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Discoidin domain-containing receptor 2 (Discoidin domain receptor 2) (EC 2.7.10.1) (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)

 DDR2_HUMAN              Reviewed;         855 AA.
Q16832; Q7Z730;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 2.
12-SEP-2018, entry version 186.
RecName: Full=Discoidin domain-containing receptor 2;
Short=Discoidin domain receptor 2;
EC=2.7.10.1;
AltName: Full=CD167 antigen-like family member B;
AltName: Full=Discoidin domain-containing receptor tyrosine kinase 2;
AltName: Full=Neurotrophic tyrosine kinase, receptor-related 3;
AltName: Full=Receptor protein-tyrosine kinase TKT;
AltName: Full=Tyrosine-protein kinase TYRO10;
AltName: CD_antigen=CD167b;
Flags: Precursor;
Name=DDR2; Synonyms=NTRKR3, TKT, TYRO10;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Heart, and Thymus;
PubMed=8247548;
Karn T., Holtrich U., Braeuninger A., Boehme B., Wolf G.,
Ruebsamen-Waigmann H., Strebhardt K.;
"Structure, expression and chromosomal mapping of TKT from man and
mouse: a new subclass of receptor tyrosine kinases with a factor VIII-
like domain.";
Oncogene 8:3433-3440(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Hair follicle dermal papilla, and Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION AS COLLAGEN RECEPTOR AND IN UP-REGULATION OF MMP1,
PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
PubMed=9659899; DOI=10.1016/S1097-2765(00)80003-9;
Vogel W., Gish G.D., Alves F., Pawson T.;
"The discoidin domain receptor tyrosine kinases are activated by
collagen.";
Mol. Cell 1:13-23(1997).
[7]
FUNCTION IN REGULATION OF MMP1 AND MMP2, PHOSPHORYLATION AT TYR-736;
TYR-740 AND TYR-741, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
INTERACTION WITH SHC1, AND MUTAGENESIS OF LYS-608; TYR-736; TYR-740
AND TYR-741.
PubMed=16186108; DOI=10.1074/jbc.M506921200;
Yang K., Kim J.H., Kim H.J., Park I.S., Kim I.Y., Yang B.S.;
"Tyrosine 740 phosphorylation of discoidin domain receptor 2 by Src
stimulates intramolecular autophosphorylation and Shc signaling
complex formation.";
J. Biol. Chem. 280:39058-39066(2005).
[8]
FUNCTION AS COLLAGEN RECEPTOR, AND PHOSPHORYLATION.
PubMed=16186104; DOI=10.1074/jbc.M508226200;
Wall S.J., Werner E., Werb Z., DeClerck Y.A.;
"Discoidin domain receptor 2 mediates tumor cell cycle arrest induced
by fibrillar collagen.";
J. Biol. Chem. 280:40187-40194(2005).
[9]
FUNCTION IN UP-REGULATION OF MMP13, INDUCTION, AND TISSUE SPECIFICITY.
PubMed=17665456; DOI=10.1002/art.22761;
Xu L., Peng H., Glasson S., Lee P.L., Hu K., Ijiri K., Olsen B.R.,
Goldring M.B., Li Y.;
"Increased expression of the collagen receptor discoidin domain
receptor 2 in articular cartilage as a key event in the pathogenesis
of osteoarthritis.";
Arthritis Rheum. 56:2663-2673(2007).
[10]
FUNCTION AS COLLAGEN RECEPTOR, SUBCELLULAR LOCATION, PHOSPHORYLATION,
AND SUBUNIT.
PubMed=18201965; DOI=10.1074/jbc.M709290200;
Konitsiotis A.D., Raynal N., Bihan D., Hohenester E., Farndale R.W.,
Leitinger B.;
"Characterization of high affinity binding motifs for the discoidin
domain receptor DDR2 in collagen.";
J. Biol. Chem. 283:6861-6868(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[13]
FUNCTION IN OSTEOBLAST DIFFERENTIATION VIA ACTIVATION OF RUNX2,
INDUCTION, AND TISSUE SPECIFICITY.
PubMed=20564243; DOI=10.1002/jbmr.159;
Lin K.L., Chou C.H., Hsieh S.C., Hwa S.Y., Lee M.T., Wang F.F.;
"Transcriptional upregulation of DDR2 by ATF4 facilitates osteoblastic
differentiation through p38 MAPK-mediated Runx2 activation.";
J. Bone Miner. Res. 25:2489-2503(2010).
[14]
FUNCTION IN OSTEOBLAST DIFFERENTIATION AND CHONDROCYTE MATURATION VIA
ACTIVATION OF RUNX2.
PubMed=20734453; DOI=10.1002/jbmr.225;
Zhang Y., Su J., Yu J., Bu X., Ren T., Liu X., Yao L.;
"An essential role of discoidin domain receptor 2 (DDR2) in osteoblast
differentiation and chondrocyte maturation via modulation of Runx2
activation.";
J. Bone Miner. Res. 26:604-617(2011).
[15]
REVIEW.
PubMed=16626936; DOI=10.1016/j.cellsig.2006.02.012;
Vogel W.F., Abdulhussein R., Ford C.E.;
"Sensing extracellular matrix: an update on discoidin domain receptor
function.";
Cell. Signal. 18:1108-1116(2006).
[16]
REVIEW.
PubMed=21568710; DOI=10.1146/annurev-cellbio-092910-154013;
Leitinger B.;
"Transmembrane collagen receptors.";
Annu. Rev. Cell Dev. Biol. 27:265-290(2011).
[17]
STRUCTURE BY NMR OF 22-186, INTERACTION WITH COLLAGEN, AND DISULFIDE
BONDS.
PubMed=17703188; DOI=10.1038/sj.emboj.7601833;
Ichikawa O., Osawa M., Nishida N., Goshima N., Nomura N., Shimada I.;
"Structural basis of the collagen-binding mode of discoidin domain
receptor 2.";
EMBO J. 26:4168-4176(2007).
[18]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 26-190 IN COMPLEX WITH
COLLAGEN PEPTIDE, DISULFIDE BONDS, MUTAGENESIS OF TRP-52, FUNCTION IN
COLLAGEN BINDING, CATALYTIC ACTIVITY, AND PHOSPHORYLATION.
PubMed=20004161; DOI=10.1016/j.str.2009.10.012;
Carafoli F., Bihan D., Stathopoulos S., Konitsiotis A.D.,
Kvansakul M., Farndale R.W., Leitinger B., Hohenester E.;
"Crystallographic insight into collagen recognition by discoidin
domain receptor 2.";
Structure 17:1573-1581(2009).
[19]
VARIANT [LARGE SCALE ANALYSIS] SER-105.
PubMed=16140923; DOI=10.1158/0008-5472.CAN-05-1855;
Davies H., Hunter C., Smith R., Stephens P., Greenman C., Bignell G.,
Teague J., Butler A., Edkins S., Stevens C., Parker A., O'Meara S.,
Avis T., Barthorpe S., Brackenbury L., Buck G., Clements J., Cole J.,
Dicks E., Edwards K., Forbes S., Gorton M., Gray K., Halliday K.,
Harrison R., Hills K., Hinton J., Jones D., Kosmidou V., Laman R.,
Lugg R., Menzies A., Perry J., Petty R., Raine K., Shepherd R.,
Small A., Solomon H., Stephens Y., Tofts C., Varian J., Webb A.,
West S., Widaa S., Yates A., Brasseur F., Cooper C.S., Flanagan A.M.,
Green A., Knowles M., Leung S.Y., Looijenga L.H., Malkowicz B.,
Pierotti M.A., Teh B.T., Yuen S.T., Lakhani S.R., Easton D.F.,
Weber B.L., Goldstraw P., Nicholson A.G., Wooster R., Stratton M.R.,
Futreal P.A.;
"Somatic mutations of the protein kinase gene family in human lung
cancer.";
Cancer Res. 65:7591-7595(2005).
[20]
VARIANTS [LARGE SCALE ANALYSIS] SER-105; ILE-441; CYS-478 AND PHE-543.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[21]
VARIANTS SEMD-SL ILE-713; ARG-726 AND CYS-752.
PubMed=19110212; DOI=10.1016/j.ajhg.2008.12.004;
Bargal R., Cormier-Daire V., Ben-Neriah Z., Le Merrer M., Sosna J.,
Melki J., Zangen D.H., Smithson S.F., Borochowitz Z., Belostotsky R.,
Raas-Rothschild A.;
"Mutations in DDR2 gene cause SMED with short limbs and abnormal
calcifications.";
Am. J. Hum. Genet. 84:80-84(2009).
[22]
VARIANT SEMD-SL LYS-113, CHARACTERIZATION OF VARIANTS SEMD-SL LYS-113;
ILE-713; ARG-726 AND CYS-752, MUTAGENESIS OF TRP-52, GLYCOSYLATION,
AND SUBCELLULAR LOCATION.
PubMed=20223752; DOI=10.1093/hmg/ddq103;
Ali B.R., Xu H., Akawi N.A., John A., Karuvantevida N.S., Langer R.,
Al-Gazali L., Leitinger B.;
"Trafficking defects and loss of ligand binding are the underlying
causes of all reported DDR2 missense mutations found in SMED-SL
patients.";
Hum. Mol. Genet. 19:2239-2250(2010).
[23]
VARIANT SEMD-SL TRP-124.
PubMed=26463668; DOI=10.1002/ajmg.a.37426;
Mansouri M., Kayserili H., Elalaoui S.C., Nishimura G., Iida A.,
Lyahyai J., Miyake N., Matsumoto N., Sefiani A., Ikegawa S.;
"Novel DDR2 mutation identified by whole exome sequencing in a
Moroccan patient with spondylo-meta-epiphyseal dysplasia, short limb-
abnormal calcification type.";
Am. J. Med. Genet. A 170:460-465(2016).
-!- FUNCTION: Tyrosine kinase that 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.
{ECO:0000269|PubMed:16186104, ECO:0000269|PubMed:16186108,
ECO:0000269|PubMed:17665456, ECO:0000269|PubMed:18201965,
ECO:0000269|PubMed:20004161, ECO:0000269|PubMed:20564243,
ECO:0000269|PubMed:20734453, ECO:0000269|PubMed:9659899}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:16186108,
ECO:0000269|PubMed:20004161}.
-!- ACTIVITY REGULATION: 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. {ECO:0000269|PubMed:16186108}.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:16186108,
ECO:0000269|PubMed:17703188, ECO:0000269|PubMed:18201965,
ECO:0000269|PubMed:20004161}.
-!- INTERACTION:
P13942:COL11A2; NbExp=2; IntAct=EBI-1381484, EBI-2515504;
P08238:HSP90AB1; NbExp=2; IntAct=EBI-1381484, EBI-352572;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18201965,
ECO:0000269|PubMed:20223752, ECO:0000269|PubMed:9659899}; Single-
pass type I membrane protein {ECO:0000269|PubMed:18201965,
ECO:0000269|PubMed:20223752, ECO:0000269|PubMed:9659899}.
-!- TISSUE SPECIFICITY: 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. {ECO:0000269|PubMed:17665456,
ECO:0000269|PubMed:20564243, ECO:0000269|PubMed:8247548}.
-!- INDUCTION: Up-regulated during osteoblast differentiation (in
vitro). Up-regulated in cartilage from osteoarthritis patients.
{ECO:0000269|PubMed:17665456, ECO:0000269|PubMed:20564243}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:20223752}.
-!- PTM: Tyrosine phosphorylated in response to collagen binding.
Phosphorylated by SRC; this is required for activation and
subsequent autophosphorylation on additional tyrosine residues.
{ECO:0000269|PubMed:16186104, ECO:0000269|PubMed:16186108,
ECO:0000269|PubMed:18201965, ECO:0000269|PubMed:20004161,
ECO:0000269|PubMed:9659899}.
-!- DISEASE: Spondyloepimetaphyseal dysplasia short limb-hand type
(SEMD-SL) [MIM:271665]: A 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.
{ECO:0000269|PubMed:19110212, ECO:0000269|PubMed:20223752,
ECO:0000269|PubMed:26463668}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; X74764; CAA52777.1; -; mRNA.
EMBL; AK314388; BAG37013.1; -; mRNA.
EMBL; AK095975; BAG53183.1; -; mRNA.
EMBL; AL445197; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471067; EAW90713.1; -; Genomic_DNA.
EMBL; BC052998; AAH52998.1; -; mRNA.
CCDS; CCDS1241.1; -.
PIR; S42621; S42621.
RefSeq; NP_001014796.1; NM_001014796.1.
RefSeq; NP_006173.2; NM_006182.2.
RefSeq; XP_006711407.1; XM_006711344.3.
RefSeq; XP_011507888.1; XM_011509586.2.
RefSeq; XP_011507889.1; XM_011509587.2.
UniGene; Hs.275757; -.
UniGene; Hs.593833; -.
PDB; 2WUH; X-ray; 1.60 A; A=26-190.
PDB; 2Z4F; NMR; -; A=26-186.
PDBsum; 2WUH; -.
PDBsum; 2Z4F; -.
ProteinModelPortal; Q16832; -.
SMR; Q16832; -.
BioGrid; 110975; 10.
DIP; DIP-39699N; -.
IntAct; Q16832; 8.
MINT; Q16832; -.
STRING; 9606.ENSP00000356898; -.
BindingDB; Q16832; -.
ChEMBL; CHEMBL5122; -.
DrugBank; DB08896; Regorafenib.
GuidetoPHARMACOLOGY; 1844; -.
iPTMnet; Q16832; -.
PhosphoSitePlus; Q16832; -.
SwissPalm; Q16832; -.
BioMuta; DDR2; -.
DMDM; 215273969; -.
EPD; Q16832; -.
MaxQB; Q16832; -.
PaxDb; Q16832; -.
PeptideAtlas; Q16832; -.
PRIDE; Q16832; -.
ProteomicsDB; 61095; -.
DNASU; 4921; -.
Ensembl; ENST00000367921; ENSP00000356898; ENSG00000162733.
Ensembl; ENST00000367922; ENSP00000356899; ENSG00000162733.
GeneID; 4921; -.
KEGG; hsa:4921; -.
UCSC; uc001gcg.4; human.
CTD; 4921; -.
DisGeNET; 4921; -.
EuPathDB; HostDB:ENSG00000162733.16; -.
GeneCards; DDR2; -.
HGNC; HGNC:2731; DDR2.
HPA; HPA070112; -.
MalaCards; DDR2; -.
MIM; 191311; gene.
MIM; 271665; phenotype.
neXtProt; NX_Q16832; -.
OpenTargets; ENSG00000162733; -.
Orphanet; 93358; Spondyloepimetaphyseal dysplasia - short limb - abnormal calcification.
PharmGKB; PA27196; -.
eggNOG; KOG1094; Eukaryota.
eggNOG; ENOG410XQAI; LUCA.
GeneTree; ENSGT00760000118818; -.
HOGENOM; HOG000043102; -.
HOVERGEN; HBG005461; -.
InParanoid; Q16832; -.
KO; K05125; -.
OMA; MSGGHIP; -.
OrthoDB; EOG091G05Y8; -.
PhylomeDB; Q16832; -.
TreeFam; TF317840; -.
BRENDA; 2.7.10.1; 2681.
Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
SignaLink; Q16832; -.
SIGNOR; Q16832; -.
ChiTaRS; DDR2; human.
EvolutionaryTrace; Q16832; -.
GeneWiki; Discoidin_domain-containing_receptor_2; -.
GenomeRNAi; 4921; -.
PRO; PR:Q16832; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000162733; Expressed in 225 organ(s), highest expression level in adipose tissue.
CleanEx; HS_DDR2; -.
CleanEx; HS_TKT; -.
ExpressionAtlas; Q16832; baseline and differential.
Genevisible; Q16832; HS.
GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005518; F:collagen binding; IDA:UniProtKB.
GO; GO:0038062; F:protein tyrosine kinase collagen receptor activity; IDA:UniProtKB.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0031214; P:biomineral tissue development; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0035988; P:chondrocyte proliferation; ISS:UniProtKB.
GO; GO:0030199; P:collagen fibril organization; ISS:UniProtKB.
GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IDA:UniProtKB.
GO; GO:0003416; P:endochondral bone growth; ISS:UniProtKB.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IMP:UniProtKB.
GO; GO:0090091; P:positive regulation of extracellular matrix disassembly; ISS:UniProtKB.
GO; GO:0010763; P:positive regulation of fibroblast migration; ISS:UniProtKB.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISS:UniProtKB.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:UniProtKB.
GO; GO:0045860; P:positive regulation of protein kinase activity; IMP:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0030500; P:regulation of bone mineralization; IMP:UniProtKB.
GO; GO:0010715; P:regulation of extracellular matrix disassembly; TAS:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd00057; FA58C; 1.
Gene3D; 2.60.120.260; -; 1.
InterPro; IPR034299; DDR2.
InterPro; IPR000421; FA58C.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
PANTHER; PTHR24416:SF295; PTHR24416:SF295; 1.
Pfam; PF00754; F5_F8_type_C; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00231; FA58C; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS01285; FA58C_1; 1.
PROSITE; PS01286; FA58C_2; 1.
PROSITE; PS50022; FA58C_3; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Cell membrane; Complete proteome;
Disease mutation; Disulfide bond; Dwarfism; Glycoprotein; Kinase;
Membrane; Nucleotide-binding; Osteogenesis; Phosphoprotein;
Polymorphism; Receptor; Reference proteome; Signal; Transferase;
Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 855 Discoidin domain-containing receptor 2.
/FTId=PRO_0000016746.
TOPO_DOM 22 399 Extracellular. {ECO:0000255}.
TRANSMEM 400 421 Helical. {ECO:0000255}.
TOPO_DOM 422 855 Cytoplasmic. {ECO:0000255}.
DOMAIN 30 185 F5/8 type C. {ECO:0000255|PROSITE-
ProRule:PRU00081}.
DOMAIN 563 849 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 569 577 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 710 710 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 608 608 ATP. {ECO:0000305}.
MOD_RES 471 471 Phosphotyrosine; by SRC and
autocatalysis.
{ECO:0000250|UniProtKB:Q62371}.
MOD_RES 736 736 Phosphotyrosine; by SRC and
autocatalysis.
{ECO:0000269|PubMed:16186108}.
MOD_RES 740 740 Phosphotyrosine; by SRC and
autocatalysis.
{ECO:0000269|PubMed:16186108}.
MOD_RES 741 741 Phosphotyrosine; by SRC and
autocatalysis.
{ECO:0000269|PubMed:16186108}.
CARBOHYD 121 121 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 213 213 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 261 261 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 280 280 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 372 372 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 30 185
DISULFID 73 177
VARIANT 105 105 R -> S (in a lung large cell carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:16140923,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_041498.
VARIANT 113 113 E -> K (in SEMD-SL; abolishes collagen
binding; dbSNP:rs397514747).
{ECO:0000269|PubMed:20223752}.
/FTId=VAR_065719.
VARIANT 124 124 R -> W (in SEMD-SL).
{ECO:0000269|PubMed:26463668}.
/FTId=VAR_075417.
VARIANT 441 441 M -> I (in dbSNP:rs34722354).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041499.
VARIANT 478 478 R -> C (in dbSNP:rs34869543).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041500.
VARIANT 543 543 V -> F (in dbSNP:rs55973200).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041501.
VARIANT 713 713 T -> I (in SEMD-SL; causes retention in
an intracellular compartment and thereby
abolishes signaling in response collagen
binding; dbSNP:rs121964865).
{ECO:0000269|PubMed:19110212,
ECO:0000269|PubMed:20223752}.
/FTId=VAR_063050.
VARIANT 726 726 I -> R (in SEMD-SL; causes retention in
an intracellular compartment and thereby
abolishes signaling in response collagen
binding; dbSNP:rs121964864).
{ECO:0000269|PubMed:19110212,
ECO:0000269|PubMed:20223752}.
/FTId=VAR_063051.
VARIANT 752 752 R -> C (in SEMD-SL; causes retention in
an intracellular compartment and thereby
abolishes signaling in response collagen
binding; dbSNP:rs121964863).
{ECO:0000269|PubMed:19110212,
ECO:0000269|PubMed:20223752}.
/FTId=VAR_063052.
MUTAGEN 52 52 W->A: Abolishes collagen binding.
{ECO:0000269|PubMed:20004161,
ECO:0000269|PubMed:20223752}.
MUTAGEN 608 608 K->A: Abolishes kinase activity.
{ECO:0000269|PubMed:16186108}.
MUTAGEN 736 736 Y->F: Reduces autophosphorylation.
Abolishes phosphorylation by SRC; when
associated with F-740 and F-741.
{ECO:0000269|PubMed:16186108}.
MUTAGEN 740 740 Y->F: Promotes autophosphorylation.
Abolishes phosphorylation by SRC; when
associated with F-736 and F-741.
{ECO:0000269|PubMed:16186108}.
MUTAGEN 741 741 Y->F: Reduces autophosphorylation.
Abolishes phosphorylation by SRC; when
associated with F-736 and F-740.
{ECO:0000269|PubMed:16186108}.
CONFLICT 642 642 A -> S (in Ref. 1; CAA52777).
{ECO:0000305}.
TURN 27 29 {ECO:0000244|PDB:2WUH}.
STRAND 33 35 {ECO:0000244|PDB:2Z4F}.
TURN 36 38 {ECO:0000244|PDB:2WUH}.
STRAND 39 41 {ECO:0000244|PDB:2WUH}.
HELIX 43 45 {ECO:0000244|PDB:2WUH}.
STRAND 46 49 {ECO:0000244|PDB:2WUH}.
HELIX 54 56 {ECO:0000244|PDB:2WUH}.
HELIX 58 60 {ECO:0000244|PDB:2WUH}.
STRAND 70 72 {ECO:0000244|PDB:2WUH}.
STRAND 87 103 {ECO:0000244|PDB:2WUH}.
HELIX 107 109 {ECO:0000244|PDB:2WUH}.
STRAND 116 128 {ECO:0000244|PDB:2WUH}.
STRAND 139 142 {ECO:0000244|PDB:2Z4F}.
STRAND 145 149 {ECO:0000244|PDB:2WUH}.
STRAND 151 169 {ECO:0000244|PDB:2WUH}.
STRAND 171 174 {ECO:0000244|PDB:2Z4F}.
STRAND 178 186 {ECO:0000244|PDB:2WUH}.
SEQUENCE 855 AA; 96736 MW; 78662021BC53E1A0 CRC64;
MILIPRMLLV LFLLLPILSS AKAQVNPAIC RYPLGMSGGQ IPDEDITASS QWSESTAAKY
GRLDSEEGDG AWCPEIPVEP DDLKEFLQID LHTLHFITLV GTQGRHAGGH GIEFAPMYKI
NYSRDGTRWI SWRNRHGKQV LDGNSNPYDI FLKDLEPPIV ARFVRFIPVT DHSMNVCMRV
ELYGCVWLDG LVSYNAPAGQ QFVLPGGSII YLNDSVYDGA VGYSMTEGLG QLTDGVSGLD
DFTQTHEYHV WPGYDYVGWR NESATNGYIE IMFEFDRIRN FTTMKVHCNN MFAKGVKIFK
EVQCYFRSEA SEWEPNAISF PLVLDDVNPS ARFVTVPLHH RMASAIKCQY HFADTWMMFS
EITFQSDAAM YNNSEALPTS PMAPTTYDPM LKVDDSNTRI LIGCLVAIIF ILLAIIVIIL
WRQFWQKMLE KASRRMLDDE MTVSLSLPSD SSMFNNNRSS SPSEQGSNST YDRIFPLRPD
YQEPSRLIRK LPEFAPGEEE SGCSGVVKPV QPSGPEGVPH YAEADIVNLQ GVTGGNTYSV
PAVTMDLLSG KDVAVEEFPR KLLTFKEKLG EGQFGEVHLC EVEGMEKFKD KDFALDVSAN
QPVLVAVKML RADANKNARN DFLKEIKIMS RLKDPNIIHL LAVCITDDPL CMITEYMENG
DLNQFLSRHE PPNSSSSDVR TVSYTNLKFM ATQIASGMKY LSSLNFVHRD LATRNCLVGK
NYTIKIADFG MSRNLYSGDY YRIQGRAVLP IRWMSWESIL LGKFTTASDV WAFGVTLWET
FTFCQEQPYS QLSDEQVIEN TGEFFRDQGR QTYLPQPAIC PDSVYKLMLS CWRRDTKNRP
SFQEIHLLLL QQGDE


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