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UniProtKB - Q9Y233 (PDE10_HUMAN)

Protein

cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A

Gene

PDE10A

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

Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. Can hydrolyze both cAMP and cGMP, but has higher affinity for cAMP and is more efficient with cAMP as substrate. May play a critical role in regulating cAMP and cGMP levels in the striatum, a region of the brain that contributes to the control of movement and cognition.By similarity1 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

a divalent metal cation1 PublicationNote: Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions.1 Publication

<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 dipyridamole and moderately by IBMX. cAMP acts as an allosteric activator.1 Publication

<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

  1. KM=56 nM for cAMP1 Publication
  2. KM=4.4 µM for cGMP1 Publication
  1. Vmax=507 nmol/min/mg enzyme for cAMP1 Publication
  2. Vmax=1860 nmol/min/mg enzyme for cGMP1 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: 3',5'-cyclic AMP degradation

This protein is involved in step 1 of the subpathway that synthesizes AMP from 3',5'-cyclic AMP.
Proteins known to be involved in this subpathway in this organism are:
  1. High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A (PDE8A), High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A (PDE7A), cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A (PDE10A), cAMP-specific 3',5'-cyclic phosphodiesterase 4D (PDE4D), cAMP-specific 3',5'-cyclic phosphodiesterase 4C (PDE4C), High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B (PDE8B), cAMP-specific 3',5'-cyclic phosphodiesterase 4A (PDE4A), cAMP-specific 3',5'-cyclic phosphodiesterase 4B (PDE4B), cAMP-specific 3',5'-cyclic phosphodiesterase 7B (PDE7B)
This subpathway is part of the pathway 3',5'-cyclic AMP degradation, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes AMP from 3',5'-cyclic AMP, the pathway 3',5'-cyclic AMP degradation and in Purine metabolism.

Pathwayi: 3',5'-cyclic GMP degradation

This protein is involved in step 1 of the subpathway that synthesizes GMP from 3',5'-cyclic GMP.
Proteins known to be involved in this subpathway in this organism are:
  1. cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A (PDE10A), High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A (PDE9A), cGMP-specific 3',5'-cyclic phosphodiesterase (PDE5A)
This subpathway is part of the pathway 3',5'-cyclic GMP degradation, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes GMP from 3',5'-cyclic GMP, the pathway 3',5'-cyclic GMP degradation and in Purine metabolism.

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 sitei364Allosteric effector1
Binding sitei383Allosteric effector1
<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 sitei515Proton donorBy similarity1
Binding sitei515Substrate1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi519Divalent metal cation 11
Metal bindingi553Divalent metal cation 11
Metal bindingi554Divalent metal cation 11
Metal bindingi554Divalent metal cation 21
Metal bindingi664Divalent metal cation 11
Binding sitei716Substrate1

<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

  • 3',5'-cyclic-AMP phosphodiesterase activity Source: Reactome
  • 3',5'-cyclic-GMP phosphodiesterase activity Source: Reactome
  • 3',5'-cyclic-nucleotide phosphodiesterase activity Source: GO_Central
  • cAMP binding Source: UniProtKB
  • cGMP binding Source: UniProtKB
  • cGMP-stimulated cyclic-nucleotide phosphodiesterase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
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 functionAllosteric enzyme, Hydrolase
LigandcAMP, cAMP-binding, cGMP, cGMP-binding, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.1.4.17 2681

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-418457 cGMP effects
R-HSA-418555 G alpha (s) signalling events

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		Q9Y233

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q9Y233

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

More...UniPathwayi
UPA00762;UER00747

UPA00763;UER00748

<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:
cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A (EC:3.1.4.17, EC:3.1.4.35)
<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:PDE10A
<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 6

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000112541.13

Human Gene Nomenclature Database

More...HGNCi		HGNC:8772 PDE10A

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		610652 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q9Y233

<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

Keywords - Cellular componenti

Cytoplasm

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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Dyskinesia, limb and orofacial, infantile-onset (IOLOD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive, early-onset hyperkinetic movement disorder characterized by axial hypotonia, dyskinesia of the limbs and trunk, orofacial dyskinesia, drooling, and dysarthria. The severity of the hyperkinesis is variable.
See also OMIM:616921
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_07679897Y → C in IOLOD; decreased protein abundance. 1 PublicationCorresponds to variant dbSNP:rs778899140Ensembl.1
Natural variantiVAR_076799106A → P in IOLOD; decreased protein abundance. 1 PublicationCorresponds to variant dbSNP:rs875989839Ensembl.1
Striatal degeneration, autosomal dominant 2 (ADSD2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disorder characterized by striatal degeneration and dysfunction of basal ganglia, resulting in hyperkinesis.
See also OMIM:616922
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_076800290F → L in ADSD2; no effect on basal 3',5'-cyclic-nucleotide phosphodiesterase activity; the mutation severely disrupts the stimulatory effect on the enzyme activity mediated by cAMP binding. 1 PublicationCorresponds to variant dbSNP:rs875989841Ensembl.1
Natural variantiVAR_076801324F → L in ADSD2; no effect on basal 3',5'-cyclic-nucleotide phosphodiesterase activity; the mutation severely disrupts the stimulatory effect on the enzyme activity mediated by cAMP binding. 1 PublicationCorresponds to variant dbSNP:rs875989840Ensembl.1

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>Mutagenesisi554D → A: Loss of activity and of zinc binding. 1 Publication1
Mutagenesisi554D → N: Reduces activity 1000-fold. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...DisGeNETi		10846

MalaCards human disease database

More...MalaCardsi		PDE10A
MIMi616921 phenotype
616922 phenotype

Open Targets

More...OpenTargetsi		ENSG00000112541

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

More...Orphaneti		494541 Childhood-onset benign chorea with striatal involvement
494526 Infantile-onset generalized dyskinesia with orofacial involvement

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA33120

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4409

Drug and drug target database

More...DrugBanki		DB08384 2-({4-[4-(pyridin-4-ylmethyl)-1H-pyrazol-3-yl]phenoxy}methyl)quinoline
DB08387 2-{[4-(1-methyl-4-pyridin-4-yl-1H-pyrazol-3-yl)phenoxy]methyl}quinoline
DB08386 2-{[4-(4-pyridin-4-yl-1H-pyrazol-3-yl)phenoxy]methyl}quinoline
DB00201 Caffeine
DB00975 Dipyridamole
DB01113 Papaverine
DB08811 Tofisopam
DB08814 Triflusal

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		1310

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		PDE10A

Domain mapping of disease mutations (DMDM)

More...DMDMi		7993747

<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_00001988431 – 779cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10AAdd BLAST779

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Isoform PDE10A2 (identifier: Q9Y233-2)
<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 residuei16Phosphothreonine1 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

Isoform PDE10A2: Phosphorylated on Thr-16.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q9Y233

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

More...PaxDbi		Q9Y233

PeptideAtlas

More...PeptideAtlasi		Q9Y233

PRoteomics IDEntifications database

More...PRIDEi		Q9Y233

ProteomicsDB human proteome resource

More...ProteomicsDBi		85625
85626 [Q9Y233-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9Y233

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

More...PhosphoSitePlusi		Q9Y233

SwissPalm database of S-palmitoylation events

More...SwissPalmi		Q9Y233

<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

Abundant in the putamen and caudate nucleus regions of brain and testis, moderately expressed in the thyroid gland, pituitary gland, thalamus and cerebellum.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000112541 Expressed in 158 organ(s), highest expression level in caudate nucleus

CleanEx database of gene expression profiles

More...CleanExi		HS_PDE10A

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q9Y233 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9Y233 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB045998
HPA047200

<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.1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		116057, 3 interactors

Protein interaction database and analysis system

More...IntActi		Q9Y233, 1 interactor

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000438284

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q9Y233

<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

1779
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		Q9Y233

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

More...SMRi		Q9Y233

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		Q9Y233

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini91 – 234GAF 1Add BLAST144
Domaini266 – 412GAF 2Add BLAST147
Domaini442 – 759PDEasePROSITE-ProRule annotationAdd BLAST318

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>Regioni286 – 287Allosteric effector binding2
Regioni330 – 331Allosteric effector binding2

<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

The tandem GAF domains bind cAMP, and regulate enzyme activity. The binding of cAMP stimulates enzyme activity.
Composed of a C-terminal catalytic domain containing two divalent metal sites and an N-terminal regulatory domain which contains one cyclic nucleotide-binding region.

<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 cyclic nucleotide phosphodiesterase family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3689 Eukaryota
ENOG410XRI7 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000156543

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000007068

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG082113

KEGG Orthology (KO)

More...KOi		K18438

Identification of Orthologs from Complete Genome Data

More...OMAi		ESAVWIS

Database of Orthologous Groups

More...OrthoDBi		EOG091G037C

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9Y233

TreeFam database of animal gene trees

More...TreeFami		TF316499

Family and domain databases

Conserved Domains Database

More...CDDi		cd00077 HDc, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.1300.10, 1 hit
3.30.450.40, 2 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR003018 GAF
IPR029016 GAF-like_dom_sf
IPR003607 HD/PDEase_dom
IPR023088 PDEase
IPR002073 PDEase_catalytic_dom
IPR036971 PDEase_catalytic_dom_sf
IPR023174 PDEase_CS

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01590 GAF, 2 hits
PF00233 PDEase_I, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00387 PDIESTERASE1

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00065 GAF, 2 hits
SM00471 HDc, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00126 PDEASE_I_1, 1 hit
PS51845 PDEASE_I_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>Sequences (2+)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 2 <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
Note: Isoforms differ in their N-terminal region.

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform PDE10A1 (identifier: Q9Y233-1) [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.

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        10         20         30         40         50
MRIEERKSQH LTGLTDEKVK AYLSLHPQVL DEFVSESVSA ETVEKWLKRK 
        60         70         80         90        100
NNKSEDESAP KEVSRYQDTN MQGVVYELNS YIEQRLDTGG DNQLLLYELS 
       110        120        130        140        150
SIIKIATKAD GFALYFLGEC NNSLCIFTPP GIKEGKPRLI PAGPITQGTT 
       160        170        180        190        200
VSAYVAKSRK TLLVEDILGD ERFPRGTGLE SGTRIQSVLC LPIVTAIGDL 
       210        220        230        240        250
IGILELYRHW GKEAFCLSHQ EVATANLAWA SVAIHQVQVC RGLAKQTELN 
       260        270        280        290        300
DFLLDVSKTY FDNIVAIDSL LEHIMIYAKN LVNADRCALF QVDHKNKELY 
       310        320        330        340        350
SDLFDIGEEK EGKPVFKKTK EIRFSIEKGI AGQVARTGEV LNIPDAYADP 
       360        370        380        390        400
RFNREVDLYT GYTTRNILCM PIVSRGSVIG VVQMVNKISG SAFSKTDENN 
       410        420        430        440        450
FKMFAVFCAL ALHCANMYHR IRHSECIYRV TMEKLSYHSI CTSEEWQGLM 
       460        470        480        490        500
QFTLPVRLCK EIELFHFDIG PFENMWPGIF VYMVHRSCGT SCFELEKLCR 
       510        520        530        540        550
FIMSVKKNYR RVPYHNWKHA VTVAHCMYAI LQNNHTLFTD LERKGLLIAC 
       560        570        580        590        600
LCHDLDHRGF SNSYLQKFDH PLAALYSTST MEQHHFSQTV SILQLEGHNI 
       610        620        630        640        650
FSTLSSSEYE QVLEIIRKAI IATDLALYFG NRKQLEEMYQ TGSLNLNNQS 
       660        670        680        690        700
HRDRVIGLMM TACDLCSVTK LWPVTKLTAN DIYAEFWAEG DEMKKLGIQP 
       710        720        730        740        750
IPMMDRDKKD EVPQGQLGFY NAVAIPCYTT LTQILPPTEP LLKACRDNLS 
       760        770 
QWEKVIRGEE TATWISSPSV AQKAAASED
Length:779
Mass (Da):88,412
Last modified:November 1, 1999 - v1
<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:iC5651BBB524A32B7
GO
Isoform PDE10A2 (identifier: Q9Y233-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: MRIEERKSQHLTG → MEDGPSNNASCFRRLTECFLSPS

Show »
Length:789
Mass (Da):89,390
Checksum:i7CC35F16735FB3C2
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
A0A087WUD0A0A087WUD0_HUMAN
cAMP and cAMP-inhibited cGMP 3',5'-...
PDE10A
183Annotation 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAD32596 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

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 conflicti657G → S in CAG38804 (Ref. 4) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07679897Y → C in IOLOD; decreased protein abundance. 1 PublicationCorresponds to variant dbSNP:rs778899140Ensembl.1
Natural variantiVAR_076799106A → P in IOLOD; decreased protein abundance. 1 PublicationCorresponds to variant dbSNP:rs875989839Ensembl.1
Natural variantiVAR_076800290F → L in ADSD2; no effect on basal 3',5'-cyclic-nucleotide phosphodiesterase activity; the mutation severely disrupts the stimulatory effect on the enzyme activity mediated by cAMP binding. 1 PublicationCorresponds to variant dbSNP:rs875989841Ensembl.1
Natural variantiVAR_008797303L → P. 1
Natural variantiVAR_076801324F → L in ADSD2; no effect on basal 3',5'-cyclic-nucleotide phosphodiesterase activity; the mutation severely disrupts the stimulatory effect on the enzyme activity mediated by cAMP binding. 1 PublicationCorresponds to variant dbSNP:rs875989840Ensembl.1
Natural variantiVAR_047822706R → K. Corresponds to variant dbSNP:rs2224252Ensembl.1
Natural variantiVAR_047823707D → N. Corresponds to variant dbSNP:rs2860112Ensembl.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_0046011 – 13MRIEE…QHLTG → MEDGPSNNASCFRRLTECFL SPS in isoform PDE10A2. 2 PublicationsAdd 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
AB026816 mRNA Translation: BAA84467.1
AB020593 mRNA Translation: BAA78034.1
AF127479 mRNA Translation: AAD32595.1
AF127480 mRNA Translation: AAD32596.1 Different initiation.
CR536567 mRNA Translation: CAG38804.1
AL117345 Genomic DNA No translation available.
AL136130 Genomic DNA No translation available.
AL160160 Genomic DNA No translation available.
BC104858 mRNA Translation: AAI04859.1
BC104860 mRNA Translation: AAI04861.1
AB041798 Genomic DNA Translation: BAB16383.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS47513.1 [Q9Y233-2]
CCDS5289.1 [Q9Y233-1]

NCBI Reference Sequences

More...RefSeqi		NP_001124162.1, NM_001130690.2 [Q9Y233-2]
NP_006652.1, NM_006661.3 [Q9Y233-1]
XP_011533690.1, XM_011535388.2 [Q9Y233-1]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.348762

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000366882; ENSP00000355847; ENSG00000112541 [Q9Y233-2]
ENST00000650117; ENSP00000497426; ENSG00000112541 [Q9Y233-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		10846

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:10846

UCSC genome browser

More...UCSCi		uc003quo.4 human [Q9Y233-1]

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
AB026816 mRNA Translation: BAA84467.1
AB020593 mRNA Translation: BAA78034.1
AF127479 mRNA Translation: AAD32595.1
AF127480 mRNA Translation: AAD32596.1 Different initiation.
CR536567 mRNA Translation: CAG38804.1
AL117345 Genomic DNA No translation available.
AL136130 Genomic DNA No translation available.
AL160160 Genomic DNA No translation available.
BC104858 mRNA Translation: AAI04859.1
BC104860 mRNA Translation: AAI04861.1
AB041798 Genomic DNA Translation: BAB16383.1
CCDSiCCDS47513.1 [Q9Y233-2]
CCDS5289.1 [Q9Y233-1]
RefSeqiNP_001124162.1, NM_001130690.2 [Q9Y233-2]
NP_006652.1, NM_006661.3 [Q9Y233-1]
XP_011533690.1, XM_011535388.2 [Q9Y233-1]
UniGeneiHs.348762

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
1LRBmodel-A501-757[»]
2OUNX-ray1.56A/B439-766[»]
2OUPX-ray1.56A/B439-766[»]
2OUQX-ray1.90A/B439-766[»]
2OURX-ray1.45A/B439-766[»]
2OUSX-ray1.45A/B439-766[»]
2OUUX-ray1.52A/B439-766[»]
2OUVX-ray1.56A/B439-766[»]
2OUYX-ray1.90A/B439-766[»]
2WEYX-ray2.80A/B439-779[»]
2Y0JX-ray2.43A/B432-764[»]
2ZMFX-ray2.10A/B246-427[»]
3SN7X-ray1.82A/B439-779[»]
3SNIX-ray1.90A/B439-779[»]
3SNLX-ray2.40A/B439-779[»]
3UI7X-ray2.28A/B432-760[»]
3UUOX-ray2.11A/B432-760[»]
3WI2X-ray2.26A/B439-779[»]
3WS8X-ray2.60A/B439-779[»]
3WS9X-ray2.99A/B439-779[»]
3WYKX-ray2.50A/B442-779[»]
3WYLX-ray2.68A/B442-779[»]
3WYMX-ray2.00A/B442-779[»]
4AELX-ray2.20A/B439-779[»]
4AJDX-ray2.30A/D439-764[»]
4AJFX-ray1.90A/D439-764[»]
4AJGX-ray2.30A/D439-764[»]
4AJMX-ray2.40A/D439-764[»]
4BBXX-ray2.50A/B443-769[»]
4DDLX-ray2.07A/B442-779[»]
4DFFX-ray2.11A/B432-779[»]
4FCBX-ray2.10A/B439-779[»]
4FCDX-ray2.02A/B439-779[»]
4HEUX-ray2.00A/B442-759[»]
4HF4X-ray2.00A/B442-759[»]
4LKQX-ray1.62A/B439-779[»]
4LLJX-ray1.56A/B439-779[»]
4LLKX-ray1.55A/B439-779[»]
4LLPX-ray1.75A/B439-779[»]
4LLXX-ray1.75A/B439-779[»]
4LM0X-ray1.66A/B439-779[»]
4LM1X-ray1.60A/B439-779[»]
4LM2X-ray1.55A/B439-779[»]
4LM3X-ray1.49A/B439-779[»]
4LM4X-ray1.48A/B439-779[»]
4MRWX-ray1.96A/B439-779[»]
4MRZX-ray1.58A/B439-779[»]
4MS0X-ray1.79A/B439-779[»]
4MSAX-ray1.62A/B439-779[»]
4MSCX-ray2.47A/B439-779[»]
4MSEX-ray2.81A/B439-779[»]
4MSHX-ray2.30A/B439-779[»]
4MSNX-ray2.30A/B439-779[»]
4MUWX-ray2.64A/B442-779[»]
4MVHX-ray2.50A/B442-779[»]
4P0NX-ray2.08A/B442-779[»]
4P1RX-ray2.24A/B442-779[»]
4PHWX-ray2.50A/B442-779[»]
4TPMX-ray2.77A/B442-779[»]
4TPPX-ray2.65A/B442-779[»]
4WN1X-ray3.13A/B439-779[»]
4XY2X-ray2.03A/B439-779[»]
4YQHX-ray2.31A/B439-759[»]
4YS7X-ray2.50A/B439-759[»]
4ZO5X-ray2.50A/B439-759[»]
5AXPX-ray1.95A/B442-779[»]
5AXQX-ray1.77A/B442-779[»]
5B4KX-ray2.90A/B442-779[»]
5B4LX-ray2.40A/B442-779[»]
5C1WX-ray1.70A/B439-779[»]
5C28X-ray1.56A/B439-779[»]
5C29X-ray2.05A/B439-779[»]
5C2AX-ray2.00A/B439-779[»]
5C2EX-ray2.10A/B439-779[»]
5C2HX-ray2.09A/B439-779[»]
5DH4X-ray2.20A/B439-779[»]
5DH5X-ray2.00A/B439-779[»]
5EDEX-ray2.20A/C/D447-760[»]
B448-760[»]
5EDGX-ray2.30A/B/C/D447-760[»]
5EDHX-ray2.03A/B/C/D448-760[»]
5EDIX-ray2.20A/B/C/D442-760[»]
5I2RX-ray2.50A/B/C/D447-763[»]
5K9RX-ray2.70A/B448-759[»]
5UWFX-ray1.87C/D439-779[»]
5XUIX-ray2.77A/B439-779[»]
5XUJX-ray2.44A/B439-779[»]
ProteinModelPortaliQ9Y233
SMRiQ9Y233
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116057, 3 interactors
IntActiQ9Y233, 1 interactor
STRINGi9606.ENSP00000438284

Chemistry databases

BindingDBiQ9Y233
ChEMBLiCHEMBL4409
DrugBankiDB08384 2-({4-[4-(pyridin-4-ylmethyl)-1H-pyrazol-3-yl]phenoxy}methyl)quinoline
DB08387 2-{[4-(1-methyl-4-pyridin-4-yl-1H-pyrazol-3-yl)phenoxy]methyl}quinoline
DB08386 2-{[4-(4-pyridin-4-yl-1H-pyrazol-3-yl)phenoxy]methyl}quinoline
DB00201 Caffeine
DB00975 Dipyridamole
DB01113 Papaverine
DB08811 Tofisopam
DB08814 Triflusal
GuidetoPHARMACOLOGYi1310

PTM databases

iPTMnetiQ9Y233
PhosphoSitePlusiQ9Y233
SwissPalmiQ9Y233

Polymorphism and mutation databases

BioMutaiPDE10A
DMDMi7993747

Proteomic databases

EPDiQ9Y233
PaxDbiQ9Y233
PeptideAtlasiQ9Y233
PRIDEiQ9Y233
ProteomicsDBi85625
85626 [Q9Y233-2]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366882; ENSP00000355847; ENSG00000112541 [Q9Y233-2]
ENST00000650117; ENSP00000497426; ENSG00000112541 [Q9Y233-1]
GeneIDi10846
KEGGihsa:10846
UCSCiuc003quo.4 human [Q9Y233-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		10846
DisGeNETi10846
EuPathDBiHostDB:ENSG00000112541.13

GeneCards: human genes, protein and diseases

More...GeneCardsi		PDE10A
HGNCiHGNC:8772 PDE10A
HPAiCAB045998
HPA047200
MalaCardsiPDE10A
MIMi610652 gene
616921 phenotype
616922 phenotype
neXtProtiNX_Q9Y233
OpenTargetsiENSG00000112541
Orphaneti494541 Childhood-onset benign chorea with striatal involvement
494526 Infantile-onset generalized dyskinesia with orofacial involvement
PharmGKBiPA33120

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3689 Eukaryota
ENOG410XRI7 LUCA
GeneTreeiENSGT00940000156543
HOGENOMiHOG000007068
HOVERGENiHBG082113
KOiK18438
OMAiESAVWIS
OrthoDBiEOG091G037C
PhylomeDBiQ9Y233
TreeFamiTF316499

Enzyme and pathway databases

UniPathwayi
UPA00762;UER00747

UPA00763;UER00748

BRENDAi3.1.4.17 2681
ReactomeiR-HSA-418457 cGMP effects
R-HSA-418555 G alpha (s) signalling events
SABIO-RKiQ9Y233
SIGNORiQ9Y233

Miscellaneous databases

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

More...ChiTaRSi		PDE10A human
EvolutionaryTraceiQ9Y233

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		PDE10A

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

More...GenomeRNAii		10846

Protein Ontology

More...PROi		PR:Q9Y233

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000112541 Expressed in 158 organ(s), highest expression level in caudate nucleus
CleanExiHS_PDE10A
ExpressionAtlasiQ9Y233 baseline and differential
GenevisibleiQ9Y233 HS

Family and domain databases

CDDicd00077 HDc, 1 hit
Gene3Di1.10.1300.10, 1 hit
3.30.450.40, 2 hits
InterProiView protein in InterPro
IPR003018 GAF
IPR029016 GAF-like_dom_sf
IPR003607 HD/PDEase_dom
IPR023088 PDEase
IPR002073 PDEase_catalytic_dom
IPR036971 PDEase_catalytic_dom_sf
IPR023174 PDEase_CS
PfamiView protein in Pfam
PF01590 GAF, 2 hits
PF00233 PDEase_I, 1 hit
PRINTSiPR00387 PDIESTERASE1
SMARTiView protein in SMART
SM00065 GAF, 2 hits
SM00471 HDc, 1 hit
PROSITEiView protein in PROSITE
PS00126 PDEASE_I_1, 1 hit
PS51845 PDEASE_I_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 nameiPDE10_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: Q9Y233
Secondary accession number(s): Q6FHX1
, Q9HCP9, Q9NTV4, Q9ULW9, Q9Y5T1
<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: May 30, 2000
Last sequence update: November 1, 1999
Last modified: December 5, 2018
This is version 181 of the entry and version 1 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 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
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