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Q08345 (DDR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Epithelial discoidin domain-containing receptor 1

Short name=Epithelial discoidin domain receptor 1
EC=2.7.10.1
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
Gene names
Name:DDR1
Synonyms:CAK, EDDR1, NEP, NTRK4, PTK3A, RTK6, TRKE
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length913 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.18 Ref.19 Ref.20 Ref.21 Ref.23 Ref.25 Ref.26 Ref.27 Ref.28

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Subunit structure

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. Ref.18 Ref.20 Ref.22 Ref.23 Ref.25 Ref.26 Ref.29

Subcellular location

Isoform 1: Cell membrane; Single-pass type I membrane protein Ref.18 Ref.23.

Isoform 2: Cell membrane; Single-pass type I membrane protein Ref.18 Ref.23.

Isoform 3: Secreted Potential Ref.18 Ref.23.

Isoform 4: Cell membrane; Single-pass type I membrane protein Ref.18 Ref.23.

Tissue specificity

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. Ref.3 Ref.15 Ref.17

Domain

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

Post-translational modification

Autophosphorylated in response to fibrillar collagen binding. Ref.18 Ref.20 Ref.23 Ref.28

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.

Sequence caution

The sequence ACF47649.1 differs from that shown. Reason: Erroneous termination at position 287. Translated as Cys.

The sequence BAE06103.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processLactation
Pregnancy
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
Transmembrane
Transmembrane helix
   LigandATP-binding
Calcium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbranching involved in mammary gland duct morphogenesis

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Traceable author statement Ref.4. Source: ProtInc

collagen-activated tyrosine kinase receptor signaling pathway

Inferred from direct assay Ref.28Ref.18. Source: UniProtKB

ear development

Inferred from electronic annotation. Source: Ensembl

embryo implantation

Inferred from electronic annotation. Source: Ensembl

extracellular matrix organization

Traceable author statement. Source: Reactome

lactation

Inferred from electronic annotation. Source: UniProtKB-KW

mammary gland alveolus development

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

peptidyl-tyrosine autophosphorylation

Inferred from direct assay Ref.28. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay Ref.18. Source: UniProtKB

regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

regulation of cell-matrix adhesion

Inferred from electronic annotation. Source: Ensembl

regulation of extracellular matrix disassembly

Inferred from mutant phenotype Ref.19. Source: UniProtKB

smooth muscle cell migration

Inferred from mutant phenotype Ref.19. Source: UniProtKB

smooth muscle cell-matrix adhesion

Inferred from mutant phenotype Ref.19. Source: UniProtKB

wound healing, spreading of cells

Inferred from mutant phenotype Ref.19. Source: UniProtKB

   Cellular_componentextracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

integral component of plasma membrane

Traceable author statement Ref.2. Source: ProtInc

plasma membrane

Traceable author statement. Source: Reactome

receptor complex

Inferred from direct assay PubMed 23382219. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

collagen binding

Inferred from direct assay Ref.18. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein tyrosine kinase collagen receptor activity

Inferred from direct assay Ref.28Ref.18. Source: UniProtKB

transmembrane receptor protein tyrosine kinase activity

Traceable author statement Ref.18. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NCK2O436393EBI-711879,EBI-713635
PTPN11Q061244EBI-711879,EBI-297779

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q08345-1)

Also known as: CAK I; DDR1b;

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; DDR1a; Short;

The sequence of this isoform differs from the canonical sequence as follows:
     506-542: Missing.
Isoform 3 (identifier: Q08345-4)

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.
Isoform 4 (identifier: Q08345-5)

The sequence of this isoform differs from the canonical sequence as follows:
     665-665: A → ASFSLFS
Isoform 5 (identifier: Q08345-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MSLPRCCPHPLRPEGSGAM
     506-542: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 913895Epithelial discoidin domain-containing receptor 1
PRO_0000016742

Regions

Topological domain21 – 417397Extracellular Potential
Transmembrane418 – 43821Helical; Potential
Topological domain439 – 913475Cytoplasmic Potential
Domain31 – 185155F5/8 type C
Domain610 – 905296Protein kinase
Nucleotide binding616 – 6249ATP By similarity
Region192 – 367176DS-like domain
Motif481 – 4844PPxY motif
Compositional bias377 – 41539Gly/Pro-rich
Compositional bias476 – 601126Gly/Pro-rich

Sites

Active site7661Proton acceptor By similarity
Metal binding2111Calcium 1; via carbonyl oxygen
Metal binding2301Calcium 1
Metal binding2301Calcium 2; via carbonyl oxygen
Metal binding2331Calcium 2
Metal binding2351Calcium 2; via carbonyl oxygen
Metal binding2531Calcium 1; via carbonyl oxygen
Metal binding2551Calcium 1; via carbonyl oxygen
Metal binding3601Calcium 2; via carbonyl oxygen
Metal binding3611Calcium 2
Binding site6551ATP By similarity

Amino acid modifications

Modified residue5131Phosphotyrosine; by autocatalysis Ref.18
Modified residue6311Phosphoserine Ref.24
Modified residue7401Phosphotyrosine; by autocatalysis Probable
Modified residue7921Phosphotyrosine; by autocatalysis By similarity
Modified residue7961Phosphotyrosine; by autocatalysis By similarity
Modified residue7971Phosphotyrosine; by autocatalysis By similarity
Glycosylation2111N-linked (GlcNAc...) Potential
Glycosylation2601N-linked (GlcNAc...) Potential
Glycosylation3711N-linked (GlcNAc...) Potential
Glycosylation3941N-linked (GlcNAc...) Potential
Disulfide bond31 ↔ 185 Ref.29
Disulfide bond74 ↔ 177 Ref.29
Disulfide bond303 ↔ 348 Ref.29

Natural variations

Alternative sequence11M → MSLPRCCPHPLRPEGSGAM in isoform 5.
VSP_043582
Alternative sequence190 – 24354GLLSY…DDFRK → CSMGVWASWQMVWWGWMTLG RVRSCGSGQAMTMWDGATTA SPVAMWRWSLSLTG in isoform 3.
VSP_036916
Alternative sequence244 – 913670Missing in isoform 3.
VSP_036917
Alternative sequence506 – 54237Missing in isoform 2 and isoform 5.
VSP_002953
Alternative sequence6651A → ASFSLFS in isoform 4.
VSP_038057
Natural variant171S → G. Ref.30
Corresponds to variant rs55901302 [ dbSNP | Ensembl ].
VAR_041492
Natural variant1001V → A. Ref.30
Corresponds to variant rs34544756 [ dbSNP | Ensembl ].
VAR_041493
Natural variant1691R → Q. Ref.30
Corresponds to variant rs55980643 [ dbSNP | Ensembl ].
VAR_041494
Natural variant1701A → D. Ref.30
Corresponds to variant rs56231803 [ dbSNP | Ensembl ].
VAR_041495
Natural variant3061R → W. Ref.30
Corresponds to variant rs56024191 [ dbSNP | Ensembl ].
VAR_041496
Natural variant4961S → A in a lung squamous cell carcinoma sample; somatic mutation. Ref.30
VAR_041497
Natural variant8331L → V. Ref.2 Ref.5
Corresponds to variant rs2524235 [ dbSNP | Ensembl ].
VAR_049716

Experimental info

Mutagenesis7401Y → F: Abolishes interaction with PTPN11. Ref.20
Sequence conflict941L → V in AAA02866. Ref.2
Sequence conflict941L → V in AAC50917. Ref.5
Sequence conflict1651R → H in AAH70070. Ref.14
Sequence conflict285 – 2862VH → MW in ACF47649. Ref.8
Sequence conflict7411P → Q in AAH70070. Ref.14
Sequence conflict847 – 86721QLTDE…DQGRQ → SAHRRAGHRERGGVLPGPGP A in CAA66871. Ref.6

Secondary structure

.................................................................................................................... 913
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (CAK I) (DDR1b) [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: C96913EA906C481E

FASTA913101,128
        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 

« Hide

Isoform 2 (CAK II) (DDR1a) (Short) [UniParc].

Checksum: E02881598CC7CD0B
Show »

FASTA87697,174
Isoform 3 (DDR1d) [UniParc].

Checksum: 36872B8FB29835D0
Show »

FASTA24327,130
Isoform 4 [UniParc].

Checksum: 2094224F6AE943F5
Show »

FASTA919101,796
Isoform 5 [UniParc].

Checksum: D46EECFC939B7585
Show »

FASTA89499,064

References

« Hide 'large scale' references
[1]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Brain and Keratinocyte.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-833.
Tissue: Placenta.
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
Tissue: Ovary.
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Fetal liver.
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-833.
[6]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Lung.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 1-286 (ISOFORMS 1/2/4).
[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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5).
Tissue: Brain and 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. expand/collapse author list , Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T., Inoko H., Bahram S.
Genetics 173:1555-1570(2006) [PubMed] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain and Muscle.
[15]"Distinct structural characteristics of discoidin I subfamily receptor tyrosine kinases and complementary expression in human cancer."
Alves F., Vogel W., Mossie K., Millauer B., Hoefler H., Ullrich A.
Oncogene 10:609-618(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 501-550 (ISOFORMS 1/4), NUCLEOTIDE SEQUENCE [MRNA] OF 501-550 AND 651-694 (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 651-694 (ISOFORM 4), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
Tissue: Mammary carcinoma.
[16]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 771-824 (ISOFORMS 1/2/4).
[17]"A survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes."
Lee S.-T., Strunk K.M., Spritz R.A.
Oncogene 8:3403-3410(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 772-823 (ISOFORMS 1/2/4), TISSUE SPECIFICITY.
Tissue: Melanocyte.
[18]"The discoidin domain receptor tyrosine kinases are activated by collagen."
Vogel W., Gish G.D., Alves F., Pawson T.
Mol. Cell 1:13-23(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS COLLAGEN RECEPTOR, PHOSPHORYLATION AT TYR-513, INTERACTION WITH SHC1, AUTOPHOSPHORYLATION, SUBCELLULAR LOCATION.
[19]"Tyrosine kinase activity of discoidin domain receptor 1 is necessary for smooth muscle cell migration and matrix metalloproteinase expression."
Hou G., Vogel W.F., Bendeck M.P.
Circ. Res. 90:1147-1149(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[20]"Pinpointing phosphotyrosine-dependent interactions downstream of the collagen receptor DDR1."
Koo D.H., McFadden C., Huang Y., Abdulhussein R., Friese-Hamim M., Vogel W.F.
FEBS Lett. 580:15-22(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PTPN11 AND NCK2, PHOSPHORYLATION AT TYR-740, MUTAGENESIS OF TYR-740.
[21]"Discoidin domain receptor-1a (DDR1a) promotes glioma cell invasion and adhesion in association with matrix metalloproteinase-2."
Ram R., Lorente G., Nikolich K., Urfer R., Foehr E., Nagavarapu U.
J. Neurooncol. 76:239-248(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[22]"KIBRA interacts with discoidin domain receptor 1 to modulate collagen-induced signalling."
Hilton H.N., Stanford P.M., Harris J., Oakes S.R., Kaplan W., Daly R.J., Ormandy C.J.
Biochim. Biophys. Acta 1783:383-393(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WWC1 AND PRKCZ.
[23]"The collagen receptor DDR1 regulates cell spreading and motility by associating with myosin IIA."
Huang Y., Arora P., McCulloch C.A., Vogel W.F.
J. Cell Sci. 122:1637-1646(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, INTERACTION WITH MYH9.
[24]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"DDR1 regulates the stabilization of cell surface E-cadherin and E-cadherin-mediated cell aggregation."
Eswaramoorthy R., Wang C.K., Chen W.C., Tang M.J., Ho M.L., Hwang C.C., Wang H.M., Wang C.Z.
J. Cell. Physiol. 224:387-397(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CDH1.
[26]"Collagen stimulates discoidin domain receptor 1-mediated migration of smooth muscle cells through Src."
Lu K.K., Trcka D., Bendeck M.P.
Cardiovasc. Pathol. 20:71-76(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SRC.
[27]"Discoidin domain receptor 1 regulates bronchial epithelial repair and matrix metalloproteinase production."
Roberts M.E., Magowan L., Hall I.P., Johnson S.R.
Eur. Respir. J. 37:1482-1493(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[28]"Collagen binding specificity of the discoidin domain receptors: binding sites on collagens II and III and molecular determinants for collagen IV recognition by DDR1."
Xu H., Raynal N., Stathopoulos S., Myllyharju J., Farndale R.W., Leitinger B.
Matrix Biol. 30:16-26(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS COLLAGEN RECEPTOR, AUTOPHOSPHORYLATION.
[29]"Structure of the discoidin domain receptor 1 extracellular region bound to an inhibitory Fab fragment reveals features important for signaling."
Carafoli F., Mayer M.C., Shiraishi K., Pecheva M.A., Chan L.Y., Nan R., Leitinger B., Hohenester E.
Structure 20:688-697(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 29-367 IN COMPLEX WITH INHIBITORY ANTIBODY, CALCIUM-BINDING SITES, DISULFIDE BONDS, SUBUNIT.
[30]"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. expand/collapse author list , 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] [Europe PMC] [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

EMBL
GenBank
DDBJ
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 expand/collapse EMBL AC list , 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. 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.
PIRA48280.
A49508.
RefSeqNP_001189450.1. NM_001202521.1.
NP_001189451.1. NM_001202522.1.
NP_001189452.1. NM_001202523.1.
NP_001945.3. NM_001954.4.
NP_054699.2. NM_013993.2.
NP_054700.2. NM_013994.2.
XP_005249443.1. XM_005249386.2.
XP_005249444.1. XM_005249387.2.
XP_005249446.1. XM_005249389.1.
XP_005272931.1. XM_005272874.2.
XP_005272932.1. XM_005272875.2.
XP_005272934.1. XM_005272877.1.
XP_005275085.1. XM_005275028.2.
XP_005275087.1. XM_005275030.2.
XP_005275088.1. XM_005275031.2.
XP_005275220.1. XM_005275163.2.
XP_005275221.1. XM_005275164.2.
XP_005275223.1. XM_005275166.1.
XP_005275515.1. XM_005275458.2.
XP_005275516.1. XM_005275459.2.
XP_005275518.1. XM_005275461.1.
UniGeneHs.631988.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZOSX-ray1.92A/B601-913[»]
4AG4X-ray2.80A29-367[»]
4BKJX-ray1.70A/B601-913[»]
4CKRX-ray2.20A601-913[»]
ProteinModelPortalQ08345.
SMRQ08345. Positions 30-369, 602-913.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107234. 10 interactions.
DIPDIP-39698N.
IntActQ08345. 12 interactions.
MINTMINT-1383336.

Chemistry

BindingDBQ08345.
ChEMBLCHEMBL5319.
DrugBankDB00619. Imatinib.
GuidetoPHARMACOLOGY1843.

PTM databases

PhosphoSiteQ08345.

Polymorphism databases

DMDM729008.

Proteomic databases

PaxDbQ08345.
PRIDEQ08345.

Protocols and materials databases

DNASU780.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000259875; 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. [Q08345-5]
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]
ENST00000446312; ENSP00000405998; ENSG00000204580. [Q08345-4]
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. [Q08345-5]
ENST00000548962; ENSP00000448115; ENSG00000230456. [Q08345-4]
ENST00000549026; ENSP00000449238; ENSG00000215522. [Q08345-4]
ENST00000550384; ENSP00000447474; ENSG00000234078. [Q08345-4]
ENST00000550395; ENSP00000449255; ENSG00000215522. [Q08345-5]
ENST00000552068; ENSP00000449190; ENSG00000234078. [Q08345-5]
ENST00000552721; ENSP00000449307; ENSG00000137332. [Q08345-4]
ENST00000553015; ENSP00000448377; ENSG00000137332. [Q08345-5]
GeneID780.
KEGGhsa:780.
UCSCuc003nrq.3. human. [Q08345-2]
uc003nrr.3. human. [Q08345-1]
uc003nrv.3. human. [Q08345-5]
uc011dms.2. human. [Q08345-6]
uc011dmu.1. human. [Q08345-4]

Organism-specific databases

CTD780.
GeneCardsGC06P030848.
GC06Pj30838.
GC06Pk30839.
GC06Pl30893.
GC06Pn30838.
HGNCHGNC:2730. DDR1.
HPACAB010162.
CAB025656.
HPA057194.
MIM600408. gene.
neXtProtNX_Q08345.
PharmGKBPA24348.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000043102.
HOVERGENHBG005461.
InParanoidQ08345.
KOK05124.
OMAFLQCRFL.
PhylomeDBQ08345.
TreeFamTF317840.

Enzyme and pathway databases

BRENDA2.7.10.1. 2681.
ReactomeREACT_118779. Extracellular matrix organization.
SignaLinkQ08345.

Gene expression databases

ArrayExpressQ08345.
BgeeQ08345.
CleanExHS_DDR1.
GenevestigatorQ08345.

Family and domain databases

Gene3D2.60.120.260. 1 hit.
InterProIPR000421. Coagulation_fac_5/8-C_type_dom.
IPR008979. Galactose-bd-like.
IPR011009. Kinase-like_dom.
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.
[Graphical view]
PfamPF00754. F5_F8_type_C. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSPR00109. TYRKINASE.
SMARTSM00231. FA58C. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS01285. 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.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDDR1. human.
GeneWikiDDR1.
GenomeRNAi780.
NextBio3152.
PMAP-CutDBQ2L6H3.
PROQ08345.
SOURCESearch...

Entry information

Entry nameDDR1_HUMAN
AccessionPrimary (citable) accession number: Q08345
Secondary accession number(s): B5A975 expand/collapse secondary AC list , B5A976, B7Z2K0, Q14196, Q16562, Q2L6H3, Q4LE50, Q5ST11, Q5ST12, Q6NSK4, Q9UD35, Q9UD36, Q9UD37, Q9UD86, Q9UDL2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 162 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries