Q12102

PR
Gene name
CFT2 (YDH1, YLR115W, L2946)
Protein name
Cleavage factor two protein 2
Names
105 kDa protein associated with polyadenylation factor I
Species
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
KEGG Pathway
sce:YLR115W
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

553-644 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

4 structures for Q12102

Entry ID Method Resolution Chain Position Source
2I7X X-ray 250 A A 1-717 PDB
7ZGQ EM 280 A C 1-720 PDB
7ZGR EM 260 A C 1-720 PDB
AF-Q12102-F1 Predicted AlphaFoldDB

16 variants for Q12102

Variant ID(s) Position Change Description Diseaes Association Provenance
s12-378127 48 E>K No SGRP
s12-378361 126 I>V No SGRP
s12-379145 387 D>G No SGRP
s12-379290 435 D>E No SGRP
s12-379576 531 A>P No SGRP
s12-379669 562 D>H No SGRP
s12-379694 570 S>N No SGRP
s12-379787 601 S>T No SGRP
s12-379795 604 I>V No SGRP
s12-379801 606 K>E No SGRP
s12-379916 644 I>T No SGRP
s12-379915 644 I>V No SGRP
s12-380249 755 K>R No SGRP
s12-380271 762 N>K No SGRP
s12-380404 807 K>E No SGRP
s12-380539 852 V>I No SGRP

No associated diseases with Q12102

3 regional properties for Q12102

Type Name Position InterPro Accession
domain FKBP-type peptidyl-prolyl cis-trans isomerase domain 165 - 251 IPR001179
domain Trigger factor, C-terminal 268 - 425 IPR008880
domain Trigger factor, ribosome-binding, bacterial 1 - 151 IPR008881

Functions

Description
EC Number
Subcellular Localization
  • Nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
mRNA cleavage and polyadenylation specificity factor complex A multisubunit complex that binds to the canonical AAUAAA hexamer and to U-rich upstream sequence elements on the pre-mRNA, thereby stimulating the otherwise weakly active and nonspecific polymerase to elongate efficiently RNAs containing a poly(A) signal.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

1 GO annotations of molecular function

Name Definition
RNA binding Binding to an RNA molecule or a portion thereof.

4 GO annotations of biological process

Name Definition
mRNA cleavage Any process in which a pre-mRNA or mRNA molecule is cleaved at specific sites or in a regulated manner.
mRNA polyadenylation The enzymatic addition of a sequence of 40-200 adenylyl residues at the 3' end of a eukaryotic mRNA primary transcript.
pre-mRNA cleavage required for polyadenylation The targeted, endonucleolytic cleavage of a pre-mRNA, required for polyadenylation of the 3' end. This cleavage is directed by binding sites near the 3' end of the mRNA and leaves a 3' hydoxyl end which then becomes a target for adenylation.
termination of RNA polymerase II transcription, poly(A)-coupled An RNA polymerase II transcription termination process in which cleavage and polyadenylylation of the mRNA 3' end are coupled to transcription termination.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9V3D6 Cpsf100 Probable cleavage and polyadenylation specificity factor subunit 2 Drosophila melanogaster (Fruit fly) PR
Q9P2I0 CPSF2 Cleavage and polyadenylation specificity factor subunit 2 Homo sapiens (Human) PR
O35218 Cpsf2 Cleavage and polyadenylation specificity factor subunit 2 Mus musculus (Mouse) PR
O17403 cpsf-2 Probable cleavage and polyadenylation specificity factor subunit 2 Caenorhabditis elegans PR
10 20 30 40 50 60
MTYKYNCCDD GSGTTVGSVV RFDNVTLLID PGWNPSKVSY EQCIKYWEKV IPEIDVIILS
70 80 90 100 110 120
QPTIECLGAH SLLYYNFTSH FISRIQVYAT LPVINLGRVS TIDSYASAGV IGPYDTNKLD
130 140 150 160 170 180
LEDIEISFDH IVPLKYSQLV DLRSRYDGLT LLAYNAGVCP GGSIWCISTY SEKLVYAKRW
190 200 210 220 230 240
NHTRDNILNA ASILDATGKP LSTLMRPSAI ITTLDRFGSS QPFKKRSKIF KDTLKKGLSS
250 260 270 280 290 300
DGSVIIPVDM SGKFLDLFTQ VHELLFESTK INAHTQVPVL ILSYARGRTL TYAKSMLEWL
310 320 330 340 350 360
SPSLLKTWEN RNNTSPFEIG SRIKIIAPNE LSKYPGSKIC FVSEVGALIN EVIIKVGNSE
370 380 390 400 410 420
KTTLILTKPS FECASSLDKI LEIVEQDERN WKTFPEDGKS FLCDNYISID TIKEEPLSKE
430 440 450 460 470 480
ETEAFKVQLK EKKRDRNKKI LLVKRESKKL ANGNAIIDDT NGERAMRNQD ILVENVNGVP
490 500 510 520 530 540
PIDHIMGGDE DDDEEEENDN LLNLLKDNSE KSAAKKNTEV PVDIIIQPSA ASKHKMFPFN
550 560 570 580 590 600
PAKIKKDDYG TVVDFTMFLP DDSDNVNQNS RKRPLKDGAK TTSPVNEEDN KNEEEDGYNM
610 620 630 640 650 660
SDPISKRSKH RASRYSGFSG TGEAENFDNL DYLKIDKTLS KRTISTVNVQ LKCSVVILNL
670 680 690 700 710 720
QSLVDQRSAS IIWPSLKSRK IVLSAPKQIQ NEEITAKLIK KNIEVVNMPL NKIVEFSTTI
730 740 750 760 770 780
KTLDISIDSN LDNLLKWQRI SDSYTVATVV GRLVKESLPQ VNNHQKTASR SKLVLKPLHG
790 800 810 820 830 840
SSRSHKTGAL SIGDVRLAQL KKLLTEKNYI AEFKGEGTLV INEKVAVRKI NDAETIIDGT
850
PSELFDTVKK LVTDMLAKI