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UniProtKB - P01213 (PDYN_HUMAN)

Protein

Proenkephalin-B

Gene

PDYN

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

Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress (By similarity).By similarity
Dynorphin peptides differentially regulate the kappa opioid receptor. Dynorphin A(1-13) has a typical opiod activity, it is 700 times more potent than Leu-enkephalin (By similarity).By similarity
Leumorphin has a typical opiod activity and may have anti-apoptotic effect.By similarity

<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

  • opioid peptide activity Source: UniProtKB-KW
  • opioid receptor binding Source: GO_Central
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 functionEndorphin, Neuropeptide, Neurotransmitter, Opioid peptide

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-111885 Opioid Signalling
R-HSA-202040 G-protein activation
R-HSA-375276 Peptide ligand-binding receptors
R-HSA-418594 G alpha (i) signalling events

SIGNOR Signaling Network Open Resource

More...SIGNORi		P01213

Protein family/group databases

Transport Classification Database

More...TCDBi		1.C.89.1.1 the dynorphin channel-forming neuropeptide (dynorphin) family

<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:
Proenkephalin-B
Alternative name(s):
Beta-neoendorphin-dynorphin
Preprodynorphin
Cleaved into the following 9 chains:
Alpha-neoendorphin
Beta-neoendorphin
Big dynorphin
Short name:
Big Dyn
Dynorphin A(1-17)
Short name:
Dyn-A17
Short name:
Dynorphin A
Dynorphin A(1-13)
Dynorphin A(1-8)
Leu-enkephalin
Rimorphin
Alternative name(s):
Dynorphin B
Short name:
Dyn-B
Dynorphin B(1-13)
Leumorphin
Alternative name(s):
Dynorphin B-29
<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:PDYN
<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 20

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000101327.8

Human Gene Nomenclature Database

More...HGNCi		HGNC:8820 PDYN

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		131340 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P01213

<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

Secreted

<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

Spinocerebellar ataxia 23 (SCA23)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionSpinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA23 is an adult-onset autosomal dominant form characterized by slowly progressive gait and limb ataxia, with variable additional features, including peripheral neuropathy and dysarthria.
See also OMIM:610245
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_07226622C → Y in SCA23. 1 PublicationCorresponds to variant dbSNP:rs773876922Ensembl.1
Natural variantiVAR_064913138R → S in SCA23; PDYN, dynorphin A and dynorphin B are located in Purkinje cells as observed in control cerebellum, but cerebellar tissue with the mutation has decreased levels of SLC1A6 and CALB1, both of which are markers of Purkinje cells; SLC1A6 accumulates and aggregates in patient cerebellar tissue. 1 PublicationCorresponds to variant dbSNP:rs267606941EnsemblClinVar.1
Natural variantiVAR_072268206R → C in SCA23. 1 PublicationCorresponds to variant dbSNP:rs575606358Ensembl.1
Natural variantiVAR_072269206R → H in SCA23. 1 PublicationCorresponds to variant dbSNP:rs1004881058Ensembl.1
Natural variantiVAR_064914211L → S in SCA23; the mutant PDYN protein is produced, but processing to opioid peptides is dramatically affected, with increased levels of dynorphin A compared to dynorphin B; these results suggest slow conversion of dynorphin A to short enkephalins; mutant S-211 dynorphin A is not neurotoxic to cultured striatal neurons; no effect on membrane property. 2 PublicationsCorresponds to variant dbSNP:rs267606940EnsemblClinVar.1
Natural variantiVAR_064915212R → W in SCA23; the mutant PDYN protein is produced, but processing to opioid peptides is dramatically affected, with increased levels of dynorphin A compared to dynorphin B; mutant dynorphin A is neurotoxic to cultured striatal neurons, suggesting a dominant-negative effect; disrupts membrane property. 2 PublicationsCorresponds to variant dbSNP:rs201486601EnsemblClinVar.1
Natural variantiVAR_064916215R → C in SCA23; the mutant PDYN protein is produced, but processing to opioid peptides is dramatically affected, resulting in an approximately 2-fold decreased level of dynorphin B compared to dynorphin A; mutant dynorphin A is neurotoxic to cultured striatal neurons, suggesting a dominant-negative effect; disrupts membrane property. 2 PublicationsCorresponds to variant dbSNP:rs267606939EnsemblClinVar.1
Natural variantiVAR_072270227G → D in SCA23. 1 Publication1

Keywords - Diseasei

Disease mutation, Neurodegeneration, Spinocerebellar ataxia

Organism-specific databases

DisGeNET

More...DisGeNETi		5173

MalaCards human disease database

More...MalaCardsi		PDYN
MIMi610245 phenotype

Open Targets

More...OpenTargetsi		ENSG00000101327

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

More...Orphaneti		101108 Spinocerebellar ataxia type 23

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA33163

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2227

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		PDYN

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 20Add BLAST20
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000000817621 – 172Add BLAST152
<p>This subsection of the ‘PTM / Processing’ section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_0000306347175 – 184Alpha-neoendorphin10
PeptideiPRO_0000008177175 – 183Beta-neoendorphin9
PeptideiPRO_0000306348175 – 179Leu-enkephalinBy similarity5
PropeptideiPRO_0000008178186 – 204Add BLAST19
PeptideiPRO_0000306349207 – 238Big dynorphinAdd BLAST32
PeptideiPRO_0000008179207 – 223Dynorphin A(1-17)Add BLAST17
PeptideiPRO_0000306350207 – 219Dynorphin A(1-13)By similarityAdd BLAST13
PeptideiPRO_0000306351207 – 214Dynorphin A(1-8)By similarity8
PeptideiPRO_0000306352207 – 211Leu-enkephalinBy similarity5
PeptideiPRO_0000008180226 – 254LeumorphinAdd BLAST29
PeptideiPRO_0000008181226 – 238RimorphinAdd BLAST13
PeptideiPRO_0000008182226 – 230Leu-enkephalin5

<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

The N-terminal domain contains 6 conserved cysteines thought to be involved in disulfide bonding and/or processing.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P01213

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P01213

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

More...PaxDbi		P01213

PeptideAtlas

More...PeptideAtlasi		P01213

PRoteomics IDEntifications database

More...PRIDEi		P01213

ProteomicsDB human proteome resource

More...ProteomicsDBi		51345

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P01213

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

More...PhosphoSitePlusi		P01213

Miscellaneous databases

CutDB - Proteolytic event database

More...PMAP-CutDBi		P01213

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000101327 Expressed in 46 organ(s), highest expression level in nucleus accumbens

CleanEx database of gene expression profiles

More...CleanExi		HS_PDYN

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P01213 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA049841
HPA053342

<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

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		111199, 11 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000217305

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P01213

<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

1254
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
2N2FNMR-A207-219[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P01213

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

More...SMRi		P01213

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 information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the opioid neuropeptide precursor family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG410IIMD Eukaryota
ENOG4111RTT LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00530000063761

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000013003

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG000063

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P01213

KEGG Orthology (KO)

More...KOi		K15840

Identification of Orthologs from Complete Genome Data

More...OMAi		VGHEDLY

Database of Orthologous Groups

More...OrthoDBi		1410356at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P01213

TreeFam database of animal gene trees

More...TreeFami		TF332620

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR006024 Opioid_neupept
IPR000750 Proenkphlin_B

The PANTHER Classification System

More...PANTHERi		PTHR11438 PTHR11438, 1 hit
PTHR11438:SF4 PTHR11438:SF4, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01160 Opiods_neuropep, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01028 OPIOIDPRCRSR
PR01030 PENKBPRCRSR

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS01252 OPIOIDS_PRECURSOR, 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>Sequencei

<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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P01213-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAWQGLVLAA CLLMFPSTTA DCLSRCSLCA VKTQDGPKPI NPLICSLQCQ 
        60         70         80         90        100
AALLPSEEWE RCQSFLSFFT PSTLGLNDKE DLGSKSVGEG PYSELAKLSG 
       110        120        130        140        150
SFLKELEKSK FLPSISTKEN TLSKSLEEKL RGLSDGFREG AESELMRDAQ 
       160        170        180        190        200
LNDGAMETGT LYLAEEDPKE QVKRYGGFLR KYPKRSSEVA GEGDGDSMGH 
       210        220        230        240        250
EDLYKRYGGF LRRIRPKLKW DNQKRYGGFL RRQFKVVTRS QEDPNAYSGE 

LFDA
Length:254
Mass (Da):28,385
Last modified:July 21, 1986 - 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:i783E7D6AC068CE68
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07226622C → Y in SCA23. 1 PublicationCorresponds to variant dbSNP:rs773876922Ensembl.1
Natural variantiVAR_07226725R → Q Very rare neutral polymorphism. 1 PublicationCorresponds to variant dbSNP:rs369559888Ensembl.1
Natural variantiVAR_064913138R → S in SCA23; PDYN, dynorphin A and dynorphin B are located in Purkinje cells as observed in control cerebellum, but cerebellar tissue with the mutation has decreased levels of SLC1A6 and CALB1, both of which are markers of Purkinje cells; SLC1A6 accumulates and aggregates in patient cerebellar tissue. 1 PublicationCorresponds to variant dbSNP:rs267606941EnsemblClinVar.1
Natural variantiVAR_072268206R → C in SCA23. 1 PublicationCorresponds to variant dbSNP:rs575606358Ensembl.1
Natural variantiVAR_072269206R → H in SCA23. 1 PublicationCorresponds to variant dbSNP:rs1004881058Ensembl.1
Natural variantiVAR_064914211L → S in SCA23; the mutant PDYN protein is produced, but processing to opioid peptides is dramatically affected, with increased levels of dynorphin A compared to dynorphin B; these results suggest slow conversion of dynorphin A to short enkephalins; mutant S-211 dynorphin A is not neurotoxic to cultured striatal neurons; no effect on membrane property. 2 PublicationsCorresponds to variant dbSNP:rs267606940EnsemblClinVar.1
Natural variantiVAR_064915212R → W in SCA23; the mutant PDYN protein is produced, but processing to opioid peptides is dramatically affected, with increased levels of dynorphin A compared to dynorphin B; mutant dynorphin A is neurotoxic to cultured striatal neurons, suggesting a dominant-negative effect; disrupts membrane property. 2 PublicationsCorresponds to variant dbSNP:rs201486601EnsemblClinVar.1
Natural variantiVAR_064916215R → C in SCA23; the mutant PDYN protein is produced, but processing to opioid peptides is dramatically affected, resulting in an approximately 2-fold decreased level of dynorphin B compared to dynorphin A; mutant dynorphin A is neurotoxic to cultured striatal neurons, suggesting a dominant-negative effect; disrupts membrane property. 2 PublicationsCorresponds to variant dbSNP:rs267606939EnsemblClinVar.1
Natural variantiVAR_072270227G → D in SCA23. 1 Publication1

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
X02536 Genomic DNA No translation available.
K02267 Genomic DNA No translation available.
AH002816 Genomic DNA Translation: AAA58456.2
X00176 Genomic DNA Translation: CAA24999.1
AK289618 mRNA Translation: BAF82307.1
AL034562 Genomic DNA No translation available.
CH471133 Genomic DNA Translation: EAX10604.1
BC026334 mRNA Translation: AAH26334.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS13023.1

Protein sequence database of the Protein Information Resource

More...PIRi		A01478 DFHU

NCBI Reference Sequences

More...RefSeqi		NP_001177821.1, NM_001190892.1
NP_001177827.1, NM_001190898.2
NP_001177828.1, NM_001190899.2
NP_001177829.1, NM_001190900.1
NP_077722.1, NM_024411.4
XP_011527546.1, XM_011529244.1
XP_011527547.1, XM_011529245.1
XP_011527548.1, XM_011529246.2
XP_011527549.1, XM_011529247.1
XP_011527550.1, XM_011529248.1
XP_011527551.1, XM_011529249.2
XP_011527552.1, XM_011529250.2
XP_016883367.1, XM_017027878.1

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.22584

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000217305; ENSP00000217305; ENSG00000101327
ENST00000539905; ENSP00000440185; ENSG00000101327
ENST00000540134; ENSP00000442259; ENSG00000101327

Database of genes from NCBI RefSeq genomes

More...GeneIDi		5173

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:5173

UCSC genome browser

More...UCSCi		uc002wfv.4 human

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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02536 Genomic DNA No translation available.
K02267 Genomic DNA No translation available.
AH002816 Genomic DNA Translation: AAA58456.2
X00176 Genomic DNA Translation: CAA24999.1
AK289618 mRNA Translation: BAF82307.1
AL034562 Genomic DNA No translation available.
CH471133 Genomic DNA Translation: EAX10604.1
BC026334 mRNA Translation: AAH26334.1
CCDSiCCDS13023.1
PIRiA01478 DFHU
RefSeqiNP_001177821.1, NM_001190892.1
NP_001177827.1, NM_001190898.2
NP_001177828.1, NM_001190899.2
NP_001177829.1, NM_001190900.1
NP_077722.1, NM_024411.4
XP_011527546.1, XM_011529244.1
XP_011527547.1, XM_011529245.1
XP_011527548.1, XM_011529246.2
XP_011527549.1, XM_011529247.1
XP_011527550.1, XM_011529248.1
XP_011527551.1, XM_011529249.2
XP_011527552.1, XM_011529250.2
XP_016883367.1, XM_017027878.1
UniGeneiHs.22584

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2N2FNMR-A207-219[»]
ProteinModelPortaliP01213
SMRiP01213
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111199, 11 interactors
STRINGi9606.ENSP00000217305

Chemistry databases

BindingDBiP01213
ChEMBLiCHEMBL2227

Protein family/group databases

TCDBi1.C.89.1.1 the dynorphin channel-forming neuropeptide (dynorphin) family

PTM databases

iPTMnetiP01213
PhosphoSitePlusiP01213

Polymorphism and mutation databases

BioMutaiPDYN

Proteomic databases

EPDiP01213
jPOSTiP01213
PaxDbiP01213
PeptideAtlasiP01213
PRIDEiP01213
ProteomicsDBi51345

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		5173
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000217305; ENSP00000217305; ENSG00000101327
ENST00000539905; ENSP00000440185; ENSG00000101327
ENST00000540134; ENSP00000442259; ENSG00000101327
GeneIDi5173
KEGGihsa:5173
UCSCiuc002wfv.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5173
DisGeNETi5173
EuPathDBiHostDB:ENSG00000101327.8

GeneCards: human genes, protein and diseases

More...GeneCardsi		PDYN
HGNCiHGNC:8820 PDYN
HPAiHPA049841
HPA053342
MalaCardsiPDYN
MIMi131340 gene
610245 phenotype
neXtProtiNX_P01213
OpenTargetsiENSG00000101327
Orphaneti101108 Spinocerebellar ataxia type 23
PharmGKBiPA33163

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG410IIMD Eukaryota
ENOG4111RTT LUCA
GeneTreeiENSGT00530000063761
HOGENOMiHOG000013003
HOVERGENiHBG000063
InParanoidiP01213
KOiK15840
OMAiVGHEDLY
OrthoDBi1410356at2759
PhylomeDBiP01213
TreeFamiTF332620

Enzyme and pathway databases

ReactomeiR-HSA-111885 Opioid Signalling
R-HSA-202040 G-protein activation
R-HSA-375276 Peptide ligand-binding receptors
R-HSA-418594 G alpha (i) signalling events
SIGNORiP01213

Miscellaneous databases

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

More...GenomeRNAii		5173
PMAP-CutDBiP01213

Protein Ontology

More...PROi		PR:P01213

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000101327 Expressed in 46 organ(s), highest expression level in nucleus accumbens
CleanExiHS_PDYN
GenevisibleiP01213 HS

Family and domain databases

InterProiView protein in InterPro
IPR006024 Opioid_neupept
IPR000750 Proenkphlin_B
PANTHERiPTHR11438 PTHR11438, 1 hit
PTHR11438:SF4 PTHR11438:SF4, 1 hit
PfamiView protein in Pfam
PF01160 Opiods_neuropep, 1 hit
PRINTSiPR01028 OPIOIDPRCRSR
PR01030 PENKBPRCRSR
PROSITEiView protein in PROSITE
PS01252 OPIOIDS_PRECURSOR, 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 nameiPDYN_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: P01213
Secondary accession number(s): A8K0Q3
<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 21, 1986
Last modified: January 16, 2019
This is version 163 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. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
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