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Protein

Podoplanin

Gene

PDPN

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

Mediates effects on cell migration and adhesion through its different partners. During development plays a role in blood and lymphatic vessels separation by binding CLEC1B, triggering CLEC1B activation in platelets and leading to platelet activation and/or aggregation (PubMed:14522983, PubMed:15231832, PubMed:17616532, PubMed:18215137, PubMed:17222411). Interaction with CD9, on the contrary, attenuates platelet aggregation induced by PDPN (PubMed:18541721). Through MSN or EZR interaction promotes epithelial-mesenchymal transition (EMT) leading to ERZ phosphorylation and triggering RHOA activation leading to cell migration increase and invasiveness (PubMed:17046996, PubMed:21376833). Interaction with CD44 promotes directional cell migration in epithelial and tumor cells (PubMed:20962267). In lymph nodes (LNs), controls fibroblastic reticular cells (FRCs) adhesion to the extracellular matrix (ECM) and contraction of the actomyosin by maintaining ERM proteins (EZR; MSN and RDX) and MYL9 activation through association with unknown transmembrane proteins. Engagement of CLEC1B by PDPN promotes FRCs relaxation by blocking lateral membrane interactions leading to reduction of ERM proteins (EZR; MSN and RDX) and MYL9 activation (By similarity). Through binding with LGALS8 may participate to connection of the lymphatic endothelium to the surrounding extracellular matrix (PubMed:19268462). In keratinocytes, induces changes in cell morphology showing an elongated shape, numerous membrane protrusions, major reorganization of the actin cytoskeleton, increased motility and decreased cell adhesion (PubMed:15515019). Controls invadopodia stability and maturation leading to efficient degradation of the extracellular matrix (ECM) in tumor cells through modulation of RHOC activity in order to activate ROCK1/ROCK2 and LIMK1/LIMK2 and inactivation of CFL1 (PubMed:25486435). Required for normal lung cell proliferation and alveolus formation at birth (By similarity). Does not function as a water channel or as a regulator of aquaporin-type water channels (PubMed:9651190). Does not have any effect on folic acid or amino acid transport (By similarity).By similarity13 Publications

<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

  • chaperone binding Source: UniProtKB
  • chemokine binding Source: UniProtKB
  • signaling receptor binding Source: UniProtKB

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDevelopmental protein
Biological processCell shape
LigandSialic acid

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-114604 GPVI-mediated activation cascade

<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:
Podoplanin1 Publication
Alternative name(s):
Aggrus1 Publication
Glycoprotein 36
Short name:
Gp361 Publication
PA2.26 antigen1 Publication
T1-alphaBy similarity
Short name:
T1ABy similarity
Cleaved into the following chain:
29kDa cytosolic podoplanin intracellular domain1 Publication
Short name:
PICD1 Publication
<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:PDPNImported
Synonyms:GP361 Publication
ORF Names:PSEC0003, PSEC0025
<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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000162493.16

Human Gene Nomenclature Database

More...
HGNCi
HGNC:29602 PDPN

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
608863 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q86YL7

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini23 – 131ExtracellularSequence analysisAdd BLAST109
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei132 – 152HelicalSequence analysisAdd BLAST21
Topological domaini153 – 162CytoplasmicSequence analysis10

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi52T → A: Eliminates induction of platelet aggregation. 1 Publication1
Mutagenesisi137Missing : Prevents self-assembly and association to lipid rafts. Reduces the recruitment to invadopodium. Disrupts assembly into adhesion rings. Fails invadopodia-mediated ECM degradation. 2 Publications1
Mutagenesisi154 – 159RKMSGR → QNMGSN: Does not affect localization at cell surface protrusions. Does not induce reorganization of the actin cytoskeleton. Increases cell migration collectively. Does not significant change RHOA activation. No effect on interaction with CD44. Impairs interaction with the EZR and MSN. Impairs epithelial to mesenchymal transition. Does not change localization at invadopodium. Fails to assemble into rings. Fails invadopodia-mediated ECM degradation. 3 Publications6
Mutagenesisi154 – 155RK → QN: Impairs interaction with the EZR and MSN. Impairs epithelial to mesenchymal transition. Does not affect localization at cell surface protrusions. Does not induce reorganization of the actin cytoskeleton. Increases cell migration collectively. 1 Publication2
Mutagenesisi159R → N: Highly decreases interaction with the EZR and MSN. Induces an intermediate phenotype between epithelial and mesenchymal. Does not affect localization at cell surface protrusions. Induces reorganization of the actin cytoskeleton oncomitantly with the induced morphological changes. Increases cell migration individually. Increases invasiveness. Enhances RHOA activity. Colocalizes at cell-surface protrusions with RHOA and RAC1. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
10630

Open Targets

More...
OpenTargetsi
ENSG00000162493

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA142671187

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
PDPN

Domain mapping of disease mutations (DMDM)

More...
DMDMi
215274223

<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 – 221 PublicationAdd BLAST22
<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_000022387523 – 162PodoplaninAdd BLAST140
<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_0000442187151 – 16229kDa cytosolic podoplanin intracellular domain1 PublicationAdd BLAST12

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi25O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi32O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi34O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi35O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi52O-linked (GalNAc...) threonine2 Publications1
Glycosylationi55O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi65O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi66O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi76O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi85O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi86O-linked (GalNAc...) serineSequence analysis1
Glycosylationi88O-linked (GalNAc...) serineSequence analysis1
Glycosylationi89O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi96O-linked (GalNAc...) serineSequence analysis1
Glycosylationi98O-linked (GalNAc...) serineSequence analysis1
Glycosylationi100O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi102O-linked (GalNAc...) serineSequence analysis1
Glycosylationi106O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi107O-linked (GalNAc...) serineSequence analysis1
Glycosylationi109O-linked (GalNAc...) serineSequence analysis1
Glycosylationi110O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi117O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi119O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi120O-linked (GalNAc...) threonineSequence analysis1

<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

Extensively O-glycosylated. Contains sialic acid residues. O-glycosylation is necessary for platelet aggregation activity. Disialylated at Thr-52; sialic acid is critical for platelet-aggregating activity and for CLEC1B interaction (PubMed:17222411, PubMed:25458834).5 Publications
The N-terminus is blocked.By similarity
Cleaved by a metalloprotease within its extracellular (EC) domain, generating a membrane-bound C-terminal fragment (PCTF33) and an extracellular fragment. The resulting membrane-bound C-terminal fragment (PCTF33) is further processed between Val-150 and Val-151 by PSEN1/gamma-secretase generating the intracellular domain of podoplanin (PICD).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei150 – 151Cleavage; by gamma-secretase1 Publication2

Keywords - PTMi

Glycoprotein

Proteomic databases

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

More...
PaxDbi
Q86YL7

PeptideAtlas

More...
PeptideAtlasi
Q86YL7

PRoteomics IDEntifications database

More...
PRIDEi
Q86YL7

ProteomicsDB human proteome resource

More...
ProteomicsDBi
70429
70430 [Q86YL7-2]
70431 [Q86YL7-3]
70432 [Q86YL7-4]

PTM databases

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

More...
PhosphoSitePlusi
Q86YL7

<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

Highly expressed in placenta, lung, skeletal muscle and brain. Weakly expressed in brain, kidney and liver. In placenta, expressed on the apical plasma membrane of endothelium. In lung, expressed in alveolar epithelium. Up-regulated in colorectal tumors and expressed in 25% of early oral squamous cell carcinomas.3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000162493 Expressed in 196 organ(s), highest expression level in tibia

CleanEx database of gene expression profiles

More...
CleanExi
HS_PDPN

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q86YL7 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q86YL7 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB008376
HPA007534

<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 (PubMed:21376833). Interacts with CLEC1B; the interaction is independent of CLEC1B glycosylation and activates CLEC1B; the interaction is dependent of sialic acid on O-glycans (PubMed:18215137, PubMed:17616532, PubMed:25458834). Interacts with CD9; this interaction is homophilic and attenuates platelet aggregation and pulmonary metastasis induced by PDPN (PubMed:18541721). Interacts with LGALS8; the interaction is glycosylation-dependent; may participate to connection of the lymphatic endothelium to the surrounding extracellular matrix (PubMed:19268462). Interacts with HSPA9 (PubMed:23541579). Interacts (via extracellular domain) with CD44; this interaction is required for PDPN-mediated directional migration and regulation of lamellipodia extension/stabilization during cell spreading and migration (PubMed:20962267). Interacts (via cytoplasmic domain) with MSN and EZR; activates RHOA and promotes epithelial-mesenchymal transition (PubMed:17046996). Interacts with CCL21; relocalized PDPN to the basolateral membrane (PubMed:14978162).10 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
CLEC1BQ9P126-12EBI-723160,EBI-16130833

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
115874, 4 interactors

Database of interacting proteins

More...
DIPi
DIP-61333N

Protein interaction database and analysis system

More...
IntActi
Q86YL7, 6 interactors

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000294489

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q86YL7

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

More...
SMRi
Q86YL7

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

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>Regioni133 – 137Requires for dimerization and lipid rafts association1 Publication5
Regioni154 – 155Requires for interaction with MSN and EZR1 Publication2

<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 cytoplasmic domain controls FRC elongation but is dispensable for contraction (By similarity). The cytoplasmic domain is essential for recruitment to invadopodia and ECM degradation (PubMed:25486435).By similarity1 Publication

<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 podoplanin family.Sequence analysis

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410J49G Eukaryota
ENOG41116TP LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000000013

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG080131

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q86YL7

KEGG Orthology (KO)

More...
KOi
K16778

Database of Orthologous Groups

More...
OrthoDBi
EOG091G0ZYJ

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q86YL7

TreeFam database of animal gene trees

More...
TreeFami
TF337068

<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 (6+)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.

<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.

This entry describes 6 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 6 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 11 Publication (identifier: Q86YL7-1) [UniParc]FASTAAdd to basket
Also known as: hT1alpha-21 Publication

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

« Hide
        10         20         30         40         50
MWKVSALLFV LGSASLWVLA EGASTGQPED DTETTGLEGG VAMPGAEDDV
60 70 80 90 100
VTPGTSEDRY KSGLTTLVAT SVNSVTGIRI EDLPTSESTV HAQEQSPSAT
110 120 130 140 150
ASNVATSHST EKVDGDTQTT VEKDGLSTVT LVGIIVGVLL AIGFIGAIIV
160
VVMRKMSGRY SP
Length:162
Mass (Da):16,698
Last modified:November 25, 2008 - v3
<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:iCD96D46FF5BD56A1
GO
Isoform 21 Publication (identifier: Q86YL7-2) [UniParc]FASTAAdd to basket
Also known as: hT1alpha-11 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-100: Missing.
     101-123: ASNVATSHSTEKVDGDTQTTVEK → MLHILSPMYFFLWGSCFFPLSSS
     162-162: P → EVNSLHPCDR...RQEVHLCPGI

Show »
Length:164
Mass (Da):18,173
Checksum:i009F6A03EE83F72A
GO
Isoform 3 (identifier: Q86YL7-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLTPLGKFST...QESNNSTGTM

Show »
Length:238
Mass (Da):24,902
Checksum:iF6A351B5583198FC
GO
Isoform 4 (identifier: Q86YL7-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLTPLGKFST...QESNNSTGTM
     160-162: YSP → P

Show »
Length:236
Mass (Da):24,652
Checksum:i5D85583198FCE2C3
GO
Isoform 5 (identifier: Q86YL7-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-42: Missing.
     160-161: Missing.

Note: No experimental confirmation available.
Show »
Length:118
Mass (Da):12,171
Checksum:i7EB21A53B3CAA7E5
GO
Isoform 6 (identifier: Q86YL7-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-42: Missing.

Note: No experimental confirmation available.
Show »
Length:120
Mass (Da):12,421
Checksum:i9DE0D2821A53B3CA
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 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H0YA72H0YA72_HUMAN
Podoplanin
PDPN
161Annotation 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>
E7ETC6E7ETC6_HUMAN
Podoplanin
PDPN
157Annotation 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>
D6RH07D6RH07_HUMAN
Podoplanin
PDPN
43Annotation 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>
H0Y8Q3H0Y8Q3_HUMAN
Podoplanin
PDPN
94Annotation 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 AAM73655 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAO22143 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC11550 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC11557 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAG35495 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.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 conflicti57E → K in BAC11557 (PubMed:16303743).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_028015105A → G. Corresponds to variant dbSNP:rs2486188Ensembl.1
Natural variantiVAR_028016147A → G7 PublicationsCorresponds to variant dbSNP:rs2486188Ensembl.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_0519491 – 100Missing in isoform 2. 1 PublicationAdd BLAST100
Alternative sequenceiVSP_0467991 – 42Missing in isoform 5 and isoform 6. CuratedAdd BLAST42
Alternative sequenceiVSP_0357531M → MLTPLGKFSTAKFAVRLPRV WEARAPSLSGAPAPTPPAPP PSRSSRLGLWPRCFLIFPQL RILLLGPQESNNSTGTM in isoform 3 and isoform 4. 5 Publications1
Alternative sequenceiVSP_051950101 – 123ASNVA…TTVEK → MLHILSPMYFFLWGSCFFPL SSS in isoform 2. 1 PublicationAdd BLAST23
Alternative sequenceiVSP_035754160 – 162YSP → P in isoform 4. 1 Publication3
Alternative sequenceiVSP_046800160 – 161Missing in isoform 5. Curated2
Alternative sequenceiVSP_051951162P → EVNSLHPCDRQMKAIVSRTQ IFELIEISDISWVWWLVPVV SAAGQLQTSLGNIVRPCLKK IISGTMVMFQSSLLGPLECS GSHLESQCFERLRRQEVHLC PGI in isoform 2. 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
AF030427 mRNA Translation: AAD01899.1
AF030428 mRNA Translation: AAD01900.1
AJ225022 mRNA Translation: CAA12352.1
AB127958 mRNA Translation: BAD04046.1
AL354712 Genomic DNA No translation available.
AL359771 Genomic DNA No translation available.
BC014668 mRNA Translation: AAH14668.2
BC022812 mRNA Translation: AAH22812.2
AY194238 mRNA Translation: AAO22143.1 Different initiation.
AK312607 mRNA Translation: BAG35495.1 Different initiation.
AK075327 mRNA Translation: BAC11550.1 Different initiation.
AK075345 mRNA Translation: BAC11557.1 Different initiation.
AF390106 mRNA Translation: AAM73655.1 Different initiation.

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS30602.1 [Q86YL7-3]
CCDS41266.1 [Q86YL7-4]
CCDS44060.1 [Q86YL7-6]
CCDS53270.1 [Q86YL7-5]

NCBI Reference Sequences

More...
RefSeqi
NP_001006625.1, NM_001006624.1 [Q86YL7-6]
NP_001006626.1, NM_001006625.1 [Q86YL7-5]
NP_006465.3, NM_006474.4 [Q86YL7-3]
NP_938203.2, NM_198389.2 [Q86YL7-4]
XP_006710358.1, XM_006710295.1 [Q86YL7-6]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.468675

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000294489; ENSP00000294489; ENSG00000162493 [Q86YL7-3]
ENST00000376057; ENSP00000365225; ENSG00000162493 [Q86YL7-4]
ENST00000376061; ENSP00000365229; ENSG00000162493 [Q86YL7-6]
ENST00000475043; ENSP00000426063; ENSG00000162493 [Q86YL7-5]
ENST00000487038; ENSP00000427537; ENSG00000162493 [Q86YL7-6]
ENST00000513143; ENSP00000425304; ENSG00000162493 [Q86YL7-6]
ENST00000617617; ENSP00000479591; ENSG00000162493 [Q86YL7-3]
ENST00000621990; ENSP00000478125; ENSG00000162493 [Q86YL7-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
10630

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:10630

UCSC genome browser

More...
UCSCi
uc001avc.4 human [Q86YL7-1]

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
AF030427 mRNA Translation: AAD01899.1
AF030428 mRNA Translation: AAD01900.1
AJ225022 mRNA Translation: CAA12352.1
AB127958 mRNA Translation: BAD04046.1
AL354712 Genomic DNA No translation available.
AL359771 Genomic DNA No translation available.
BC014668 mRNA Translation: AAH14668.2
BC022812 mRNA Translation: AAH22812.2
AY194238 mRNA Translation: AAO22143.1 Different initiation.
AK312607 mRNA Translation: BAG35495.1 Different initiation.
AK075327 mRNA Translation: BAC11550.1 Different initiation.
AK075345 mRNA Translation: BAC11557.1 Different initiation.
AF390106 mRNA Translation: AAM73655.1 Different initiation.
CCDSiCCDS30602.1 [Q86YL7-3]
CCDS41266.1 [Q86YL7-4]
CCDS44060.1 [Q86YL7-6]
CCDS53270.1 [Q86YL7-5]
RefSeqiNP_001006625.1, NM_001006624.1 [Q86YL7-6]
NP_001006626.1, NM_001006625.1 [Q86YL7-5]
NP_006465.3, NM_006474.4 [Q86YL7-3]
NP_938203.2, NM_198389.2 [Q86YL7-4]
XP_006710358.1, XM_006710295.1 [Q86YL7-6]
UniGeneiHs.468675

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
3WSRX-ray1.91C/D38-54[»]
4YO0X-ray1.56E/F38-51[»]
5XCVX-ray2.14C/F38-51[»]
ProteinModelPortaliQ86YL7
SMRiQ86YL7
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115874, 4 interactors
DIPiDIP-61333N
IntActiQ86YL7, 6 interactors
STRINGi9606.ENSP00000294489

PTM databases

PhosphoSitePlusiQ86YL7

Polymorphism and mutation databases

BioMutaiPDPN
DMDMi215274223

Proteomic databases

PaxDbiQ86YL7
PeptideAtlasiQ86YL7
PRIDEiQ86YL7
ProteomicsDBi70429
70430 [Q86YL7-2]
70431 [Q86YL7-3]
70432 [Q86YL7-4]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000294489; ENSP00000294489; ENSG00000162493 [Q86YL7-3]
ENST00000376057; ENSP00000365225; ENSG00000162493 [Q86YL7-4]
ENST00000376061; ENSP00000365229; ENSG00000162493 [Q86YL7-6]
ENST00000475043; ENSP00000426063; ENSG00000162493 [Q86YL7-5]
ENST00000487038; ENSP00000427537; ENSG00000162493 [Q86YL7-6]
ENST00000513143; ENSP00000425304; ENSG00000162493 [Q86YL7-6]
ENST00000617617; ENSP00000479591; ENSG00000162493 [Q86YL7-3]
ENST00000621990; ENSP00000478125; ENSG00000162493 [Q86YL7-1]
GeneIDi10630
KEGGihsa:10630
UCSCiuc001avc.4 human [Q86YL7-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
10630
DisGeNETi10630
EuPathDBiHostDB:ENSG00000162493.16

GeneCards: human genes, protein and diseases

More...
GeneCardsi
PDPN

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0000141
HGNCiHGNC:29602 PDPN
HPAiCAB008376
HPA007534
MIMi608863 gene
neXtProtiNX_Q86YL7
OpenTargetsiENSG00000162493
PharmGKBiPA142671187

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410J49G Eukaryota
ENOG41116TP LUCA
GeneTreeiENSGT00390000000013
HOVERGENiHBG080131
InParanoidiQ86YL7
KOiK16778
OrthoDBiEOG091G0ZYJ
PhylomeDBiQ86YL7
TreeFamiTF337068

Enzyme and pathway databases

ReactomeiR-HSA-114604 GPVI-mediated activation cascade

Miscellaneous databases

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

More...
ChiTaRSi
PDPN human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
PDPN

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

More...
GenomeRNAii
10630

Protein Ontology

More...
PROi
PR:Q86YL7

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000162493 Expressed in 196 organ(s), highest expression level in tibia
CleanExiHS_PDPN
ExpressionAtlasiQ86YL7 baseline and differential
GenevisibleiQ86YL7 HS

Family and domain databases

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 nameiPDPN_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: Q86YL7
Secondary accession number(s): A9Z1Y2
, B2R6J8, E9PB68, F6QWX5, O60836, O95128, Q7L375, Q8NBQ8, Q8NBR3
<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: February 21, 2006
Last sequence update: November 25, 2008
Last modified: December 5, 2018
This is version 132 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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