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protein coding gene - uaf2 (SPAP8A3.06) - U2 small nuclear RNA auxiliary factor small subunit, U2AF-23

Gene summary

Standard name
uaf2
Systematic ID
SPAP8A3.06
Product
U2 small nuclear RNA auxiliary factor small subunit, U2AF-23
Organism
Schizosaccharomyces pombe (fission yeast)
Synonyms
ods2
UniProt ID
Q09176
Characterisation status
biological role published
Feature type
mRNA gene
Genomic location
chromosome I: 5325594..5326435 forward strand

Annotation

Complementation

PBO:0016542 - functionally complemented by human U2AF1

References:

PBO:0002924 - functionally complemented by human U2AF35

GO biological process

GO:0000389 - mRNA 3'-splice site recognition

References:

GO:0045292 - mRNA cis splicing, via spliceosome

References:

GO cellular component

GO:0000243 - commitment complex

References:

GO:0005829 - cytosol

References:

GO:0005634 - nucleus

References:

GO:0071004 - U2-type prespliceosome

References:

GO:0089701 - U2AF complex

References:

GO molecular function

GO:0046872 - metal ion binding

References:

GO:0030628 - pre-mRNA 3'-splice site binding

References:

GO:0005515 - protein binding

References:

Modification

MOD:00046 - O-phospho-L-serine

References:

MOD:00047 - O-phospho-L-threonine

References:

MOD:01148 - ubiquitinylated lysine

References:

Protein features

PBO:0111764 - rrm RNA recognition motif

PBO:0111777 - zf-CCCH type

PBO:0111743 - zinc finger protein

Qualitative gene expression

PomGeneEx:0000019 - protein level decreased

References:

PomGeneEx:0000011 - RNA level increased

References:

Quantitative gene expression

PBO:0006310 - protein level

References:

PBO:0011963 - RNA level

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Single locus phenotype

FYPO:0003412 - decreased chromatin silencing at centromere outer repeat

References:

Genotypes:

FYPO:0008053 - decreased intron acceptor binding

References:

Genotypes:

FYPO:0003029 - decreased mRNA splicing, via spliceosome

References:

Genotypes:

FYPO:0002134 - decreased protein-RNA interaction

References:

Genotypes:

FYPO:0001355 - decreased vegetative cell population growth

References:

Genotypes:

FYPO:0003669 - exon skipping

References:

Genotypes:

FYPO:0006926 - increased nucleus:cytoplasm ratio

References:

Genotypes:

FYPO:0001908 - increased pre-mRNA level

References:

Genotypes:

FYPO:0001490 - inviable elongated vegetative cell

References:

Genotypes:

FYPO:0002061 - inviable vegetative cell population

References:

Genotypes:

FYPO:0002273 - inviable vegetative cell with abnormal cell morphology

References:

Genotypes:

FYPO:0003620 - normal pre-mRNA level

References:

Genotypes:

FYPO:0000833 - normal protein level during vegetative growth

References:

Genotypes:

FYPO:0000703 - normal protein-protein interaction

References:

Genotypes:

FYPO:0002357 - normal protein-RNA interaction

References:

Genotypes:

FYPO:0001357 - normal vegetative cell population growth

References:

Genotypes:

FYPO:0000084 - sensitive to 6-azauracil

References:

Genotypes:

FYPO:0003670 - sensitive to mycophenolic acid

References:

Genotypes:

FYPO:0002459 - viable branched, elongated vegetative cell

References:

Genotypes:

FYPO:0002060 - viable vegetative cell population

References:

Genotypes:

Taxonomic conservation

PBO:0011065 - conserved in eukaryotes

PBO:0011071 - conserved in eukaryotes only

PBO:0011064 - conserved in fungi

PBO:0011069 - conserved in metazoa

PBO:0011070 - conserved in vertebrates

PBO:0000055 - no apparent S. cerevisiae ortholog

PBO:0006222 - predominantly single copy (one to one)

Protein features

IDNameInterPro nameDB name
PF00642zf-CCCHZnf_CCCHPFAM
PF00076RRM_1RRM_domPFAM
cd12538RRM_U2AF35CDD
PS50102RRMRRM_domPROSITE_PROFILES
PS50103ZF_C3H1Znf_CCCHPROSITE_PROFILES
SM00361rrm2_1RRM_euk-typeSMART
SM00356c3hfinal6Znf_CCCHSMART
PR01848U2AUXFACTORU2AF_smallPRINTS
G3DSA:3.30.70.330:FF:000066FUNFAM
SSF54928RNA-binding domain, RBDRBD_domain_sfSUPERFAMILY
G3DSA:3.30.70.330Nucleotide-bd_a/b_plait_sfGENE3D
PTHR12620U2 SNRNP AUXILIARY FACTOR, SMALL SUBUNITU2AF_smallPANTHER
mobidb-lite-Disorderdisorder_predictionMOBIDB-Disorder

Orthologs

References / Literature

PMID:32958768 - Elucidation of the aberrant 3' splice site selection by cancer-associated mutations on the U2AF1.
Yoshida H et al. Nat Commun 2020 Sep 21;11(1):4744
PMID:30726745 - Fission Yeast NDR/LATS Kinase Orb6 Regulates Exocytosis via Phosphorylation of the Exocyst Complex.
Tay YD et al. Cell Rep 2019 Feb 05;26(6):1654-1667.e7
PMID:21511999 - Comparative functional genomics of the fission yeasts.
Rhind N et al. Science 2011 May 20;332(6032):930-6
PMID:10923022 - Mutations in the large subunit of U2AF disrupt pre-mRNA splicing, cell cycle progression and nuclear structure.
Beales M et al. Yeast 2000 Aug;16(11):1001-13
PMID:15548596 - Analysis of mutant phenotypes and splicing defects demonstrates functional collaboration between the large and small subunits of the essential splicing factor U2AF in vivo.
Webb CJ et al. Mol Biol Cell 2005 Feb;16(2):584-96
GO_REF:0000002 - Comments
PMID:23697806 - A genome-wide resource of cell cycle and cell shape genes of fission yeast.
Hayles J et al. Open Biol 2013 May 22;3(5):130053
PMID:26302002 - Cwf16p Associating with the Nineteen Complex Ensures Ordered Exon Joining in Constitutive Pre-mRNA Splicing in Fission Yeast.
Sasaki-Haraguchi N et al. PLoS One 2015;10(8):e0136336
PMID:28446597 - The histone variant H2A.Z promotes splicing of weak introns.
Nissen KE et al. Genes Dev 2017 Apr 01;31(7):688-701
PMID:39705284 - Proteomic and phosphoproteomic analyses reveal that TORC1 is reactivated by pheromone signaling during sexual reproduction in fission yeast.
Bérard M et al. PLoS Biol 2024 Dec 20;22(12):e3002963
PMID:12374752 - Pre-spliceosome formation in S.pombe requires a stable complex of SF1-U2AF(59)-U2AF(23).
Huang T et al. EMBO J 2002 Oct 15;21(20):5516-26
PMID:11686295 - Conserved Wat1/Pop3 WD-repeat protein of fission yeast secures genome stability through microtubule integrity and may be involved in mRNA maturation.
Ochotorena IL et al. J Cell Sci 2001 Aug;114(Pt 16):2911-20
PMID:32101745 - Dense Transposon Integration Reveals Essential Cleavage and Polyadenylation Factors Promote Heterochromatin Formation.
Lee SY et al. Cell Rep 2020 Feb 25;30(8):2686-2698.e8
PMID:22681890 - Hierarchical modularity and the evolution of genetic interactomes across species.
Ryan CJ et al. Mol Cell 2012 Jun 08;46(5):691-704
PMID:9371883 - Molecular characterization of a novel fission yeast gene spUAP2 that interacts with the splicing factor spU2AF59.
McKinney R et al. Curr Genet 1997 Nov;32(5):323-30
PMID:26215567 - A novel 3' splice site recognition by the two zinc fingers in the U2AF small subunit.
Yoshida H et al. Genes Dev 2015 Aug 01;29(15):1649-60
PMID:30759079 - A systematic genetic screen identifies essential factors involved in nuclear size control.
Cantwell H et al. PLoS Genet 2019 Feb;15(2):e1007929
PMID:39367033 - Quantitative proteomics and phosphoproteomics profiling of meiotic divisions in the fission yeast Schizosaccharomyces pombe.
Sivakova B et al. Sci Rep 2024 Oct 04;14(1):23105
PMID:15121844 - The splicing factor U2AF small subunit is functionally conserved between fission yeast and humans.
Webb CJ et al. Mol Cell Biol 2004 May;24(10):4229-40
PMID:20473289 - Analysis of a genome-wide set of gene deletions in the fission yeast Schizosaccharomyces pombe.
Kim DU et al. Nat Biotechnol 2010 Jun;28(6):617-623
PMID:8657565 - The small subunit of the splicing factor U2AF is conserved in fission yeast.
Wentz-Hunter K et al. Nucleic Acids Res 1996 May 15;24(10):1849-54
PMID:23695164 - Cross-species protein interactome mapping reveals species-specific wiring of stress response pathways.
Das J et al. Sci Signal 2013 May 21;6(276):ra38
PMID:26771498 - A Proteome-wide Fission Yeast Interactome Reveals Network Evolution Principles from Yeasts to Human.
Vo TV et al. Cell 2016 Jan 14;164(1-2):310-323
PMID:24713849 - Post-transcriptional regulation of meiotic genes by a nuclear RNA silencing complex.
Egan ED et al. RNA 2014 Jun;20(6):867-81
PMID:24223771 - New insights into the RNA-based mechanism of action of the anticancer drug 5'-fluorouracil in eukaryotic cells.
Mojardín L et al. PLoS One 2013;8(11):e78172
PMID:25720772 - Quantitative phosphoproteomics reveals pathways for coordination of cell growth and division by the conserved fission yeast kinase pom1.
Kettenbach AN et al. Mol Cell Proteomics 2015 May;14(5):1275-87
PMID:11414703 - The fission yeast ortholog of the coregulator SKIP interacts with the small subunit of U2AF.
Ambrozková M et al. Biochem Biophys Res Commun 2001 Jun 29;284(5):1148-54
PMID:16823372 - ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe.
Matsuyama A et al. Nat Biotechnol 2006 Jul;24(7):841-7
PMID:24763107 - Absolute proteome and phosphoproteome dynamics during the cell cycle of Schizosaccharomyces pombe (Fission Yeast).
Carpy A et al. Mol Cell Proteomics 2014 Aug;13(8):1925-36
PMID:40015273 - A comprehensive Schizosaccharomyces pombe atlas of physical transcription factor interactions with proteins and chromatin.
Skribbe M et al. Mol Cell 2025 Feb 19;
PMID:24013502 - Epe1 recruits BET family bromodomain protein Bdf2 to establish heterochromatin boundaries.
Wang J et al. Genes Dev 2013 Sep 01;27(17):1886-902
PMID:23101633 - Quantitative analysis of fission yeast transcriptomes and proteomes in proliferating and quiescent cells.
Marguerat S et al. Cell 2012 Oct 26;151(3):671-83
PMID:9671485 - A potential role for U2AF-SAP 155 interactions in recruiting U2 snRNP to the branch site.
Gozani O et al. Mol Cell Biol 1998 Aug;18(8):4752-60
PMID:17130122 - Mutations in the SF1-U2AF59-U2AF23 complex cause exon skipping in Schizosaccharomyces pombe.
Haraguchi N et al. J Biol Chem 2007 Jan 26;282(4):2221-8
PMID:37970674 - SUMOylation regulates Lem2 function in centromere clustering and silencing.
Strachan J et al. J Cell Sci 2023 Dec 01;136(23)
PMID:33823663 - A TOR (target of rapamycin) and nutritional phosphoproteome of fission yeast reveals novel targets in networks conserved in humans.
Halova L et al. Open Biol 2021 Apr;11(4):200405
PMID:28947618 - Sde2 is an intron-specific pre-mRNA splicing regulator activated by ubiquitin-like processing.
Thakran P et al. EMBO J 2018 Jan 04;37(1):89-101