Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P05089

- ARGI1_HUMAN

UniProt

P05089 - ARGI1_HUMAN

Protein

Arginase-1

Gene

ARG1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 178 (01 Oct 2014)
      Sequence version 2 (11 Jan 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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. neuronal cell body Source: Ensembl
    6. neuron projection Source: Ensembl
    7. nucleus Source: UniProt

    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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-1PRO_0000173693Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei17 – 171N6-succinyllysineBy similarity
    Modified residuei72 – 721PhosphoserineBy similarity
    Modified residuei75 – 751N6-succinyllysineBy 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.5 Publications

    Protein-protein interaction databases

    BioGridi106878. 13 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 – 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.
    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.
    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti48 – 481K → E in AAL71547. 1 PublicationCurated
    Sequence conflicti86 – 861E → Q in AAA51776. (PubMed:3540966)Curated
    Sequence conflicti202 – 2021E → K in AAL71547. 1 PublicationCurated

    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. 1 PublicationVSP_009330
    Alternative sequencei204 – 28986Missing in isoform 3. 2 PublicationsVSP_009331Add
    BLAST

    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

    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: October 1, 2014
    This is version 178 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