Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ornithine decarboxylase

Gene

ODC1

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

Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis.1 Publication

<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

pyridoxal 5'-phosphate2 Publications

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by S-nitrosylation (PubMed:10462479, PubMed:11461922). Inhibited by antizymes (AZs) OAZ1, OAZ2 and OAZ3 in response to polyamine levels. AZs inhibit the assembly of the functional homodimer by binding to ODC monomers. Additionally, OAZ1 targets ODC monomers for ubiquitin-independent proteolytic destruction by the 26S proteasome (PubMed:17900240). Inhibited by 1-amino-oxy-3-aminopropane (APA, an isosteric analog of putrescine) (PubMed:17407445). Irreversibly inhibited by alpha-difluoromethylornithine (DFMO) (PubMed:17407445).4 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 3.3 sec(-1) with L-ornithine as substrate.1 Publication
  1. KM=0.08 mM for L-ornithine1 Publication

    <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: putrescine biosynthesis via L-ornithine pathway

    This protein is involved in step 1 of the subpathway that synthesizes putrescine from L-ornithine.
    Proteins known to be involved in this subpathway in this organism are:
    1. Ornithine decarboxylase (ODC1)
    This subpathway is part of the pathway putrescine biosynthesis via L-ornithine pathway, which is itself part of Amine and polyamine biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes putrescine from L-ornithine, the pathway putrescine biosynthesis via L-ornithine pathway and in Amine and polyamine biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei197Stacks against the aromatic ring of pyridoxal phosphate and stabilizes reaction intermediatesBy similarity1
    <p>This subsection of the ‘Function’ 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 sitei200Pyridoxal phosphateCombined sources1 Publication1
    Binding sitei237Pyridoxal phosphate; via amino nitrogenCombined sources1 Publication1
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei360Proton donor; shared with dimeric partner1 Publication1
    Binding sitei361Substrate; shared with dimeric partnerBy similarity1
    Binding sitei389Pyridoxal phosphateCombined sources3 Publications1

    <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

    • ornithine decarboxylase activity Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB

    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 functionDecarboxylase, Lyase
    Biological processPolyamine biosynthesis
    LigandPyridoxal phosphate

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:HS03935-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    4.1.1.17 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-350562 Regulation of ornithine decarboxylase (ODC)
    R-HSA-351202 Metabolism of polyamines

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P11926

    SIGNOR Signaling Network Open Resource

    More...
    SIGNORi
    P11926

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

    More...
    UniPathwayi
    UPA00535;UER00288

    <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:
    Ornithine decarboxylase (EC:4.1.1.171 Publication)
    Short name:
    ODC
    <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:ODC1
    <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 2

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    HostDB:ENSG00000115758.12

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:8109 ODC1

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    165640 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_P11926

    <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; Source: COMPARTMENTS

    <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

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi360C → A: 25% decrease of in vitro nitrosylation level. 1 Publication1

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    4953

    MalaCards human disease database

    More...
    MalaCardsi
    ODC1

    Open Targets

    More...
    OpenTargetsi
    ENSG00000115758

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA31897

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL1869

    Drug and drug target database

    More...
    DrugBanki
    DB03856 Alpha-Difluoromethylornithine
    DB06243 Eflornithine
    DB04263 Geneticin
    DB04083 N'-Pyridoxyl-Lysine-5'-Monophosphate
    DB02824 N-Pyridoxyl-Glycine-5-Monophosphate
    DB01917 Putrescine
    DB00114 Pyridoxal Phosphate
    DB02209 Pyridoxine-5'-Phosphate
    DB00127 Spermine

    IUPHAR/BPS Guide to PHARMACOLOGY

    More...
    GuidetoPHARMACOLOGYi
    1276

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    ODC1

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    118377

    <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_00001498911 – 461Ornithine decarboxylaseAdd BLAST461

    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 residuei69N6-(pyridoxal phosphate)lysine1 Publication1 Publication1
    Modified residuei303Phosphoserine; by CK2By similarity1
    Modified residuei360S-nitrosocysteine; in inhibited form1 Publication1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    S-Nitrosylation inhibits the enzyme. S-Nitrosylated in vitro on 4 cysteine residues.2 Publications

    Keywords - PTMi

    Phosphoprotein, S-nitrosylation

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P11926

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

    More...
    PaxDbi
    P11926

    PeptideAtlas

    More...
    PeptideAtlasi
    P11926

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P11926

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    52813

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P11926

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

    More...
    PhosphoSitePlusi
    P11926

    <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 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

    Down-regulated in response to enterovirus 71 (EV71) infection (at protein level).1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000115758 Expressed in 228 organ(s), highest expression level in secondary oocyte

    CleanEx database of gene expression profiles

    More...
    CleanExi
    HS_ODC1

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P11926 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P11926 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    CAB035996
    HPA001536

    <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

    Homodimer. Only the dimer is catalytically active, as the active sites are constructed of residues from both monomers (Probable). Does not form a heterodimer with AZIN2 (By similarity).By similarity1 Publication

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    111007, 10 interactors

    CORUM comprehensive resource of mammalian protein complexes

    More...
    CORUMi
    P11926

    Protein interaction database and analysis system

    More...
    IntActi
    P11926, 16 interactors

    Molecular INTeraction database

    More...
    MINTi
    P11926

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000234111

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P11926

    <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

    1461
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P11926

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

    More...
    SMRi
    P11926

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P11926

    <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>Regioni274 – 277Pyridoxal phosphate bindingCombined sources3 Publications4
    Regioni331 – 332Substrate bindingBy similarity2

    <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

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG0622 Eukaryota
    COG0019 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00390000011560

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000274133

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...
    HOVERGENi
    HBG005456

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P11926

    KEGG Orthology (KO)

    More...
    KOi
    K01581

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    VVGYICE

    Database of Orthologous Groups

    More...
    OrthoDBi
    EOG091G0AJV

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P11926

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF300760

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    2.40.37.10, 1 hit
    3.20.20.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR009006 Ala_racemase/Decarboxylase_C
    IPR022643 De-COase2_C
    IPR022657 De-COase2_CS
    IPR022644 De-COase2_N
    IPR022653 De-COase2_pyr-phos_BS
    IPR000183 Orn/DAP/Arg_de-COase
    IPR002433 Orn_de-COase
    IPR029066 PLP-binding_barrel

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR11482 PTHR11482, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02784 Orn_Arg_deC_N, 1 hit
    PF00278 Orn_DAP_Arg_deC, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR01179 ODADCRBXLASE
    PR01182 ORNDCRBXLASE

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF50621 SSF50621, 1 hit
    SSF51419 SSF51419, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00878 ODR_DC_2_1, 1 hit
    PS00879 ODR_DC_2_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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)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 has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

    P11926-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MNNFGNEEFD CHFLDEGFTA KDILDQKINE VSSSDDKDAF YVADLGDILK
    60 70 80 90 100
    KHLRWLKALP RVTPFYAVKC NDSKAIVKTL AATGTGFDCA SKTEIQLVQS
    110 120 130 140 150
    LGVPPERIIY ANPCKQVSQI KYAANNGVQM MTFDSEVELM KVARAHPKAK
    160 170 180 190 200
    LVLRIATDDS KAVCRLSVKF GATLRTSRLL LERAKELNID VVGVSFHVGS
    210 220 230 240 250
    GCTDPETFVQ AISDARCVFD MGAEVGFSMY LLDIGGGFPG SEDVKLKFEE
    260 270 280 290 300
    ITGVINPALD KYFPSDSGVR IIAEPGRYYV ASAFTLAVNI IAKKIVLKEQ
    310 320 330 340 350
    TGSDDEDESS EQTFMYYVND GVYGSFNCIL YDHAHVKPLL QKRPKPDEKY
    360 370 380 390 400
    YSSSIWGPTC DGLDRIVERC DLPEMHVGDW MLFENMGAYT VAAASTFNGF
    410 420 430 440 450
    QRPTIYYVMS GPAWQLMQQF QNPDFPPEVE EQDASTLPVS CAWESGMKRH
    460
    RAACASASIN V
    Length:461
    Mass (Da):51,148
    Last modified:April 1, 1990 - 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:i8CCB88CE80E823C5
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    C9JG30C9JG30_HUMAN
    Ornithine decarboxylase
    ODC1
    68Annotation score:

    Annotation score:1 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>

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    M16650 mRNA Translation: AAA59966.2
    M31061 Genomic DNA Translation: AAA60563.1
    X16277 Genomic DNA Translation: CAA34353.1
    M33764 Genomic DNA Translation: AAA60564.1
    M34158 Genomic DNA Translation: AAA59969.1
    M81740 Genomic DNA Translation: AAA59967.1
    X55362 mRNA Translation: CAA39047.1
    AK292352 mRNA Translation: BAF85041.1
    AK312766 mRNA Translation: BAG35632.1
    AY841870 Genomic DNA Translation: AAV88093.1
    AC007249 Genomic DNA Translation: AAY15034.1
    CH471053 Genomic DNA Translation: EAX00958.1
    CH471053 Genomic DNA Translation: EAX00959.1
    BC025296 mRNA Translation: AAH25296.1
    X53271 mRNA Translation: CAA37369.1
    M20372 mRNA Translation: AAA59968.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS1672.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S06900 DCHUO

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_001274118.1, NM_001287189.1
    NP_001274119.1, NM_001287190.1
    NP_002530.1, NM_002539.2

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Hs.467701

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000234111; ENSP00000234111; ENSG00000115758
    ENST00000405333; ENSP00000385333; ENSG00000115758

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    4953

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:4953

    UCSC genome browser

    More...
    UCSCi
    uc002rao.3 human

    <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

    NIEHS-SNPs
    Wikipedia

    Ornithine decarboxylase entry

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M16650 mRNA Translation: AAA59966.2
    M31061 Genomic DNA Translation: AAA60563.1
    X16277 Genomic DNA Translation: CAA34353.1
    M33764 Genomic DNA Translation: AAA60564.1
    M34158 Genomic DNA Translation: AAA59969.1
    M81740 Genomic DNA Translation: AAA59967.1
    X55362 mRNA Translation: CAA39047.1
    AK292352 mRNA Translation: BAF85041.1
    AK312766 mRNA Translation: BAG35632.1
    AY841870 Genomic DNA Translation: AAV88093.1
    AC007249 Genomic DNA Translation: AAY15034.1
    CH471053 Genomic DNA Translation: EAX00958.1
    CH471053 Genomic DNA Translation: EAX00959.1
    BC025296 mRNA Translation: AAH25296.1
    X53271 mRNA Translation: CAA37369.1
    M20372 mRNA Translation: AAA59968.1
    CCDSiCCDS1672.1
    PIRiS06900 DCHUO
    RefSeqiNP_001274118.1, NM_001287189.1
    NP_001274119.1, NM_001287190.1
    NP_002530.1, NM_002539.2
    UniGeneiHs.467701

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1D7KX-ray2.10A/B7-427[»]
    2ON3X-ray3.00A/B1-461[»]
    2OO0X-ray1.90A/B1-461[»]
    4ZGYX-ray2.63A2-421[»]
    5BWAX-ray3.20A1-461[»]
    ProteinModelPortaliP11926
    SMRiP11926
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi111007, 10 interactors
    CORUMiP11926
    IntActiP11926, 16 interactors
    MINTiP11926
    STRINGi9606.ENSP00000234111

    Chemistry databases

    BindingDBiP11926
    ChEMBLiCHEMBL1869
    DrugBankiDB03856 Alpha-Difluoromethylornithine
    DB06243 Eflornithine
    DB04263 Geneticin
    DB04083 N'-Pyridoxyl-Lysine-5'-Monophosphate
    DB02824 N-Pyridoxyl-Glycine-5-Monophosphate
    DB01917 Putrescine
    DB00114 Pyridoxal Phosphate
    DB02209 Pyridoxine-5'-Phosphate
    DB00127 Spermine
    GuidetoPHARMACOLOGYi1276

    PTM databases

    iPTMnetiP11926
    PhosphoSitePlusiP11926

    Polymorphism and mutation databases

    BioMutaiODC1
    DMDMi118377

    Proteomic databases

    EPDiP11926
    PaxDbiP11926
    PeptideAtlasiP11926
    PRIDEiP11926
    ProteomicsDBi52813

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    4953
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000234111; ENSP00000234111; ENSG00000115758
    ENST00000405333; ENSP00000385333; ENSG00000115758
    GeneIDi4953
    KEGGihsa:4953
    UCSCiuc002rao.3 human

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    4953
    DisGeNETi4953
    EuPathDBiHostDB:ENSG00000115758.12

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    ODC1
    HGNCiHGNC:8109 ODC1
    HPAiCAB035996
    HPA001536
    MalaCardsiODC1
    MIMi165640 gene
    neXtProtiNX_P11926
    OpenTargetsiENSG00000115758
    PharmGKBiPA31897

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG0622 Eukaryota
    COG0019 LUCA
    GeneTreeiENSGT00390000011560
    HOGENOMiHOG000274133
    HOVERGENiHBG005456
    InParanoidiP11926
    KOiK01581
    OMAiVVGYICE
    OrthoDBiEOG091G0AJV
    PhylomeDBiP11926
    TreeFamiTF300760

    Enzyme and pathway databases

    UniPathwayi
    UPA00535;UER00288

    BioCyciMetaCyc:HS03935-MONOMER
    BRENDAi4.1.1.17 2681
    ReactomeiR-HSA-350562 Regulation of ornithine decarboxylase (ODC)
    R-HSA-351202 Metabolism of polyamines
    SABIO-RKiP11926
    SIGNORiP11926

    Miscellaneous databases

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

    More...
    ChiTaRSi
    ODC1 human
    EvolutionaryTraceiP11926

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    ODC1

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

    More...
    GenomeRNAii
    4953

    Protein Ontology

    More...
    PROi
    PR:P11926

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000115758 Expressed in 228 organ(s), highest expression level in secondary oocyte
    CleanExiHS_ODC1
    ExpressionAtlasiP11926 baseline and differential
    GenevisibleiP11926 HS

    Family and domain databases

    Gene3Di2.40.37.10, 1 hit
    3.20.20.10, 1 hit
    InterProiView protein in InterPro
    IPR009006 Ala_racemase/Decarboxylase_C
    IPR022643 De-COase2_C
    IPR022657 De-COase2_CS
    IPR022644 De-COase2_N
    IPR022653 De-COase2_pyr-phos_BS
    IPR000183 Orn/DAP/Arg_de-COase
    IPR002433 Orn_de-COase
    IPR029066 PLP-binding_barrel
    PANTHERiPTHR11482 PTHR11482, 1 hit
    PfamiView protein in Pfam
    PF02784 Orn_Arg_deC_N, 1 hit
    PF00278 Orn_DAP_Arg_deC, 1 hit
    PRINTSiPR01179 ODADCRBXLASE
    PR01182 ORNDCRBXLASE
    SUPFAMiSSF50621 SSF50621, 1 hit
    SSF51419 SSF51419, 1 hit
    PROSITEiView protein in PROSITE
    PS00878 ODR_DC_2_1, 1 hit
    PS00879 ODR_DC_2_2, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    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 nameiDCOR_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: P11926
    Secondary accession number(s): Q53TU3, Q6LDS9
    <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: October 1, 1989
    Last sequence update: April 1, 1990
    Last modified: December 5, 2018
    This is version 202 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    4. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again