Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 213 (31 Jul 2019)
Sequence version 1 (01 Feb 1995)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Epithelial discoidin domain-containing receptor 1

Gene

DDR1

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 that functions as cell surface receptor for fibrillar collagen and regulates cell attachment to the extracellular matrix, remodeling of the extracellular matrix, cell migration, differentiation, survival and cell proliferation. Collagen binding triggers a signaling pathway that involves SRC and leads to the activation of MAP kinases. Regulates remodeling of the extracellular matrix by up-regulation of the matrix metalloproteinases MMP2, MMP7 and MMP9, and thereby facilitates cell migration and wound healing. Required for normal blastocyst implantation during pregnancy, for normal mammary gland differentiation and normal lactation. Required for normal ear morphology and normal hearing (By similarity). Promotes smooth muscle cell migration, and thereby contributes to arterial wound healing. Also plays a role in tumor cell invasion. Phosphorylates PTPN11.By similarity9 Publications

Caution

The mutant Gln-371 studied is still likely to be glycosylated at Asn-370, but study did not include mutagenesis of Asn-370.1 Publication

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

<p>This subsection of the <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

Inhibited by the multi-targeted cancer drugs imatinib and ponatinib.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 indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi211Calcium 1; via carbonyl oxygen1
Metal bindingi230Calcium 11
Metal bindingi230Calcium 2; via carbonyl oxygen1
Metal bindingi233Calcium 21
Metal bindingi235Calcium 2; via carbonyl oxygen1
Metal bindingi253Calcium 1; via carbonyl oxygen1
Metal bindingi255Calcium 1; via carbonyl oxygen1
Metal bindingi360Calcium 2; via carbonyl oxygen1
Metal bindingi361Calcium 21
<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 sitei655ATP1
<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 sitei766Proton 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 bindingi616 – 624ATPPROSITE-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 processLactation, Pregnancy
LigandATP-binding, Calcium, Metal-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
Q08345

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q08345

<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:
Epithelial discoidin domain-containing receptor 1 (EC:2.7.10.1)
Short name:
Epithelial discoidin domain receptor 1
Alternative name(s):
CD167 antigen-like family member A
Cell adhesion kinase
Discoidin receptor tyrosine kinase
HGK2
Mammary carcinoma kinase 10
Short name:
MCK-10
Protein-tyrosine kinase 3A
Protein-tyrosine kinase RTK-6
TRK E
Tyrosine kinase DDR
Tyrosine-protein kinase CAK
CD_antigen: CD167a
<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:DDR1
Synonyms:CAK, EDDR1, NEP, NTRK4, PTK3A, RTK6, TRKE
<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 6

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:2730 DDR1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
600408 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q08345

<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 domaini21 – 417ExtracellularSequence analysisAdd BLAST397
<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>Transmembranei418 – 438HelicalSequence analysisAdd BLAST21
Topological domaini439 – 913CytoplasmicSequence analysisAdd BLAST475

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

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

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>Mutagenesisi105R → A: Inhibits collagen-induced phosphorylation. 1 Publication1
Mutagenesisi211N → A: Phosphorylates regardless of collagen presence, collagen addition does not alter significantly the levels of constitutive phosphorylation. 1 Publication1
Mutagenesisi211N → Q: Sustained phosphorylation regardless of collagen presence, collagen addition does not alter significantly the levels of constitutive phosphorylation. Located intracellularly and at the cell surface. Displays a reduced rate of receptor internalization, which is not altered in the presence of collagen. Able to bind collagen as wild-type. Exhibits enhanced collagen-independent receptor dimerization. Complete loss of the collagen-independent constitutive activation; when associated with A-655. 1 Publication1
Mutagenesisi213S → A: Phosphorylates regardless of collagen presence, collagen addition does not alter significantly the levels of constitutive phosphorylation. 1 Publication1
Mutagenesisi260N → Q: Phosphorylates in response to collagen, but at lower levels compared to wild-type. No activation in the absence of collagen. 1 Publication1
Mutagenesisi371N → Q: Phosphorylates in response to collagen, but at lower levels compared to wild-type. No activation in the absence of collagen. 1 Publication1
Mutagenesisi379T → A: Phosphorylates in response to collagen, but at lower levels compared to wild-type. Phosphorylates in response to collagen, but at lower levels compared to wild-type; when associated with A-393. 1 Publication1
Mutagenesisi393T → A: Phosphorylates in response to collagen, but at lower levels compared to wild-type. Phosphorylates in response to collagen, but at lower levels compared to wild-type; when associated with A-379. 1 Publication1
Mutagenesisi394N → Q: Phosphorylates in response to collagen, but at lower levels compared to wild-type. No activation in the absence of collagen. 1 Publication1
Mutagenesisi655K → A: Loss of kinase activity. Complete loss of the collagen-independent constitutive activation; when associated with Q-211. 1 Publication1
Mutagenesisi707G → A: Confers over 20-fold resistance to the ability of an inhibitor to inhibit autophosphorylation. 1 Publication1
Mutagenesisi740Y → F: Abolishes interaction with PTPN11. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
780

Open Targets

More...
OpenTargetsi
ENSG00000204580

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA24348

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL5319

Drug and drug target database

More...
DrugBanki
DB00619 Imatinib

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
1843

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
DDR1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
729008

<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 – 18Sequence analysisAdd BLAST18
<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_000001674219 – 913Epithelial discoidin domain-containing receptor 1Add BLAST895

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 bondi31 ↔ 185PROSITE-ProRule annotation1 Publication
Disulfide bondi74 ↔ 177PROSITE-ProRule annotation1 Publication
<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>Glycosylationi211N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi260N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi303 ↔ 348PROSITE-ProRule annotation1 Publication
Glycosylationi370N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi394N-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 residuei484Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei513Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei520Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei631PhosphoserineCombined sources1
Modified residuei740Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei792Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei796Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei797Phosphotyrosine; by 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

Autophosphorylated in response to fibrillar collagen binding.
Glycosylation of Asn-211, but apparently not of Asn-260 or Asn-394, prevents autophosphorylation from occurring in the absence of collagen.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q08345

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q08345

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q08345

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

More...
PaxDbi
Q08345

PeptideAtlas

More...
PeptideAtlasi
Q08345

PRoteomics IDEntifications database

More...
PRIDEi
Q08345

ProteomicsDB human proteome resource

More...
ProteomicsDBi
58595 [Q08345-1]
58596 [Q08345-2]
58597 [Q08345-4]
58598 [Q08345-5]
58599 [Q08345-6]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q08345

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

More...
PhosphoSitePlusi
Q08345

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
Q08345

<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 T-47D, MDA-MB-175 and HBL-100 breast carcinoma cells, A-431 epidermoid carcinoma cells, SW48 and SNU-C2B colon carcinoma cells and Hs 294T melanoma cells (at protein level). Expressed at low levels in most adult tissues and is highest in the brain, lung, placenta and kidney. Lower levels of expression are detected in melanocytes, heart, liver, skeletal muscle and pancreas. Abundant in breast carcinoma cell lines. In the colonic mucosa, expressed in epithelia but not in the connective tissue of the lamina propria. In the thyroid gland, expressed in the epithelium of the thyroid follicles. In pancreas, expressed in the islets of Langerhans cells, but not in the surrounding epithelial cells of the exocrine pancreas. In kidney, expressed in the epithelia of the distal tubules. Not expressed in connective tissue, endothelial cells, adipose tissue, muscle cells or cells of hematopoietic origin.3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000204580 Expressed in 230 organ(s), highest expression level in corpus callosum

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q08345 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q08345 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB010162
CAB025656
HPA057194

<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.

Interacts (via PPxY motif) with WWC1 (via WW domains) in a collagen-regulated manner.

Forms a tripartite complex with WWC1 and PRKCZ, but predominantly in the absence of collagen.

Interacts (tyrosine phosphorylated) with SHC1.

Interacts with SRC.

Interacts with MYH9.

Interacts with CDH1.

Interacts with PTPN11.

Interacts with NCK2.

9 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
107234, 20 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q08345

Database of interacting proteins

More...
DIPi
DIP-39698N

Protein interaction database and analysis system

More...
IntActi
Q08345, 14 interactors

Molecular INTeraction database

More...
MINTi
Q08345

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000427552

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q08345

<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

1913
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
Q08345

Database of comparative protein structure models

More...
ModBasei
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

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>Domaini31 – 185F5/8 type CPROSITE-ProRule annotationAdd BLAST155
Domaini610 – 905Protein kinasePROSITE-ProRule annotationAdd BLAST296

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>Regioni192 – 367DS-like domainAdd BLAST176

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi481 – 484PPxY motif4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi377 – 415Gly/Pro-richAdd BLAST39
Compositional biasi476 – 601Gly/Pro-richAdd BLAST126

<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 Gly/Pro-rich domains may be required for an unusual geometry of interaction with ligand or substrates.

<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

More...
GeneTreei
ENSGT00940000159733

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000043102

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q08345

KEGG Orthology (KO)

More...
KOi
K05124

Database of Orthologous Groups

More...
OrthoDBi
1576308at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q08345

TreeFam database of animal gene trees

More...
TreeFami
TF317840

Family and domain databases

Conserved Domains Database

More...
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
IPR029553 DDR1
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

More...
PANTHERi
PTHR24416:SF333 PTHR24416:SF333, 1 hit

Pfam protein domain database

More...
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

More...
PRINTSi
PR00109 TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

More...
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>Sequences (5+)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 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.<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 39 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q08345-1) [UniParc]FASTAAdd to basket
Also known as: CAK I, DDR1b

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
MGPEALSSLL LLLLVASGDA DMKGHFDPAK CRYALGMQDR TIPDSDISAS
60 70 80 90 100
SSWSDSTAAR HSRLESSDGD GAWCPAGSVF PKEEEYLQVD LQRLHLVALV
110 120 130 140 150
GTQGRHAGGL GKEFSRSYRL RYSRDGRRWM GWKDRWGQEV ISGNEDPEGV
160 170 180 190 200
VLKDLGPPMV ARLVRFYPRA DRVMSVCLRV ELYGCLWRDG LLSYTAPVGQ
210 220 230 240 250
TMYLSEAVYL NDSTYDGHTV GGLQYGGLGQ LADGVVGLDD FRKSQELRVW
260 270 280 290 300
PGYDYVGWSN HSFSSGYVEM EFEFDRLRAF QAMQVHCNNM HTLGARLPGG
310 320 330 340 350
VECRFRRGPA MAWEGEPMRH NLGGNLGDPR ARAVSVPLGG RVARFLQCRF
360 370 380 390 400
LFAGPWLLFS EISFISDVVN NSSPALGGTF PPAPWWPPGP PPTNFSSLEL
410 420 430 440 450
EPRGQQPVAK AEGSPTAILI GCLVAIILLL LLIIALMLWR LHWRRLLSKA
460 470 480 490 500
ERRVLEEELT VHLSVPGDTI LINNRPGPRE PPPYQEPRPR GNPPHSAPCV
510 520 530 540 550
PNGSALLLSN PAYRLLLATY ARPPRGPGPP TPAWAKPTNT QAYSGDYMEP
560 570 580 590 600
EKPGAPLLPP PPQNSVPHYA EADIVTLQGV TGGNTYAVPA LPPGAVGDGP
610 620 630 640 650
PRVDFPRSRL RFKEKLGEGQ FGEVHLCEVD SPQDLVSLDF PLNVRKGHPL
660 670 680 690 700
LVAVKILRPD ATKNARNDFL KEVKIMSRLK DPNIIRLLGV CVQDDPLCMI
710 720 730 740 750
TDYMENGDLN QFLSAHQLED KAAEGAPGDG QAAQGPTISY PMLLHVAAQI
760 770 780 790 800
ASGMRYLATL NFVHRDLATR NCLVGENFTI KIADFGMSRN LYAGDYYRVQ
810 820 830 840 850
GRAVLPIRWM AWECILMGKF TTASDVWAFG VTLWEVLMLC RAQPFGQLTD
860 870 880 890 900
EQVIENAGEF FRDQGRQVYL SRPPACPQGL YELMLRCWSR ESEQRPPFSQ
910
LHRFLAEDAL NTV
Length:913
Mass (Da):101,128
Last modified:February 1, 1995 - 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:iC96913EA906C481E
GO
Isoform 2 (identifier: Q08345-2) [UniParc]FASTAAdd to basket
Also known as: CAK II, DDR1a, Short

The sequence of this isoform differs from the canonical sequence as follows:
     506-542: Missing.

Show »
Length:876
Mass (Da):97,174
Checksum:iE02881598CC7CD0B
GO
Isoform 3 (identifier: Q08345-4) [UniParc]FASTAAdd to basket
Also known as: DDR1d

The sequence of this isoform differs from the canonical sequence as follows:
     190-243: GLLSYTAPVG...GVVGLDDFRK → CSMGVWASWQ...MWRWSLSLTG
     244-913: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:243
Mass (Da):27,130
Checksum:i36872B8FB29835D0
GO
Isoform 4 (identifier: Q08345-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     665-665: A → ASFSLFS

Show »
Length:919
Mass (Da):101,796
Checksum:i2094224F6AE943F5
GO
Isoform 5 (identifier: Q08345-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MSLPRCCPHPLRPEGSGAM
     506-542: Missing.

Note: No experimental confirmation available.
Show »
Length:894
Mass (Da):99,064
Checksum:iD46EECFC939B7585
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 39 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0A0MSX3A0A0A0MSX3_HUMAN
Epithelial discoidin domain-contain...
DDR1
767Annotation 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>
A2ABM8A2ABM8_HUMAN
Epithelial discoidin domain-contain...
DDR1
493Annotation 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>
E7ENJ2E7ENJ2_HUMAN
Epithelial discoidin domain-contain...
DDR1
85Annotation 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>
E7EQ23E7EQ23_HUMAN
Epithelial discoidin domain-contain...
DDR1
70Annotation 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>
E7EX99E7EX99_HUMAN
Epithelial discoidin domain-contain...
DDR1
73Annotation 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>
A0A0G2JNZ7A0A0G2JNZ7_HUMAN
Epithelial discoidin domain-contain...
DDR1
767Annotation 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>
A0A0G2JJA0A0A0G2JJA0_HUMAN
Epithelial discoidin domain-contain...
DDR1
63Annotation 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>
H0YAH6H0YAH6_HUMAN
Epithelial discoidin domain-contain...
DDR1
172Annotation 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>
A0A140T972A0A140T972_HUMAN
Epithelial discoidin domain-contain...
DDR1
493Annotation 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>
E7EXB0E7EXB0_HUMAN
Epithelial discoidin domain-contain...
DDR1
78Annotation 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>
There are more potential isoformsShow all

<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 ACF47649 differs from that shown. Reason: Erroneous termination at position 287. Translated as Cys.Curated
The sequence BAE06103 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti94L → V in AAA02866 (PubMed:8390675).Curated1
Sequence conflicti94L → V in AAC50917 (PubMed:8977099).Curated1
Sequence conflicti165R → H in AAH70070 (PubMed:15489334).Curated1
Sequence conflicti285 – 286VH → MW in ACF47649 (PubMed:18593464).Curated2
Sequence conflicti741P → Q in AAH70070 (PubMed:15489334).Curated1
Sequence conflicti847 – 867QLTDE…DQGRQ → SAHRRAGHRERGGVLPGPGP A in CAA66871 (PubMed:8796349).CuratedAdd BLAST21

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_04149217S → G1 PublicationCorresponds to variant dbSNP:rs55901302Ensembl.1
Natural variantiVAR_041493100V → A1 PublicationCorresponds to variant dbSNP:rs34544756Ensembl.1
Natural variantiVAR_041494169R → Q1 PublicationCorresponds to variant dbSNP:rs55980643Ensembl.1
Natural variantiVAR_041495170A → D1 PublicationCorresponds to variant dbSNP:rs56231803Ensembl.1
Natural variantiVAR_041496306R → W1 PublicationCorresponds to variant dbSNP:rs56024191Ensembl.1
Natural variantiVAR_041497496S → A in a lung squamous cell carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_049716833L → V2 PublicationsCorresponds to variant dbSNP:rs2524235Ensembl.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_0435821M → MSLPRCCPHPLRPEGSGAM in isoform 5. 1 Publication1
Alternative sequenceiVSP_036916190 – 243GLLSY…DDFRK → CSMGVWASWQMVWWGWMTLG RVRSCGSGQAMTMWDGATTA SPVAMWRWSLSLTG in isoform 3. 1 PublicationAdd BLAST54
Alternative sequenceiVSP_036917244 – 913Missing in isoform 3. 1 PublicationAdd BLAST670
Alternative sequenceiVSP_002953506 – 542Missing in isoform 2 and isoform 5. 7 PublicationsAdd BLAST37
Alternative sequenceiVSP_038057665A → ASFSLFS in isoform 4. 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
X74979 mRNA Translation: CAA52915.1
L11315 mRNA Translation: AAA02866.1
Z29093 mRNA Translation: CAA82335.1
L20817 mRNA Translation: AAA18019.1
U48705 Genomic DNA Translation: AAC50917.1
X98208
, X99023, X99024, X99025, X99026, X99027, X99028, X99029, X99030, X99031, X99032, X99033, X99034 Genomic DNA Translation: CAA66871.1
L57508 mRNA Translation: AAB05208.1
EU826613 mRNA Translation: ACF47649.1 Sequence problems.
EU826614 mRNA Translation: ACF47650.1
AK291621 mRNA Translation: BAF84310.1
AK294793 mRNA Translation: BAH11886.1
AB210021 mRNA Translation: BAE06103.1 Different initiation.
BA000025 Genomic DNA Translation: BAB63318.1
CR759747 Genomic DNA No translation available.
AB088102 Genomic DNA Translation: BAC54935.1
AB103608 Genomic DNA Translation: BAF31270.1
AL662854 Genomic DNA No translation available.
AL662870 Genomic DNA No translation available.
AL773541 Genomic DNA No translation available.
AL773589 Genomic DNA No translation available.
AB202100 Genomic DNA Translation: BAE78621.1
BX927194 Genomic DNA No translation available.
CH471081 Genomic DNA Translation: EAX03335.1
CH471081 Genomic DNA Translation: EAX03338.1
BC008716 mRNA Translation: AAH08716.1
BC013400 mRNA Translation: AAH13400.1
BC070070 mRNA Translation: AAH70070.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS34385.1 [Q08345-1]
CCDS4690.1 [Q08345-2]
CCDS47396.1 [Q08345-5]
CCDS56411.1 [Q08345-6]

Protein sequence database of the Protein Information Resource

More...
PIRi
A48280
A49508

NCBI Reference Sequences

More...
RefSeqi
NP_001189450.1, NM_001202521.1
NP_001189451.1, NM_001202522.1
NP_001189452.1, NM_001202523.1 [Q08345-6]
NP_001284581.1, NM_001297652.1 [Q08345-2]
NP_001284582.1, NM_001297653.1 [Q08345-2]
NP_001284583.1, NM_001297654.1 [Q08345-1]
NP_001945.3, NM_001954.4 [Q08345-2]
NP_054699.2, NM_013993.2 [Q08345-1]
NP_054700.2, NM_013994.2 [Q08345-5]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000259875; ENSP00000259875; ENSG00000137332 [Q08345-2]
ENST00000324771; ENSP00000318217; ENSG00000204580 [Q08345-1]
ENST00000376567; ENSP00000365751; ENSG00000204580 [Q08345-2]
ENST00000376568; ENSP00000365752; ENSG00000204580 [Q08345-1]
ENST00000376569; ENSP00000365753; ENSG00000204580 [Q08345-2]
ENST00000376570; ENSP00000365754; ENSG00000204580 [Q08345-2]
ENST00000376575; ENSP00000365759; ENSG00000204580 [Q08345-4]
ENST00000383377; ENSP00000372868; ENSG00000137332 [Q08345-1]
ENST00000400410; ENSP00000383261; ENSG00000137332 [Q08345-2]
ENST00000400411; ENSP00000383262; ENSG00000137332 [Q08345-2]
ENST00000400414; ENSP00000383265; ENSG00000137332 [Q08345-1]
ENST00000400486; ENSP00000383334; ENSG00000215522 [Q08345-2]
ENST00000400488; ENSP00000383336; ENSG00000215522 [Q08345-2]
ENST00000400489; ENSP00000383337; ENSG00000215522 [Q08345-2]
ENST00000400491; ENSP00000383338; ENSG00000215522 [Q08345-1]
ENST00000400492; ENSP00000383339; ENSG00000215522 [Q08345-1]
ENST00000412329; ENSP00000391805; ENSG00000230456 [Q08345-1]
ENST00000415092; ENSP00000405540; ENSG00000230456 [Q08345-2]
ENST00000418800; ENSP00000407699; ENSG00000204580 [Q08345-2]
ENST00000419412; ENSP00000416183; ENSG00000234078 [Q08345-2]
ENST00000421229; ENSP00000415730; ENSG00000234078 [Q08345-2]
ENST00000427053; ENSP00000416145; ENSG00000230456 [Q08345-2]
ENST00000429699; ENSP00000401397; ENSG00000234078 [Q08345-1]
ENST00000430933; ENSP00000397769; ENSG00000234078 [Q08345-1]
ENST00000449518; ENSP00000414285; ENSG00000230456 [Q08345-1]
ENST00000452441; ENSP00000405039; ENSG00000204580 [Q08345-1]
ENST00000453510; ENSP00000401208; ENSG00000230456 [Q08345-2]
ENST00000454612; ENSP00000406091; ENSG00000204580 [Q08345-2]
ENST00000454774; ENSP00000400393; ENSG00000234078 [Q08345-2]
ENST00000482873; ENSP00000421978; ENSG00000204580 [Q08345-4]
ENST00000508312; ENSP00000422442; ENSG00000204580 [Q08345-6]
ENST00000513240; ENSP00000427552; ENSG00000204580 [Q08345-5]
ENST00000548133; ENSP00000449611; ENSG00000230456 [Q08345-1]
ENST00000548962; ENSP00000448115; ENSG00000230456 [Q08345-6]
ENST00000549026; ENSP00000449238; ENSG00000215522 [Q08345-6]
ENST00000550384; ENSP00000447474; ENSG00000234078 [Q08345-6]
ENST00000550395; ENSP00000449255; ENSG00000215522 [Q08345-1]
ENST00000552068; ENSP00000449190; ENSG00000234078 [Q08345-1]
ENST00000552721; ENSP00000449307; ENSG00000137332 [Q08345-6]
ENST00000553015; ENSP00000448377; ENSG00000137332 [Q08345-1]
ENST00000617572; ENSP00000479195; ENSG00000215522 [Q08345-4]
ENST00000618059; ENSP00000479204; ENSG00000234078 [Q08345-4]
ENST00000620318; ENSP00000484588; ENSG00000137332 [Q08345-4]
ENST00000621544; ENSP00000484013; ENSG00000230456 [Q08345-4]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
780

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:780

UCSC genome browser

More...
UCSCi
uc003nrq.4 human [Q08345-1]

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_references_section">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

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74979 mRNA Translation: CAA52915.1
L11315 mRNA Translation: AAA02866.1
Z29093 mRNA Translation: CAA82335.1
L20817 mRNA Translation: AAA18019.1
U48705 Genomic DNA Translation: AAC50917.1
X98208
, X99023, X99024, X99025, X99026, X99027, X99028, X99029, X99030, X99031, X99032, X99033, X99034 Genomic DNA Translation: CAA66871.1
L57508 mRNA Translation: AAB05208.1
EU826613 mRNA Translation: ACF47649.1 Sequence problems.
EU826614 mRNA Translation: ACF47650.1
AK291621 mRNA Translation: BAF84310.1
AK294793 mRNA Translation: BAH11886.1
AB210021 mRNA Translation: BAE06103.1 Different initiation.
BA000025 Genomic DNA Translation: BAB63318.1
CR759747 Genomic DNA No translation available.
AB088102 Genomic DNA Translation: BAC54935.1
AB103608 Genomic DNA Translation: BAF31270.1
AL662854 Genomic DNA No translation available.
AL662870 Genomic DNA No translation available.
AL773541 Genomic DNA No translation available.
AL773589 Genomic DNA No translation available.
AB202100 Genomic DNA Translation: BAE78621.1
BX927194 Genomic DNA No translation available.
CH471081 Genomic DNA Translation: EAX03335.1
CH471081 Genomic DNA Translation: EAX03338.1
BC008716 mRNA Translation: AAH08716.1
BC013400 mRNA Translation: AAH13400.1
BC070070 mRNA Translation: AAH70070.1
CCDSiCCDS34385.1 [Q08345-1]
CCDS4690.1 [Q08345-2]
CCDS47396.1 [Q08345-5]
CCDS56411.1 [Q08345-6]
PIRiA48280
A49508
RefSeqiNP_001189450.1, NM_001202521.1
NP_001189451.1, NM_001202522.1
NP_001189452.1, NM_001202523.1 [Q08345-6]
NP_001284581.1, NM_001297652.1 [Q08345-2]
NP_001284582.1, NM_001297653.1 [Q08345-2]
NP_001284583.1, NM_001297654.1 [Q08345-1]
NP_001945.3, NM_001954.4 [Q08345-2]
NP_054699.2, NM_013993.2 [Q08345-1]
NP_054700.2, NM_013994.2 [Q08345-5]

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
3ZOSX-ray1.92A/B601-913[»]
4AG4X-ray2.80A29-367[»]
4BKJX-ray1.70A/B601-913[»]
4CKRX-ray2.20A601-913[»]
5BVKX-ray2.29A595-913[»]
5BVNX-ray2.21A595-913[»]
5BVOX-ray1.98A595-913[»]
5BVWX-ray1.94A595-913[»]
5FDPX-ray2.25A601-913[»]
5FDXX-ray2.65A/B601-913[»]
6BRJX-ray2.23A1-913[»]
6BSDX-ray2.61A1-913[»]
6FEWX-ray1.44A593-913[»]
6FEXX-ray1.29A593-913[»]
6FILX-ray1.73A593-913[»]
6FIMX-ray1.44A593-913[»]
6FINX-ray1.67A593-913[»]
6FIOX-ray1.99A593-913[»]
6FIQX-ray1.79A593-913[»]
6GWRX-ray2.07A/B601-913[»]
6HP9X-ray1.96A/B601-913[»]
SMRiQ08345
ModBaseiSearch...

Protein-protein interaction databases

BioGridi107234, 20 interactors
CORUMiQ08345
DIPiDIP-39698N
IntActiQ08345, 14 interactors
MINTiQ08345
STRINGi9606.ENSP00000427552

Chemistry databases

BindingDBiQ08345
ChEMBLiCHEMBL5319
DrugBankiDB00619 Imatinib
GuidetoPHARMACOLOGYi1843

PTM databases

iPTMnetiQ08345
PhosphoSitePlusiQ08345

Polymorphism and mutation databases

BioMutaiDDR1
DMDMi729008

Proteomic databases

EPDiQ08345
jPOSTiQ08345
MaxQBiQ08345
PaxDbiQ08345
PeptideAtlasiQ08345
PRIDEiQ08345
ProteomicsDBi58595 [Q08345-1]
58596 [Q08345-2]
58597 [Q08345-4]
58598 [Q08345-5]
58599 [Q08345-6]

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...
ABCDi
Q08345

The DNASU plasmid repository

More...
DNASUi
780
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000259875; ENSP00000259875; ENSG00000137332 [Q08345-2]
ENST00000324771; ENSP00000318217; ENSG00000204580 [Q08345-1]
ENST00000376567; ENSP00000365751; ENSG00000204580 [Q08345-2]
ENST00000376568; ENSP00000365752; ENSG00000204580 [Q08345-1]
ENST00000376569; ENSP00000365753; ENSG00000204580 [Q08345-2]
ENST00000376570; ENSP00000365754; ENSG00000204580 [Q08345-2]
ENST00000376575; ENSP00000365759; ENSG00000204580 [Q08345-4]
ENST00000383377; ENSP00000372868; ENSG00000137332 [Q08345-1]
ENST00000400410; ENSP00000383261; ENSG00000137332 [Q08345-2]
ENST00000400411; ENSP00000383262; ENSG00000137332 [Q08345-2]
ENST00000400414; ENSP00000383265; ENSG00000137332 [Q08345-1]
ENST00000400486; ENSP00000383334; ENSG00000215522 [Q08345-2]
ENST00000400488; ENSP00000383336; ENSG00000215522 [Q08345-2]
ENST00000400489; ENSP00000383337; ENSG00000215522 [Q08345-2]
ENST00000400491; ENSP00000383338; ENSG00000215522 [Q08345-1]
ENST00000400492; ENSP00000383339; ENSG00000215522 [Q08345-1]
ENST00000412329; ENSP00000391805; ENSG00000230456 [Q08345-1]
ENST00000415092; ENSP00000405540; ENSG00000230456 [Q08345-2]
ENST00000418800; ENSP00000407699; ENSG00000204580 [Q08345-2]
ENST00000419412; ENSP00000416183; ENSG00000234078 [Q08345-2]
ENST00000421229; ENSP00000415730; ENSG00000234078 [Q08345-2]
ENST00000427053; ENSP00000416145; ENSG00000230456 [Q08345-2]
ENST00000429699; ENSP00000401397; ENSG00000234078 [Q08345-1]
ENST00000430933; ENSP00000397769; ENSG00000234078 [Q08345-1]
ENST00000449518; ENSP00000414285; ENSG00000230456 [Q08345-1]
ENST00000452441; ENSP00000405039; ENSG00000204580 [Q08345-1]
ENST00000453510; ENSP00000401208; ENSG00000230456 [Q08345-2]
ENST00000454612; ENSP00000406091; ENSG00000204580 [Q08345-2]
ENST00000454774; ENSP00000400393; ENSG00000234078 [Q08345-2]
ENST00000482873; ENSP00000421978; ENSG00000204580 [Q08345-4]
ENST00000508312; ENSP00000422442; ENSG00000204580 [Q08345-6]
ENST00000513240; ENSP00000427552; ENSG00000204580 [Q08345-5]
ENST00000548133; ENSP00000449611; ENSG00000230456 [Q08345-1]
ENST00000548962; ENSP00000448115; ENSG00000230456 [Q08345-6]
ENST00000549026; ENSP00000449238; ENSG00000215522 [Q08345-6]
ENST00000550384; ENSP00000447474; ENSG00000234078 [Q08345-6]
ENST00000550395; ENSP00000449255; ENSG00000215522 [Q08345-1]
ENST00000552068; ENSP00000449190; ENSG00000234078 [Q08345-1]
ENST00000552721; ENSP00000449307; ENSG00000137332 [Q08345-6]
ENST00000553015; ENSP00000448377; ENSG00000137332 [Q08345-1]
ENST00000617572; ENSP00000479195; ENSG00000215522 [Q08345-4]
ENST00000618059; ENSP00000479204; ENSG00000234078 [Q08345-4]
ENST00000620318; ENSP00000484588; ENSG00000137332 [Q08345-4]
ENST00000621544; ENSP00000484013; ENSG00000230456 [Q08345-4]
GeneIDi780
KEGGihsa:780
UCSCiuc003nrq.4 human [Q08345-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
780
DisGeNETi780

GeneCards: human genes, protein and diseases

More...
GeneCardsi
DDR1
HGNCiHGNC:2730 DDR1
HPAiCAB010162
CAB025656
HPA057194
MIMi600408 gene
neXtProtiNX_Q08345
OpenTargetsiENSG00000204580
PharmGKBiPA24348

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1094 Eukaryota
ENOG410XQAI LUCA
GeneTreeiENSGT00940000159733
HOGENOMiHOG000043102
InParanoidiQ08345
KOiK05124
OrthoDBi1576308at2759
PhylomeDBiQ08345
TreeFamiTF317840

Enzyme and pathway databases

BRENDAi2.7.10.1 2681
ReactomeiR-HSA-3000171 Non-integrin membrane-ECM interactions
SignaLinkiQ08345
SIGNORiQ08345

Miscellaneous databases

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

More...
ChiTaRSi
DDR1 human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
DDR1

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

More...
GenomeRNAii
780
PMAP-CutDBiQ08345

Protein Ontology

More...
PROi
PR:Q08345

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000204580 Expressed in 230 organ(s), highest expression level in corpus callosum
ExpressionAtlasiQ08345 baseline and differential
GenevisibleiQ08345 HS

Family and domain databases

CDDicd00057 FA58C, 1 hit
Gene3Di2.60.120.260, 1 hit
InterProiView protein in InterPro
IPR029553 DDR1
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:SF333 PTHR24416:SF333, 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 nameiDDR1_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: Q08345
Secondary accession number(s): B5A975
, B5A976, B7Z2K0, Q14196, Q16562, Q2L6H3, Q4LE50, Q5ST11, Q5ST12, Q6NSK4, Q9UD35, Q9UD36, Q9UD37, Q9UD86, Q9UDL2
<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 1, 1995
Last sequence update: February 1, 1995
Last modified: July 31, 2019
This is version 213 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

3D-structure, Complete proteome, 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 chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  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 and mouse protein kinases
    Human and mouse protein kinases: classification and index
  8. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
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