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Entry version 224 (16 Oct 2019)
Sequence version 2 (11 Jan 2001)
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Protein

Arginase-1

Gene

ARG1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Key element of the urea cycle converting L-arginine to urea and L-ornithine, which is further metabolized into metabolites proline and polyamides that drive collagen synthesis and bioenergetic pathways critical for cell proliferation, respectively; the urea cycle takes place primarily in the liver and, to a lesser extent, in the kidneys.Curated
Functions in L-arginine homeostasis in nonhepatic tissues characterized by the competition between nitric oxide synthase (NOS) and arginase for the available intracellular substrate arginine. Arginine metabolism is a critical regulator of innate and adaptive immune responses. Involved in an antimicrobial effector pathway in polymorphonuclear granulocytes (PMN). Upon PMN cell death is liberated from the phagolysosome and depletes arginine in the microenvironment leading to suppressed T cell and natural killer (NK) cell proliferation and cytokine secretion (PubMed:15546957, PubMed:16709924, PubMed:19380772). In group 2 innate lymphoid cells (ILC2s) promotes acute type 2 inflammation in the lung and is involved in optimal ILC2 proliferation but not survival (By similarity). In humans, the immunological role in the monocytic/macrophage/dendritic cell (DC) lineage is unsure.By similarity3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mn2+4 PublicationsNote: Binds 2 manganese ions per subunit.4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: urea cycle

This protein is involved in step 1 of the subpathway that synthesizes L-ornithine and urea from L-arginine.1 Publication
Proteins known to be involved in this subpathway in this organism are:
  1. Arginase (ARG2), Arginase-1 (ARG1), Arginase-2, mitochondrial (ARG2)
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)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi101Manganese 1Combined sources4 Publications1
Metal bindingi124Manganese 1Combined sources4 Publications1
Metal bindingi124Manganese 2Combined sources4 Publications1
Metal bindingi126Manganese 2Combined sources4 Publications1
Metal bindingi128Manganese 1Combined sources4 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei183SubstrateCombined sources1
Metal bindingi232Manganese 1Combined sources4 Publications1
Metal bindingi232Manganese 2Combined sources4 Publications1
Metal bindingi234Manganese 2Combined sources4 Publications1
Binding sitei246SubstrateBy similarity1
Binding sitei277SubstrateBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase
Biological processAdaptive immunity, Arginine metabolism, Immunity, Innate immunity, Urea cycle
LigandManganese, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:HS04231-MONOMER

BRENDA Comprehensive Enzyme Information System

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BRENDAi
3.5.3.1 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-6798695 Neutrophil degranulation
R-HSA-70635 Urea cycle

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
P05089

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P05089

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00158;UER00270

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Arginase-1 (EC:3.5.3.12 Publications)
Alternative name(s):
Liver-type arginase
Type I arginase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ARG1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 6

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:663 ARG1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
608313 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P05089

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_01559411I → T in ARGIN; 12% of wild-type activity. 2 PublicationsCorresponds to variant dbSNP:rs28941474EnsemblClinVar.1
Natural variantiVAR_07216427G → D in ARGIN; 5.2% of wild-type activity. 1 PublicationCorresponds to variant dbSNP:rs1326930389EnsemblClinVar.1
Natural variantiVAR_07216574G → V in ARGIN; 9.3% of wild-type activity. 1 Publication1
Natural variantiVAR_072166125A → V in ARGIN; decreases erythrocyte arginase activity. 1 Publication1
Natural variantiVAR_072167134T → I in ARGIN; 9.3% of wild-type activity. 1 Publication1
Natural variantiVAR_015595138G → V in ARGIN. 1 PublicationCorresponds to variant dbSNP:rs104893943EnsemblClinVar.1
Natural variantiVAR_072168180R → T in ARGIN; decreases erythrocyte arginase activity. 1 Publication1
Natural variantiVAR_000674235G → R in ARGIN; decreases erythrocyte arginase activity. 2 PublicationsCorresponds to variant dbSNP:rs104893948EnsemblClinVar.1
Natural variantiVAR_072169308R → Q in ARGIN; 20.8% of wild-type activity. 1 PublicationCorresponds to variant dbSNP:rs377280518EnsemblClinVar.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
383

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
ARG1

MalaCards human disease database

More...
MalaCardsi
ARG1
MIMi207800 phenotype

Open Targets

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OpenTargetsi
ENSG00000118520

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
90 Argininemia

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA24947

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
P05089

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1075097

Drug and drug target database

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DrugBanki
DB01983 2(S)-Amino-6-Boronohexanoic Acid
DB04585 DEHYDRO-2(S)-AMINO-6-BORONOHEXANOIC ACID
DB04197 Descarboxy-nor-N(Omega)-Hydroxy-L-Arginine
DB02499 Dinor-N(Omega)-Hydroxy-L-Arginine
DB06757 Manganese
DB03144 N-Omega-Hydroxy-L-Arginine
DB02381 nor-NOHA
DB00129 Ornithine
DB04530 S,S-(2-Hydroxyethyl)Thiocysteine
DB03731 S-2-(Boronoethyl)-L-Cysteine
DB04648 S-propylamine-L-cysteine
DB02689 S-{2-[Amino(Dihydroxy)-Lambda~4~-Sulfanyl]Ethyl}-D-Cysteine
DB03904 Urea

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1244

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
ARG1

Domain mapping of disease mutations (DMDM)

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DMDMi
12230985

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001736931 – 322Arginase-1Add BLAST322

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei17N6-succinyllysineBy similarity1
Modified residuei62PhosphoserineCombined sources1
Modified residuei72PhosphoserineBy similarity1
Modified residuei75N6-succinyllysineBy similarity1
Modified residuei163PhosphoserineCombined sources1
Modified residuei217PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P05089

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P05089

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
P05089

MaxQB - The MaxQuant DataBase

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MaxQBi
P05089

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P05089

PeptideAtlas

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PeptideAtlasi
P05089

PRoteomics IDEntifications database

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PRIDEi
P05089

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
51784 [P05089-1]
51785 [P05089-2]
51786 [P05089-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P05089

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P05089

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Within the immune system initially reported to be selectively expressed in granulocytes (polymorphonuclear leukocytes [PMNs]) (PubMed:15546957). Also detected in macrophages mycobacterial granulomas (PubMed:23749634). Expressed in group2 innate lymphoid cells (ILC2s) during lung disease (PubMed:27043409).2 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By arginine or homoarginine.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000118520 Expressed in 123 organ(s), highest expression level in liver

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P05089 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB009434
CAB056159
HPA003595
HPA024006

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotrimer (PubMed:16141327, PubMed:17469833, PubMed:17562323, PubMed:18802628, PubMed:2241902).

Interacts with CMTM6 (PubMed:28813417).

6 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
106878, 48 interactors

Protein interaction database and analysis system

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IntActi
P05089, 28 interactors

Molecular INTeraction database

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MINTi
P05089

STRING: functional protein association networks

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STRINGi
9606.ENSP00000349446

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P05089

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1322
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P05089

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P05089

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni126 – 130Substrate bindingCombined sources5
Regioni137 – 139Substrate bindingCombined sources3

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the arginase family.PROSITE-ProRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG2965 Eukaryota
COG0010 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00950000183195

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000204319

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P05089

KEGG Orthology (KO)

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KOi
K01476

Identification of Orthologs from Complete Genome Data

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OMAi
EHYIVKT

Database of Orthologous Groups

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OrthoDBi
138195at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P05089

TreeFam database of animal gene trees

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TreeFami
TF300034

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR014033 Arginase
IPR006035 Ureohydrolase
IPR023696 Ureohydrolase_dom_sf
IPR020855 Ureohydrolase_Mn_BS

Pfam protein domain database

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Pfami
View protein in Pfam
PF00491 Arginase, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF036979 Arginase, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00116 ARGINASE

Superfamily database of structural and functional annotation

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SUPFAMi
SSF52768 SSF52768, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR01229 rocF_arginase, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS01053 ARGINASE_1, 1 hit
PS51409 ARGINASE_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: P05089-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti48K → E in AAL71547 (Ref. 3) Curated1
Sequence conflicti86E → Q in AAA51776 (PubMed:3540966).Curated1
Sequence conflicti202E → K in AAL71547 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01559411I → T in ARGIN; 12% of wild-type activity. 2 PublicationsCorresponds to variant dbSNP:rs28941474EnsemblClinVar.1
Natural variantiVAR_07216427G → D in ARGIN; 5.2% of wild-type activity. 1 PublicationCorresponds to variant dbSNP:rs1326930389EnsemblClinVar.1
Natural variantiVAR_07216574G → V in ARGIN; 9.3% of wild-type activity. 1 Publication1
Natural variantiVAR_072166125A → V in ARGIN; decreases erythrocyte arginase activity. 1 Publication1
Natural variantiVAR_072167134T → I in ARGIN; 9.3% of wild-type activity. 1 Publication1
Natural variantiVAR_015595138G → V in ARGIN. 1 PublicationCorresponds to variant dbSNP:rs104893943EnsemblClinVar.1
Natural variantiVAR_072168180R → T in ARGIN; decreases erythrocyte arginase activity. 1 Publication1
Natural variantiVAR_000674235G → R in ARGIN; decreases erythrocyte arginase activity. 2 PublicationsCorresponds to variant dbSNP:rs104893948EnsemblClinVar.1
Natural variantiVAR_000675290T → S1 PublicationCorresponds to variant dbSNP:rs104893942EnsemblClinVar.1
Natural variantiVAR_072169308R → Q in ARGIN; 20.8% of wild-type activity. 1 PublicationCorresponds to variant dbSNP:rs377280518EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_00933043Q → QVTQNFLIL in isoform 2. 1 Publication1
Alternative sequenceiVSP_009331204 – 289Missing in isoform 3. 2 PublicationsAdd BLAST86

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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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

The Consensus CDS (CCDS) project

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CCDSi
CCDS5145.1 [P05089-1]
CCDS59038.1 [P05089-2]

Protein sequence database of the Protein Information Resource

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PIRi
S02132 A26370

NCBI Reference Sequences

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RefSeqi
NP_000036.2, NM_000045.3 [P05089-1]
NP_001231367.1, NM_001244438.1 [P05089-2]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000356962; ENSP00000349446; ENSG00000118520 [P05089-2]
ENST00000368087; ENSP00000357066; ENSG00000118520 [P05089-1]
ENST00000640973; ENSP00000492623; ENSG00000118520 [P05089-3]

Database of genes from NCBI RefSeq genomes

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GeneIDi
383

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:383

UCSC genome browser

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UCSCi
uc003qcp.3 human [P05089-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB 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[»]
SMRiP05089
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi106878, 48 interactors
IntActiP05089, 28 interactors
MINTiP05089
STRINGi9606.ENSP00000349446

Chemistry databases

BindingDBiP05089
ChEMBLiCHEMBL1075097
DrugBankiDB01983 2(S)-Amino-6-Boronohexanoic Acid
DB04585 DEHYDRO-2(S)-AMINO-6-BORONOHEXANOIC ACID
DB04197 Descarboxy-nor-N(Omega)-Hydroxy-L-Arginine
DB02499 Dinor-N(Omega)-Hydroxy-L-Arginine
DB06757 Manganese
DB03144 N-Omega-Hydroxy-L-Arginine
DB02381 nor-NOHA
DB00129 Ornithine
DB04530 S,S-(2-Hydroxyethyl)Thiocysteine
DB03731 S-2-(Boronoethyl)-L-Cysteine
DB04648 S-propylamine-L-cysteine
DB02689 S-{2-[Amino(Dihydroxy)-Lambda~4~-Sulfanyl]Ethyl}-D-Cysteine
DB03904 Urea
GuidetoPHARMACOLOGYi1244

PTM databases

iPTMnetiP05089
PhosphoSitePlusiP05089

Polymorphism and mutation databases

BioMutaiARG1
DMDMi12230985

Proteomic databases

EPDiP05089
jPOSTiP05089
MassIVEiP05089
MaxQBiP05089
PaxDbiP05089
PeptideAtlasiP05089
PRIDEiP05089
ProteomicsDBi51784 [P05089-1]
51785 [P05089-2]
51786 [P05089-3]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
383

Genome annotation databases

EnsembliENST00000356962; ENSP00000349446; ENSG00000118520 [P05089-2]
ENST00000368087; ENSP00000357066; ENSG00000118520 [P05089-1]
ENST00000640973; ENSP00000492623; ENSG00000118520 [P05089-3]
GeneIDi383
KEGGihsa:383
UCSCiuc003qcp.3 human [P05089-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
383
DisGeNETi383

GeneCards: human genes, protein and diseases

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GeneCardsi
ARG1
GeneReviewsiARG1
HGNCiHGNC:663 ARG1
HPAiCAB009434
CAB056159
HPA003595
HPA024006
MalaCardsiARG1
MIMi207800 phenotype
608313 gene
neXtProtiNX_P05089
OpenTargetsiENSG00000118520
Orphaneti90 Argininemia
PharmGKBiPA24947

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2965 Eukaryota
COG0010 LUCA
GeneTreeiENSGT00950000183195
HOGENOMiHOG000204319
InParanoidiP05089
KOiK01476
OMAiEHYIVKT
OrthoDBi138195at2759
PhylomeDBiP05089
TreeFamiTF300034

Enzyme and pathway databases

UniPathwayiUPA00158;UER00270
BioCyciMetaCyc:HS04231-MONOMER
BRENDAi3.5.3.1 2681
ReactomeiR-HSA-6798695 Neutrophil degranulation
R-HSA-70635 Urea cycle
SABIO-RKiP05089
SIGNORiP05089

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
ARG1 human
EvolutionaryTraceiP05089

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
383
PharosiP05089

Protein Ontology

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PROi
PR:P05089

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000118520 Expressed in 123 organ(s), highest expression level in liver
GenevisibleiP05089 HS

Family and domain databases

InterProiView protein in InterPro
IPR014033 Arginase
IPR006035 Ureohydrolase
IPR023696 Ureohydrolase_dom_sf
IPR020855 Ureohydrolase_Mn_BS
PfamiView protein in Pfam
PF00491 Arginase, 1 hit
PIRSFiPIRSF036979 Arginase, 1 hit
PRINTSiPR00116 ARGINASE
SUPFAMiSSF52768 SSF52768, 1 hit
TIGRFAMsiTIGR01229 rocF_arginase, 1 hit
PROSITEiView protein in PROSITE
PS01053 ARGINASE_1, 1 hit
PS51409 ARGINASE_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiARGI1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P05089
Secondary accession number(s): A6NEA0
, Q5JWT5, Q5JWT6, Q8TE72, Q9BS50
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 11, 2001
Last modified: October 16, 2019
This is version 224 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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