089-2]

Polymorphism databases

DMDMi12230985.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Arginase entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS5145.1. [P05089-1 ]
CCDS59038.1. [P05089-2 ]
PIRi S02132. A26370.
RefSeqi NP_000036.2. NM_000045.3. [P05089-1 ]
NP_001231367.1. NM_001244438.1. [P05089-2 ]
UniGenei Hs.440934.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P05089.
SMRi P05089. Positions 5-318.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106878. 13 interactions.
IntActi P05089. 8 interactions.
MINTi MINT-3974693.
STRINGi 9606.ENSP00000357066.

Chemistry

BindingDBi P05089.
ChEMBLi CHEMBL1075097.
DrugBanki DB00129. L-Ornithine.

PTM databases

PhosphoSitei P05089.

Polymorphism databases

DMDMi 12230985.

Proteomic databases

MaxQBi P05089.
PaxDbi P05089.
PRIDEi P05089.

Protocols and materials databases

DNASUi 383.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000356962 ; ENSP00000349446 ; ENSG00000118520 . [P05089-2 ]
ENST00000368087 ; ENSP00000357066 ; ENSG00000118520 . [P05089-1 ]
GeneIDi 383.
KEGGi hsa:383.
UCSCi uc003qco.2. human. [P05089-1 ]
uc010kfm.2. human. [P05089-2 ]

Organism-specific databases

CTDi 383.
GeneCardsi GC06P131936.
GeneReviewsi ARG1.
HGNCi HGNC:663. ARG1.
HPAi CAB009434.
CAB056159.
HPA003595.
HPA024006.
MIMi 207800. phenotype.
608313. gene.
neXtProti NX_P05089.
Orphaneti 90. Argininemia.
PharmGKBi PA24947.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0010.
HOGENOMi HOG000204319.
HOVERGENi HBG003030.
KOi K01476.
OMAi KEQECDV.
OrthoDBi EOG747PJ5.
PhylomeDBi P05089.
TreeFami TF300034.

Enzyme and pathway databases

UniPathwayi UPA00158 ; UER00270 .
BioCyci MetaCyc:HS04231-MONOMER.
Reactomei REACT_847. Urea cycle.
SABIO-RK P05089.

Miscellaneous databases

EvolutionaryTracei P05089.
GenomeRNAii 383.
NextBioi 1603.
PROi P05089.
SOURCEi Search...

Gene expression databases

Bgeei P05089.
CleanExi HS_ARG1.
Genevestigatori P05089.

Family and domain databases

Gene3Di 3.40.800.10. 1 hit.
InterProi IPR014033. Arginase.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view ]
PANTHERi PTHR11358. PTHR11358. 1 hit.
Pfami PF00491. Arginase. 1 hit.
[Graphical view ]
PIRSFi PIRSF036979. Arginase. 1 hit.
PRINTSi PR00116. ARGINASE.
TIGRFAMsi TIGR01229. rocF_arginase. 1 hit.
PROSITEi PS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "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, IDENTIFICATION BY 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. Cited for: VARIANTS ARGIN THR-11 AND VAL-138.

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: September 3, 2014
This is version 177 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

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