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Entry version 196 (16 Oct 2019)
Sequence version 2 (25 Nov 2008)
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Protein

Discoidin domain-containing receptor 2

Gene

DDR2

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

Tyrosine kinase involved in the regulation of tissues remodeling (PubMed:30449416). It functions as cell surface receptor for fibrillar collagen and regulates cell differentiation, remodeling of the extracellular matrix, cell migration and cell proliferation. Required for normal bone development. Regulates osteoblast differentiation and chondrocyte maturation via a signaling pathway that involves MAP kinases and leads to the activation of the transcription factor RUNX2. Regulates remodeling of the extracellular matrix by up-regulation of the collagenases MMP1, MMP2 and MMP13, and thereby facilitates cell migration and tumor cell invasion. Promotes fibroblast migration and proliferation, and thereby contributes to cutaneous wound healing.9 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Present in an inactive state in the absence of collagen binding and phosphorylation by SRC. Tyrosine phosphorylation enhances the affinity for ATP and the catalytic activity.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei608ATPCurated1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei710Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi569 – 577ATPPROSITE-ProRule annotation9

<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

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 functionKinase, Receptor, Transferase, Tyrosine-protein kinase
Biological processOsteogenesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.10.1 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-3000171 Non-integrin membrane-ECM interactions

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
Q16832

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q16832

<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:
Discoidin domain-containing receptor 2 (EC:2.7.10.1)
Short name:
Discoidin domain receptor 2
Alternative name(s):
CD167 antigen-like family member B
Discoidin domain-containing receptor tyrosine kinase 2
Neurotrophic tyrosine kinase, receptor-related 3
Receptor protein-tyrosine kinase TKT
Tyrosine-protein kinase TYRO10
CD_antigen: CD167b
<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:DDR2
Synonyms:NTRKR3, TKT, TYRO10
<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

Human Gene Nomenclature Database

More...
HGNCi
HGNC:2731 DDR2

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
191311 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q16832

<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

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 domaini22 – 399ExtracellularSequence analysisAdd BLAST378
<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>Transmembranei400 – 421HelicalSequence analysisAdd BLAST22
Topological domaini422 – 855CytoplasmicSequence analysisAdd BLAST434

Keywords - Cellular componenti

Cell membrane, 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

<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

Spondyloepimetaphyseal dysplasia short limb-hand type (SEMD-SL)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA bone disease characterized by short-limbed dwarfism, a narrow chest with pectus excavatum, brachydactyly in the hands and feet, a characteristic craniofacial appearance and premature calcifications. The radiological findings are distinctive and comprise short long bones throughout the skeleton with striking epiphyses that are stippled, flattened and fragmented and flared, irregular metaphyses. Platyspondyly in the spine with wide intervertebral spaces is observed and some vertebral bodies are pear-shaped with central humps, anterior protrusions and posterior scalloping.
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_065719113E → K in SEMD-SL; abolishes collagen binding. 1 PublicationCorresponds to variant dbSNP:rs397514747EnsemblClinVar.1
Natural variantiVAR_075417124R → W in SEMD-SL. 1 Publication1
Natural variantiVAR_063050713T → I in SEMD-SL; causes retention in an intracellular compartment and thereby abolishes signaling in response collagen binding. 2 PublicationsCorresponds to variant dbSNP:rs121964865EnsemblClinVar.1
Natural variantiVAR_063051726I → R in SEMD-SL; causes retention in an intracellular compartment and thereby abolishes signaling in response collagen binding. 2 PublicationsCorresponds to variant dbSNP:rs121964864EnsemblClinVar.1
Natural variantiVAR_063052752R → C in SEMD-SL; causes retention in an intracellular compartment and thereby abolishes signaling in response collagen binding. 2 PublicationsCorresponds to variant dbSNP:rs121964863EnsemblClinVar.1
Warburg-Cinotti syndrome (WRCN)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disease characterized by progressive corneal neovascularization, keloid formation, chronic skin ulcers, wasting of subcutaneous tissue, flexion contractures of the fingers, and acro-osteolysis.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_081931610L → P in WRCN; increased autophosphorylation in patient fibroblasts. 1 Publication1
Natural variantiVAR_081932740Y → C in WRCN; increased autophosphorylation in patient fibroblasts. 1 Publication1

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>Mutagenesisi52W → A: Abolishes collagen binding. 2 Publications1
Mutagenesisi608K → A: Abolishes kinase activity. 1 Publication1
Mutagenesisi736Y → F: Reduces autophosphorylation. Abolishes phosphorylation by SRC; when associated with F-740 and F-741. 1 Publication1
Mutagenesisi740Y → F: Promotes autophosphorylation. Abolishes phosphorylation by SRC; when associated with F-736 and F-741. 1 Publication1
Mutagenesisi741Y → F: Reduces autophosphorylation. Abolishes phosphorylation by SRC; when associated with F-736 and F-740. 1 Publication1

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

DisGeNET

More...
DisGeNETi
4921

MalaCards human disease database

More...
MalaCardsi
DDR2
MIMi271665 phenotype
618175 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000162733

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

More...
Orphaneti
93358 Spondyloepimetaphyseal dysplasia-short limb-abnormal calcification syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA27196

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q16832

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL5122

Drug and drug target database

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DrugBanki
DB12010 Fostamatinib
DB08896 Regorafenib

DrugCentral

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DrugCentrali
Q16832

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1844

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
DDR2

Domain mapping of disease mutations (DMDM)

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DMDMi
215273969

<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 – 21Sequence analysisAdd BLAST21
<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_000001674622 – 855Discoidin domain-containing receptor 2Add BLAST834

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi30 ↔ 185
Disulfide bondi73 ↔ 177
<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>Glycosylationi121N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi213N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi261N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi280N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi372N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei471Phosphotyrosine; by SRC and autocatalysisBy similarity1
Modified residuei736Phosphotyrosine; by SRC and autocatalysis1 Publication1
Modified residuei740Phosphotyrosine; by SRC and autocatalysis1 Publication1
Modified residuei741Phosphotyrosine; by SRC and autocatalysis1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

N-glycosylated.1 Publication
Tyrosine phosphorylated in response to collagen binding. Phosphorylated by SRC; this is required for activation and subsequent autophosphorylation on additional tyrosine residues.5 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q16832

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q16832

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q16832

MaxQB - The MaxQuant DataBase

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MaxQBi
Q16832

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

More...
PaxDbi
Q16832

PeptideAtlas

More...
PeptideAtlasi
Q16832

PRoteomics IDEntifications database

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PRIDEi
Q16832

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
61095

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q16832

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

More...
PhosphoSitePlusi
Q16832

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q16832

<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 osteocytes, osteoblastic cells in subchondral bone, bone lining cells, tibia and cartilage (at protein level). Detected at high levels in heart and lung, and at low levels in brain, placenta, liver, skeletal muscle, pancreas, and kidney.3 Publications

<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

Up-regulated during osteoblast differentiation (in vitro). Up-regulated in cartilage from osteoarthritis patients.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000162733 Expressed in 225 organ(s), highest expression level in adipose tissue

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q16832 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q16832 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA070112

<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

Binds hydroxyproline-rich sequence motifs in fibrillar, glycosylated collagen, such as the GQOGVMGFO motif, where O stands for hydroxyproline.

Interacts with SRC.

Interacts (tyrosine phosphorylated) with SHC1.

4 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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
110975, 19 interactors

Database of interacting proteins

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DIPi
DIP-39699N

Protein interaction database and analysis system

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IntActi
Q16832, 9 interactors

Molecular INTeraction database

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MINTi
Q16832

STRING: functional protein association networks

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STRINGi
9606.ENSP00000356899

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q16832

<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

1855
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

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SMRi
Q16832

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q16832

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini30 – 185F5/8 type CPROSITE-ProRule annotationAdd BLAST156
Domaini563 – 849Protein kinasePROSITE-ProRule annotationAdd BLAST287

<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 protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1094 Eukaryota
ENOG410XQAI LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000154842

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000043102

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q16832

KEGG Orthology (KO)

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KOi
K05125

Identification of Orthologs from Complete Genome Data

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OMAi
RNYTIKI

Database of Orthologous Groups

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OrthoDBi
227725at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q16832

TreeFam database of animal gene trees

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TreeFami
TF317840

Family and domain databases

Conserved Domains Database

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CDDi
cd00057 FA58C, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.120.260, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR034299 DDR2
IPR000421 FA58C
IPR008979 Galactose-bd-like_sf
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
IPR002011 Tyr_kinase_rcpt_2_CS

The PANTHER Classification System

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PANTHERi
PTHR24416:SF295 PTHR24416:SF295, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00754 F5_F8_type_C, 1 hit
PF07714 Pkinase_Tyr, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00109 TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00231 FA58C, 1 hit
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF49785 SSF49785, 1 hit
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01285 FA58C_1, 1 hit
PS01286 FA58C_2, 1 hit
PS50022 FA58C_3, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS00239 RECEPTOR_TYR_KIN_II, 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>. 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>Sequence (1+)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 has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

Q16832-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MILIPRMLLV LFLLLPILSS AKAQVNPAIC RYPLGMSGGQ IPDEDITASS
60 70 80 90 100
QWSESTAAKY GRLDSEEGDG AWCPEIPVEP DDLKEFLQID LHTLHFITLV
110 120 130 140 150
GTQGRHAGGH GIEFAPMYKI NYSRDGTRWI SWRNRHGKQV LDGNSNPYDI
160 170 180 190 200
FLKDLEPPIV ARFVRFIPVT DHSMNVCMRV ELYGCVWLDG LVSYNAPAGQ
210 220 230 240 250
QFVLPGGSII YLNDSVYDGA VGYSMTEGLG QLTDGVSGLD DFTQTHEYHV
260 270 280 290 300
WPGYDYVGWR NESATNGYIE IMFEFDRIRN FTTMKVHCNN MFAKGVKIFK
310 320 330 340 350
EVQCYFRSEA SEWEPNAISF PLVLDDVNPS ARFVTVPLHH RMASAIKCQY
360 370 380 390 400
HFADTWMMFS EITFQSDAAM YNNSEALPTS PMAPTTYDPM LKVDDSNTRI
410 420 430 440 450
LIGCLVAIIF ILLAIIVIIL WRQFWQKMLE KASRRMLDDE MTVSLSLPSD
460 470 480 490 500
SSMFNNNRSS SPSEQGSNST YDRIFPLRPD YQEPSRLIRK LPEFAPGEEE
510 520 530 540 550
SGCSGVVKPV QPSGPEGVPH YAEADIVNLQ GVTGGNTYSV PAVTMDLLSG
560 570 580 590 600
KDVAVEEFPR KLLTFKEKLG EGQFGEVHLC EVEGMEKFKD KDFALDVSAN
610 620 630 640 650
QPVLVAVKML RADANKNARN DFLKEIKIMS RLKDPNIIHL LAVCITDDPL
660 670 680 690 700
CMITEYMENG DLNQFLSRHE PPNSSSSDVR TVSYTNLKFM ATQIASGMKY
710 720 730 740 750
LSSLNFVHRD LATRNCLVGK NYTIKIADFG MSRNLYSGDY YRIQGRAVLP
760 770 780 790 800
IRWMSWESIL LGKFTTASDV WAFGVTLWET FTFCQEQPYS QLSDEQVIEN
810 820 830 840 850
TGEFFRDQGR QTYLPQPAIC PDSVYKLMLS CWRRDTKNRP SFQEIHLLLL

QQGDE
Length:855
Mass (Da):96,736
Last modified:November 25, 2008 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i78662021BC53E1A0
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 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5T241Q5T241_HUMAN
Discoidin domain-containing recepto...
DDR2
166Annotation 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>
H0Y570H0Y570_HUMAN
Discoidin domain-containing recepto...
DDR2
171Annotation 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>
Q5T244Q5T244_HUMAN
Discoidin domain-containing recepto...
DDR2
148Annotation 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 conflicti642A → S in CAA52777 (PubMed:8247548).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_041498105R → S in a lung large cell carcinoma sample; somatic mutation. 2 Publications1
Natural variantiVAR_065719113E → K in SEMD-SL; abolishes collagen binding. 1 PublicationCorresponds to variant dbSNP:rs397514747EnsemblClinVar.1
Natural variantiVAR_075417124R → W in SEMD-SL. 1 Publication1
Natural variantiVAR_041499441M → I1 PublicationCorresponds to variant dbSNP:rs34722354Ensembl.1
Natural variantiVAR_041500478R → C1 PublicationCorresponds to variant dbSNP:rs34869543Ensembl.1
Natural variantiVAR_041501543V → F1 PublicationCorresponds to variant dbSNP:rs55973200Ensembl.1
Natural variantiVAR_081931610L → P in WRCN; increased autophosphorylation in patient fibroblasts. 1 Publication1
Natural variantiVAR_063050713T → I in SEMD-SL; causes retention in an intracellular compartment and thereby abolishes signaling in response collagen binding. 2 PublicationsCorresponds to variant dbSNP:rs121964865EnsemblClinVar.1
Natural variantiVAR_063051726I → R in SEMD-SL; causes retention in an intracellular compartment and thereby abolishes signaling in response collagen binding. 2 PublicationsCorresponds to variant dbSNP:rs121964864EnsemblClinVar.1
Natural variantiVAR_081932740Y → C in WRCN; increased autophosphorylation in patient fibroblasts. 1 Publication1
Natural variantiVAR_063052752R → C in SEMD-SL; causes retention in an intracellular compartment and thereby abolishes signaling in response collagen binding. 2 PublicationsCorresponds to variant dbSNP:rs121964863EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X74764 mRNA Translation: CAA52777.1
AK314388 mRNA Translation: BAG37013.1
AK095975 mRNA Translation: BAG53183.1
AL445197 Genomic DNA No translation available.
CH471067 Genomic DNA Translation: EAW90713.1
BC052998 mRNA Translation: AAH52998.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS1241.1

Protein sequence database of the Protein Information Resource

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PIRi
S42621

NCBI Reference Sequences

More...
RefSeqi
NP_001014796.1, NM_001014796.1
NP_006173.2, NM_006182.2
XP_006711407.1, XM_006711344.3
XP_011507888.1, XM_011509586.2
XP_011507889.1, XM_011509587.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000367921; ENSP00000356898; ENSG00000162733
ENST00000367922; ENSP00000356899; ENSG00000162733
ENST00000446985; ENSP00000400309; ENSG00000162733

Database of genes from NCBI RefSeq genomes

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GeneIDi
4921

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:4921

UCSC genome browser

More...
UCSCi
uc001gcg.4 human

Keywords - Coding sequence diversityi

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
X74764 mRNA Translation: CAA52777.1
AK314388 mRNA Translation: BAG37013.1
AK095975 mRNA Translation: BAG53183.1
AL445197 Genomic DNA No translation available.
CH471067 Genomic DNA Translation: EAW90713.1
BC052998 mRNA Translation: AAH52998.1
CCDSiCCDS1241.1
PIRiS42621
RefSeqiNP_001014796.1, NM_001014796.1
NP_006173.2, NM_006182.2
XP_006711407.1, XM_006711344.3
XP_011507888.1, XM_011509586.2
XP_011507889.1, XM_011509587.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WUHX-ray1.60A26-190[»]
2Z4FNMR-A26-186[»]
6FERX-ray2.87A/B/C/D/E/F/G/H/I/J/K/L553-855[»]
SMRiQ16832
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi110975, 19 interactors
DIPiDIP-39699N
IntActiQ16832, 9 interactors
MINTiQ16832
STRINGi9606.ENSP00000356899

Chemistry databases

BindingDBiQ16832
ChEMBLiCHEMBL5122
DrugBankiDB12010 Fostamatinib
DB08896 Regorafenib
DrugCentraliQ16832
GuidetoPHARMACOLOGYi1844

PTM databases

iPTMnetiQ16832
PhosphoSitePlusiQ16832
SwissPalmiQ16832

Polymorphism and mutation databases

BioMutaiDDR2
DMDMi215273969

Proteomic databases

EPDiQ16832
jPOSTiQ16832
MassIVEiQ16832
MaxQBiQ16832
PaxDbiQ16832
PeptideAtlasiQ16832
PRIDEiQ16832
ProteomicsDBi61095

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
4921

Genome annotation databases

EnsembliENST00000367921; ENSP00000356898; ENSG00000162733
ENST00000367922; ENSP00000356899; ENSG00000162733
ENST00000446985; ENSP00000400309; ENSG00000162733
GeneIDi4921
KEGGihsa:4921
UCSCiuc001gcg.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4921
DisGeNETi4921

GeneCards: human genes, protein and diseases

More...
GeneCardsi
DDR2
HGNCiHGNC:2731 DDR2
HPAiHPA070112
MalaCardsiDDR2
MIMi191311 gene
271665 phenotype
618175 phenotype
neXtProtiNX_Q16832
OpenTargetsiENSG00000162733
Orphaneti93358 Spondyloepimetaphyseal dysplasia-short limb-abnormal calcification syndrome
PharmGKBiPA27196

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1094 Eukaryota
ENOG410XQAI LUCA
GeneTreeiENSGT00940000154842
HOGENOMiHOG000043102
InParanoidiQ16832
KOiK05125
OMAiRNYTIKI
OrthoDBi227725at2759
PhylomeDBiQ16832
TreeFamiTF317840

Enzyme and pathway databases

BRENDAi2.7.10.1 2681
ReactomeiR-HSA-3000171 Non-integrin membrane-ECM interactions
SignaLinkiQ16832
SIGNORiQ16832

Miscellaneous databases

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

More...
ChiTaRSi
DDR2 human
EvolutionaryTraceiQ16832

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
Discoidin_domain-containing_receptor_2

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

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GenomeRNAii
4921
PharosiQ16832

Protein Ontology

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PROi
PR:Q16832

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000162733 Expressed in 225 organ(s), highest expression level in adipose tissue
ExpressionAtlasiQ16832 baseline and differential
GenevisibleiQ16832 HS

Family and domain databases

CDDicd00057 FA58C, 1 hit
Gene3Di2.60.120.260, 1 hit
InterProiView protein in InterPro
IPR034299 DDR2
IPR000421 FA58C
IPR008979 Galactose-bd-like_sf
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
IPR002011 Tyr_kinase_rcpt_2_CS
PANTHERiPTHR24416:SF295 PTHR24416:SF295, 1 hit
PfamiView protein in Pfam
PF00754 F5_F8_type_C, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PRINTSiPR00109 TYRKINASE
SMARTiView protein in SMART
SM00231 FA58C, 1 hit
SM00219 TyrKc, 1 hit
SUPFAMiSSF49785 SSF49785, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS01285 FA58C_1, 1 hit
PS01286 FA58C_2, 1 hit
PS50022 FA58C_3, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS00239 RECEPTOR_TYR_KIN_II, 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 nameiDDR2_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: Q16832
Secondary accession number(s): Q7Z730
<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: November 1, 1997
Last sequence update: November 25, 2008
Last modified: October 16, 2019
This is version 196 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  8. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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