CC85C_HUMAN - dbPTM
CC85C_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CC85C_HUMAN
UniProt AC A6NKD9
Protein Name Coiled-coil domain-containing protein 85C
Gene Name CCDC85C
Organism Homo sapiens (Human).
Sequence Length 419
Subcellular Localization Cell junction, tight junction. Localizes to the apical junction of radial glia in the wall of lateral ventricles of the developing brain. Colocalizes with TJP1 on the meshwork-like structure of adherens junctions on the lateral ventricles wall..
Protein Description May play an important role in cortical development, especially in the maintenance of radial glia..
Protein Sequence MAKPAATAAAASEELSQVPDEELLRWSKEELARRLRRAEGEKVGLMLEHGGLMRDVNRRLQQHLLEIRGLKDVNQRLQDDNQELRELCCFLDDDRQKGRKLAREWQRFGRHAAGAVWHEVARSQQKLRELEARQEALLRENLELKELVLLLDEERAALAATGAASGGGGGGGGAGSRSSIDSQASLSGPLSGGAPGAGARDVGDGSSTSSAGSGGSPDHHHHVPPPLLPPGPHKAPDGKAGATRRSLDDLSAPPHHRSIPNGLHDPSSTYIRQLESKVRLLEGDKLLAQQAGSGEFRTLRKGFSPYHSESQLASLPPSYQDSLQNGPACPAPELPSPPSAGYSPAGQKPEAVVHAMKVLEVHENLDRQLQDSCEEDLSEKEKAIVREMCNVVWRKLGDAASSKPSIRQHLSGNQFKGPL
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
2Acetylation------MAKPAATAA
------CCCHHHHHH		26.9222814378
7Phosphorylation-MAKPAATAAAASEE
-CCCHHHHHHHHHHH		20.95-
12PhosphorylationAATAAAASEELSQVP
HHHHHHHHHHHHCCC		27.20-
16PhosphorylationAAASEELSQVPDEEL
HHHHHHHHCCCHHHH		32.20-
27PhosphorylationDEELLRWSKEELARR
HHHHHHHCHHHHHHH		24.61-
28UbiquitinationEELLRWSKEELARRL
HHHHHHCHHHHHHHH		48.5329967540
161PhosphorylationERAALAATGAASGGG
HHHHHHHHCCCCCCC		23.0330624053
165PhosphorylationLAATGAASGGGGGGG
HHHHCCCCCCCCCCC		37.1228985074
176PhosphorylationGGGGGAGSRSSIDSQ
CCCCCCCCCHHCCCC		28.5830624053
178PhosphorylationGGGAGSRSSIDSQAS
CCCCCCCHHCCCCCC		33.0925159151
179PhosphorylationGGAGSRSSIDSQASL
CCCCCCHHCCCCCCC		29.3325159151
182PhosphorylationGSRSSIDSQASLSGP
CCCHHCCCCCCCCCC		26.4430631047
185PhosphorylationSSIDSQASLSGPLSG
HHCCCCCCCCCCCCC		18.5424275569
187PhosphorylationIDSQASLSGPLSGGA
CCCCCCCCCCCCCCC		35.5527251275
191PhosphorylationASLSGPLSGGAPGAG
CCCCCCCCCCCCCCC		38.0127251275
206PhosphorylationARDVGDGSSTSSAGS
CCCCCCCCCCCCCCC		34.8720873877
207PhosphorylationRDVGDGSSTSSAGSG
CCCCCCCCCCCCCCC		37.5320873877
208PhosphorylationDVGDGSSTSSAGSGG
CCCCCCCCCCCCCCC		28.5320873877
209PhosphorylationVGDGSSTSSAGSGGS
CCCCCCCCCCCCCCC		21.8220873877
210PhosphorylationGDGSSTSSAGSGGSP
CCCCCCCCCCCCCCC		36.4220873877
213PhosphorylationSSTSSAGSGGSPDHH
CCCCCCCCCCCCCCC		39.4329116813
216PhosphorylationSSAGSGGSPDHHHHV
CCCCCCCCCCCCCCC		30.5829116813
243PhosphorylationPDGKAGATRRSLDDL
CCCCCCCCCCCHHHC		26.2029414761
246PhosphorylationKAGATRRSLDDLSAP
CCCCCCCCHHHCCCC		32.6230266825
251PhosphorylationRRSLDDLSAPPHHRS
CCCHHHCCCCCCCCC		45.8023403867
258PhosphorylationSAPPHHRSIPNGLHD
CCCCCCCCCCCCCCC		37.7330266825
267PhosphorylationPNGLHDPSSTYIRQL
CCCCCCCCHHHHHHH		41.1730266825
268PhosphorylationNGLHDPSSTYIRQLE
CCCCCCCHHHHHHHH		30.5330266825
269PhosphorylationGLHDPSSTYIRQLES
CCCCCCHHHHHHHHH		27.5730266825
270PhosphorylationLHDPSSTYIRQLESK
CCCCCHHHHHHHHHH		8.9630266825
285UbiquitinationVRLLEGDKLLAQQAG
HHHHHHCHHHHHHCC		57.1529967540
293PhosphorylationLLAQQAGSGEFRTLR
HHHHHCCCCCCCHHC		37.8628555341
298PhosphorylationAGSGEFRTLRKGFSP
CCCCCCCHHCCCCCC		35.9128555341
306PhosphorylationLRKGFSPYHSESQLA
HCCCCCCCCCHHHHH		19.4422817900
372PhosphorylationLDRQLQDSCEEDLSE
HHHHHHHHHHHHCHH		15.5128985074
403UbiquitinationLGDAASSKPSIRQHL
HHHHHHCCCCHHHHH		40.0529967540
4032-HydroxyisobutyrylationLGDAASSKPSIRQHL
HHHHHHCCCCHHHHH		40.05-
405PhosphorylationDAASSKPSIRQHLSG
HHHHCCCCHHHHHCC		33.8528555341
416MethylationHLSGNQFKGPL----
HHCCCCCCCCC----		50.26-
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 CC85C_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CC85C_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 CC85C_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CC85C_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 CC85C_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-179, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-179, AND MASS SPECTROMETRY.

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