DCA15_HUMAN - dbPTM
DCA15_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DCA15_HUMAN
UniProt AC Q66K64
Protein Name DDB1- and CUL4-associated factor 15
Gene Name DCAF15
Organism Homo sapiens (Human).
Sequence Length 600
Subcellular Localization
Protein Description May be involved in ubiquitination and degradation through a DBB1-CUL4 E3 protein-ubiquitin ligase..
Protein Sequence MAPSSKSERNSGAGSGGGGPGGAGGKRAAGRRREHVLKQLERVKISGQLSPRLFRKLPPRVCVSLKNIVDEDFLYAGHIFLGFSKCGRYVLSYTSSSGDDDFSFYIYHLYWWEFNVHSKLKLVRQVRLFQDEEIYSDLYLTVCEWPSDASKVIVFGFNTRSANGMLMNMMMMSDENHRDIYVSTVAVPPPGRCAACQDASRAHPGDPNAQCLRHGFMLHTKYQVVYPFPTFQPAFQLKKDQVVLLNTSYSLVACAVSVHSAGDRSFCQILYDHSTCPLAPASPPEPQSPELPPALPSFCPEAAPARSSGSPEPSPAIAKAKEFVADIFRRAKEAKGGVPEEARPALCPGPSGSRCRAHSEPLALCGETAPRDSPPASEAPASEPGYVNYTKLYYVLESGEGTEPEDELEDDKISLPFVVTDLRGRNLRPMRERTAVQGQYLTVEQLTLDFEYVINEVIRHDATWGHQFCSFSDYDIVILEVCPETNQVLINIGLLLLAFPSPTEEGQLRPKTYHTSLKVAWDLNTGIFETVSVGDLTEVKGQTSGSVWSSYRKSCVDMVMKWLVPESSGRYVNRMTNEALHKGCSLKVLADSERYTWIVL
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
11PhosphorylationSSKSERNSGAGSGGG
CCCCCCCCCCCCCCC		35.9228985074
15PhosphorylationERNSGAGSGGGGPGG
CCCCCCCCCCCCCCC		33.4623403867
26AcetylationGPGGAGGKRAAGRRR
CCCCCCCCHHCHHHH		37.6430588003
38UbiquitinationRRREHVLKQLERVKI
HHHHHHHHHHHHCCC		52.3129967540
46PhosphorylationQLERVKISGQLSPRL
HHHHCCCCCCCCHHH		18.1226434776
50PhosphorylationVKISGQLSPRLFRKL
CCCCCCCCHHHHHHC		10.4922617229
230PhosphorylationQVVYPFPTFQPAFQL
EEEEECCCCCCCEEC		34.97-
282PhosphorylationTCPLAPASPPEPQSP
CCCCCCCCCCCCCCC		39.6728348404
288PhosphorylationASPPEPQSPELPPAL
CCCCCCCCCCCCCCC		30.9328348404
307PhosphorylationPEAAPARSSGSPEPS
CCCCCCCCCCCCCCC		40.9529255136
308PhosphorylationEAAPARSSGSPEPSP
CCCCCCCCCCCCCCH		37.4229255136
310PhosphorylationAPARSSGSPEPSPAI
CCCCCCCCCCCCHHH		28.2129255136
314PhosphorylationSSGSPEPSPAIAKAK
CCCCCCCCHHHHHHH		25.8725159151
359PhosphorylationGSRCRAHSEPLALCG
CCCCCCCCCCCEECC		39.6723663014
368PhosphorylationPLALCGETAPRDSPP
CCEECCCCCCCCCCC		27.5226074081
373PhosphorylationGETAPRDSPPASEAP
CCCCCCCCCCCCCCC		33.7825849741
377PhosphorylationPRDSPPASEAPASEP
CCCCCCCCCCCCCCC		39.8128985074
382PhosphorylationPASEAPASEPGYVNY
CCCCCCCCCCCEECE		43.1726074081
386PhosphorylationAPASEPGYVNYTKLY
CCCCCCCEECEEEEE		9.0226074081
389PhosphorylationSEPGYVNYTKLYYVL
CCCCEECEEEEEEEE		8.6626074081
390PhosphorylationEPGYVNYTKLYYVLE
CCCEECEEEEEEEEE		14.9026074081
391UbiquitinationPGYVNYTKLYYVLES
CCEECEEEEEEEEEC		24.9229967540
393PhosphorylationYVNYTKLYYVLESGE
EECEEEEEEEEECCC		7.9626074081
554PhosphorylationVWSSYRKSCVDMVMK
HHHHHHHHHHHHHHH		15.46-
567PhosphorylationMKWLVPESSGRYVNR
HHHHCCCCCCCHHHH		31.83-
568PhosphorylationKWLVPESSGRYVNRM
HHHCCCCCCCHHHHH		26.15-
571PhosphorylationVPESSGRYVNRMTNE
CCCCCCCHHHHHHHH		12.95-
582UbiquitinationMTNEALHKGCSLKVL
HHHHHHHCCCCEEEE		63.5629967540
587UbiquitinationLHKGCSLKVLADSER
HHCCCCEEEEECCCC		20.93-
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 DCA15_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DCA15_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 DCA15_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DDB1_HUMANDDB1physical
16949367
CUL4A_HUMANCUL4Aphysical
16949367
LMBD2_HUMANLMBRD2physical
26186194
DMWD_HUMANDMWDphysical
26186194
BCOR_HUMANBCORphysical
26186194
ZEB1_HUMANZEB1physical
26186194
ZO2_HUMANTJP2physical
26186194
RUFY3_HUMANRUFY3physical
26186194
STIL_HUMANSTILphysical
26186194
DUSTY_HUMANDSTYKphysical
26186194
TRI33_HUMANTRIM33physical
26186194
ZN503_HUMANZNF503physical
26186194
RB3GP_HUMANRAB3GAP1physical
26186194
UGPA_HUMANUGP2physical
26186194
ARNT_HUMANARNTphysical
26186194
ZEB1_HUMANZEB1physical
28514442
ZO2_HUMANTJP2physical
28514442
RUFY3_HUMANRUFY3physical
28514442
BCOR_HUMANBCORphysical
28514442
UGPA_HUMANUGP2physical
28514442
ARNT_HUMANARNTphysical
28514442
LMBD2_HUMANLMBRD2physical
28514442
DUSTY_HUMANDSTYKphysical
28514442
STIL_HUMANSTILphysical
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 DCA15_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310 AND SER-314, ANDMASS SPECTROMETRY.

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