Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

30-kDa cleavage and polyadenylation specificity factor 30

Gene

CPSF30

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation. May interact with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition (By similarity). Mediates poly(A) site selection (PubMed:23136375). Binds RNA in a calcium-dependent manner (PubMed:16500995, PubMed:17576667, PubMed:20214900). Exhibits endonuclease activity with an ability to nick and degrade linear as well as circular single-stranded RNA that leaves RNA 3' ends with hydroxyl groups, thus mediating processing of the pre-mRNA as a prelude to the polyadenylation (PubMed:17576667). Involved in the post-transcriptional control, probably via poly(A) addition, of the responses of plants to stress, especially genes mediating tolerance to oxidative stress (PubMed:18545667). Plays a role in the regulation of salicylic acid (SA) production via the control of messenger RNA 3' end processing, thus being a key component of programmed cell death and plant immune responses required for resistance to virulent Pseudomonas syringae pv tomato DC3000 (Pst) (PubMed:24706550).By similarity6 Publications

Enzyme regulationi

Endonuclease activity is repressed by the N-terminal domain of FIPS5 (PubMed:17576667). Nuclease activity is inhibited by zinc (>100 µM), cadmium in a progressive manner (50 percent activity at 1 mM Cd2+), and high salt levels (e.g. KCl or NaCl >600 mM). Stimulated by ATP in the presence of Zn2+, even at inhibitory zinc concentrations. Elevated temperatures prevent RNA-binding at 55 degrees Celsius, but endonuclease activity at 70 degrees Celsius. The sulfhydryl reagent dithiothreitol (DTT) inhibits both RNA-binding and nuclease activities (PubMed:18331819).2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri60 – 8728C3H1-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri88 – 11225C3H1-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri114 – 14128C3H1-type 3PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • calmodulin binding Source: TAIR
  • DNA binding Source: UniProtKB-KW
  • endonuclease activity Source: TAIR
  • endoribonuclease activity Source: TAIR
  • metal ion binding Source: UniProtKB-KW
  • RNA binding Source: UniProtKB

GO - Biological processi

  • mRNA 3'-end processing Source: UniProtKB
  • mRNA polyadenylation Source: TAIR
  • nucleic acid phosphodiester bond hydrolysis Source: GOC
  • plant-type hypersensitive response Source: UniProtKB-KW
  • positive regulation of plant-type hypersensitive response Source: UniProtKB
  • positive regulation of programmed cell death Source: UniProtKB
  • regulation of mRNA polyadenylation Source: UniProtKB
  • regulation of salicylic acid mediated signaling pathway Source: UniProtKB
  • response to oxidative stress Source: TAIR
  • RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
  • RNA processing Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Apoptosis, Hypersensitive response, mRNA processing, Plant defense

Keywords - Ligandi

DNA-binding, Metal-binding, RNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
30-kDa cleavage and polyadenylation specificity factor 301 Publication (EC:3.1.21.-1 Publication)
Alternative name(s):
Protein OXIDATIVE STRESS TOLERANT 61 Publication
Zinc finger CCCH domain-containing protein 11
Short name:
AtC3H11
Gene namesi
Name:CPSF301 Publication
Synonyms:OXT61 Publication
Ordered Locus Names:At1g30460Imported
ORF Names:F26G16.5Imported, F26G16.6Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G30460.

Subcellular locationi

  • Nucleus 2 Publications
  • Cytoplasm 1 Publication

  • Note: Localized in the cytoplasm when not in complex or when associated with CPSF100, but move to the nucleus when associated with the cleavage and polyadenylation specificity factor (CPSF) subunits CPSF160 or CPSF73s.1 Publication

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • mRNA cleavage and polyadenylation specificity factor complex Source: TAIR
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

In oxt6, small plants, especially at temperatures above 22 degrees Celsius. Enhanced tolerance to oxidative stress associated with elevated constitutive expression of genes that encode proteins containing thioredoxin- and glutaredoxin- related domains (PubMed:18545667). Altered poly(A) site choice (PubMed:18545667, PubMed:23136375). Suppresses cell death in lesion-mimic mutants (e.g. mips1, lsd1, mkk4, cpr5, and cat2). Enhanced sensitivity to virulent Pseudomonas syringae pv tomato DC3000 (Pst) (PubMed:24706550).3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi80 – 867CGFLHQF → STFLYQ: Loss of RNA-binding, but normal endonuclease activity. 1 Publication
Mutagenesisi108 – 1125CVYKH → QDSTYKY: Reduced endonuclease activity, but slightly increased RNA-binding. 1 Publication
Mutagenesisi134 – 1385CRYRH → STYRY: Loss of endonuclease activity, slighty reduced RNA-binding, and loss of interaction with FIPS5. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 63163130-kDa cleavage and polyadenylation specificity factor 30PRO_0000371970Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei610 – 6101PhosphoserineCombined sources
Modified residuei612 – 6121PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiA9LNK9.
PRIDEiA9LNK9.

PTM databases

iPTMnetiA9LNK9.

Expressioni

Tissue specificityi

Expressed in seedlings, roots, leaves, siliques, stems and flowers.2 Publications

Inductioni

Isoform 2 is up-regulated by exposure to the oxidative agent methyl viologen (MV).1 Publication

Gene expression databases

GenevisibleiA9LNK9. AT.

Interactioni

Subunit structurei

Component of the cleavage and polyadenylation specificity factor (CPSF) complex (Probable). Can form homodimers (PubMed:18479511). Binds to calmodulin (PubMed:16500995, PubMed:16897494). Forms a complex with cleavage and polyadenylation specificity factor (CPSF) subunits CPSF73-I, CPSF73-II, CPSF100, CPSF160, CFIS2, FIPS3, FIPS5, PAPS2, PAPS3, CLPS3, PCFS1, PCFS4, CSTF50 and CSTF77 (PubMed:16282318, PubMed:18479511, PubMed:20214900, PubMed:17576667, PubMed:19573236).Curated7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CPSF100Q9LKF93EBI-962511,EBI-1775444
CSTF77Q8GUP12EBI-962511,EBI-1775543
FIPS5F4KDH93EBI-962511,EBI-962489
PAPS2O823123EBI-962511,EBI-1775513

GO - Molecular functioni

  • calmodulin binding Source: TAIR

Protein-protein interaction databases

BioGridi25160. 14 interactions.
IntActiA9LNK9. 13 interactions.
MINTiMINT-7712508.
STRINGi3702.AT1G30460.1.

Structurei

3D structure databases

ProteinModelPortaliA9LNK9.
SMRiA9LNK9. Positions 62-120, 238-371.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini237 – 372136YTHPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi142 – 1476Poly-Pro
Compositional biasi199 – 21214Poly-GlnAdd
BLAST
Compositional biasi417 – 43115Poly-GluAdd
BLAST
Compositional biasi435 – 553119Gly-richAdd
BLAST

Sequence similaritiesi

Belongs to the CPSF4/YTH1 family.Curated
Contains 3 C3H1-type zinc fingers.PROSITE-ProRule annotation
Contains 1 YTH domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri60 – 8728C3H1-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri88 – 11225C3H1-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri114 – 14128C3H1-type 3PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1040. Eukaryota.
KOG1902. Eukaryota.
COG5084. LUCA.
HOGENOMiHOG000242019.
InParanoidiA9LNK9.
KOiK14404.
OMAiDYGECRE.
PhylomeDBiA9LNK9.

Family and domain databases

Gene3Di4.10.1000.10. 1 hit.
InterProiIPR007275. YTH_domain.
IPR000571. Znf_CCCH.
[Graphical view]
PfamiPF04146. YTH. 1 hit.
[Graphical view]
SMARTiSM00356. ZnF_C3H1. 3 hits.
[Graphical view]
SUPFAMiSSF90229. SSF90229. 1 hit.
PROSITEiPS50882. YTH. 1 hit.
PS50103. ZF_C3H1. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: A9LNK9-1) [UniParc]FASTAAdd to basket

Also known as: AtCPSF30-YT521B

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
MEDADGLSFD FEGGLDSGPV QNTASVPVAP PENSSSAAVN VAPTYDHSSA
60 70 80 90 100
TVAGAGRGRS FRQTVCRHWL RGLCMKGDAC GFLHQFDKAR MPICRFFRLY
110 120 130 140 150
GECREQDCVY KHTNEDIKEC NMYKLGFCPN GPDCRYRHAK LPGPPPPVEE
160 170 180 190 200
VLQKIQQLTT YNYGTNRLYQ ARNVAPQLQD RPQGQVPMQG QPQESGNLQQ
210 220 230 240 250
QQQQQPQQSQ HQVSQTLIPN PADQTNRTSH PLPQGVNRYF VVKSNNRENF
260 270 280 290 300
ELSVQQGVWA TQRSNEAKLN EAFDSVENVI LIFSVNRTRH FQGCAKMTSR
310 320 330 340 350
IGGYIGGGNW KHEHGTAQYG RNFSVKWLKL CELSFHKTRN LRNPYNENLP
360 370 380 390 400
VKISRDCQEL EPSVGEQLAS LLYLEPDSEL MAISIAAEAK REEEKAKGVN
410 420 430 440 450
PESRAENPDI VPFEDNEEEE EEEDESEEEE ESMAGGPQGR GRGRGIMWPP
460 470 480 490 500
QMPLGRGIRP MPGMGGFPLG VMGPGDAFPY GPGGYNGMPD PFGMGPRPFG
510 520 530 540 550
PYGPRFGGDF RGPVPGMMFP GRPPQQFPHG GYGMMGGGRG PHMGGMGNAP
560 570 580 590 600
RGGRPMYYPP ATSSARPGPS NRKTPERSDE RGVSGDQQNQ DASHDMEQFE
610 620 630
VGNSLRNEES ESEDEDEAPR RSRHGEGKKR R
Length:631
Mass (Da):70,015
Last modified:February 5, 2008 - v1
Checksum:i120272CD4142355F
GO
Isoform 2 (identifier: A9LNK9-2) [UniParc]FASTAAdd to basket

Also known as: AtCPSF30

The sequence of this isoform differs from the canonical sequence as follows:
     239-250: YFVVKSNNRENF → CVQSPKVFNWVL
     251-631: Missing.

Note: No experimental confirmation available.
Show »
Length:250
Mass (Da):27,969
Checksum:i0E404CD1EEB168A5
GO

Sequence cautioni

The sequence AAF19746.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei239 – 25012YFVVK…NRENF → CVQSPKVFNWVL in isoform 2. 1 PublicationVSP_037127Add
BLAST
Alternative sequencei251 – 631381Missing in isoform 2. 1 PublicationVSP_037128Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU250988 mRNA. Translation: ABX26048.1.
AY140901 mRNA. Translation: AAN41459.1.
AC009917 Genomic DNA. Translation: AAF19746.1. Sequence problems.
AC009917 Genomic DNA. Translation: AAF19747.1.
CP002684 Genomic DNA. Translation: AEE31221.1.
CP002684 Genomic DNA. Translation: AEE31222.1.
PIRiB86429.
C86429.
RefSeqiNP_001077629.1. NM_001084160.1. [A9LNK9-2]
NP_174334.2. NM_102782.3. [A9LNK9-1]
UniGeneiAt.40546.
At.69479.

Genome annotation databases

EnsemblPlantsiAT1G30460.1; AT1G30460.1; AT1G30460. [A9LNK9-1]
GeneIDi839925.
KEGGiath:AT1G30460.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU250988 mRNA. Translation: ABX26048.1.
AY140901 mRNA. Translation: AAN41459.1.
AC009917 Genomic DNA. Translation: AAF19746.1. Sequence problems.
AC009917 Genomic DNA. Translation: AAF19747.1.
CP002684 Genomic DNA. Translation: AEE31221.1.
CP002684 Genomic DNA. Translation: AEE31222.1.
PIRiB86429.
C86429.
RefSeqiNP_001077629.1. NM_001084160.1. [A9LNK9-2]
NP_174334.2. NM_102782.3. [A9LNK9-1]
UniGeneiAt.40546.
At.69479.

3D structure databases

ProteinModelPortaliA9LNK9.
SMRiA9LNK9. Positions 62-120, 238-371.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi25160. 14 interactions.
IntActiA9LNK9. 13 interactions.
MINTiMINT-7712508.
STRINGi3702.AT1G30460.1.

PTM databases

iPTMnetiA9LNK9.

Proteomic databases

PaxDbiA9LNK9.
PRIDEiA9LNK9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G30460.1; AT1G30460.1; AT1G30460. [A9LNK9-1]
GeneIDi839925.
KEGGiath:AT1G30460.

Organism-specific databases

TAIRiAT1G30460.

Phylogenomic databases

eggNOGiKOG1040. Eukaryota.
KOG1902. Eukaryota.
COG5084. LUCA.
HOGENOMiHOG000242019.
InParanoidiA9LNK9.
KOiK14404.
OMAiDYGECRE.
PhylomeDBiA9LNK9.

Miscellaneous databases

PROiA9LNK9.

Gene expression databases

GenevisibleiA9LNK9. AT.

Family and domain databases

Gene3Di4.10.1000.10. 1 hit.
InterProiIPR007275. YTH_domain.
IPR000571. Znf_CCCH.
[Graphical view]
PfamiPF04146. YTH. 1 hit.
[Graphical view]
SMARTiSM00356. ZnF_C3H1. 3 hits.
[Graphical view]
SUPFAMiSSF90229. SSF90229. 1 hit.
PROSITEiPS50882. YTH. 1 hit.
PS50103. ZF_C3H1. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Calmodulin interacts with and regulates the RNA-binding activity of an Arabidopsis polyadenylation factor subunit."
    Delaney K.J., Xu R., Zhang J., Li Q.Q., Yun K.-Y., Falcone D.L., Hunt A.G.
    Plant Physiol. 140:1507-1521(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
    Strain: cv. Columbia.
  2. "The 73 kD subunit of the cleavage and polyadenylation specificity factor (CPSF) complex affects reproductive development in Arabidopsis."
    Xu R., Zhao H., Dinkins R.D., Cheng X., Carberry G., Li Q.Q.
    Plant Mol. Biol. 61:799-815(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBUNIT, TISSUE SPECIFICITY.
  3. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "An Arabidopsis Fip1 homolog interacts with RNA and provides conceptual links with a number of other polyadenylation factor subunits."
    Forbes K.P., Addepalli B., Hunt A.G.
    J. Biol. Chem. 281:176-186(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, INTERACTION WITH FIPS5.
  6. "A novel endonuclease activity associated with the Arabidopsis ortholog of the 30-kDa subunit of cleavage and polyadenylation specificity factor."
    Addepalli B., Hunt A.G.
    Nucleic Acids Res. 35:4453-4463(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING, MUTAGENESIS OF 80-CYS--PHE-86; 108-CYS--HIS-112 AND 134-CYS--HIS-138, ENZYME REGULATION, INTERACTION WITH FIPS5.
  7. "Redox and heavy metal effects on the biochemical activities of an Arabidopsis polyadenylation factor subunit."
    Addepalli B., Hunt A.G.
    Arch. Biochem. Biophys. 473:88-95(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  8. "A polyadenylation factor subunit implicated in regulating oxidative signaling in Arabidopsis thaliana."
    Zhang J., Addepalli B., Yun K.Y., Hunt A.G., Xu R., Rao S., Li Q.Q., Falcone D.L.
    PLoS ONE 3:E2410-E2410(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INDUCTION BY METHYL VIOLOGEN.
  9. "Genome-wide analysis of CCCH zinc finger family in Arabidopsis and rice."
    Wang D., Guo Y., Wu C., Yang G., Li Y., Zheng C.
    BMC Genomics 9:44-44(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NOMENCLATURE.
  10. "Arabidopsis mRNA polyadenylation machinery: comprehensive analysis of protein-protein interactions and gene expression profiling."
    Hunt A.G., Xu R., Addepalli B., Rao S., Forbes K.P., Meeks L.R., Xing D., Mo M., Zhao H., Bandyopadhyay A., Dampanaboina L., Marion A., Von Lanken C., Li Q.Q.
    BMC Genomics 9:220-220(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, HOMODIMER, INTERACTION WITH CPSF100; CPSF160; CFIS2; CLPS3; CSTF77; CSTF50; PAPS2; PAPS3; PCFS1; PCFS4; FIPS3 AND FIPS5, GENE FAMILY, NOMENCLATURE.
  11. "Distinctive interactions of the Arabidopsis homolog of the 30 kD subunit of the cleavage and polyadenylation specificity factor (AtCPSF30) with other polyadenylation factor subunits."
    Rao S., Dinkins R.D., Hunt A.G.
    BMC Cell Biol. 10:51-51(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CPSF73-I; CPSF73-II; CPSF100 AND CPSF160.
  12. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
    Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
    Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-610 AND SER-612, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "The Arabidopsis ortholog of the 77 kDa subunit of the cleavage stimulatory factor (AtCstF-77) involved in mRNA polyadenylation is an RNA-binding protein."
    Bell S.A., Hunt A.G.
    FEBS Lett. 584:1449-1454(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CSTF77, RNA-BINDING.
  14. "A disulfide linkage in a CCCH zinc finger motif of an Arabidopsis CPSF30 ortholog."
    Addepalli B., Limbach P.A., Hunt A.G.
    FEBS Lett. 584:4408-4412(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF 134-CYS--HIS-138.
  15. "Genome-wide control of polyadenylation site choice by CPSF30 in Arabidopsis."
    Thomas P.E., Wu X., Liu M., Gaffney B., Ji G., Li Q.Q., Hunt A.G.
    Plant Cell 24:4376-4388(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  16. "The polyadenylation factor subunit CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR30: A key factor of programmed cell death and a regulator of immunity in Arabidopsis."
    Bruggeman Q., Garmier M., de Bont L., Soubigou-Taconnat L., Mazubert C., Benhamed M., Raynaud C., Bergounioux C., Delarue M.
    Plant Physiol. 165:732-746(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    Strain: cv. Columbia.

Entry informationi

Entry nameiCPSF_ARATH
AccessioniPrimary (citable) accession number: A9LNK9
Secondary accession number(s): Q9S9Q5, Q9S9Q6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: February 5, 2008
Last modified: June 8, 2016
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.