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Protein

Ornithine decarboxylase

Gene

Odc1

Organism
Mus musculus (Mouse)
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.2 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

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 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.By similarity

<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 intermediates1 Publication1
<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 phosphateBy similarity1
Binding sitei237Pyridoxal phosphate; via amino nitrogen1 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 partner3 Publications1
Binding sitei361Substrate; shared with dimeric partnerBy similarity1
Binding sitei389Pyridoxal phosphate1 Publication1

<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

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.1.1.17 3474

Reactome - a knowledgebase of biological pathways and processes

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

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:4.1.1.17)
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
Synonyms:Odc
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 12

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:97402 Odc1

<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>Mutagenesisi387G → A: Partial loss of activity. 1 Publication1
Mutagenesisi387G → C, D, E, F, H, I, K, L, M, N, P, Q, R, S, T, V, W or Y: Loss of activity. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2840

<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_00001498921 – 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)lysineCombined sources2 Publications1
Modified residuei303Phosphoserine; by CK21 Publication1
Modified residuei360S-nitrosocysteineBy similarity1

Keywords - PTMi

Phosphoprotein, S-nitrosylation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P00860

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P00860

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

More...
PaxDbi
P00860

PRoteomics IDEntifications database

More...
PRIDEi
P00860

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P00860

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

More...
PhosphoSitePlusi
P00860

<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

Expressed during testis development in the outer part of the seminiferous tubules.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000011179 Expressed in 103 organ(s), highest expression level in adult mammalian kidney

CleanEx database of gene expression profiles

More...
CleanExi
MM_ODC1

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P00860 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P00860 MM

<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 (PubMed:8106349, PubMed:10378276). Does not form a heterodimer with AZIN2 (PubMed:24967154).3 Publications

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

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IntActi
P00860, 1 interactor

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000128661

<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

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ProteinModelPortali
P00860

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

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SMRi
P00860

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P00860

<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 binding1 Publication4
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

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GeneTreei
ENSGT00390000011560

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000274133

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG005456

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P00860

KEGG Orthology (KO)

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KOi
K01581

Identification of Orthologs from Complete Genome Data

More...
OMAi
VVGYICE

Database of Orthologous Groups

More...
OrthoDBi
EOG091G0AJV

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

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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 2 potential isoforms that are computationally mapped.Show allAlign All

P00860-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSSFTKDEFD CHILDEGFTA KDILDQKINE VSSSDDKDAF YVADLGDILK
60 70 80 90 100
KHLRWLKALP RVTPFYAVKC NDSRAIVSTL AAIGTGFDCA SKTEIQLVQG
110 120 130 140 150
LGVPAERVIY ANPCKQVSQI KYAASNGVQM MTFDSEIELM KVARAHPKAK
160 170 180 190 200
LVLRIATDDS KAVCRLSVKF GATLKTSRLL LERAKELNID VIGVSFHVGS
210 220 230 240 250
GCTDPETFVQ AVSDARCVFD MATEVGFSMH LLDIGGGFPG SEDTKLKFEE
260 270 280 290 300
ITSVINPALD KYFPSDSGVR IIAEPGRYYV ASAFTLAVNI IAKKTVWKEQ
310 320 330 340 350
PGSDDEDESN EQTFMYYVND GVYGSFNCIL YDHAHVKALL QKRPKPDEKY
360 370 380 390 400
YSSSIWGPTC DGLDRIVERC NLPEMHVGDW MLFENMGAYT VAAASTFNGF
410 420 430 440 450
QRPNIYYVMS RPMWQLMKQI QSHGFPPEVE EQDDGTLPMS CAQESGMDRH
460
PAACASARIN V
Length:461
Mass (Da):51,177
Last modified:July 27, 2011 - 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:iB581753F57AC0A30
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 are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A1Y7VJC5A0A1Y7VJC5_MOUSE
Ornithine decarboxylase
Odc1
197Annotation 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>
A0A1Y7VMF9A0A1Y7VMF9_MOUSE
Ornithine decarboxylase
Odc1
42Annotation 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>

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 conflicti178R → W in AAA39846 (PubMed:3456155).Curated1
Sequence conflicti206E → D in AAA51638 (PubMed:2982844).Curated1
Sequence conflicti206E → D in AAA39845 (PubMed:3856848).Curated1
Sequence conflicti206E → D in CAA30301 (PubMed:3362685).Curated1
Sequence conflicti206E → D in AAA39849 (PubMed:3372502).Curated1
Sequence conflicti206E → D in AAB27809 (PubMed:8350350).Curated1
Sequence conflicti350Y → H in AAA39848 (PubMed:3456155).Curated1

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
M20617 mRNA Translation: AAA51638.1
M10624 mRNA Translation: AAA39845.1
X07392 Genomic DNA Translation: CAA30301.1
J03733 Genomic DNA Translation: AAA39849.1
S64539 mRNA Translation: AAB27809.1
EU684749 mRNA Translation: ACD81645.1
AK139610 mRNA Translation: BAE24082.1
CH466582 Genomic DNA Translation: EDK98494.1
BC059826 mRNA Translation: AAH59826.1
BC083122 mRNA Translation: AAH83122.1
M12330 mRNA Translation: AAA39846.1
M12331 mRNA Translation: AAA39848.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS25829.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A01077 DCMSO
I56477

NCBI Reference Sequences

More...
RefSeqi
NP_038642.2, NM_013614.2
XP_017170479.1, XM_017314990.1

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Mm.34102
Mm.472891

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000171737; ENSMUSP00000128661; ENSMUSG00000011179

Database of genes from NCBI RefSeq genomes

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GeneIDi
18263

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:18263

UCSC genome browser

More...
UCSCi
uc007ncv.1 mouse

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20617 mRNA Translation: AAA51638.1
M10624 mRNA Translation: AAA39845.1
X07392 Genomic DNA Translation: CAA30301.1
J03733 Genomic DNA Translation: AAA39849.1
S64539 mRNA Translation: AAB27809.1
EU684749 mRNA Translation: ACD81645.1
AK139610 mRNA Translation: BAE24082.1
CH466582 Genomic DNA Translation: EDK98494.1
BC059826 mRNA Translation: AAH59826.1
BC083122 mRNA Translation: AAH83122.1
M12330 mRNA Translation: AAA39846.1
M12331 mRNA Translation: AAA39848.1
CCDSiCCDS25829.1
PIRiA01077 DCMSO
I56477
RefSeqiNP_038642.2, NM_013614.2
XP_017170479.1, XM_017314990.1
UniGeneiMm.34102
Mm.472891

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
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
7ODCX-ray1.60A1-424[»]
ProteinModelPortaliP00860
SMRiP00860
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP00860, 1 interactor
STRINGi10090.ENSMUSP00000128661

Chemistry databases

ChEMBLiCHEMBL2840

PTM databases

iPTMnetiP00860
PhosphoSitePlusiP00860

Proteomic databases

EPDiP00860
MaxQBiP00860
PaxDbiP00860
PRIDEiP00860

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000171737; ENSMUSP00000128661; ENSMUSG00000011179
GeneIDi18263
KEGGimmu:18263
UCSCiuc007ncv.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
4953
MGIiMGI:97402 Odc1

Phylogenomic databases

eggNOGiKOG0622 Eukaryota
COG0019 LUCA
GeneTreeiENSGT00390000011560
HOGENOMiHOG000274133
HOVERGENiHBG005456
InParanoidiP00860
KOiK01581
OMAiVVGYICE
OrthoDBiEOG091G0AJV
TreeFamiTF300760

Enzyme and pathway databases

UniPathwayi
UPA00535;UER00288

BRENDAi4.1.1.17 3474
ReactomeiR-MMU-350562 Regulation of ornithine decarboxylase (ODC)
R-MMU-351202 Metabolism of polyamines

Miscellaneous databases

EvolutionaryTraceiP00860

Protein Ontology

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PROi
PR:P00860

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSMUSG00000011179 Expressed in 103 organ(s), highest expression level in adult mammalian kidney
CleanExiMM_ODC1
ExpressionAtlasiP00860 baseline and differential
GenevisibleiP00860 MM

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

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ProtoNeti
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<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_MOUSE
<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: P00860
Secondary accession number(s): Q61997, Q61998, Q6PB87
<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: July 21, 1986
Last sequence update: July 27, 2011
Last modified: December 5, 2018
This is version 166 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

<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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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