Reviewed, UniProtKB/Swiss-Prot Q08345 (DDR1_HUMAN)

Names and origin

Protein names

Recommended name:
    Epithelial discoidin domain-containing receptor 1
      Short name=Epithelial discoidin domain receptor 1
    EC=2.7.10.1
Alternative name(s):
    Tyrosine kinase DDR
    Discoidin receptor tyrosine kinase
    Tyrosine-protein kinase CAK
    Cell adhesion kinase
    TRK E
    Protein-tyrosine kinase RTK 6
    HGK2
    CD167 antigen-like family member A
    CD_antigen=CD167a

Gene names

Name:	DDR1
Synonyms:	CAK, EDDR1, NEP, NTRK4, PTK3A, RTK6, TRKE

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	913 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May be involved in cell-cell interactions and recognition.
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subcellular location	Isoform 1: Membrane; Single-pass type I membrane protein. Isoform 2: Membrane; Single-pass type I membrane protein. Isoform 3: Secreted Potential. Isoform 4: Secreted Potential.
Tissue specificity	Expressed at low levels in most adult tissues and is highest in the brain and lung. Abundant in breast carcinoma cell lines.
Domain	The Gly/Pro-rich domains may be required for an unusual geometry of interaction with ligand or substrates.
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily. Contains 1 F5/8 type C domain. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal Transmembrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell adhesion Ref.1 Traceable author statement. Source: ProtInc protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro transmembrane receptor protein tyrosine kinase signaling pathway Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Ref.2 Traceable author statement. Source: ProtInc
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct transmembrane receptor protein tyrosine kinase activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
IRS1	P35568	1	EBI-711903,EBI-517592

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q08345-1)

Also known as: CAK I;

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

Isoform 2 (identifier: Q08345-2)

Also known as: CAK II; Short;

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

Isoform 3 (identifier: Q08345-3)

Also known as: Soluble DDR1 variant 1;

The sequence of this isoform differs from the canonical sequence as follows:
     285-286: VH → MW
     287-913: Missing.

Isoform 4 (identifier: Q08345-4)

Also known as: Soluble DDR1 variant 2;

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	Potential
	Chain	19 – 913	895	Epithelial discoidin domain-containing receptor 1		PRO_0000016742
Regions
	Topological domain	19 – 416	398	Extracellular Potential
	Transmembrane	417 – 443	27	Potential
	Topological domain	444 – 913	470	Cytoplasmic Potential
	Domain	31 – 185	155	F5/8 type C
	Domain	610 – 905	296	Protein kinase
	Nucleotide binding	616 – 624	9	ATP By similarity
	Compositional bias	377 – 415	39	Gly/Pro-rich
	Compositional bias	476 – 601	126	Gly/Pro-rich
Sites
	Active site	766	1	Proton acceptor By similarity
	Binding site	655	1	ATP By similarity
Amino acid modifications
	Modified residue	513	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	792	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	796	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	797	1	Phosphotyrosine; by autocatalysis By similarity
	Glycosylation	211	1	N-linked (GlcNAc...) Potential
	Glycosylation	260	1	N-linked (GlcNAc...) Potential
	Glycosylation	371	1	N-linked (GlcNAc...) Potential
	Glycosylation	394	1	N-linked (GlcNAc...) Potential
	Disulfide bond	31 ↔ 185		By similarity
Natural variations
	Alternative sequence	190 – 243	54	GLLSY…DDFRK → CSMGVWASWQMVWWGWMTLG RVRSCGSGQAMTMWDGATTA SPVAMWRWSLSLTG in isoform 4.		VSP_036916
	Alternative sequence	244 – 913	670	Missing in isoform 4.		VSP_036917
	Alternative sequence	285 – 286	2	VH → MW in isoform 3.		VSP_036918
	Alternative sequence	287 – 913	627	Missing in isoform 3.		VSP_036919
	Alternative sequence	506 – 542	37	Missing in isoform 2.		VSP_002953
	Natural variant	17	1	S → G Ref.17		VAR_041492
	Natural variant	100	1	V → A Ref.17		VAR_041493
	Natural variant	169	1	R → Q Ref.17		VAR_041494
	Natural variant	170	1	A → D Ref.17		VAR_041495
	Natural variant	306	1	R → W Ref.17		VAR_041496
	Natural variant	496	1	S → A in a lung squamous cell carcinoma sample; somatic mutation. Ref.17		VAR_041497
	Natural variant	833	1	L → V: dbSNP rs2524235. Ref.2 Ref.3		VAR_049716
Experimental info
	Sequence conflict	94	1	L → V in AAA02866. Ref.2
	Sequence conflict	94	1	L → V in AAC50917. Ref.3
	Sequence conflict	165	1	R → H in AAH70070. Ref.14
	Sequence conflict	741	1	P → Q in AAH70070. Ref.14
	Sequence conflict	847 – 867	21	QLTDE…DQGRQ → SAHRRAGHRERGGVLPGPGP A in CAA66871. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (CAK I) [UniParc]. Last modified February 1, 1995. Version 1. Checksum: C96913EA906C481E	FASTA	913	101,128
	10 20 30 40 50 60 MGPEALSSLL LLLLVASGDA DMKGHFDPAK CRYALGMQDR TIPDSDISAS SSWSDSTAAR 70 80 90 100 110 120 HSRLESSDGD GAWCPAGSVF PKEEEYLQVD LQRLHLVALV GTQGRHAGGL GKEFSRSYRL 130 140 150 160 170 180 RYSRDGRRWM GWKDRWGQEV ISGNEDPEGV VLKDLGPPMV ARLVRFYPRA DRVMSVCLRV 190 200 210 220 230 240 ELYGCLWRDG LLSYTAPVGQ TMYLSEAVYL NDSTYDGHTV GGLQYGGLGQ LADGVVGLDD 250 260 270 280 290 300 FRKSQELRVW PGYDYVGWSN HSFSSGYVEM EFEFDRLRAF QAMQVHCNNM HTLGARLPGG 310 320 330 340 350 360 VECRFRRGPA MAWEGEPMRH NLGGNLGDPR ARAVSVPLGG RVARFLQCRF LFAGPWLLFS 370 380 390 400 410 420 EISFISDVVN NSSPALGGTF PPAPWWPPGP PPTNFSSLEL EPRGQQPVAK AEGSPTAILI 430 440 450 460 470 480 GCLVAIILLL LLIIALMLWR LHWRRLLSKA ERRVLEEELT VHLSVPGDTI LINNRPGPRE 490 500 510 520 530 540 PPPYQEPRPR GNPPHSAPCV PNGSALLLSN PAYRLLLATY ARPPRGPGPP TPAWAKPTNT 550 560 570 580 590 600 QAYSGDYMEP EKPGAPLLPP PPQNSVPHYA EADIVTLQGV TGGNTYAVPA LPPGAVGDGP 610 620 630 640 650 660 PRVDFPRSRL RFKEKLGEGQ FGEVHLCEVD SPQDLVSLDF PLNVRKGHPL LVAVKILRPD 670 680 690 700 710 720 ATKNARNDFL KEVKIMSRLK DPNIIRLLGV CVQDDPLCMI TDYMENGDLN QFLSAHQLED 730 740 750 760 770 780 KAAEGAPGDG QAAQGPTISY PMLLHVAAQI ASGMRYLATL NFVHRDLATR NCLVGENFTI 790 800 810 820 830 840 KIADFGMSRN LYAGDYYRVQ GRAVLPIRWM AWECILMGKF TTASDVWAFG VTLWEVLMLC 850 860 870 880 890 900 RAQPFGQLTD EQVIENAGEF FRDQGRQVYL SRPPACPQGL YELMLRCWSR ESEQRPPFSQ 910 LHRFLAEDAL NTV
	Isoform 2 (CAK II) (Short). Checksum: E02881598CC7CD0B	FASTA	876	97,174
	10 20 30 40 50 60 MGPEALSSLL LLLLVASGDA DMKGHFDPAK CRYALGMQDR TIPDSDISAS SSWSDSTAAR 70 80 90 100 110 120 HSRLESSDGD GAWCPAGSVF PKEEEYLQVD LQRLHLVALV GTQGRHAGGL GKEFSRSYRL 130 140 150 160 170 180 RYSRDGRRWM GWKDRWGQEV ISGNEDPEGV VLKDLGPPMV ARLVRFYPRA DRVMSVCLRV 190 200 210 220 230 240 ELYGCLWRDG LLSYTAPVGQ TMYLSEAVYL NDSTYDGHTV GGLQYGGLGQ LADGVVGLDD 250 260 270 280 290 300 FRKSQELRVW PGYDYVGWSN HSFSSGYVEM EFEFDRLRAF QAMQVHCNNM HTLGARLPGG 310 320 330 340 350 360 VECRFRRGPA MAWEGEPMRH NLGGNLGDPR ARAVSVPLGG RVARFLQCRF LFAGPWLLFS 370 380 390 400 410 420 EISFISDVVN NSSPALGGTF PPAPWWPPGP PPTNFSSLEL EPRGQQPVAK AEGSPTAILI 430 440 450 460 470 480 GCLVAIILLL LLIIALMLWR LHWRRLLSKA ERRVLEEELT VHLSVPGDTI LINNRPGPRE 490 500 510 520 530 540 PPPYQEPRPR GNPPHSAPCV PNGSAYSGDY MEPEKPGAPL LPPPPQNSVP HYAEADIVTL 550 560 570 580 590 600 QGVTGGNTYA VPALPPGAVG DGPPRVDFPR SRLRFKEKLG EGQFGEVHLC EVDSPQDLVS 610 620 630 640 650 660 LDFPLNVRKG HPLLVAVKIL RPDATKNARN DFLKEVKIMS RLKDPNIIRL LGVCVQDDPL 670 680 690 700 710 720 CMITDYMENG DLNQFLSAHQ LEDKAAEGAP GDGQAAQGPT ISYPMLLHVA AQIASGMRYL 730 740 750 760 770 780 ATLNFVHRDL ATRNCLVGEN FTIKIADFGM SRNLYAGDYY RVQGRAVLPI RWMAWECILM 790 800 810 820 830 840 GKFTTASDVW AFGVTLWEVL MLCRAQPFGQ LTDEQVIENA GEFFRDQGRQ VYLSRPPACP 850 860 870 QGLYELMLRC WSRESEQRPP FSQLHRFLAE DALNTV
	Isoform 3 (Soluble DDR1 variant 1). Checksum: 580147E5BC08E3AD	FASTA	286	32,021
	10 20 30 40 50 60 MGPEALSSLL LLLLVASGDA DMKGHFDPAK CRYALGMQDR TIPDSDISAS SSWSDSTAAR 70 80 90 100 110 120 HSRLESSDGD GAWCPAGSVF PKEEEYLQVD LQRLHLVALV GTQGRHAGGL GKEFSRSYRL 130 140 150 160 170 180 RYSRDGRRWM GWKDRWGQEV ISGNEDPEGV VLKDLGPPMV ARLVRFYPRA DRVMSVCLRV 190 200 210 220 230 240 ELYGCLWRDG LLSYTAPVGQ TMYLSEAVYL NDSTYDGHTV GGLQYGGLGQ LADGVVGLDD 250 260 270 280 FRKSQELRVW PGYDYVGWSN HSFSSGYVEM EFEFDRLRAF QAMQMW
	Isoform 4 (Soluble DDR1 variant 2). Checksum: 36872B8FB29835D0	FASTA	243	27,130
	10 20 30 40 50 60 MGPEALSSLL LLLLVASGDA DMKGHFDPAK CRYALGMQDR TIPDSDISAS SSWSDSTAAR 70 80 90 100 110 120 HSRLESSDGD GAWCPAGSVF PKEEEYLQVD LQRLHLVALV GTQGRHAGGL GKEFSRSYRL 130 140 150 160 170 180 RYSRDGRRWM GWKDRWGQEV ISGNEDPEGV VLKDLGPPMV ARLVRFYPRA DRVMSVCLRV 190 200 210 220 230 240 ELYGCLWRDC SMGVWASWQM VWWGWMTLGR VRSCGSGQAM TMWDGATTAS PVAMWRWSLS LTG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and chromosomal mapping of a receptor tyrosine kinase with a putative phospholipid binding sequence in its ectodomain." Perez J.L., Shen X., Finkernagel S., Sciorra L., Jenkins N.A., Gilbert D.J., Copeland N.G., Wong T.W. Oncogene 9:211-219(1994) [PubMed: 8302582] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Fetal liver.
[2]	"A receptor tyrosine kinase found in breast carcinoma cells has an extracellular discoidin I-like domain." Johnson J.D., Edman J.C., Rutter W.J. Proc. Natl. Acad. Sci. U.S.A. 90:5677-5681(1993) [PubMed: 8390675] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-833. Tissue: Placenta.
[3]	"Receptor protein tyrosine kinase DDR is up-regulated by p53 protein." Sakuma S., Tada M., Saya H., Sawamura Y., Shinohe Y., Abe H. FEBS Lett. 398:165-169(1996) [PubMed: 8977099] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-833.
[4]	"The genomic structure of discoidin receptor tyrosine kinase." Playford M.P., Butler R.J., Wang X.C., Katso R.M., Cooke I.E., Ganesan T.S. Genome Res. 6:620-627(1996) [PubMed: 8796349] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Identification of two isoforms of the Cak receptor kinase that are coexpressed in breast tumor cell lines." Perez J.L., Jing S.Q., Wong T.W. Oncogene 12:1469-1477(1996) [PubMed: 8622863] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Lung.
[6]	"Molecular cloning of trkE, a novel trk-related putative tyrosine kinase receptor isolated from normal human keratinocytes and widely expressed by normal human tissues." di Marco E., Cutuli N., Guerra L., Cancedda R., de Luca M. J. Biol. Chem. 268:24290-24295(1993) [PubMed: 8226977] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Brain and Keratinocyte.
[7]	"Isolation and characterization of an epithelial-specific receptor tyrosine kinase from an ovarian cancer cell line." Laval S., Butler R., Shelling A.N., Hanby A.M., Poulsom R., Ganesan T.S. Cell Growth Differ. 5:1173-1183(1994) [PubMed: 7848919] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Ovary.
[8]	"Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis." Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D., Phillips S., Feldmann M., Shepard H.M., Paleolog E.M. Arthritis Res. Ther. 10:R73-R73(2008) [PubMed: 18593464] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
[9]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Placenta.
[10]	"Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method." Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[11]	"Rapid evolution of major histocompatibility complex class I genes in primates generates new disease alleles in humans via hitchhiking diversity." Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M., Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K., Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A. , Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T., Inoko H., Bahram S. Genetics 173:1555-1570(2006) [PubMed: 16702430] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Tissue: Peripheral blood leukocyte.
[12]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[14]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain and Muscle.
[15]	"Expression of growth factor receptors, the focal adhesion kinase, and other tyrosine kinases in human soft tissue tumors." Weiner T.M., Liu E.T., Craven R.J., Cance W.G. Ann. Surg. Oncol. 1:18-27(1994) [PubMed: 7834423] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 771-824.
[16]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-792; TYR-796 AND TYR-797, MASS SPECTROMETRY.
[17]	"Patterns of somatic mutation in human cancer genomes." 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. Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLY-17; ALA-100; GLN-169; ASP-170; TRP-306 AND ALA-496.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L20817 mRNA. Translation: AAA18019.1. L11315 mRNA. Translation: AAA02866.1. 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. X74979 mRNA. Translation: CAA52915.1. Z29093 mRNA. Translation: CAA82335.1. EU826613 mRNA. Translation: ACF47649.1. EU826614 mRNA. Translation: ACF47650.1. AK291621 mRNA. Translation: BAF84310.1. AB210021 mRNA. Translation: BAE06103.1. Different initiation. BA000025 Genomic DNA. Translation: BAB63318.1. CR759747 Genomic DNA. Translation: CAQ06757.1. CR759747 Genomic DNA. Translation: CAQ06756.1. AB088102 Genomic DNA. Translation: BAC54935.1. AB103608 Genomic DNA. Translation: BAF31270.1. AL662854 Genomic DNA. Translation: CAI17434.1. AL662870 Genomic DNA. Translation: CAI18441.1. AL773541, AL773589 Genomic DNA. Translation: CAI18450.1. AL773589, AL773541 Genomic DNA. Translation: CAI18534.1. AL662854 Genomic DNA. Translation: CAI17433.1. AL662870 Genomic DNA. Translation: CAI18442.1. AL773541, AL773589 Genomic DNA. Translation: CAI18451.1. AL773589, AL773541 Genomic DNA. Translation: CAI18533.1. AB202100 Genomic DNA. Translation: BAE78621.1. BX927194 Genomic DNA. Translation: CAQ09768.1. BX927194 Genomic DNA. Translation: CAQ09767.1. 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.
IPI	IPI00001477. IPI00219996. IPI00910318. IPI00925878.
PIR	A48280. A49508.
RefSeq	NP_001945.3. NP_054699.2. NP_054700.2.
UniGene	Hs.631988
3D structure databases
HSSP	HSSP built from PDB template 1LUF based on UniProtKB Q62838.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q08345. 12 interactions.
PTM databases
PhosphoSite	Q08345.
Proteomic databases
PRIDE	Q08345.
Genome annotation databases
Ensembl	ENSG00000137332. Homo sapiens. [Contig view] ENSG00000204580. Homo sapiens. [Contig view] ENSG00000215522. Homo sapiens. [Contig view]
GeneID	780.
KEGG	hsa:780.
UCSC	uc003nrr.1. human.
Organism-specific databases
GeneCards	GC06P030960.
H-InvDB	HIX0025035. HIX0058006. HIX0058118.
HGNC	HGNC:2730. DDR1.
HPA	CAB010162.
MIM	600408. gene.
PharmGKB	PA24348.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q08345.
HOVERGEN	Q08345.
OMA	Q08345. LGLYELM.
Enzyme and pathway databases
BRENDA	2.7.10.1. 247.
Gene expression databases
ArrayExpress	Q08345.
CleanEx	HS_DDR1.
GermOnline	ENSG00000204580. Homo sapiens.
Family and domain databases
InterPro	IPR000421. Coagulation_factor_5/8-type_C. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR002011. Recept_tyr_kinase-II_CS. IPR001245. Tyr_pkinase. IPR008266. Tyr_pkinase_AS. [Graphical view]
Pfam	PF00754. F5_F8_type_C. 1 hit. PF07714. Pkinase_Tyr. 1 hit. [Graphical view]
PRINTS	PR00109. TYRKINASE.
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00231. FA58C. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
PROSITE	PS01285. FA58C_1. 1 hit. PS01286. FA58C_2. 1 hit. PS50022. FA58C_3. 1 hit. PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00109. PROTEIN_KINASE_TYR. 1 hit. PS00239. RECEPTOR_TYR_KIN_II. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00619. Imatinib.
NextBio	3152.
PMAP-CutDB	Q08345.
SOURCE	Search...

Entry information

Entry name

DDR1_HUMAN

Accession

Primary (citable) accession number: Q08345
Secondary accession number(s): B5A975 , B5A976, Q14196, Q16562, Q2L6H3, Q4LE50, Q5ST11, Q5ST12, Q6NSK4, Q9UD37

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	July 7, 2009
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)