DOK3_HUMAN - dbPTM
DOK3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DOK3_HUMAN
UniProt AC Q7L591
Protein Name Docking protein 3
Gene Name DOK3
Organism Homo sapiens (Human).
Sequence Length 496
Subcellular Localization Cytoplasm. Cell membrane
Peripheral membrane protein
Cytoplasmic side.
Protein Description DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK3 is a negative regulator of JNK signaling in B-cells through interaction with INPP5D/SHIP1. May modulate ABL1 function (By similarity)..
Protein Sequence MTRGARLRSDARAQLNQLSLDGGTGSGQKGKCEEFPSSLSSVSPGLEAAALLLAVTMDPLETPIKDGILYQQHVKFGKKCWRKVWALLYAGGPSGVARLESWEVRDGGLGAAGDRSAGPGRRGERRVIRLADCVSVLPADGESCPRDTGAFLLTTTERSHLLAAQHRQAWMGPICQLAFPGTGEASSGSTDAQSPKRGLVPMEENSIYSSWQEVGEFPVVVQRTEAATRCQLKGPALLVLGPDAIQLREAKGTQALYSWPYHFLRKFGSDKGVFSFEAGRRCHSGEGLFAFSTPCAPDLCRAVAGAIARQRERLPELTRPQPCPLPRATSLPSLDTPGELREMPPGPEPPTSRKMHLAEPGPQSLPLLLGPEPNDLASGLYASVCKRASGPPGNEHLYENLCVLEASPTLHGGEPEPHEGPGSRSPTTSPIYHNGQDLSWPGPANDSTLEAQYRRLLELDQVEGTGRPDPQAGFKAKLVTLLSRERRKGPAPCDRP
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
9PhosphorylationTRGARLRSDARAQLN
CCCHHHHHHHHHHHH		39.97-
62PhosphorylationVTMDPLETPIKDGIL
HHCCCCCCCCCCCCC		37.6928450419
89PhosphorylationRKVWALLYAGGPSGV
HHHHHHHHCCCCCHH		12.21-
101PhosphorylationSGVARLESWEVRDGG
CHHEEEEEEEECCCC		32.8824247654
122MethylationRSAGPGRRGERRVIR
CCCCCCCCCCCEEEE		58.18-
135 (in isoform 2)Phosphorylation-25.0326471730
136 (in isoform 2)Phosphorylation-3.5626471730
147 (in isoform 4)Phosphorylation-34.3326471730
148 (in isoform 4)Phosphorylation-31.5226471730
179 (in isoform 2)Phosphorylation-8.57-
182PhosphorylationCQLAFPGTGEASSGS
HEEECCCCCCCCCCC		31.8928450419
186PhosphorylationFPGTGEASSGSTDAQ
CCCCCCCCCCCCCCC		30.8128450419
187PhosphorylationPGTGEASSGSTDAQS
CCCCCCCCCCCCCCC		43.7628450419
189PhosphorylationTGEASSGSTDAQSPK
CCCCCCCCCCCCCCC		25.6825262027
190PhosphorylationGEASSGSTDAQSPKR
CCCCCCCCCCCCCCC		38.5925262027
191 (in isoform 4)Phosphorylation-44.28-
194PhosphorylationSGSTDAQSPKRGLVP
CCCCCCCCCCCCCCC		33.8223401153
208PhosphorylationPMEENSIYSSWQEVG
CCCCCCHHCCCHHCC		9.1122817900
209PhosphorylationMEENSIYSSWQEVGE
CCCCCHHCCCHHCCC		24.3527251275
210PhosphorylationEENSIYSSWQEVGEF
CCCCHHCCCHHCCCC		18.7927251275
249 (in isoform 3)Phosphorylation-64.4226471730
250 (in isoform 3)Phosphorylation-14.7826471730
293 (in isoform 3)Phosphorylation-18.88-
329PhosphorylationPCPLPRATSLPSLDT
CCCCCCCCCCCCCCC		31.8820164059
330PhosphorylationCPLPRATSLPSLDTP
CCCCCCCCCCCCCCC		36.9823401153
333PhosphorylationPRATSLPSLDTPGEL
CCCCCCCCCCCCCCC		44.1420058876
336PhosphorylationTSLPSLDTPGELREM
CCCCCCCCCCCCCCC		38.1920058876
351PhosphorylationPPGPEPPTSRKMHLA
CCCCCCCCCCCCCCC		52.45-
352PhosphorylationPGPEPPTSRKMHLAE
CCCCCCCCCCCCCCC		35.36-
364PhosphorylationLAEPGPQSLPLLLGP
CCCCCCCCCCCHHCC		34.7820058876
378PhosphorylationPEPNDLASGLYASVC
CCCCCHHHHHHHHHH		36.3126657352
381PhosphorylationNDLASGLYASVCKRA
CCHHHHHHHHHHHHC		10.6028060719
389PhosphorylationASVCKRASGPPGNEH
HHHHHHCCCCCCCHH		56.7326657352
398PhosphorylationPPGNEHLYENLCVLE
CCCCHHHHHCEEEEE		12.5124927040
407PhosphorylationNLCVLEASPTLHGGE
CEEEEECCCCCCCCC		14.7228060719
409PhosphorylationCVLEASPTLHGGEPE
EEEECCCCCCCCCCC		28.9728060719
425PhosphorylationHEGPGSRSPTTSPIY
CCCCCCCCCCCCCCE		28.4428450419
427PhosphorylationGPGSRSPTTSPIYHN
CCCCCCCCCCCCEEC		40.9528450419
428PhosphorylationPGSRSPTTSPIYHNG
CCCCCCCCCCCEECC		35.5728450419
429PhosphorylationGSRSPTTSPIYHNGQ
CCCCCCCCCCEECCC		16.2728450419
432PhosphorylationSPTTSPIYHNGQDLS
CCCCCCCEECCCCCC		7.8228450419
439PhosphorylationYHNGQDLSWPGPAND
EECCCCCCCCCCCCC		39.2428450419
447PhosphorylationWPGPANDSTLEAQYR
CCCCCCCCHHHHHHH		34.4027486199
448PhosphorylationPGPANDSTLEAQYRR
CCCCCCCHHHHHHHH		31.3327486199
453PhosphorylationDSTLEAQYRRLLELD
CCHHHHHHHHHHHHH		12.5422817900
477AcetylationPQAGFKAKLVTLLSR
CCCCHHHHHHHHHHH		44.0419608861
480PhosphorylationGFKAKLVTLLSRERR
CHHHHHHHHHHHHHH		32.2028060719
483O-linked_GlycosylationAKLVTLLSRERRKGP
HHHHHHHHHHHHCCC		34.9030379171
483PhosphorylationAKLVTLLSRERRKGP
HHHHHHHHHHHHCCC		34.9028450419
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 DOK3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DOK3_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 DOK3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DCAM_HUMANAMD1physical
26186194
TPP2_HUMANTPP2physical
26186194
DPP9_HUMANDPP9physical
26186194
MIO_HUMANMIOSphysical
26186194
WDR34_HUMANWDR34physical
26186194
UH1BL_HUMANUHRF1BP1Lphysical
26186194
DPP8_HUMANDPP8physical
26186194
WDR54_HUMANWDR54physical
26186194
DOK4_HUMANDOK4physical
25814554
TPP2_HUMANTPP2physical
28514442
UH1BL_HUMANUHRF1BP1Lphysical
28514442
MIO_HUMANMIOSphysical
28514442
DCAM_HUMANAMD1physical
28514442
WDR54_HUMANWDR54physical
28514442
DPP8_HUMANDPP8physical
28514442
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 DOK3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-477, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330, AND MASSSPECTROMETRY.

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