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UniProtKB - O15229 (KMO_HUMAN)

Protein

Kynurenine 3-monooxygenase

Gene

KMO

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 hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn) (PubMed:29429898, PubMed:23575632, PubMed:26752518, PubMed:28604669, PubMed:29208702). Required for synthesis of quinolinic acid, a neurotoxic NMDA receptor antagonist and potential endogenous inhibitor of NMDA receptor signaling in axonal targeting, synaptogenesis and apoptosis during brain development. Quinolinic acid may also affect NMDA receptor signaling in pancreatic beta cells, osteoblasts, myocardial cells, and the gastrointestinal tract (Probable).1 Publication5 Publications

Miscellaneous

Increased in neuroinflammatory conditions. Inhibitors are investigated as potential neuroprotective drugs since they lead to an increased level of kynurenic acid, a neuroprotective NMDA receptor agonist.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

FADUniRule annotation2 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 0.24 sec(-1) for L-kynurenine.1 Publication
  1. KM=24.1 µM for L-kynurenine3 Publications
  2. KM=2 µM for L-kynurenine1 Publication
  3. KM=78 µM for L-kynurenine1 Publication
  1. Vmax=8.5 µmol/min/mg enzyme2 Publications

pH dependencei

Optimum pH is 7.5.2 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: NAD(+) biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes quinolinate from L-kynurenine.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Kynurenine 3-monooxygenase (KMO), Kynurenine 3-monooxygenase (KMO), Kynurenine 3-monooxygenase (KMO), Kynurenine 3-monooxygenase (KMO)
  2. Kynureninase (KYNU), Kynureninase (KYNU), Kynureninase (KYNU)
  3. 3-hydroxyanthranilate 3,4-dioxygenase (HAAO)
This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes quinolinate from L-kynurenine, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei19FAD; via amide nitrogenCombined sources1 Publication1
Binding sitei57FAD; via amide nitrogen and carbonyl oxygenCombined sources1 Publication1
Binding sitei85L-kynurenineBy similarity1
Binding sitei99L-kynurenineBy similarity1
Binding sitei111FADCombined sources1 Publication1
Binding sitei136FAD; via amide nitrogen and carbonyl oxygenCombined sources1 Publication1
Binding sitei172FADCombined sources1 Publication1
Binding sitei304FAD; via amide nitrogenCombined sources1 Publication1
Binding sitei363L-kynurenineBy similarity1
Binding sitei398L-kynurenineBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi37 – 40FADCombined sources1 Publication4
Nucleotide bindingi317 – 318FADCombined sources1 Publication2

<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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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 functionMonooxygenase, Oxidoreductase
Biological processPyridine nucleotide biosynthesis
LigandFAD, Flavoprotein, NADP

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:HS04082-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-71240 Tryptophan catabolism

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		O15229

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

More...UniPathwayi
UPA00253;UER00328

<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:
Kynurenine 3-monooxygenaseUniRule annotation (EC:1.14.13.9UniRule annotation)
Alternative name(s):
Kynurenine 3-hydroxylaseUniRule annotation
<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:KMOUniRule annotationImported
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000117009.11

Human Gene Nomenclature Database

More...HGNCi		HGNC:6381 KMO

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		603538 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_O15229

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei385 – 404HelicalUniRule annotationAdd BLAST20
Transmembranei425 – 445HelicalUniRule annotationAdd BLAST21

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

<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>Mutagenesisi85R → A or K: Abolishes kynurenine 3-monooxygenase activity. 1 Publication1
Mutagenesisi99Y → A: Abolishes kynurenine 3-monooxygenase activity. 1 Publication1
Mutagenesisi99Y → F: Strongly decreases kynurenine 3-monooxygenase activity. 1 Publication1
Mutagenesisi312 – 313FF → AA: Abolishes NADPH oxidase activity. 1 Publication2
Mutagenesisi312F → A: Decreases to 30% NADPH oxidase activity. 1 Publication1
Mutagenesisi313F → A: Decreases to 50% NADPH oxidase activity. 1 Publication1
Mutagenesisi363N → A: Strongly decreases kynurenine 3-monooxygenase activity. 1 Publication1
Mutagenesisi363N → D: Abolishes kynurenine 3-monooxygenase activity. 1 Publication1
Mutagenesisi366E → A or Q: Strongly decreases kynurenine 3-monooxygenase activity. 1 Publication1
Mutagenesisi367M → A: Strongly decreases kynurenine 3-monooxygenase activity. 1 Publication1
Mutagenesisi367M → L: Strongly decreases kynurenine 3-monooxygenase activity. 1 Publication1
Mutagenesisi398Y → A or F: Abolishes kynurenine 3-monooxygenase activity. 1 Publication1
Mutagenesisi465N → A: Not glycosylted. Reduces to 80% kynurenine 3-monooxygenase activity. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		8564

Open Targets

More...OpenTargetsi		ENSG00000117009

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA30172

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2145

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2886

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		KMO

<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_00002297421 – 486Kynurenine 3-monooxygenaseCuratedAdd BLAST486

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi465N-linked (GlcNAc...) asparagine1 Publication1

Keywords - PTMi

Glycoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		O15229

MaxQB - The MaxQuant DataBase

More...MaxQBi		O15229

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

More...PaxDbi		O15229

PeptideAtlas

More...PeptideAtlasi		O15229

PRoteomics IDEntifications database

More...PRIDEi		O15229

ProteomicsDB human proteome resource

More...ProteomicsDBi		48519
48520 [O15229-2]
48521 [O15229-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		O15229

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

More...PhosphoSitePlusi		O15229

<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

Highest levels in placenta and liver. Detectable in kidney.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000117009 Expressed in 128 organ(s), highest expression level in placenta

CleanEx database of gene expression profiles

More...CleanExi		HS_KMO

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		O15229 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		O15229 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA031115
HPA056942

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		114133, 4 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000355517

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		O15229

<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

1486
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
5X68X-ray2.10A/B1-374[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		O15229

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

More...SMRi		O15229

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<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

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Transmembrane domains are required for enzymatic activity.2 Publications

<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 aromatic-ring hydroxylase family. KMO subfamily.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2614 Eukaryota
COG0654 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00390000000747

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG057213

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O15229

KEGG Orthology (KO)

More...KOi		K00486

Identification of Orthologs from Complete Genome Data

More...OMAi		MHGRMIH

Database of Orthologous Groups

More...OrthoDBi		497681at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		O15229

TreeFam database of animal gene trees

More...TreeFami		TF312990

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.50.50.60, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_01971 Kynurenine_monooxygenase, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR002938 FAD-bd
IPR036188 FAD/NAD-bd_sf
IPR027545 Kynurenine_monooxygenase

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01494 FAD_binding_3, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF51905 SSF51905, 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>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

This entry has 3 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 12 Publications (identifier: O15229-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MDSSVIQRKK VAVIGGGLVG SLQACFLAKR NFQIDVYEAR EDTRVATFTR 
        60         70         80         90        100
GRSINLALSH RGRQALKAVG LEDQIVSQGI PMRARMIHSL SGKKSAIPYG 
       110        120        130        140        150
TKSQYILSVS RENLNKDLLT AAEKYPNVKM HFNHRLLKCN PEEGMITVLG 
       160        170        180        190        200
SDKVPKDVTC DLIVGCDGAY STVRSHLMKK PRFDYSQQYI PHGYMELTIP 
       210        220        230        240        250
PKNGDYAMEP NYLHIWPRNT FMMIALPNMN KSFTCTLFMP FEEFEKLLTS 
       260        270        280        290        300
NDVVDFFQKY FPDAIPLIGE KLLVQDFFLL PAQPMISVKC SSFHFKSHCV 
       310        320        330        340        350
LLGDAAHAIV PFFGQGMNAG FEDCLVFDEL MDKFSNDLSL CLPVFSRLRI 
       360        370        380        390        400
PDDHAISDLS MYNYIEMRAH VNSSWFIFQK NMERFLHAIM PSTFIPLYTM 
       410        420        430        440        450
VTFSRIRYHE AVQRWHWQKK VINKGLFFLG SLIAISSTYL LIHYMSPRSF 
       460        470        480 
LRLRRPWNWI AHFRNTTCFP AKAVDSLEQI SNLISR
Length:486
Mass (Da):55,810
Last modified:February 20, 2007 - 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:i164870D52E62A08A
GO
Isoform 21 Publication (identifier: O15229-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     367-379: Missing.

Note: Gene model based on cDNA data. No experimental confirmation available.
Show »
Length:473
Mass (Da):54,205
Checksum:i9D898B2A91A76782
GO
Isoform 31 Publication (identifier: O15229-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     367-400: Missing.

Note: Gene model based on mouse cDNA data. No experimental confirmation available.
Show »
Length:452
Mass (Da):51,682
Checksum:i59D707C5D8F21C03
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
H0Y320H0Y320_HUMAN
Kynurenine 3-monooxygenase
KMO
182Annotation 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>

Natural variant

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_030845452R → C2 PublicationsCorresponds to variant dbSNP:rs1053230Ensembl.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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_051972367 – 400Missing in isoform 3. 1 PublicationAdd BLAST34
Alternative sequenceiVSP_051973367 – 379Missing in isoform 2. 1 PublicationAdd BLAST13

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
Y13153 mRNA Translation: CAA73613.1
AF056032 mRNA Translation: AAC62615.1
AL133390 Genomic DNA No translation available.
FO393423 Genomic DNA No translation available.

The Consensus CDS (CCDS) project

More...CCDSi		CCDS1618.1 [O15229-1]

NCBI Reference Sequences

More...RefSeqi		NP_003670.2, NM_003679.4 [O15229-1]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.731056
Hs.744065

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000366557; ENSP00000355515; ENSG00000117009 [O15229-3]
ENST00000366558; ENSP00000355516; ENSG00000117009 [O15229-2]
ENST00000366559; ENSP00000355517; ENSG00000117009 [O15229-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		8564

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:8564

UCSC genome browser

More...UCSCi		uc001hyy.4 human [O15229-1]

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13153 mRNA Translation: CAA73613.1
AF056032 mRNA Translation: AAC62615.1
AL133390 Genomic DNA No translation available.
FO393423 Genomic DNA No translation available.
CCDSiCCDS1618.1 [O15229-1]
RefSeqiNP_003670.2, NM_003679.4 [O15229-1]
UniGeneiHs.731056
Hs.744065

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5X68X-ray2.10A/B1-374[»]
ProteinModelPortaliO15229
SMRiO15229
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114133, 4 interactors
STRINGi9606.ENSP00000355517

Chemistry databases

BindingDBiO15229
ChEMBLiCHEMBL2145
GuidetoPHARMACOLOGYi2886

PTM databases

iPTMnetiO15229
PhosphoSitePlusiO15229

Polymorphism and mutation databases

BioMutaiKMO

Proteomic databases

jPOSTiO15229
MaxQBiO15229
PaxDbiO15229
PeptideAtlasiO15229
PRIDEiO15229
ProteomicsDBi48519
48520 [O15229-2]
48521 [O15229-3]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366557; ENSP00000355515; ENSG00000117009 [O15229-3]
ENST00000366558; ENSP00000355516; ENSG00000117009 [O15229-2]
ENST00000366559; ENSP00000355517; ENSG00000117009 [O15229-1]
GeneIDi8564
KEGGihsa:8564
UCSCiuc001hyy.4 human [O15229-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		8564
DisGeNETi8564
EuPathDBiHostDB:ENSG00000117009.11

GeneCards: human genes, protein and diseases

More...GeneCardsi		KMO
HGNCiHGNC:6381 KMO
HPAiHPA031115
HPA056942
MIMi603538 gene
neXtProtiNX_O15229
OpenTargetsiENSG00000117009
PharmGKBiPA30172

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG2614 Eukaryota
COG0654 LUCA
GeneTreeiENSGT00390000000747
HOVERGENiHBG057213
InParanoidiO15229
KOiK00486
OMAiMHGRMIH
OrthoDBi497681at2759
PhylomeDBiO15229
TreeFamiTF312990

Enzyme and pathway databases

UniPathwayi
UPA00253;UER00328

BioCyciMetaCyc:HS04082-MONOMER
ReactomeiR-HSA-71240 Tryptophan catabolism
SABIO-RKiO15229

Miscellaneous databases

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

More...ChiTaRSi		KMO human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		KMO_(gene)

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

More...GenomeRNAii		8564

Protein Ontology

More...PROi		PR:O15229

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000117009 Expressed in 128 organ(s), highest expression level in placenta
CleanExiHS_KMO
ExpressionAtlasiO15229 baseline and differential
GenevisibleiO15229 HS

Family and domain databases

Gene3Di3.50.50.60, 1 hit
HAMAPiMF_01971 Kynurenine_monooxygenase, 1 hit
InterProiView protein in InterPro
IPR002938 FAD-bd
IPR036188 FAD/NAD-bd_sf
IPR027545 Kynurenine_monooxygenase
PfamiView protein in Pfam
PF01494 FAD_binding_3, 1 hit
SUPFAMiSSF51905 SSF51905, 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 nameiKMO_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: O15229
Secondary accession number(s): A2A2U8
, A2A2U9, A2A2V0, Q5SY07, Q5SY08, Q5SY09
<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: April 4, 2006
Last sequence update: February 20, 2007
Last modified: January 16, 2019
This is version 155 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. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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