Basic Information

NameCyclin CCL1
Uniprot IDP37366
Systematic gene nameYPR025C
Standard gene nameCCL1
Gene namesCCL1 YPR025C YP9367.05C
Description from SGDYPR025C CCL1 SGDID:S000006229, Chr XVI from 614558-613377, Genome Release 64-3-1, reverse complement, Verified ORF, "Cyclin partner of the cyclin-dependent kinase (CDK) Kin28p; regulates the activity of Kin28p, a TFIIH-associated carboxy-terminal domain (CTD) kinase that facilitates recruitment of mRNA 5'-capping and polyadenylation factors to the RNAPII holoenzyme complex, and has a minor role in RNAPII transcription; subunit of TFIIK, a TFIIH subassembly; human homolog CCNH allows growth of a yeast ccl1 temperature-sensitive mutant at restrictive temperature"
Protein length393
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MTDIQLNGKS TLDTPSATMS AKEKEAKLKS ADENNKPPNY KRISDDDLYR
HSSQYRMWSY TKDQLQEKRV DTNARAIAYI EENLLKFREA HNLTEEEIKV
LEAKAIPLTM EEELDLVNFY AKKVQVIAQH LNLPTEVVAT AISFFRRFFL
ENSVMQIDPK SIVHTTIFLA CKSENYFISV DSFAQKAKST RDSVLKFEFK
LLESLKFSLL NHHPYKPLHG FFLDIQNVLY GKVDLNYMGQ IYDRCKKRIT
AALLTDVVYF YTPPQITLAT LLIEDEALVT RYLETKFPSR EGSQESVPGN
EKEEPQNDAS TTEKNKEKST ESEEYSIDSA KLLTIIRECK SIIEDCKPPS
TEEAKKIAAK NYYCQNPSTL IQKLKRKLNG EDTSSTVEKK QKT

Legend

  • X Phoshorylation

Structure

Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.


Use imported representation

Loading structure from server... It may take a while.

If you believe something went wrong, please make sure PDB ID is correct.
Please also make sure that WebGL is enabled in your browser.

References

[14, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[14, Phos]Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications)
[44, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[193, Phos]Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications)
[193, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[293, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[293, Phos]Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications)
[293, Phos]Swaney, D.L.,  Beltrao, P.,  Starita, L.,  Guo, A.,  Rush, J.,  Fields, S.,  Krogan, N.J.,  Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications)
[293, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[296, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[296, Phos]Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications)
[296, Phos]Swaney, D.L.,  Beltrao, P.,  Starita, L.,  Guo, A.,  Rush, J.,  Fields, S.,  Krogan, N.J.,  Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications)
[296, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[319, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[319, Phos]Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications)
[319, Phos]Breitkreutz, A.,  Choi, H.,  Sharom, J.R.,  Boucher, L.,  Neduva, V.,  Larsen, B.,  Lin, Z.Y.,  Breitkreutz, B.J.,  Stark, C.,  Liu, G., Ahn, J.,  Dewar-Darch, D.,  Reguly, T.,  Tang, X.,  Almeida, R.,  Qin, Z.S.,  Pawson, T.,  Gingras, A.C.,  Nesvizhskii, A.I.,  Tyers, M. (2010). A global protein kinase and phosphatase interaction network in yeast. Science 328: 1043-1046. (Publication) (All modifications)
[319, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[320, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)