Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Cyclin-C  

UniProtKB / Swiss-Prot ID :  CCNC_HUMAN

Gene Name (Synonyms) : 
CCNC  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus (Probable). 

Protein Function :  Component of the Mediator complex, a coactivator involved in regulated gene transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Binds to and activates cyclin-dependent kinase CDK8 that phosphorylates the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAp II), which may inhibit the formation of a transcription initiation complex. 

Protein Sequence MAGNFWQSSHYLQWILDKQDLLKERQKDLKFLSEEEYWKLQIFFTNVIQALGEHLKLRQQVIATATVYFK...
Predicted Secondary Structure CCCCHHHHHHHHHHHCCHHEECCCHHHHHHHHHHHCCHHHHHHCCCCCCCCCCHHHHHHHHHHHHHHHHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
30Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QKDLKFLSE
HHHHHHHHH
55.16Phosphositeplus
Link
37PhosphotyrosineSEEEYWKLQ
HHHCCHHHH
15.89HPRD
Link
104PhosphoserineFGVVSNTRL
CCCHHHHHH
30.03Phosphositeplus
Link
104Phosphoserine.FGVVSNTRL
CCCHHHHHH
30.03UniProtKB
Link
117Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TSVLKTRFS
HHHHHCCCC
35.18Phosphositeplus
Link
121PhosphoserineKTRFSYAFP
HCCCCCCCH
16.56HPRD
Link
121Phosphoserine.KTRFSYAFP
HCCCCCCCH
16.56UniProtKB
Link
122PhosphotyrosineTRFSYAFPK
CCCCCCCHH
15.00HPRD
Link
122Phosphotyrosine.TRFSYAFPK
CCCCCCCHH
15.00UniProtKB
Link
126Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YAFPKEFPY
CCCHHHEEH
66.58Phosphositeplus
Link
252PhosphothreonineKEMATILSK
HHHHHHHHH
22.57HPRD
Link
252PhosphothreonineKEMATILSK
HHHHHHHHH
22.57Phosphositeplus
Link
275PhosphoserineGPNGSQNSS
HHHHHHCCC
32.59HPRD
Link-
275PhosphoserineGPNGSQNSS
HHHHHHCCC
32.59PhosphoELM
Link-
275PhosphoserineGPNGSQNSS
HHHHHHCCC
32.59Phosphositeplus
Link-
275Phosphoserine.GPNGSQNSS
HHHHHHCCC
32.59UniProtKB
Link-
278PhosphoserineGSQNSSYSQ
HHHCCCCCC
24.02HPRD
Link-
279PhosphoserineSQNSSYSQS
HHCCCCCCC
36.03HPRD
Link-
279PhosphoserineSQNSSYSQS
HHCCCCCCC
36.03PhosphoELM
Link-
279PhosphoserineSQNSSYSQS
HHCCCCCCC
36.03Phosphositeplus
Link-
279Phosphoserine.SQNSSYSQS
HHCCCCCCC
36.03UniProtKB
Link-
281PhosphoserineNSSYSQS
CCCCCCCCC
26.37HPRD
Link-
281PhosphoserineNSSYSQS
CCCCCCCCC
26.37PhosphoELM
Link-
281PhosphoserineNSSYSQS
CCCCCCCCC
26.37Phosphositeplus
Link-
281Phosphoserine.NSSYSQS
CCCCCCCCC
26.37UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
CDK3_HUMANin vivoHPRD:00456HPRD15084261
MED6_HUMANENSP00000319027STRING
MED6_HUMANENSP00000319027STRING
MED6_HUMANENSP00000319027STRING
MED6_HUMANENSP00000319027STRING
CDK2_HUMANENSP00000319027STRING
MED21_HUMANENSP00000319027STRING
MED21_HUMANENSP00000319027STRING
CDK3_HUMANENSP00000319027STRING
MED1_HUMANENSP00000319027STRING
MED1_HUMANENSP00000319027STRING
MED1_HUMANENSP00000319027STRING
RPB1_HUMANENSP00000319027STRING
MED14_HUMANENSP00000319027STRING
MED14_HUMANENSP00000319027STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-121 AND TYR-122, ANDMASS SPECTROMETRY.
"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-275; SER-279 ANDSER-281, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures