CCD82_HUMAN - dbPTM
CCD82_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CCD82_HUMAN
UniProt AC Q8N4S0
Protein Name Coiled-coil domain-containing protein 82
Gene Name CCDC82
Organism Homo sapiens (Human).
Sequence Length 544
Subcellular Localization
Protein Description
Protein Sequence MIHVRRHETRRNSKSHVPEQKSRVDWRRTKRSSISQLLDSDEELDSEEFDSDEELDSDESFENDEELDSNKGPDCNKTPGSERELNLSKIQSEGNDSKCLINSGNGSTYEEETNKIKHRNIDLQDQEKHLSQEDNDLNKQTGQIIEDDQEKHLSQEDNDLNKQTGQIIEDDLEEEDIKRGKRKRLSSVMCDSDESDDSDILVRKVGVKRPRRVVEDEGSSVEMEQKTPEKTLAAQKREKLQKLKELSKQRSRQRRSSGRDFEDSEKESCPSSDEVDEEEEEDNYESDEDGDDYIIDDFVVQDEEGDEENKNQQGEKLTTSQLKLVKQNSLYSFSDHYTHFERVVKALLINALDESFLGTLYDGTRQKSYAKDMLTSLHYLDNRFVQPRLESLVSRSRWKEQYKERVENYSNVSIHLKNPENCSCQACGLHRYCKYSVHLSGELYNTRTMQIDNFMSHDKQVFTVGRICASRTRIYHKLKHFKFKLYQECCTIAMTEEVEDEQVKETVERIFRRSKENGWIKEKYGQLEEYLNFADYFQEEKFEL
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
13PhosphorylationRHETRRNSKSHVPEQ
CCCCCCCCCCCCCHH		33.4523312004
15PhosphorylationETRRNSKSHVPEQKS
CCCCCCCCCCCHHHH		29.5424719451
81PhosphorylationDCNKTPGSERELNLS
CCCCCCCCHHHHCHH		34.3825159151
88PhosphorylationSERELNLSKIQSEGN
CHHHHCHHHHHCCCC		27.0021815630
92PhosphorylationLNLSKIQSEGNDSKC
HCHHHHHCCCCCCCE		51.4430576142
107PhosphorylationLINSGNGSTYEEETN
EEECCCCCCCHHHHH		31.6430576142
108PhosphorylationINSGNGSTYEEETNK
EECCCCCCCHHHHHC		36.0330576142
131PhosphorylationQDQEKHLSQEDNDLN
HHHHHHHCHHHCHHH		31.1029255136
141PhosphorylationDNDLNKQTGQIIEDD
HCHHHHHHCCCCCHH		32.4427690223
154PhosphorylationDDQEKHLSQEDNDLN
HHHHHHHCHHCCHHH		31.1029255136
164PhosphorylationDNDLNKQTGQIIEDD
CCHHHHHHCCCCHHC		32.4428450419
186PhosphorylationRGKRKRLSSVMCDSD
HCCCCCHHHCCCCCC		25.5620873877
187PhosphorylationGKRKRLSSVMCDSDE
CCCCCHHHCCCCCCC		20.6120873877
192PhosphorylationLSSVMCDSDESDDSD
HHHCCCCCCCCCCCC		38.0522617229
195PhosphorylationVMCDSDESDDSDILV
CCCCCCCCCCCCCEE		52.2722617229
198PhosphorylationDSDESDDSDILVRKV
CCCCCCCCCCEEHHC		31.3822617229
219PhosphorylationRVVEDEGSSVEMEQK
EEEECCCCCCCHHHC		29.2123401153
220PhosphorylationVVEDEGSSVEMEQKT
EEECCCCCCCHHHCC		32.7129255136
223SulfoxidationDEGSSVEMEQKTPEK
CCCCCCCHHHCCHHH		6.5721406390
227PhosphorylationSVEMEQKTPEKTLAA
CCCHHHCCHHHHHHH		36.0529255136
230AcetylationMEQKTPEKTLAAQKR
HHHCCHHHHHHHHHH		50.4723749302
236AcetylationEKTLAAQKREKLQKL
HHHHHHHHHHHHHHH		58.7725953088
256PhosphorylationQRSRQRRSSGRDFED
HHHHHHHHCCCCCCH		39.0624719451
264PhosphorylationSGRDFEDSEKESCPS
CCCCCCHHCCCCCCC		43.2921815630
316UbiquitinationNKNQQGEKLTTSQLK
CCCHHCCCCCHHHHH		58.94-
319PhosphorylationQQGEKLTTSQLKLVK
HHCCCCCHHHHHHHH		25.5529396449
320PhosphorylationQGEKLTTSQLKLVKQ
HCCCCCHHHHHHHHH		28.4229396449
323UbiquitinationKLTTSQLKLVKQNSL
CCCHHHHHHHHHCCC		43.53-
326UbiquitinationTSQLKLVKQNSLYSF
HHHHHHHHHCCCCCC		54.95-
329PhosphorylationLKLVKQNSLYSFSDH
HHHHHHCCCCCCCCC		26.6214702039
331PhosphorylationLVKQNSLYSFSDHYT
HHHHCCCCCCCCCHH		13.9022912867
368PhosphorylationYDGTRQKSYAKDMLT
CCCCCCHHHHHHHHH		23.2222468782
369PhosphorylationDGTRQKSYAKDMLTS
CCCCCHHHHHHHHHH		25.3822468782
371UbiquitinationTRQKSYAKDMLTSLH
CCCHHHHHHHHHHHH		35.12-
375PhosphorylationSYAKDMLTSLHYLDN
HHHHHHHHHHHHHHH		23.7022468782
391PhosphorylationFVQPRLESLVSRSRW
CCHHHHHHHHCHHHH		38.3723025827
435PhosphorylationGLHRYCKYSVHLSGE
CCHHHCCEEEECCCC		16.6222817900
444PhosphorylationVHLSGELYNTRTMQI
EECCCCCEECCEEEE		15.3622817900
448PhosphorylationGELYNTRTMQIDNFM
CCCEECCEEEECCCH		16.0528188228
463PhosphorylationSHDKQVFTVGRICAS
HCCCCEEEHHHHHHH		24.1628188228
536PhosphorylationEYLNFADYFQEEKFE
HHHCHHHHHHHHHCC		12.06-
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
154SPhosphorylationKinaseATRQ13535
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CCD82_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 CCD82_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPB5_HUMANSERPINB5physical
28514442
PKP3_HUMANPKP3physical
28514442
PKP1_HUMANPKP1physical
28514442
TOM34_HUMANTOMM34physical
28514442
TRI29_HUMANTRIM29physical
28514442
CALL3_HUMANCALML3physical
28514442
LY66C_HUMANLY6G6Cphysical
28514442
TRFE_HUMANTFphysical
28514442
ALBU_HUMANALBphysical
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 CCD82_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, 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-154; SER-192; SER-195AND SER-198, AND MASS SPECTROMETRY.

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