DUSTY_HUMAN - dbPTM
DUSTY_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DUSTY_HUMAN
UniProt AC Q6XUX3
Protein Name Dual serine/threonine and tyrosine protein kinase
Gene Name DSTYK
Organism Homo sapiens (Human).
Sequence Length 929
Subcellular Localization Cytoplasm . Cell membrane . Apical cell membrane . Basolateral cell membrane . Cell junction . Detected at apical cell-cell junctions. Colocalized with FGF receptors to the cell membrane (By similarity). Detected in basolateral and apical membranes o
Protein Description Acts as a positive regulator of ERK phosphorylation downstream of fibroblast growth factor-receptor activation. [PubMed: 23862974]
Protein Sequence MEGDGVPWGSEPVSGPGPGGGGMIRELCRGFGRYRRYLGRLRQNLRETQKFFRDIKCSHNHTCLSSLTGGGGAERGPAGDVAETGLQAGQLSCISFPPKEEKYLQQIVDCLPCILILGQDCNVKCQLLNLLLGVQVLPTTKLGSEESCKLRRLRFTYGTQTRVSLALPGQYELVHTLVAHQGNWETIPEEDLEVQENNEDAAHVLAELEVTMHHALLQEVDVVVAPCQGLRPTVDVLGDLVNDFLPVITYALHKDELSERDEQELQEIRKYFSFPVFFFKVPKLGSEIIDSSTRRMESERSPLYRQLIDLGYLSSSHWNCGAPGQDTKAQSMLVEQSEKLRHLSTFSHQVLQTRLVDAAKALNLVHCHCLDIFINQAFDMQRDLQITPKRLEYTRKKENELYESLMNIANRKQEEMKDMIVETLNTMKEELLDDATNMEFKDVIVPENGEPVGTREIKCCIRQIQELIISRLNQAVANKLISSVDYLRESFVGTLERCLQSLEKSQDVSVHITSNYLKQILNAAYHVEVTFHSGSSVTRMLWEQIKQIIQRITWVSPPAITLEWKRKVAQEAIESLSASKLAKSICSQFRTRLNSSHEAFAASLRQLEAGHSGRLEKTEDLWLRVRKDHAPRLARLSLESCSLQDVLLHRKPKLGQELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLPKHERLVDLHGSVIDYNYGGGSSIAVLLIMERLHRDLYTGLKAGLTLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGSIVGTPIHMAPELFTGKYDNSVDVYAFGILFWYICSGSVKLPEAFERCASKDHLWNNVRRGARPERLPVFDEECWQLMEACWDGDPLKRPLLGIVQPMLQGIMNRLCKSNSEQPNRGLDDST
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
29MethylationGMIRELCRGFGRYRR
HHHHHHHHHHHHHHH		56.98-
56UbiquitinationQKFFRDIKCSHNHTC
HHHHHHCCCCCCCCC		33.6929967540
286PhosphorylationFKVPKLGSEIIDSST
EECCCCCHHHHCHHC		35.74-
339UbiquitinationMLVEQSEKLRHLSTF
HHHHHHHHHHHHHHH		56.9429967540
347PhosphorylationLRHLSTFSHQVLQTR
HHHHHHHHHHHHHHH		17.0724719451
353PhosphorylationFSHQVLQTRLVDAAK
HHHHHHHHHHHHHHH		23.0824719451
387PhosphorylationMQRDLQITPKRLEYT
HHHHCCCCHHHHHHH		15.1430266825
389UbiquitinationRDLQITPKRLEYTRK
HHCCCCHHHHHHHHH		62.0529967540
397UbiquitinationRLEYTRKKENELYES
HHHHHHHHHHHHHHH		63.5829967540
402PhosphorylationRKKENELYESLMNIA
HHHHHHHHHHHHHHH		9.4027642862
404PhosphorylationKENELYESLMNIANR
HHHHHHHHHHHHHHH		21.2525849741
479UbiquitinationLNQAVANKLISSVDY
HHHHHHHHHHHHHHH		37.14-
482PhosphorylationAVANKLISSVDYLRE
HHHHHHHHHHHHHHH		34.4429449344
483PhosphorylationVANKLISSVDYLRES
HHHHHHHHHHHHHHH		16.4129449344
490PhosphorylationSVDYLRESFVGTLER
HHHHHHHHHHHHHHH		20.8523403867
490O-linked_GlycosylationSVDYLRESFVGTLER
HHHHHHHHHHHHHHH		20.8530620550
494PhosphorylationLRESFVGTLERCLQS
HHHHHHHHHHHHHHH		21.8323403867
501PhosphorylationTLERCLQSLEKSQDV
HHHHHHHHHHHCCCE		26.0829978859
505PhosphorylationCLQSLEKSQDVSVHI
HHHHHHHCCCEEEEE		23.4129978859
509PhosphorylationLEKSQDVSVHITSNY
HHHCCCEEEEECHHH		19.1029978859
513PhosphorylationQDVSVHITSNYLKQI
CCEEEEECHHHHHHH		8.9529978859
514PhosphorylationDVSVHITSNYLKQIL
CEEEEECHHHHHHHH		23.9129978859
516PhosphorylationSVHITSNYLKQILNA
EEEECHHHHHHHHHH		18.2929978859
567UbiquitinationITLEWKRKVAQEAIE
CCHHHHHHHHHHHHH		37.8929967540
575PhosphorylationVAQEAIESLSASKLA
HHHHHHHHCCHHHHH		22.8523312004
577PhosphorylationQEAIESLSASKLAKS
HHHHHHCCHHHHHHH		39.5123312004
579PhosphorylationAIESLSASKLAKSIC
HHHHCCHHHHHHHHH		25.4823312004
580UbiquitinationIESLSASKLAKSICS
HHHCCHHHHHHHHHH		52.7829967540
595PhosphorylationQFRTRLNSSHEAFAA
HHHHHCCCHHHHHHH		37.3529255136
596PhosphorylationFRTRLNSSHEAFAAS
HHHHCCCHHHHHHHH		25.0329255136
617UbiquitinationGHSGRLEKTEDLWLR
CCCCCCEECHHHHHH		62.90-
642PhosphorylationRLSLESCSLQDVLLH
HHCHHHCCHHHHHHH		38.0420873877
743PhosphorylationRLHRDLYTGLKAGLT
HHHHHHHHHHHCCCC		43.2524719451
781UbiquitinationVHRDIKLKNVLLDKQ
CCCCCCHHHHEECCC		39.7529967540
787UbiquitinationLKNVLLDKQNRAKIT
HHHHEECCCCCCCCC		49.8229967540
792MethylationLDKQNRAKITDLGFC
ECCCCCCCCCCCCCC		42.79-
794PhosphorylationKQNRAKITDLGFCKP
CCCCCCCCCCCCCCH		25.1924043423
800MethylationITDLGFCKPEAMMSG
CCCCCCCCHHHHHCC		43.56-
806PhosphorylationCKPEAMMSGSIVGTP
CCHHHHHCCCCCCCC		19.1224043423
808PhosphorylationPEAMMSGSIVGTPIH
HHHHHCCCCCCCCCC		13.5424043423
812PhosphorylationMSGSIVGTPIHMAPE
HCCCCCCCCCCCCCH		14.2624043423
822PhosphorylationHMAPELFTGKYDNSV
CCCCHHHCCCCCCCC		45.4424043423
824AcetylationAPELFTGKYDNSVDV
CCHHHCCCCCCCCEE		46.508082911
825MethylationPELFTGKYDNSVDVY
CHHHCCCCCCCCEEE		23.00-
828MethylationFTGKYDNSVDVYAFG
HCCCCCCCCEEEHHH		19.45-
870UbiquitinationNNVRRGARPERLPVF
HHHCCCCCCHHCCCC		36.1129967540
884PhosphorylationFDEECWQLMEACWDG
CCHHHHHHHHHHHCC		1.1333259812
915UbiquitinationGIMNRLCKSNSEQPN
HHHHHHHHCCCCCCC		58.2129967540
928PhosphorylationPNRGLDDST------
CCCCCCCCC------		35.3725159151
929PhosphorylationNRGLDDST-------
CCCCCCCC-------		50.0125159151
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

Oops, there are no upstream regulatory protein records of DUSTY_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DUSTY_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 DUSTY_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAB14_HUMANRAB14physical
17353931
CH10_HUMANHSPE1physical
17353931
MTPN_HUMANMTPNphysical
17353931
PSB1_HUMANPSMB1physical
17353931
UBE2K_HUMANUBE2Kphysical
17353931
PSB3_HUMANPSMB3physical
17353931
MD2L1_HUMANMAD2L1physical
17353931
AT5F1_HUMANATP5F1physical
17353931
RS9_HUMANRPS9physical
17353931
DOPD_HUMANDDTphysical
17353931
LSM12_HUMANLSM12physical
17353931
RAB5C_HUMANRAB5Cphysical
17353931
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
610805Congenital anomalies of the kidney and urinary tract (CAKUT)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DUSTY_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-928, AND MASSSPECTROMETRY.

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