CCD86_HUMAN - dbPTM
CCD86_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CCD86_HUMAN
UniProt AC Q9H6F5
Protein Name Coiled-coil domain-containing protein 86
Gene Name CCDC86
Organism Homo sapiens (Human).
Sequence Length 360
Subcellular Localization Nucleus.
Protein Description
Protein Sequence MDTPLRRSRRLGGLRPESPESLTSVSRTRRALVEFESNPEETREPGSPPSVQRAGLGSPERPPKTSPGSPRLQQGAGLESPQGQPEPGAASPQRQQDLHLESPQRQPEYSPESPRCQPKPSEEAPKCSQDQGVLASELAQNKEELTPGAPQHQLPPVPGSPEPYPGQQAPGPEPSQPLLELTPRAPGSPRGQHEPSKPPPAGETVTGGFGAKKRKGSSSQAPASKKLNKEELPVIPKGKPKSGRVWKDRSKKRFSQMLQDKPLRTSWQRKMKERQERKLAKDFARHLEEEKERRRQEKKQRRAENLKRRLENERKAEVVQVIRNPAKLKRAKKKQLRSIEKRDTLALLQKQPPQQPAAKI
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
3Phosphorylation-----MDTPLRRSRR
-----CCCCCHHHHH		23.9523401153
8PhosphorylationMDTPLRRSRRLGGLR
CCCCCHHHHHCCCCC		18.4726074081
15MethylationSRRLGGLRPESPESL
HHHCCCCCCCCHHHH		35.89-
18PhosphorylationLGGLRPESPESLTSV
CCCCCCCCHHHHHHH		36.3322167270
21PhosphorylationLRPESPESLTSVSRT
CCCCCHHHHHHHHHH		40.0925159151
23PhosphorylationPESPESLTSVSRTRR
CCCHHHHHHHHHHHH		36.0423927012
24PhosphorylationESPESLTSVSRTRRA
CCHHHHHHHHHHHHH		24.3225159151
26PhosphorylationPESLTSVSRTRRALV
HHHHHHHHHHHHHHE		27.9223927012
28PhosphorylationSLTSVSRTRRALVEF
HHHHHHHHHHHHEEE		19.5926074081
30MethylationTSVSRTRRALVEFES
HHHHHHHHHHEEECC		31.49-
37PhosphorylationRALVEFESNPEETRE
HHHEEECCCHHHHCC		64.1130266825
42PhosphorylationFESNPEETREPGSPP
ECCCHHHHCCCCCCC		38.3729255136
47PhosphorylationEETREPGSPPSVQRA
HHHCCCCCCCCHHCC		44.3329255136
50PhosphorylationREPGSPPSVQRAGLG
CCCCCCCCHHCCCCC		33.9829255136
58PhosphorylationVQRAGLGSPERPPKT
HHCCCCCCCCCCCCC		28.7329255136
65PhosphorylationSPERPPKTSPGSPRL
CCCCCCCCCCCCCCC		46.0222167270
66PhosphorylationPERPPKTSPGSPRLQ
CCCCCCCCCCCCCCC		33.1322167270
69PhosphorylationPPKTSPGSPRLQQGA
CCCCCCCCCCCCCCC		15.3822167270
80PhosphorylationQQGAGLESPQGQPEP
CCCCCCCCCCCCCCC		27.8029255136
91PhosphorylationQPEPGAASPQRQQDL
CCCCCCCCHHHHHHC		22.4919664994
94UbiquitinationPGAASPQRQQDLHLE
CCCCCHHHHHHCCCC		39.24-
102PhosphorylationQQDLHLESPQRQPEY
HHHCCCCCCCCCCCC		32.4729255136
109PhosphorylationSPQRQPEYSPESPRC
CCCCCCCCCCCCCCC		35.8923927012
110PhosphorylationPQRQPEYSPESPRCQ
CCCCCCCCCCCCCCC		22.1129255136
113PhosphorylationQPEYSPESPRCQPKP
CCCCCCCCCCCCCCC		22.4929255136
121PhosphorylationPRCQPKPSEEAPKCS
CCCCCCCCCCCCCCC		54.9523663014
126UbiquitinationKPSEEAPKCSQDQGV
CCCCCCCCCCHHCCH		54.2733845483
128PhosphorylationSEEAPKCSQDQGVLA
CCCCCCCCHHCCHHH		42.8129255136
136PhosphorylationQDQGVLASELAQNKE
HHCCHHHHHHHHCHH		29.0523663014
146PhosphorylationAQNKEELTPGAPQHQ
HHCHHHCCCCCCHHH		23.9826055452
160PhosphorylationQLPPVPGSPEPYPGQ
HCCCCCCCCCCCCCC		21.7425159151
164PhosphorylationVPGSPEPYPGQQAPG
CCCCCCCCCCCCCCC		20.5225159151
175PhosphorylationQAPGPEPSQPLLELT
CCCCCCCCCCCCCCC		42.6523663014
182PhosphorylationSQPLLELTPRAPGSP
CCCCCCCCCCCCCCC		11.0125159151
188PhosphorylationLTPRAPGSPRGQHEP
CCCCCCCCCCCCCCC		15.4625159151
196PhosphorylationPRGQHEPSKPPPAGE
CCCCCCCCCCCCCCC		55.6028464451
197AcetylationRGQHEPSKPPPAGET
CCCCCCCCCCCCCCC		72.7225953088
197UbiquitinationRGQHEPSKPPPAGET
CCCCCCCCCCCCCCC		72.7233845483
204PhosphorylationKPPPAGETVTGGFGA
CCCCCCCCCCCCCCC		23.5824732914
206PhosphorylationPPAGETVTGGFGAKK
CCCCCCCCCCCCCCC		38.7224732914
212AcetylationVTGGFGAKKRKGSSS
CCCCCCCCCCCCCCC		54.1923749302
213AcetylationTGGFGAKKRKGSSSQ
CCCCCCCCCCCCCCC		59.83130169
217PhosphorylationGAKKRKGSSSQAPAS
CCCCCCCCCCCCCHH		29.8328176443
218PhosphorylationAKKRKGSSSQAPASK
CCCCCCCCCCCCHHH		34.8328176443
219PhosphorylationKKRKGSSSQAPASKK
CCCCCCCCCCCHHHC		31.8728176443
224PhosphorylationSSSQAPASKKLNKEE
CCCCCCHHHCCCHHH		29.3022496350
225AcetylationSSQAPASKKLNKEEL
CCCCCHHHCCCHHHC		64.4830583965
229AcetylationPASKKLNKEELPVIP
CHHHCCCHHHCCCCC		64.1026051181
229UbiquitinationPASKKLNKEELPVIP
CHHHCCCHHHCCCCC		64.1033845483
237UbiquitinationEELPVIPKGKPKSGR
HHCCCCCCCCCCCCC		69.3333845483
250PhosphorylationGRVWKDRSKKRFSQM
CCCCCHHHHHHHHHH		53.3020068231
255PhosphorylationDRSKKRFSQMLQDKP
HHHHHHHHHHHHCCC		20.7925159151
257SulfoxidationSKKRFSQMLQDKPLR
HHHHHHHHHHCCCCH		3.3428183972
261UbiquitinationFSQMLQDKPLRTSWQ
HHHHHHCCCCHHHHH		32.7521890473
2612-HydroxyisobutyrylationFSQMLQDKPLRTSWQ
HHHHHHCCCCHHHHH		32.75-
261AcetylationFSQMLQDKPLRTSWQ
HHHHHHCCCCHHHHH		32.7523749302
261UbiquitinationFSQMLQDKPLRTSWQ
HHHHHHCCCCHHHHH		32.7521890473
265PhosphorylationLQDKPLRTSWQRKMK
HHCCCCHHHHHHHHH		41.8426434776
266PhosphorylationQDKPLRTSWQRKMKE
HCCCCHHHHHHHHHH		18.1225159151
281UbiquitinationRQERKLAKDFARHLE
HHHHHHHHHHHHHHH		64.9133845483
291UbiquitinationARHLEEEKERRRQEK
HHHHHHHHHHHHHHH		60.8529967540
315UbiquitinationRRLENERKAEVVQVI
HHHHHHHHHHHHHHH		42.6033845483
333MethylationAKLKRAKKKQLRSIE
HHHHHHHHHHHHHHH		44.78-
338PhosphorylationAKKKQLRSIEKRDTL
HHHHHHHHHHHHHHH		43.6320860994
342CitrullinationQLRSIEKRDTLALLQ
HHHHHHHHHHHHHHH		29.38-
342CitrullinationQLRSIEKRDTLALLQ
HHHHHHHHHHHHHHH		29.38-
344PhosphorylationRSIEKRDTLALLQKQ
HHHHHHHHHHHHHCC		20.2620068231
350UbiquitinationDTLALLQKQPPQQPA
HHHHHHHCCCCCCCC		65.8233845483
350AcetylationDTLALLQKQPPQQPA
HHHHHHHCCCCCCCC		65.8226051181
359AcetylationPPQQPAAKI------
CCCCCCCCC------		51.5625953088
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
255SPhosphorylationKinaseAURKBQ96GD4
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CCD86_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 CCD86_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ODO2_HUMANDLSTphysical
16169070
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 CCD86_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-18; SER-21; SER-47;SER-50; SER-80 AND SER-91, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; THR-65; SER-69;SER-80; SER-91; SER-110; SER-113 AND SER-128, AND MASS SPECTROMETRY.
"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-18; SER-21; SER-24;SER-47; SER-50; SER-58; THR-65; SER-66; SER-69; SER-80; SER-91;SER-102 AND SER-110, AND MASS SPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-21; THR-23;SER-24; SER-26; SER-47; SER-50; SER-80 AND SER-91, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-47; SER-50;SER-58; SER-80; SER-91; SER-102 AND SER-110, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-110, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-91, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-47; SER-58;SER-80; SER-91; SER-102; SER-113; SER-188 AND SER-338, AND MASSSPECTROMETRY.

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