CCDC9_HUMAN - dbPTM
CCDC9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CCDC9_HUMAN
UniProt AC Q9Y3X0
Protein Name Coiled-coil domain-containing protein 9
Gene Name CCDC9
Organism Homo sapiens (Human).
Sequence Length 531
Subcellular Localization
Protein Description
Protein Sequence MAATLDLKSKEEKDAELDKRIEALRRKNEALIRRYQEIEEDRKKAELEGVAVTAPRKGRSVEKENVAVESEKNLGPSRRSPGTPRPPGASKGGRTPPQQGGRAGMGRASRSWEGSPGEQPRGGGAGGRGRRGRGRGSPHLSGAGDTSISDRKSKEWEERRRQNIEKMNEEMEKIAEYERNQREGVLEPNPVRNFLDDPRRRSGPLEESERDRREESRRHGRNWGGPDFERVRCGLEHERQGRRAGLGSAGDMTLSMTGRERSEYLRWKQEREKIDQERLQRHRKPTGQWRREWDAEKTDGMFKDGPVPAHEPSHRYDDQAWARPPKPPTFGEFLSQHKAEASSRRRRKSSRPQAKAAPRAYSDHDDRWETKEGAASPAPETPQPTSPETSPKETPMQPPEIPAPAHRPPEDEGEENEGEEDEEWEDISEDEEEEEIEVEEGDEEEPAQDHQAPEAAPTGIPCSEQAHGVPFSPEEPLLEPQAPGTPSSPFSPPSGHQPVSDWGEEVELNSPRTTHLAGALSPGEAWPFESV
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
35PhosphorylationNEALIRRYQEIEEDR
HHHHHHHHHHHHHHH		10.7228796482
53PhosphorylationELEGVAVTAPRKGRS
HHCCCEEECCCCCCC		22.6228555341
60PhosphorylationTAPRKGRSVEKENVA
ECCCCCCCCCHHCEE		43.2126055452
77PhosphorylationSEKNLGPSRRSPGTP
CCCCCCCCCCCCCCC		38.2329214152
80PhosphorylationNLGPSRRSPGTPRPP
CCCCCCCCCCCCCCC		26.9429255136
83PhosphorylationPSRRSPGTPRPPGAS
CCCCCCCCCCCCCCC		21.3630266825
90PhosphorylationTPRPPGASKGGRTPP
CCCCCCCCCCCCCCC		37.4422167270
94MethylationPGASKGGRTPPQQGG
CCCCCCCCCCCCCCC		53.37-
95PhosphorylationGASKGGRTPPQQGGR
CCCCCCCCCCCCCCC		42.4626055452
102MethylationTPPQQGGRAGMGRAS
CCCCCCCCCCCCCCC		34.49-
107MethylationGGRAGMGRASRSWEG
CCCCCCCCCCCCCCC		22.09-
109PhosphorylationRAGMGRASRSWEGSP
CCCCCCCCCCCCCCC		26.0330576142
110MethylationAGMGRASRSWEGSPG
CCCCCCCCCCCCCCC		44.82-
111PhosphorylationGMGRASRSWEGSPGE
CCCCCCCCCCCCCCC		27.3030576142
115PhosphorylationASRSWEGSPGEQPRG
CCCCCCCCCCCCCCC		20.4430576142
121MethylationGSPGEQPRGGGAGGR
CCCCCCCCCCCCCCC		56.96-
128MethylationRGGGAGGRGRRGRGR
CCCCCCCCCCCCCCC		34.23-
130MethylationGGAGGRGRRGRGRGS
CCCCCCCCCCCCCCC		36.20-
131MethylationGAGGRGRRGRGRGSP
CCCCCCCCCCCCCCC		41.8224129315
131Asymmetric dimethylarginineGAGGRGRRGRGRGSP
CCCCCCCCCCCCCCC		41.82-
133MethylationGGRGRRGRGRGSPHL
CCCCCCCCCCCCCCC		29.8024129315
133Asymmetric dimethylarginineGGRGRRGRGRGSPHL
CCCCCCCCCCCCCCC		29.80-
135MethylationRGRRGRGRGSPHLSG
CCCCCCCCCCCCCCC		40.8424129315
135Asymmetric dimethylarginineRGRRGRGRGSPHLSG
CCCCCCCCCCCCCCC		40.84-
137PhosphorylationRRGRGRGSPHLSGAG
CCCCCCCCCCCCCCC		14.0523927012
141PhosphorylationGRGSPHLSGAGDTSI
CCCCCCCCCCCCCCH		24.4623927012
166UbiquitinationRRRQNIEKMNEEMEK
HHHHHHHHHHHHHHH		43.14-
177PhosphorylationEMEKIAEYERNQREG
HHHHHHHHHHHHCCC		15.92-
202PhosphorylationLDDPRRRSGPLEESE
CCCHHHCCCCCCHHH		42.8426055452
208PhosphorylationRSGPLEESERDRREE
CCCCCCHHHHHHHHH		28.6724732914
221MethylationEESRRHGRNWGGPDF
HHHHHHCCCCCCCCH		29.60-
243MethylationEHERQGRRAGLGSAG
HHHHCCCCCCCCCCC		39.57-
248PhosphorylationGRRAGLGSAGDMTLS
CCCCCCCCCCCCEEC		33.8428450419
253PhosphorylationLGSAGDMTLSMTGRE
CCCCCCCEECCCCCC		22.0323186163
255PhosphorylationSAGDMTLSMTGRERS
CCCCCEECCCCCCHH		12.7228857561
257PhosphorylationGDMTLSMTGRERSEY
CCCEECCCCCCHHHH		29.7028555341
262PhosphorylationSMTGRERSEYLRWKQ
CCCCCCHHHHHHHHH		26.3227251275
264PhosphorylationTGRERSEYLRWKQER
CCCCHHHHHHHHHHH		11.65-
284MalonylationERLQRHRKPTGQWRR
HHHHHHCCCCCHHHH		40.5832601280
286PhosphorylationLQRHRKPTGQWRREW
HHHHCCCCCHHHHHC		45.0722817900
316PhosphorylationAHEPSHRYDDQAWAR
CCCCCCCCCCCCCCC		20.60-
335PhosphorylationPTFGEFLSQHKAEAS
CCHHHHHHHHHHHHH		35.2425159151
343PhosphorylationQHKAEASSRRRRKSS
HHHHHHHHHHHHHHH		36.5330387612
348AcetylationASSRRRRKSSRPQAK
HHHHHHHHHHCHHHH		51.4719823125
349PhosphorylationSSRRRRKSSRPQAKA
HHHHHHHHHCHHHHH		29.75-
350PhosphorylationSRRRRKSSRPQAKAA
HHHHHHHHCHHHHHC		51.52-
355AcetylationKSSRPQAKAAPRAYS
HHHCHHHHHCCCCCC		39.5719823133
361PhosphorylationAKAAPRAYSDHDDRW
HHHCCCCCCCCCCCC		18.8626657352
362PhosphorylationKAAPRAYSDHDDRWE
HHCCCCCCCCCCCCC		27.7323401153
370PhosphorylationDHDDRWETKEGAASP
CCCCCCCCCCCCCCC		27.6930624053
376PhosphorylationETKEGAASPAPETPQ
CCCCCCCCCCCCCCC		22.5129255136
381PhosphorylationAASPAPETPQPTSPE
CCCCCCCCCCCCCCC		26.6030266825
385PhosphorylationAPETPQPTSPETSPK
CCCCCCCCCCCCCCC		52.2229255136
386PhosphorylationPETPQPTSPETSPKE
CCCCCCCCCCCCCCC		27.6729255136
389PhosphorylationPQPTSPETSPKETPM
CCCCCCCCCCCCCCC		54.4329255136
390PhosphorylationQPTSPETSPKETPMQ
CCCCCCCCCCCCCCC		32.1129255136
394PhosphorylationPETSPKETPMQPPEI
CCCCCCCCCCCCCCC		30.1328111955
485PhosphorylationLEPQAPGTPSSPFSP
CCCCCCCCCCCCCCC		20.95-
488PhosphorylationQAPGTPSSPFSPPSG
CCCCCCCCCCCCCCC		31.03-
510PhosphorylationGEEVELNSPRTTHLA
CCEEECCCCCCCCCC		28.5126074081
513PhosphorylationVELNSPRTTHLAGAL
EECCCCCCCCCCCCC		23.1923403867
514PhosphorylationELNSPRTTHLAGALS
ECCCCCCCCCCCCCC		19.0323403867
521PhosphorylationTHLAGALSPGEAWPF
CCCCCCCCCCCCCCC		30.2625159151
530PhosphorylationGEAWPFESV------
CCCCCCCCC------		33.2428176443
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 CCDC9_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CCDC9_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 CCDC9_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CCDC9_HUMAN !!
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 CCDC9_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-202 AND SER-521, ANDMASS 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-376; THR-385; SER-386AND SER-390, 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-202 AND SER-521, ANDMASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386 AND SER-521, ANDMASS SPECTROMETRY.
"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 THR-385, AND MASSSPECTROMETRY.

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