Basic Information
Name | Protein CFT1 (Cleavage factor two protein 1) |
Uniprot ID | Q06632 |
Systematic gene name | YDR301W |
Standard gene name | CFT1 |
Gene names | CFT1 YHH1 YDR301W |
Description from SGD | YDR301W CFT1 SGDID:S000002709, Chr IV from 1063352-1067425, Genome Release 64-3-1, Verified ORF, "RNA-binding subunit of the mRNA cleavage and polyadenylation factor; involved in poly(A) site recognition and required for both pre-mRNA cleavage and polyadenylation, 51% sequence similarity with mammalian AAUAA-binding subunit of CPSF" |
Protein length | 1357 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MNVYDDVLDA TVVSHSLATH FTTSDYEELL VVRTNILSVY RPTRDGKLYL
TDEFKFHGLI TDIGLIPQKD SPLSCLLLCT GVAKISILKF NTLTNSIDTL
SLHYYEGKFK GKSLVELAKI STLRMDPGSS CALLFNNDII AFLPFHVNKN
DDDEEEEDED ENIDDSELIH SMNQKSQGTN TFNKRKRTKL GDKFTAPSVV
LVASELYEGA KNIIDIQFLK NFTKPTIALL YQPKLVWAGN TTISKLPTQY
VILTLNIQPA ESATKIESTT IAFVKELPWD LHTIVPVSNG AIIVGTNELA
FLDNTGVLQS TVLLNSFADK ELQKTKIINN SSLEIMFREK NTTSIWIPSS
KSKNGGSNND ETLLLMDLKS NIYYIQMEAE GRLLIKFDIF KLPIVNDLLK
ENSNPKCITR LNATNSNKNM DLFIGFGSGN ALVLRLNNLK STIETREAHN
PSSGTNSLMD INDDDDEEMD DLYADEAPEN GLTTNDSKGT VETVQPFDIE
LLSSLRNVGP ITSLTVGKVS SIDDVVKGLP NPNKNEYSLV ATSGNGSGSH
LTVIQTSVQP EIELALKFIS ITQIWNLKIK GRDRYLITTD STKSRSDIYE
SDNNFKLHKG GRLRRDATTV YISMFGEEKR IIQVTTNHLY LYDTHFRRLT
TIKFDYEVIH VSVMDPYILV TVSRGDIKIF ELEEKNKRKL LKVDLPEILN
EMVITSGLIL KSNMCNEFLI GLSKSQEEQL LFTFVTADNQ IIFFTKDHND
RIFQLNGVDQ LNESLYISTY QLGDEIVPDP SIKQVMINKL GHDNKEEYLT
ILTFGGEIYQ YRKLPQRRSR FYRNVTRNDL AITGAPDNAY AKGVSSIERI
MHYFPDYNGY SVIFVTGSVP YILIKEDDST PKIFKFGNIP LVSVTPWSER
SVMCVDDIKN ARVYTLTTDN MYYGNKLPLK QIKISNVLDD YKTLQKLVYH
ERAQLFLVSY CKRVPYEALG EDGEKVIGYD ENVPHAEGFQ SGILLINPKS
WKVIDKIDFP KNSVVNEMRS SMIQINSKTK RKREYIIAGV ANATTEDTPP
TGAFHIYDVI EVVPEPGKPD TNYKLKEIFQ EEVSGTVSTV CEVSGRFMIS
QSQKVLVRDI QEDNSVIPVA FLDIPVFVTD SKSFGNLLII GDAMQGFQFI
GFDAEPYRMI SLGRSMSKFQ TMSLEFLVNG GDMYFAATDA DRNVHVLKYA
PDEPNSLSGQ RLVHCSSFTL HSTNSCMMLL PRNEEFGSPQ VPSFQNVGGQ
VDGSVFKIVP LSEEKYRRLY VIQQQIIDRE LQLGGLNPRM ERLANDFYQM
GHSMRPMLDF NVIRRFCGLA IDRRKSIAQK AGRHAHFEAW RDIINIEFSM
RSLCQGK
TDEFKFHGLI TDIGLIPQKD SPLSCLLLCT GVAKISILKF NTLTNSIDTL
SLHYYEGKFK GKSLVELAKI STLRMDPGSS CALLFNNDII AFLPFHVNKN
DDDEEEEDED ENIDDSELIH SMNQKSQGTN TFNKRKRTKL GDKFTAPSVV
LVASELYEGA KNIIDIQFLK NFTKPTIALL YQPKLVWAGN TTISKLPTQY
VILTLNIQPA ESATKIESTT IAFVKELPWD LHTIVPVSNG AIIVGTNELA
FLDNTGVLQS TVLLNSFADK ELQKTKIINN SSLEIMFREK NTTSIWIPSS
KSKNGGSNND ETLLLMDLKS NIYYIQMEAE GRLLIKFDIF KLPIVNDLLK
ENSNPKCITR LNATNSNKNM DLFIGFGSGN ALVLRLNNLK STIETREAHN
PSSGTNSLMD INDDDDEEMD DLYADEAPEN GLTTNDSKGT VETVQPFDIE
LLSSLRNVGP ITSLTVGKVS SIDDVVKGLP NPNKNEYSLV ATSGNGSGSH
LTVIQTSVQP EIELALKFIS ITQIWNLKIK GRDRYLITTD STKSRSDIYE
SDNNFKLHKG GRLRRDATTV YISMFGEEKR IIQVTTNHLY LYDTHFRRLT
TIKFDYEVIH VSVMDPYILV TVSRGDIKIF ELEEKNKRKL LKVDLPEILN
EMVITSGLIL KSNMCNEFLI GLSKSQEEQL LFTFVTADNQ IIFFTKDHND
RIFQLNGVDQ LNESLYISTY QLGDEIVPDP SIKQVMINKL GHDNKEEYLT
ILTFGGEIYQ YRKLPQRRSR FYRNVTRNDL AITGAPDNAY AKGVSSIERI
MHYFPDYNGY SVIFVTGSVP YILIKEDDST PKIFKFGNIP LVSVTPWSER
SVMCVDDIKN ARVYTLTTDN MYYGNKLPLK QIKISNVLDD YKTLQKLVYH
ERAQLFLVSY CKRVPYEALG EDGEKVIGYD ENVPHAEGFQ SGILLINPKS
WKVIDKIDFP KNSVVNEMRS SMIQINSKTK RKREYIIAGV ANATTEDTPP
TGAFHIYDVI EVVPEPGKPD TNYKLKEIFQ EEVSGTVSTV CEVSGRFMIS
QSQKVLVRDI QEDNSVIPVA FLDIPVFVTD SKSFGNLLII GDAMQGFQFI
GFDAEPYRMI SLGRSMSKFQ TMSLEFLVNG GDMYFAATDA DRNVHVLKYA
PDEPNSLSGQ RLVHCSSFTL HSTNSCMMLL PRNEEFGSPQ VPSFQNVGGQ
VDGSVFKIVP LSEEKYRRLY VIQQQIIDRE LQLGGLNPRM ERLANDFYQM
GHSMRPMLDF NVIRRFCGLA IDRRKSIAQK AGRHAHFEAW RDIINIEFSM
RSLCQGK
Legend
- X Phoshorylation
- X Ubiquitination
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[914, 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) |
[914, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[915, 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) |
[915, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[917, 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) |
[917, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[918, 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) |
[918, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[942, Ubi] | 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) |