DDR1_HUMAN - dbPTM
DDR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDR1_HUMAN
UniProt AC Q08345
Protein Name Epithelial discoidin domain-containing receptor 1
Gene Name DDR1
Organism Homo sapiens (Human).
Sequence Length 913
Subcellular Localization Isoform 1: Cell membrane
Single-pass type I membrane protein.
Isoform 2: Cell membrane
Single-pass type I membrane protein.
Isoform 3: Secreted .
Isoform 4: Cell membrane
Single-pass type I membrane protein.
Protein Description 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..
Protein Sequence MGPEALSSLLLLLLVASGDADMKGHFDPAKCRYALGMQDRTIPDSDISASSSWSDSTAARHSRLESSDGDGAWCPAGSVFPKEEEYLQVDLQRLHLVALVGTQGRHAGGLGKEFSRSYRLRYSRDGRRWMGWKDRWGQEVISGNEDPEGVVLKDLGPPMVARLVRFYPRADRVMSVCLRVELYGCLWRDGLLSYTAPVGQTMYLSEAVYLNDSTYDGHTVGGLQYGGLGQLADGVVGLDDFRKSQELRVWPGYDYVGWSNHSFSSGYVEMEFEFDRLRAFQAMQVHCNNMHTLGARLPGGVECRFRRGPAMAWEGEPMRHNLGGNLGDPRARAVSVPLGGRVARFLQCRFLFAGPWLLFSEISFISDVVNNSSPALGGTFPPAPWWPPGPPPTNFSSLELEPRGQQPVAKAEGSPTAILIGCLVAIILLLLLIIALMLWRLHWRRLLSKAERRVLEEELTVHLSVPGDTILINNRPGPREPPPYQEPRPRGNPPHSAPCVPNGSALLLSNPAYRLLLATYARPPRGPGPPTPAWAKPTNTQAYSGDYMEPEKPGAPLLPPPPQNSVPHYAEADIVTLQGVTGGNTYAVPALPPGAVGDGPPRVDFPRSRLRFKEKLGEGQFGEVHLCEVDSPQDLVSLDFPLNVRKGHPLLVAVKILRPDATKNARNDFLKEVKIMSRLKDPNIIRLLGVCVQDDPLCMITDYMENGDLNQFLSAHQLEDKAAEGAPGDGQAAQGPTISYPMLLHVAAQIASGMRYLATLNFVHRDLATRNCLVGENFTIKIADFGMSRNLYAGDYYRVQGRAVLPIRWMAWECILMGKFTTASDVWAFGVTLWEVLMLCRAQPFGQLTDEQVIENAGEFFRDQGRQVYLSRPPACPQGLYELMLRCWSRESEQRPPFSQLHRFLAEDALNTV
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
16 (in isoform 6)Phosphorylation-14.0424719451
25 (in isoform 6)Phosphorylation-20.5824719451
35 (in isoform 6)Phosphorylation-4.3224719451
45PhosphorylationQDRTIPDSDISASSS
CCCCCCCCCCCCCCC		31.33-
48PhosphorylationTIPDSDISASSSWSD
CCCCCCCCCCCCCCC		27.3930576142
52PhosphorylationSDISASSSWSDSTAA
CCCCCCCCCCCCHHH		28.2730576142
57PhosphorylationSSSWSDSTAARHSRL
CCCCCCCHHHHHHCC		29.3530576142
62PhosphorylationDSTAARHSRLESSDG
CCHHHHHHCCCCCCC		32.7630576142
66PhosphorylationARHSRLESSDGDGAW
HHHHCCCCCCCCCCC		38.0230576142
112UbiquitinationRHAGGLGKEFSRSYR
CCCCCCCCCCCHHEE		61.7121906983
112 (in isoform 4)Ubiquitination-61.7121906983
112 (in isoform 1)Ubiquitination-61.7121906983
130 (in isoform 2)Ubiquitination-4.3221906983
153 (in isoform 4)Ubiquitination-39.0221906983
153 (in isoform 1)Ubiquitination-39.0221906983
153 (in isoform 2)Ubiquitination-39.02-
153UbiquitinationDPEGVVLKDLGPPMV
CCCCCEECCCCHHHH		39.022190698
171 (in isoform 2)Ubiquitination-45.0121906983
211N-linked_GlycosylationLSEAVYLNDSTYDGH
EEEEEEECCCCCCCC		24.4124509848
260N-linked_GlycosylationYDYVGWSNHSFSSGY
CCCEEECCCCCCCCE		28.4524509848
370N-linked_GlycosylationSFISDVVNNSSPALG
HHHHHHHCCCCCCCC		42.38UniProtKB CARBOHYD
371N-linked_GlycosylationFISDVVNNSSPALGG
HHHHHHCCCCCCCCC		32.05UniProtKB CARBOHYD
394N-linked_GlycosylationPPGPPPTNFSSLELE
CCCCCCCCCCCCEEC		40.34UniProtKB CARBOHYD
449UbiquitinationHWRRLLSKAERRVLE
HHHHHHHHHHHHHHH		54.99-
469PhosphorylationHLSVPGDTILINNRP
EEECCCCEEEECCCC		24.49-
484PhosphorylationGPREPPPYQEPRPRG
CCCCCCCCCCCCCCC		31.1424927040
496PhosphorylationPRGNPPHSAPCVPNG
CCCCCCCCCCCCCCC		39.4121945579
509PhosphorylationNGSALLLSNPAYRLL
CCCEEEECCHHHHHH		40.5121945579
513PhosphorylationLLLSNPAYRLLLATY
EEECCHHHHHHHHHH		11.7521945579
519PhosphorylationAYRLLLATYARPPRG
HHHHHHHHHCCCCCC		20.0628152594
520PhosphorylationYRLLLATYARPPRGP
HHHHHHHHCCCCCCC		8.5918180459
613MethylationPRSRLRFKEKLGEGQ
CHHHHHHHHHHCCCC		47.72-
615MethylationSRLRFKEKLGEGQFG
HHHHHHHHHCCCCCC		63.48-
626 (in isoform 2)Ubiquitination-3.00-
631PhosphorylationVHLCEVDSPQDLVSL
EEEEECCCCCCEEEC		29.6322817900
634 (in isoform 2)Ubiquitination-53.04-
637PhosphorylationDSPQDLVSLDFPLNV
CCCCCEEECCCCCCC		29.5328102081
646UbiquitinationDFPLNVRKGHPLLVA
CCCCCCCCCCCEEEE		58.24-
662PhosphorylationKILRPDATKNARNDF
EECCCCCCHHHHHHH		32.0128348404
663UbiquitinationILRPDATKNARNDFL
ECCCCCCHHHHHHHH		50.78-
664PhosphorylationLRPDATKNARNDFLK
CCCCCCHHHHHHHHH		39.51-
671UbiquitinationNARNDFLKEVKIMSR
HHHHHHHHHHHHHHH		61.53-
680UbiquitinationVKIMSRLKDPNIIRL
HHHHHHCCCCCHHHH		70.77-
701PhosphorylationDDPLCMITDYMENGD
CCCEEEEECCCCCCC		8.32-
703PhosphorylationPLCMITDYMENGDLN
CEEEEECCCCCCCHH		9.5522817900
740PhosphorylationAQGPTISYPMLLHVA
CCCCCCCHHHHHHHH		6.7122817900
788PhosphorylationKIADFGMSRNLYAGD
EEEEECCCCCEECCC		20.5612023960
792PhosphorylationFGMSRNLYAGDYYRV
ECCCCCEECCCCEEE		16.4621945579
796PhosphorylationRNLYAGDYYRVQGRA
CCEECCCCEEECCEE		7.7021945579
797PhosphorylationNLYAGDYYRVQGRAV
CEECCCCEEECCEEE		14.7321945579
798PhosphorylationLYAGDYYRVQGRAVL
EECCCCEEECCEEEE		14.1924719451
802PhosphorylationDYYRVQGRAVLPIRW
CCEEECCEEEEEHHH		12.3924719451
803PhosphorylationYYRVQGRAVLPIRWM
CEEECCEEEEEHHHH		17.6427642862
869PhosphorylationRDQGRQVYLSRPPAC
HHCCCEEEECCCCCC		7.2222817900
881PhosphorylationPACPQGLYELMLRCW
CCCCHHHHHHHHHHH		17.5322817900
912PhosphorylationLAEDALNTV------
HHHHHHHCC------		28.5724719451
918PhosphorylationNTV------------
HCC------------		24719451
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
788SPhosphorylationKinaseNEK6Q9HC98
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
211NGlycosylation

24509848
211NPhosphorylation

24509848
260NGlycosylation

24509848
260NPhosphorylation

24509848
394NGlycosylation

24509848
394NPhosphorylation

24509848
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 DDR1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SNR40_HUMANSNRNP40physical
16169070
SNAPN_HUMANSNAPINphysical
16169070
TTHY_HUMANTTRphysical
16169070
CADH1_HUMANCDH1physical
20432435
CADH2_HUMANCDH2physical
20432435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DDR1_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-631, AND MASSSPECTROMETRY.
"The discoidin domain receptor tyrosine kinases are activated bycollagen.";
Vogel W., Gish G.D., Alves F., Pawson T.;
Mol. Cell 1:13-23(1997).
Cited for: FUNCTION AS COLLAGEN RECEPTOR, PHOSPHORYLATION AT TYR-513, INTERACTIONWITH SHC1, AUTOPHOSPHORYLATION, AND SUBCELLULAR LOCATION.

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