DDR2_HUMAN - dbPTM
DDR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDR2_HUMAN
UniProt AC Q16832
Protein Name Discoidin domain-containing receptor 2
Gene Name DDR2
Organism Homo sapiens (Human).
Sequence Length 855
Subcellular Localization Cell membrane
Single-pass type I membrane protein .
Protein Description 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..
Protein Sequence MILIPRMLLVLFLLLPILSSAKAQVNPAICRYPLGMSGGQIPDEDITASSQWSESTAAKYGRLDSEEGDGAWCPEIPVEPDDLKEFLQIDLHTLHFITLVGTQGRHAGGHGIEFAPMYKINYSRDGTRWISWRNRHGKQVLDGNSNPYDIFLKDLEPPIVARFVRFIPVTDHSMNVCMRVELYGCVWLDGLVSYNAPAGQQFVLPGGSIIYLNDSVYDGAVGYSMTEGLGQLTDGVSGLDDFTQTHEYHVWPGYDYVGWRNESATNGYIEIMFEFDRIRNFTTMKVHCNNMFAKGVKIFKEVQCYFRSEASEWEPNAISFPLVLDDVNPSARFVTVPLHHRMASAIKCQYHFADTWMMFSEITFQSDAAMYNNSEALPTSPMAPTTYDPMLKVDDSNTRILIGCLVAIIFILLAIIVIILWRQFWQKMLEKASRRMLDDEMTVSLSLPSDSSMFNNNRSSSPSEQGSNSTYDRIFPLRPDYQEPSRLIRKLPEFAPGEEESGCSGVVKPVQPSGPEGVPHYAEADIVNLQGVTGGNTYSVPAVTMDLLSGKDVAVEEFPRKLLTFKEKLGEGQFGEVHLCEVEGMEKFKDKDFALDVSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQEQPYSQLSDEQVIENTGEFFRDQGRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLLLQQGDE
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
37PhosphorylationCRYPLGMSGGQIPDE
HCCCCCCCCCCCCCC		37.66-
119UbiquitinationIEFAPMYKINYSRDG
CEECCEEEEEECCCC		20.44-
121N-linked_GlycosylationFAPMYKINYSRDGTR
ECCEEEEEECCCCCC		25.28UniProtKB CARBOHYD
131PhosphorylationRDGTRWISWRNRHGK
CCCCCEEEEECCCCC		17.0224719451
213N-linked_GlycosylationGGSIIYLNDSVYDGA
CCEEEEECCCCCCCC		23.65UniProtKB CARBOHYD
261N-linked_GlycosylationYDYVGWRNESATNGY
CCEEEECCCCCCCCE		40.86UniProtKB CARBOHYD
280N-linked_GlycosylationFEFDRIRNFTTMKVH
EEECCCCCCCCCEEE		35.92UniProtKB CARBOHYD
372N-linked_GlycosylationQSDAAMYNNSEALPT
CCCHHHCCCCCCCCC		32.25UniProtKB CARBOHYD
459PhosphorylationSMFNNNRSSSPSEQG
HHCCCCCCCCCCCCC		36.9722199227
460PhosphorylationMFNNNRSSSPSEQGS
HCCCCCCCCCCCCCC		42.9322199227
461PhosphorylationFNNNRSSSPSEQGSN
CCCCCCCCCCCCCCC		33.4226055452
463PhosphorylationNNRSSSPSEQGSNST
CCCCCCCCCCCCCCC		44.4922199227
467PhosphorylationSSPSEQGSNSTYDRI
CCCCCCCCCCCCCEE		27.5726356563
469PhosphorylationPSEQGSNSTYDRIFP
CCCCCCCCCCCEEEC		30.0025884760
470PhosphorylationSEQGSNSTYDRIFPL
CCCCCCCCCCEEECC		33.4225884760
471PhosphorylationEQGSNSTYDRIFPLR
CCCCCCCCCEEECCC		11.7521082442
473MethylationGSNSTYDRIFPLRPD
CCCCCCCEEECCCCC		23.25-
481PhosphorylationIFPLRPDYQEPSRLI
EECCCCCCCCHHHHH		19.9126657352
485PhosphorylationRPDYQEPSRLIRKLP
CCCCCCHHHHHHHCC		38.6825884760
501PhosphorylationFAPGEEESGCSGVVK
CCCCCCCCCCCCCCC		48.6720068231
504PhosphorylationGEEESGCSGVVKPVQ
CCCCCCCCCCCCCCC		37.8420068231
521PhosphorylationGPEGVPHYAEADIVN
CCCCCCCCEEEEEEE		10.4825884760
598PhosphorylationKDFALDVSANQPVLV
CCEEEECCCCCCCEE		22.5922210691
674PhosphorylationSRHEPPNSSSSDVRT
HCCCCCCCCCCCCEE		37.0523312004
675PhosphorylationRHEPPNSSSSDVRTV
CCCCCCCCCCCCEEE		40.2722817900
676PhosphorylationHEPPNSSSSDVRTVS
CCCCCCCCCCCEEEE		30.3123312004
677PhosphorylationEPPNSSSSDVRTVSY
CCCCCCCCCCEEEEC		41.9123312004
681PhosphorylationSSSSDVRTVSYTNLK
CCCCCCEEEECCCHH		17.4120068231
684PhosphorylationSDVRTVSYTNLKFMA
CCCEEEECCCHHHHH		8.7023822953
720AcetylationTRNCLVGKNYTIKIA
CCCCCCCCCEEEEEE		39.027826059
732PhosphorylationKIADFGMSRNLYSGD
EEEEECCCCCCCCCC		20.5625003641
736PhosphorylationFGMSRNLYSGDYYRI
ECCCCCCCCCCCEEE		17.7321082442
737PhosphorylationGMSRNLYSGDYYRIQ
CCCCCCCCCCCEEEC		28.4926356563
740PhosphorylationRNLYSGDYYRIQGRA
CCCCCCCCEEECCEE		9.7321082442
741PhosphorylationNLYSGDYYRIQGRAV
CCCCCCCEEECCEEE		13.1425884760
813PhosphorylationRDQGRQTYLPQPAIC
HHCCCCEECCCCCCC		14.1923822953
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
471YPhosphorylationKinaseSRCP12931
Uniprot
736YPhosphorylationKinaseDDR2Q16832
GPS
736YPhosphorylationKinaseSRCP12931
Uniprot
740YPhosphorylationKinaseDDR2Q16832
GPS
740YPhosphorylationKinaseSRCP12931
Uniprot
741YPhosphorylationKinaseDDR2Q16832
GPS
741YPhosphorylationKinaseSRCP12931
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DDR2_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of DDR2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SHC1_HUMANSHC1physical
11884411
SRC_HUMANSRCphysical
11884411
HS90A_HUMANHSP90AA1physical
22939624
CBLB_HUMANCBLBphysical
24631539
CADH1_HUMANCDH1physical
20432435
CADH2_HUMANCDH2physical
20432435
CBLB_HUMANCBLBphysical
26826182
Drug and Disease Associations
Kegg Disease
H00777 Spondylometaepiphyseal dysplasia, short limb-hand type; Spondylometaepiphyseal dysplasia, short limb
OMIM Disease
271665Spondyloepimetaphyseal dysplasia short limb-hand type (SEMD-SL)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DDR2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461 AND SER-674, ANDMASS SPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-736 AND TYR-740, ANDMASS SPECTROMETRY.

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