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Protein

Cyclin-C

Gene

CCNC

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Biological processi

  1. gene expression Source: Reactome
  2. Notch signaling pathway Source: Reactome
  3. positive regulation of transcription from RNA polymerase II promoter Source: Reactome
  4. regulation of cyclin-dependent protein serine/threonine kinase activity Source: InterPro
  5. transcription, DNA-templated Source: Reactome
  6. transcription initiation from RNA polymerase II promoter Source: Reactome
  7. transforming growth factor beta receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Activator, Cyclin, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_116145. PPARA activates gene expression.
REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
REACT_12627. Generic Transcription Pathway.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinkiP24863.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-C
Alternative name(s):
SRB11 homolog
Short name:
hSRB11
Gene namesi
Name:CCNC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:1581. CCNC.

Subcellular locationi

  1. Nucleus Curated

GO - Cellular componenti

  1. DNA-directed RNA polymerase II, holoenzyme Source: InterPro
  2. mediator complex Source: Ensembl
  3. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26149.

Polymorphism and mutation databases

BioMutaiCCNC.
DMDMi166214910.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 283283Cyclin-CPRO_0000080420Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei275 – 2751Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP24863.
PaxDbiP24863.
PRIDEiP24863.

PTM databases

PhosphoSiteiP24863.

Expressioni

Tissue specificityi

Highest levels in pancreas. High levels in heart, liver, skeletal muscle and kidney. Low levels in brain.

Gene expression databases

BgeeiP24863.
CleanExiHS_CCNC.
ExpressionAtlasiP24863. baseline and differential.
GenevestigatoriP24863.

Organism-specific databases

HPAiCAB010499.

Interactioni

Subunit structurei

Component of the Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. The cylin/CDK pair formed by CCNC/CDK8 also associates with the large subunit of RNA polymerase II.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDK8P4933624EBI-395261,EBI-394377
CRXO431863EBI-395261,EBI-748171
DYDC1Q8WWB33EBI-395261,EBI-740680
FOXP2O154093EBI-395261,EBI-983612
GLYR1Q49A263EBI-395261,EBI-2804292
GOLGA2Q083793EBI-395261,EBI-618309
KRT13A1A4E93EBI-395261,EBI-10171552
KRT15P190123EBI-395261,EBI-739566
KRT31Q153233EBI-395261,EBI-948001
LZTS2Q9BRK43EBI-395261,EBI-741037
MBIPQ9NS73-53EBI-395261,EBI-10182361
MEOX2A4D1273EBI-395261,EBI-10172134
MGST3O148803EBI-395261,EBI-724754
NEFLI6L9F63EBI-395261,EBI-10178578
NMNAT1Q9HAN93EBI-395261,EBI-3917542
PBXIP1Q96AQ63EBI-395261,EBI-740845
PNMA5Q96PV43EBI-395261,EBI-10171633
PUF60Q9UHX13EBI-395261,EBI-1053259
TADA3O755283EBI-395261,EBI-473249
TRIM39Q9HCM93EBI-395261,EBI-739510
ZNF18P170224EBI-395261,EBI-8648067

Protein-protein interaction databases

BioGridi107333. 70 interactions.
DIPiDIP-32920N.
IntActiP24863. 48 interactions.
STRINGi9606.ENSP00000358222.

Structurei

Secondary structure

283
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni1 – 33Combined sources
Helixi5 – 73Combined sources
Helixi9 – 135Combined sources
Helixi18 – 2912Combined sources
Helixi34 – 5421Combined sources
Helixi59 – 7517Combined sources
Turni78 – 803Combined sources
Helixi83 – 9715Combined sources
Beta strandi98 – 1003Combined sources
Helixi105 – 11915Combined sources
Turni121 – 1233Combined sources
Helixi132 – 14514Combined sources
Turni146 – 1483Combined sources
Helixi156 – 16611Combined sources
Helixi169 – 18315Combined sources
Turni184 – 1874Combined sources
Helixi188 – 1914Combined sources
Helixi194 – 20815Combined sources
Helixi214 – 2185Combined sources
Helixi224 – 24320Combined sources
Helixi246 – 25611Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3RGFX-ray2.20B1-283[»]
4F6SX-ray2.60B1-283[»]
4F6UX-ray2.10B1-283[»]
4F6WX-ray2.39B1-283[»]
4F70X-ray3.00B1-283[»]
4F7JX-ray2.60B1-283[»]
4F7LX-ray2.90B1-283[»]
4F7NX-ray2.65B1-283[»]
4F7SX-ray2.20B1-283[»]
4G6LX-ray2.70B1-283[»]
ProteinModelPortaliP24863.
SMRiP24863. Positions 1-257.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 14499Cyclin N-terminalAdd
BLAST

Sequence similaritiesi

Belongs to the cyclin family. Cyclin C subfamily.Curated
Contains 1 cyclin N-terminal domain.Curated

Phylogenomic databases

eggNOGiCOG5333.
GeneTreeiENSGT00760000119191.
HOGENOMiHOG000008007.
HOVERGENiHBG050836.
InParanoidiP24863.
KOiK15161.
OMAiAYTQEFP.
OrthoDBiEOG7WX08X.
PhylomeDBiP24863.

Family and domain databases

Gene3Di1.10.472.10. 1 hit.
InterProiIPR013763. Cyclin-like.
IPR015429. Cyclin_C/H/T/L.
IPR006671. Cyclin_N.
[Graphical view]
PANTHERiPTHR10026. PTHR10026. 1 hit.
PfamiPF00134. Cyclin_N. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 2 hits.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P24863-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAGNFWQSSH YLQWILDKQD LLKERQKDLK FLSEEEYWKL QIFFTNVIQA
60 70 80 90 100
LGEHLKLRQQ VIATATVYFK RFYARYSLKS IDPVLMAPTC VFLASKVEEF
110 120 130 140 150
GVVSNTRLIA AATSVLKTRF SYAFPKEFPY RMNHILECEF YLLELMDCCL
160 170 180 190 200
IVYHPYRPLL QYVQDMGQED MLLPLAWRIV NDTYRTDLCL LYPPFMIALA
210 220 230 240 250
CLHVACVVQQ KDARQWFAEL SVDMEKILEI IRVILKLYEQ WKNFDERKEM
260 270 280
ATILSKMPKP KPPPNSEGEQ GPNGSQNSSY SQS
Length:283
Mass (Da):33,243
Last modified:January 15, 2008 - v2
Checksum:iCF8AC5E94E621F4C
GO
Isoform 2 (identifier: P24863-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-85: Missing.

Note: No experimental confirmation available.

Show »
Length:198
Mass (Da):22,945
Checksum:i1A22C22167A775E7
GO

Sequence cautioni

The sequence AAC50825.1 differs from that shown. Reason: Erroneous initiation. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8585Missing in isoform 2. 1 PublicationVSP_043075Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74091 mRNA. No translation available.
U40739
, U40728, U40729, U40730, U40731, U40732, U40733, U40734, U40735, U40736, U40737, U40738 Genomic DNA. Translation: AAC50825.1. Different initiation.
AK298558 mRNA. Translation: BAG60753.1.
AL137784 Genomic DNA. Translation: CAC14563.1.
CCDSiCCDS34502.1. [P24863-1]
CCDS47461.1. [P24863-2]
PIRiA40268.
RefSeqiNP_001013417.1. NM_001013399.1. [P24863-2]
NP_005181.2. NM_005190.3. [P24863-1]
UniGeneiHs.430646.
Hs.633351.

Genome annotation databases

EnsembliENST00000520429; ENSP00000428982; ENSG00000112237. [P24863-1]
ENST00000523799; ENSP00000430014; ENSG00000112237. [P24863-2]
ENST00000523985; ENSP00000430119; ENSG00000112237. [P24863-2]
GeneIDi892.
KEGGihsa:892.
UCSCiuc003pqd.3. human. [P24863-1]

Polymorphism and mutation databases

BioMutaiCCNC.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74091 mRNA. No translation available.
U40739
, U40728, U40729, U40730, U40731, U40732, U40733, U40734, U40735, U40736, U40737, U40738 Genomic DNA. Translation: AAC50825.1. Different initiation.
AK298558 mRNA. Translation: BAG60753.1.
AL137784 Genomic DNA. Translation: CAC14563.1.
CCDSiCCDS34502.1. [P24863-1]
CCDS47461.1. [P24863-2]
PIRiA40268.
RefSeqiNP_001013417.1. NM_001013399.1. [P24863-2]
NP_005181.2. NM_005190.3. [P24863-1]
UniGeneiHs.430646.
Hs.633351.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3RGFX-ray2.20B1-283[»]
4F6SX-ray2.60B1-283[»]
4F6UX-ray2.10B1-283[»]
4F6WX-ray2.39B1-283[»]
4F70X-ray3.00B1-283[»]
4F7JX-ray2.60B1-283[»]
4F7LX-ray2.90B1-283[»]
4F7NX-ray2.65B1-283[»]
4F7SX-ray2.20B1-283[»]
4G6LX-ray2.70B1-283[»]
ProteinModelPortaliP24863.
SMRiP24863. Positions 1-257.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107333. 70 interactions.
DIPiDIP-32920N.
IntActiP24863. 48 interactions.
STRINGi9606.ENSP00000358222.

Chemistry

ChEMBLiCHEMBL3038474.

PTM databases

PhosphoSiteiP24863.

Polymorphism and mutation databases

BioMutaiCCNC.
DMDMi166214910.

Proteomic databases

MaxQBiP24863.
PaxDbiP24863.
PRIDEiP24863.

Protocols and materials databases

DNASUi892.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000520429; ENSP00000428982; ENSG00000112237. [P24863-1]
ENST00000523799; ENSP00000430014; ENSG00000112237. [P24863-2]
ENST00000523985; ENSP00000430119; ENSG00000112237. [P24863-2]
GeneIDi892.
KEGGihsa:892.
UCSCiuc003pqd.3. human. [P24863-1]

Organism-specific databases

CTDi892.
GeneCardsiGC06M099990.
HGNCiHGNC:1581. CCNC.
HPAiCAB010499.
MIMi123838. gene.
neXtProtiNX_P24863.
PharmGKBiPA26149.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5333.
GeneTreeiENSGT00760000119191.
HOGENOMiHOG000008007.
HOVERGENiHBG050836.
InParanoidiP24863.
KOiK15161.
OMAiAYTQEFP.
OrthoDBiEOG7WX08X.
PhylomeDBiP24863.

Enzyme and pathway databases

ReactomeiREACT_116145. PPARA activates gene expression.
REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
REACT_12627. Generic Transcription Pathway.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinkiP24863.

Miscellaneous databases

GeneWikiiCCNC_(gene).
GenomeRNAii892.
NextBioi3690.
PROiP24863.
SOURCEiSearch...

Gene expression databases

BgeeiP24863.
CleanExiHS_CCNC.
ExpressionAtlasiP24863. baseline and differential.
GenevestigatoriP24863.

Family and domain databases

Gene3Di1.10.472.10. 1 hit.
InterProiIPR013763. Cyclin-like.
IPR015429. Cyclin_C/H/T/L.
IPR006671. Cyclin_N.
[Graphical view]
PANTHERiPTHR10026. PTHR10026. 1 hit.
PfamiPF00134. Cyclin_N. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 2 hits.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of three novel human cyclins by rescue of G1 cyclin (Cln) function in yeast."
    Lew D.J., Dulic V., Reed S.I.
    Cell 66:1197-1206(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Molecular cloning and chromosomal localization of the human cyclin C (CCNC) and cyclin E (CCNE) genes: deletion of the CCNC gene in human tumors."
    Li H., Lahti J.M., Valentine M., Saito M., Reed S.I., Look A.T., Kidd V.J.
    Genomics 32:253-259(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  4. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Cyclin C/CDK8 is a novel CTD kinase associated with RNA polymerase II."
    Rickert P., Seghezzi W., Shanahan F., Cho H., Lees E.
    Oncogene 12:2631-2640(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "NAT, a human complex containing Srb polypeptides that functions as a negative regulator of activated transcription."
    Sun X., Zhang Y., Cho H., Rickert P., Lees E., Lane W.S., Reinberg D.
    Mol. Cell 2:213-222(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A FORM OF THE MEDIATOR COMPLEX.
  7. "A novel human SRB/MED-containing cofactor complex, SMCC, involved in transcription regulation."
    Gu W., Malik S., Ito M., Yuan C.-X., Fondell J.D., Zhang X., Martinez E., Qin J., Roeder R.G.
    Mol. Cell 3:97-108(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SMCC COMPLEX.
  8. "TFIIH is negatively regulated by cdk8-containing mediator complexes."
    Akoulitchev S., Chuikov S., Reinberg D.
    Nature 407:102-106(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MED6.
  9. "A set of consensus mammalian mediator subunits identified by multidimensional protein identification technology."
    Sato S., Tomomori-Sato C., Parmely T.J., Florens L., Zybailov B., Swanson S.K., Banks C.A.S., Jin J., Cai Y., Washburn M.P., Conaway J.W., Conaway R.C.
    Mol. Cell 14:685-691(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX.
  10. "Human Mediator enhances basal transcription by facilitating recruitment of transcription factor IIB during preinitiation complex assembly."
    Baek H.J., Kang Y.K., Roeder R.G.
    J. Biol. Chem. 281:15172-15181(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MED1 AND MED10.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "The structure of CDK8/CycC implicates specificity in the CDK/cyclin family and reveals interaction with a deep pocket binder."
    Schneider E.V., Bottcher J., Blaesse M., Neumann L., Huber R., Maskos K.
    J. Mol. Biol. 412:251-266(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH CDK8 AND INHIBITOR.

Entry informationi

Entry nameiCCNC_HUMAN
AccessioniPrimary (citable) accession number: P24863
Secondary accession number(s): B4DPZ1, Q9H543
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 15, 2008
Last modified: April 29, 2015
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.