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Protein

mRNA 3'-end-processing protein RNA14

Gene

RNA14

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the cleavage factor IA (CFIA) complex, which is involved in the endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with the cleavage factor NAB4/CFIB and the cleavage and polyadenylation factor (CPF) complex.2 Publications

GO - Molecular functioni

  • protein heterodimerization activity Source: SGD

GO - Biological processi

  • mRNA cleavage Source: SGD
  • mRNA polyadenylation Source: SGD
  • response to DNA damage checkpoint signaling Source: SGD
Complete GO annotation...

Keywords - Biological processi

mRNA processing

Enzyme and pathway databases

BioCyciYEAST:G3O-32764-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
mRNA 3'-end-processing protein RNA14
Gene namesi
Name:RNA14
Ordered Locus Names:YMR061W
ORF Names:YM9796.14
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XIII

Organism-specific databases

CYGDiYMR061w.
EuPathDBiFungiDB:YMR061W.
SGDiS000004665. RNA14.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
  • mitochondrion Source: SGD
  • mRNA cleavage factor complex Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 677677mRNA 3'-end-processing protein RNA14PRO_0000205761Add
BLAST

Proteomic databases

MaxQBiP25298.
PaxDbiP25298.
PRIDEiP25298.

Interactioni

Subunit structurei

Component of the CFIA complex, which is composed of RNA14, RNA15, PCF11 and CLP1. Interacts with FIP1, PFS2, YSH1 and probably also with RNA15. Probably interacts with the phosphorylated CTD domain of RPB1/RNA polymerase II.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PCF11P3908112EBI-15632,EBI-12980
RNA15P252998EBI-15632,EBI-15640

Protein-protein interaction databases

BioGridi35236. 101 interactions.
DIPiDIP-1488N.
IntActiP25298. 41 interactions.
MINTiMINT-400599.

Structurei

Secondary structure

1
677
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi633 – 6419Combined sources
Helixi645 – 6484Combined sources
Helixi655 – 66410Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L9BNMR-B626-677[»]
ProteinModelPortaliP25298.
SMRiP25298. Positions 30-669.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati56 – 8833HAT 1Add
BLAST
Repeati90 – 12435HAT 2Add
BLAST
Repeati138 – 17033HAT 3Add
BLAST
Repeati181 – 21434HAT 4Add
BLAST
Repeati257 – 28933HAT 5Add
BLAST
Repeati298 – 33033HAT 6Add
BLAST

Sequence similaritiesi

Contains 6 HAT repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5107.
GeneTreeiENSGT00390000006758.
HOGENOMiHOG000000753.
KOiK14408.
OMAiYTKWENE.
OrthoDBiEOG79CZ7K.

Family and domain databases

Gene3Di1.25.40.10. 3 hits.
InterProiIPR003107. HAT.
IPR008847. Suf.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PfamiPF05843. Suf. 1 hit.
[Graphical view]
SMARTiSM00386. HAT. 8 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25298-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSSTTPDLL YPSADKVAEP SDNIHGDELR LRERIKDNPT NILSYFQLIQ
60 70 80 90 100
YLETQESYAK VREVYEQFHN TFPFYSPAWT LQLKGELARD EFETVEKILA
110 120 130 140 150
QCLSGKLENN DLSLWSTYLD YIRRKNNLIT GGQEARAVIV KAFQLVMQKC
160 170 180 190 200
AIFEPKSSSF WNEYLNFLEQ WKPFNKWEEQ QRIDMLREFY KKMLCVPFDN
210 220 230 240 250
LEKMWNRYTQ WEQEINSLTA RKFIGELSAE YMKARSLYQE WLNVTNGLKR
260 270 280 290 300
ASPINLRTAN KKNIPQPGTS DSNIQQLQIW LNWIKWEREN KLMLSEDMLS
310 320 330 340 350
QRISYVYKQG IQYMIFSAEM WYDYSMYISE NSDRQNILYT ALLANPDSPS
360 370 380 390 400
LTFKLSECYE LDNDSESVSN CFDKCTQTLL SQYKKIASDV NSGEDNNTEY
410 420 430 440 450
EQELLYKQRE KLTFVFCVYM NTMKRISGLS AARTVFGKCR KLKRILTHDV
460 470 480 490 500
YVENAYLEFQ NQNDYKTAFK VLELGLKYFQ NDGVYINKYL DFLIFLNKDS
510 520 530 540 550
QIKTLFETSV EKVQDLTQLK EIYKKMISYE SKFGNLNNVY SLEKRFFERF
560 570 580 590 600
PQENLIEVFT SRYQIQNSNL IKKLELTYMY NEEEDSYFSS GNGDGHHGSY
610 620 630 640 650
NMSSSDRKRL MEETGNNGNF SNKKFKRDSE LPTEVLDLLS VIPKRQYFNT
660 670
NLLDAQKLVN FLNDQVEIPT VESTKSG
Length:677
Mass (Da):79,960
Last modified:February 1, 1996 - v2
Checksum:i102433295FE7CD63
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73461 Genomic DNA. Translation: AAA21300.1.
Z49703 Genomic DNA. Translation: CAA89771.1.
BK006946 Genomic DNA. Translation: DAA09959.1.
PIRiS54561.
RefSeqiNP_013777.1. NM_001182559.1.

Genome annotation databases

EnsemblFungiiYMR061W; YMR061W; YMR061W.
GeneIDi855083.
KEGGisce:YMR061W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73461 Genomic DNA. Translation: AAA21300.1.
Z49703 Genomic DNA. Translation: CAA89771.1.
BK006946 Genomic DNA. Translation: DAA09959.1.
PIRiS54561.
RefSeqiNP_013777.1. NM_001182559.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L9BNMR-B626-677[»]
ProteinModelPortaliP25298.
SMRiP25298. Positions 30-669.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35236. 101 interactions.
DIPiDIP-1488N.
IntActiP25298. 41 interactions.
MINTiMINT-400599.

Proteomic databases

MaxQBiP25298.
PaxDbiP25298.
PRIDEiP25298.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR061W; YMR061W; YMR061W.
GeneIDi855083.
KEGGisce:YMR061W.

Organism-specific databases

CYGDiYMR061w.
EuPathDBiFungiDB:YMR061W.
SGDiS000004665. RNA14.

Phylogenomic databases

eggNOGiCOG5107.
GeneTreeiENSGT00390000006758.
HOGENOMiHOG000000753.
KOiK14408.
OMAiYTKWENE.
OrthoDBiEOG79CZ7K.

Enzyme and pathway databases

BioCyciYEAST:G3O-32764-MONOMER.

Miscellaneous databases

NextBioi978372.
PROiP25298.

Family and domain databases

Gene3Di1.25.40.10. 3 hits.
InterProiIPR003107. HAT.
IPR008847. Suf.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PfamiPF05843. Suf. 1 hit.
[Graphical view]
SMARTiSM00386. HAT. 8 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mutations in the yeast RNA14 and RNA15 genes result in an abnormal mRNA decay rate; sequence analysis reveals an RNA-binding domain in the RNA15 protein."
    Minvielle-Sebastia L., Winsor B., Bonneaud N., Lacroute F.
    Mol. Cell. Biol. 11:3075-3087(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 28383 / FL100 / VTT C-80102.
  2. Bonneaud N.
    Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "RNA14 and RNA15 proteins as components of a yeast pre-mRNA 3'-end processing factor."
    Minvielle-Sebastia L., Preker P.J., Keller W.
    Science 266:1702-1705(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Purification of the Saccharomyces cerevisiae cleavage/polyadenylation factor I. Separation into two components that are required for both cleavage and polyadenylation of mRNA 3' ends."
    Kessler M.M., Zhao J., Moore C.L.
    J. Biol. Chem. 271:27167-27175(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: COMPOSITION OF THE CFIA COMPLEX.
  7. "The major yeast poly(A)-binding protein is associated with cleavage factor IA and functions in premessenger RNA 3'-end formation."
    Minvielle-Sebastia L., Preker P.J., Wiederkehr T., Strahm Y., Keller W.
    Proc. Natl. Acad. Sci. U.S.A. 94:7897-7902(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE CFIA COMPLEX.
  8. "The WD-repeat protein pfs2p bridges two essential factors within the yeast pre-mRNA 3'-end-processing complex."
    Ohnacker M., Barabino S.M.L., Preker P.J., Keller W.
    EMBO J. 19:37-47(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FIP1; PFS2 AND YSH1.
  9. "Five subunits are required for reconstitution of the cleavage and polyadenylation activities of Saccharomyces cerevisiae cleavage factor I."
    Gross S., Moore C.
    Proc. Natl. Acad. Sci. U.S.A. 98:6080-6085(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE CFIA COMPLEX.
  10. "Independent functions of yeast Pcf11p in pre-mRNA 3' end processing and in transcription termination."
    Sadowski M., Dichtl B., Huebner W., Keller W.
    EMBO J. 22:2167-2177(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RBP1.
  11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRNA14_YEAST
AccessioniPrimary (citable) accession number: P25298
Secondary accession number(s): D6VZN5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: February 1, 1996
Last modified: July 22, 2015
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 5350 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

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.