Skip Header

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

UniProtKB - P15428 (PGDH_HUMAN)

Entry version 201 (17 Jun 2020)
Sequence version 1 (01 Apr 1990)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

15-hydroxyprostaglandin dehydrogenase [NAD(+)]

Gene

HPGD

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

Primary enzyme catalyzing the conversion of hydroxylated arachidonic acid species to their corresponding oxidized metabolites (Probable). Prostaglandin inactivation, catalyzes the first step in the catabolic pathway of the prostaglandins. Contributes to the regulation of events that are under the control of prostaglandin levels (PubMed:15574495, PubMed:16828555, PubMed:8086429). Catalyzes the NAD-dependent dehydrogenation of lipoxin A4 to form 15-oxo-lipoxin A4 (PubMed:10837478). Converts 11(R)-HETE to 11-oxo-5,8,12,14-(Z,Z,E,Z)-eicosatetraenoic acid (ETE) (PubMed:21916491). Has hydroxylated docosahexaenoic acid metabolites as substrates (PubMed:25586183). Converts resolvins E1, D1 and D2 to their oxo products which represents a mode of resolvins inactivation and stabilizes their anti-inflammatory actions (PubMed:16757471, PubMed:22844113).1 Publication8 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 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 8.6 min(-1) with (11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoate and (5Z,8Z,11Z,13E,15S)-hydroxyeicosatetraenoate as substrates.1 Publication
  1. KM=3.4 µM for prostaglandin E22 Publications
  2. KM=5.5 µM for prostaglandin E11 Publication
  3. KM=4.5 µM for prostaglandin A11 Publication
  4. KM=22 µM for prostaglandin A21 Publication
  5. KM=3.42 µM for (11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoate1 Publication
  6. KM=1.65 µM for (5Z,8Z,11Z,13E,15S)-hydroxyeicosatetraenoate1 Publication
  7. KM=22 µM for NAD1 Publication
  8. KM=38 µM for NAD1 Publication
  1. Vmax=296 nmol/min/mg enzyme toward (11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoate1 Publication
  2. Vmax=403.8 nmol/min/mg enzyme toward (5Z,8Z,11Z,13E,15S)-hydroxyeicosatetraenoate1 Publication
  3. Vmax=13.1 µmol/min/mg enzyme toward prostaglandin A21 Publication
  4. Vmax=21.58 µmol/min/mg enzyme toward prostaglandin A11 Publication
  5. Vmax=24.98 µmol/min/mg enzyme toward NAD1 Publication
  6. Vmax=22.8 µmol/min/mg enzyme toward prostaglandin E11 Publication
  7. Vmax=24.6 µmol/min/mg enzyme toward prostaglandin E21 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei91NAD; via carbonyl oxygen1 Publication1
Binding sitei138SubstrateCurated1
Binding sitei148SubstrateCurated1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei151Proton acceptor1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi12 – 20NAD1 Publication9
Nucleotide bindingi36 – 37NAD1 Publication2
Nucleotide bindingi63 – 65NAD1 Publication3
Nucleotide bindingi151 – 155NAD1 Publication5
Nucleotide bindingi186 – 188NAD1 Publication3

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

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 functionOxidoreductase
Biological processFatty acid metabolism, Lipid metabolism, Prostaglandin metabolism
LigandNAD

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.1.1.141 2681

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-2142700 Synthesis of Lipoxins (LX)
R-HSA-2162123 Synthesis of Prostaglandins (PG) and Thromboxanes (TX)
R-HSA-9018676 Biosynthesis of D-series resolvins
R-HSA-9018896 Biosynthesis of E-series 18(S)-resolvins

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P15428

SIGNOR Signaling Network Open Resource

More...SIGNORi		P15428

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...SwissLipidsi		SLP:000000732

<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%5Fand%5Ftaxonomy%5Fsection">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:
15-hydroxyprostaglandin dehydrogenase [NAD(+)]Curated (EC:1.1.1.1411 Publication)
Short name:
15-PGDH
Alternative name(s):
Prostaglandin dehydrogenase 1
Short chain dehydrogenase/reductase family 36C member 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:HPGDImported
Synonyms:PGDH1, SDR36C1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 4

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000164120.13

Human Gene Nomenclature Database

More...HGNCi		HGNC:5154 HPGD

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		601688 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P15428

<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 & Seán O’Donoghue; 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

Hypertrophic osteoarthropathy, primary, autosomal recessive, 1 (PHOAR1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by digital clubbing, periostosis, acroosteolysis, painful joint enlargement, and variable features of pachydermia that include thickened facial skin and a thickened scalp. Other developmental anomalies include delayed closure of the cranial sutures and congenital heart disease.
Related information in OMIM
Cranioosteoarthropathy (COA)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of osteoarthropathy characterized by swelling of the joints, digital clubbing, hyperhidrosis, delayed closure of the fontanels, periostosis, and variable patent ductus arteriosus. Pachydermia is not a prominent feature.
Related information in OMIM
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_046209140A → P in COA; inactive. 1 PublicationCorresponds to variant dbSNP:rs121434480EnsemblClinVar.1
Isolated congenital nail clubbing (ICNC)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare genodermatosis characterized by enlargement of the nail plate and terminal segments of the fingers and toes, resulting from proliferation of the connective tissues between the nail matrix and the distal phalanx. It is usually symmetrical and bilateral (in some cases unilateral). In nail clubbing usually the distal end of the nail matrix is relatively high compared to the proximal end, while the nail plate is complete but its dimensions and diameter more or less vary in comparison to normal. There may be different fingers and toes involved to varying degrees. Some fingers or toes are spared, but the thumbs are almost always involved.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_060792193S → P in ICNC. 1 PublicationCorresponds to variant dbSNP:rs121434481EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi148Q → A: Loss of activity. 1 Publication1
Mutagenesisi148Q → E, H or N: Reduced affinity for NAD and prostaglandin E2. 1 Publication1
Mutagenesisi151Y → A: Loss of activity. 1 Publication1
Mutagenesisi151Y → F: Loss 15-hydroxyprostaglandin dehydrogenase activity. 1 Publication1
Mutagenesisi155K → Q: Loss 15-hydroxyprostaglandin dehydrogenase activity. 1 Publication1

Keywords - Diseasei

Disease mutation, Tumor suppressor

Organism-specific databases

DisGeNET

More...DisGeNETi		3248

MalaCards human disease database

More...MalaCardsi		HPGD
MIMi119900 phenotype
259100 phenotype

Open Targets

More...OpenTargetsi		ENSG00000164120

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

More...Orphaneti		1525 Cranio-osteoarthropathy
217059 Isolated congenital digital clubbing
2796 Pachydermoperiostosis

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA29424

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P15428 Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1293255

Drug and drug target database

More...DrugBanki		DB00157 NADH

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		1384

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		HPGD

Domain mapping of disease mutations (DMDM)

More...DMDMi		129889

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000547441 – 26615-hydroxyprostaglandin dehydrogenase [NAD(+)]Add BLAST266

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P15428

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P15428

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P15428

MaxQB - The MaxQuant DataBase

More...MaxQBi		P15428

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

More...PaxDbi		P15428

PeptideAtlas

More...PeptideAtlasi		P15428

PRoteomics IDEntifications database

More...PRIDEi		P15428

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		18546
48016
5156
53141 [P15428-1]
53142 [P15428-2]

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P15428

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P15428

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

More...PhosphoSitePlusi		P15428

<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

Detected in colon epithelium (at protein level).1 Publication

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Down-regulated by cortisol, dexamethasone and betamethasone. Down-regulated in colon cancer. Up-regulated by TGFB1.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000164120 Expressed in metanephros and 174 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P15428 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P15428 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000164120 Tissue enhanced (placenta)

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

1 Publication

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		109485, 2 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000296522

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P15428

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P15428 protein

<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

1266
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P15428

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P15428

<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 short-chain dehydrogenases/reductases (SDR) family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG4169 Eukaryota
COG1028 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000154593

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_010194_2_19_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P15428

KEGG Orthology (KO)

More...KOi		K00069

Identification of Orthologs from Complete Genome Data

More...OMAi		TTSLHYE

Database of Orthologous Groups

More...OrthoDBi		1053465at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P15428

TreeFam database of animal gene trees

More...TreeFami		TF324093

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR036291 NAD(P)-bd_dom_sf
IPR020904 Sc_DH/Rdtase_CS
IPR002347 SDR_fam

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00106 adh_short, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00081 GDHRDH
PR00080 SDRFAMILY

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF51735 SSF51735, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00061 ADH_SHORT, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (5+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 5 <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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 5 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P15428-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MHVNGKVALV TGAAQGIGRA FAEALLLKGA KVALVDWNLE AGVQCKAALD 
        60         70         80         90        100
EQFEPQKTLF IQCDVADQQQ LRDTFRKVVD HFGRLDILVN NAGVNNEKNW 
       110        120        130        140        150
EKTLQINLVS VISGTYLGLD YMSKQNGGEG GIIINMSSLA GLMPVAQQPV 
       160        170        180        190        200
YCASKHGIVG FTRSAALAAN LMNSGVRLNA ICPGFVNTAI LESIEKEENM 
       210        220        230        240        250
GQYIEYKDHI KDMIKYYGIL DPPLIANGLI TLIEDDALNG AIMKITTSKG 
       260 
IHFQDYDTTP FQAKTQ
Length:266
Mass (Da):28,977
Last modified:April 1, 1990 - 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:iB860D2DE80E49514
GO
Isoform 2 (identifier: P15428-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     167-266: LAANLMNSGV...DTTPFQAKTQ → PTIDCQWIDNTH

Show »
Length:178
Mass (Da):19,284
Checksum:i685B577B3CA27EE3
GO
Isoform 3 (identifier: P15428-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-121: Missing.

Show »
Length:145
Mass (Da):15,696
Checksum:i7113DD63B7540112
GO
Isoform 4 (identifier: P15428-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     140-143: AGLM → AAHH
     144-266: Missing.

Show »
Length:143
Mass (Da):15,534
Checksum:i67C9DD0CC7E3366C
GO
Isoform 5 (identifier: P15428-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     73-140: Missing.

Show »
Length:198
Mass (Da):21,526
Checksum:i1D571F22D8738F64
GO

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

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D6RA66D6RA66_HUMAN
15-hydroxyprostaglandin dehydrogena...
HPGD
97Annotation 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>
D6RA83D6RA83_HUMAN
15-hydroxyprostaglandin dehydrogena...
HPGD
99Annotation 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>
E9PBZ2E9PBZ2_HUMAN
15-hydroxyprostaglandin dehydrogena...
HPGD
176Annotation 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>
D6RHF8D6RHF8_HUMAN
15-hydroxyprostaglandin dehydrogena...
HPGD
37Annotation 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>
E9PD69E9PD69_HUMAN
15-hydroxyprostaglandin dehydrogena...
HPGD
87Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti50D → H in AAA89175 (PubMed:1697582).Curated1
Sequence conflicti50D → H in AAA89174 (PubMed:1697582).Curated1
Sequence conflicti97E → K in CAA57843 (PubMed:7557451).Curated1
Sequence conflicti219I → V in BAG61916 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_046209140A → P in COA; inactive. 1 PublicationCorresponds to variant dbSNP:rs121434480EnsemblClinVar.1
Natural variantiVAR_060792193S → P in ICNC. 1 PublicationCorresponds to variant dbSNP:rs121434481EnsemblClinVar.1
Natural variantiVAR_006972217Y → C. Corresponds to variant dbSNP:rs140209262Ensembl.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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0451061 – 121Missing in isoform 3. 1 PublicationAdd BLAST121
Alternative sequenceiVSP_04557973 – 140Missing in isoform 5. 1 PublicationAdd BLAST68
Alternative sequenceiVSP_045107140 – 143AGLM → AAHH in isoform 4. 1 Publication4
Alternative sequenceiVSP_045108144 – 266Missing in isoform 4. 1 PublicationAdd BLAST123
Alternative sequenceiVSP_043032167 – 266LAANL…QAKTQ → PTIDCQWIDNTH in isoform 2. 2 PublicationsAdd BLAST100

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
L76465 mRNA Translation: AAA89175.1
J05594 mRNA Translation: AAA89174.1
X82460 mRNA Translation: CAA57843.1
U63296 mRNA Translation: AAB53034.1
AK296642 mRNA Translation: BAH12408.1
AK300125 mRNA Translation: BAG61916.1
AK300524 mRNA Translation: BAG62236.1
AK300940 mRNA Translation: BAG62569.1
AK314624 mRNA Translation: BAG37190.1
DQ903072 Genomic DNA Translation: ABI75347.1
AC096751 Genomic DNA No translation available.
CH471056 Genomic DNA Translation: EAX04734.1
CH471056 Genomic DNA Translation: EAX04735.1
CH471056 Genomic DNA Translation: EAX04736.1
CH471056 Genomic DNA Translation: EAX04737.1
BC018986 mRNA Translation: AAH18986.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS3821.1 [P15428-1]
CCDS54821.1 [P15428-2]
CCDS58933.1 [P15428-3]
CCDS58934.1 [P15428-5]
CCDS58935.1 [P15428-4]

Protein sequence database of the Protein Information Resource

More...PIRi		A35802

NCBI Reference Sequences

More...RefSeqi		NP_000851.2, NM_000860.5 [P15428-1]
NP_001139288.1, NM_001145816.2 [P15428-2]
NP_001243230.1, NM_001256301.1 [P15428-3]
NP_001243234.1, NM_001256305.1 [P15428-4]
NP_001243235.1, NM_001256306.1 [P15428-5]
NP_001243236.1, NM_001256307.1 [P15428-3]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000296521; ENSP00000296521; ENSG00000164120 [P15428-2]
ENST00000296522; ENSP00000296522; ENSG00000164120 [P15428-1]
ENST00000422112; ENSP00000398720; ENSG00000164120 [P15428-5]
ENST00000510901; ENSP00000422418; ENSG00000164120 [P15428-3]
ENST00000541923; ENSP00000438017; ENSG00000164120 [P15428-3]
ENST00000542498; ENSP00000443644; ENSG00000164120 [P15428-4]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		3248

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:3248

UCSC genome browser

More...UCSCi		uc003itu.3 human [P15428-1]

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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L76465 mRNA Translation: AAA89175.1
J05594 mRNA Translation: AAA89174.1
X82460 mRNA Translation: CAA57843.1
U63296 mRNA Translation: AAB53034.1
AK296642 mRNA Translation: BAH12408.1
AK300125 mRNA Translation: BAG61916.1
AK300524 mRNA Translation: BAG62236.1
AK300940 mRNA Translation: BAG62569.1
AK314624 mRNA Translation: BAG37190.1
DQ903072 Genomic DNA Translation: ABI75347.1
AC096751 Genomic DNA No translation available.
CH471056 Genomic DNA Translation: EAX04734.1
CH471056 Genomic DNA Translation: EAX04735.1
CH471056 Genomic DNA Translation: EAX04736.1
CH471056 Genomic DNA Translation: EAX04737.1
BC018986 mRNA Translation: AAH18986.1
CCDSiCCDS3821.1 [P15428-1]
CCDS54821.1 [P15428-2]
CCDS58933.1 [P15428-3]
CCDS58934.1 [P15428-5]
CCDS58935.1 [P15428-4]
PIRiA35802
RefSeqiNP_000851.2, NM_000860.5 [P15428-1]
NP_001139288.1, NM_001145816.2 [P15428-2]
NP_001243230.1, NM_001256301.1 [P15428-3]
NP_001243234.1, NM_001256305.1 [P15428-4]
NP_001243235.1, NM_001256306.1 [P15428-5]
NP_001243236.1, NM_001256307.1 [P15428-3]

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
2GDZX-ray1.65A3-256[»]
SMRiP15428
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi109485, 2 interactors
STRINGi9606.ENSP00000296522

Chemistry databases

BindingDBiP15428
ChEMBLiCHEMBL1293255
DrugBankiDB00157 NADH
GuidetoPHARMACOLOGYi1384
SwissLipidsiSLP:000000732

PTM databases

iPTMnetiP15428
PhosphoSitePlusiP15428

Polymorphism and mutation databases

BioMutaiHPGD
DMDMi129889

2D gel databases

SWISS-2DPAGEiP15428

Proteomic databases

EPDiP15428
jPOSTiP15428
MassIVEiP15428
MaxQBiP15428
PaxDbiP15428
PeptideAtlasiP15428
PRIDEiP15428
ProteomicsDBi18546
48016
5156
53141 [P15428-1]
53142 [P15428-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		1511 496 antibodies

Genome annotation databases

EnsembliENST00000296521; ENSP00000296521; ENSG00000164120 [P15428-2]
ENST00000296522; ENSP00000296522; ENSG00000164120 [P15428-1]
ENST00000422112; ENSP00000398720; ENSG00000164120 [P15428-5]
ENST00000510901; ENSP00000422418; ENSG00000164120 [P15428-3]
ENST00000541923; ENSP00000438017; ENSG00000164120 [P15428-3]
ENST00000542498; ENSP00000443644; ENSG00000164120 [P15428-4]
GeneIDi3248
KEGGihsa:3248
UCSCiuc003itu.3 human [P15428-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		3248
DisGeNETi3248
EuPathDBiHostDB:ENSG00000164120.13

GeneCards: human genes, protein and diseases

More...GeneCardsi		HPGD
HGNCiHGNC:5154 HPGD
HPAiENSG00000164120 Tissue enhanced (placenta)
MalaCardsiHPGD
MIMi119900 phenotype
259100 phenotype
601688 gene
neXtProtiNX_P15428
OpenTargetsiENSG00000164120
Orphaneti1525 Cranio-osteoarthropathy
217059 Isolated congenital digital clubbing
2796 Pachydermoperiostosis
PharmGKBiPA29424

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG4169 Eukaryota
COG1028 LUCA
GeneTreeiENSGT00940000154593
HOGENOMiCLU_010194_2_19_1
InParanoidiP15428
KOiK00069
OMAiTTSLHYE
OrthoDBi1053465at2759
PhylomeDBiP15428
TreeFamiTF324093

Enzyme and pathway databases

BRENDAi1.1.1.141 2681
ReactomeiR-HSA-2142700 Synthesis of Lipoxins (LX)
R-HSA-2162123 Synthesis of Prostaglandins (PG) and Thromboxanes (TX)
R-HSA-9018676 Biosynthesis of D-series resolvins
R-HSA-9018896 Biosynthesis of E-series 18(S)-resolvins
SABIO-RKiP15428
SIGNORiP15428

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		3248 2 hits in 791 CRISPR screens

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

More...ChiTaRSi		HPGD human
EvolutionaryTraceiP15428

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		HPGD

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

More...GenomeRNAii		3248
PharosiP15428 Tchem

Protein Ontology

More...PROi		PR:P15428
RNActiP15428 protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000164120 Expressed in metanephros and 174 other tissues
ExpressionAtlasiP15428 baseline and differential
GenevisibleiP15428 HS

Family and domain databases

InterProiView protein in InterPro
IPR036291 NAD(P)-bd_dom_sf
IPR020904 Sc_DH/Rdtase_CS
IPR002347 SDR_fam
PfamiView protein in Pfam
PF00106 adh_short, 1 hit
PRINTSiPR00081 GDHRDH
PR00080 SDRFAMILY
SUPFAMiSSF51735 SSF51735, 1 hit
PROSITEiView protein in PROSITE
PS00061 ADH_SHORT, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 nameiPGDH_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: P15428
Secondary accession number(s): B4DTA4
, B4DU74, B4DV57, D3DP43, E7EV11, O00749, Q06F08, Q12998
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 17, 2020
This is version 201 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, Direct protein sequencing, 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 entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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

Do not show this banner again