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protein coding gene - pli1 (SPAC1687.05) - SUMO E3 ligase Pli1

Gene summary

Standard name
pli1
Systematic ID
SPAC1687.05
Product
SUMO E3 ligase Pli1
Organism
Schizosaccharomyces pombe (fission yeast)
UniProt ID
O94451
ORFeome ID
28/28A05
Characterisation status
biological role published
Feature type
mRNA gene
Genomic location
chromosome I: 908696..911854 forward strand

Annotation

GO biological process

GO:0072766 - centromere clustering at the mitotic interphase nuclear envelope

References:

GO:0030999 - linear element assembly

References:

GO:0036299 - non-recombinational interstrand cross-link repair

References:

GO:0016925 - protein sumoylation

References:

GO:0007131 - reciprocal meiotic recombination

References:

GO:0031297 - replication fork processing

References:

GO:0120290 - stalled replication fork localization to nuclear periphery

References:

GO cellular component

GO:0005634 - nucleus

References:

GO:0035861 - site of double-strand break

References:

GO:0106068 - SUMO ligase complex

References:

GO molecular function

GO:0005515 - protein binding

References:

GO:0061665 - SUMO ligase activity

References:

GO:0008270 - zinc ion binding

References:

Modification

MOD:00046 - O-phospho-L-serine

References:

MOD:00047 - O-phospho-L-threonine

References:

MOD:00696 - phosphorylated residue

References:

MOD:01149 - sumoylated lysine

References:

MOD:01148 - ubiquitinylated lysine

References:

Multi-locus phenotype

FYPO:0000204 - abnormal mRNA export from nucleus

References:

Genotypes:

FYPO:0000278 - decreased cell population growth following spore germination

References:

Genotypes:

FYPO:0001407 - decreased cell population growth on glucose carbon source

References:

Genotypes:

FYPO:0005630 - decreased cellular HMW SUMO conjugate level

References:

Genotypes:

FYPO:0006800 - decreased centromere clustering at nuclear periphery during mitotic interphase

References:

Genotypes:

FYPO:0003411 - decreased chromatin silencing at centromere inner repeat

References:

Genotypes:

FYPO:0007532 - decreased replication fork colocalization with nuclear pore complex

References:

Genotypes:

FYPO:0004003 - delayed onset of replication fork processing

References:

Genotypes:

FYPO:0002019 - elongated telomeres during vegetative growth

References:

Genotypes:

FYPO:0005629 - increased cellular HMW SUMO conjugate level

References:

Genotypes:

FYPO:0000614 - increased duration of mitotic S phase

References:

Genotypes:

FYPO:0005619 - increased level of sumoylated protein in cell

References:

Genotypes:

FYPO:0002082 - increased protein ubiquitination during vegetative growth

References:

Genotypes:

FYPO:0002150 - inviable spore population

References:

Genotypes:

FYPO:0002061 - inviable vegetative cell population

References:

Genotypes:

FYPO:0000969 - normal growth during cellular response to UV

References:

Genotypes:

FYPO:0001690 - normal growth on camptothecin

References:

Genotypes:

FYPO:0000833 - normal protein level during vegetative growth

References:

Genotypes:

FYPO:0006320 - normal replication slippage during replication fork processing

References:

Genotypes:

FYPO:0002687 - normal telomere length during vegetative growth

References:

Genotypes:

FYPO:0000085 - sensitive to camptothecin

References:

Genotypes:

FYPO:0000102 - sensitive to cisplatin

References:

Genotypes:

FYPO:0000088 - sensitive to hydroxyurea

References:

Genotypes:

FYPO:0000089 - sensitive to methyl methanesulfonate

References:

Genotypes:

FYPO:0000091 - sensitive to thiabendazole

References:

Genotypes:

FYPO:0000268 - sensitive to UV during vegetative growth

References:

Genotypes:

FYPO:0001234 - slow vegetative cell population growth

References:

Genotypes:

FYPO:0002060 - viable vegetative cell population

References:

Genotypes:

Protein features

PBO:0111804 - SAP domain

PBO:0111803 - zf-MIZ

PBO:0111743 - zinc finger protein

Quantitative gene expression

PBO:0006310 - protein level

References:

PBO:0011963 - RNA level

References:

Single locus phenotype

FYPO:0000443 - abnormal protein localization during vegetative growth

References:

Genotypes:

FYPO:0000909 - abnormal protein localization to linear element

References:

Genotypes:

FYPO:0000544 - abolished protein modification during vegetative growth

References:

Genotypes:

FYPO:0005934 - abolished protein sumoylation during vegetative growth

References:

Genotypes:

FYPO:0005630 - decreased cellular HMW SUMO conjugate level

References:

Genotypes:

FYPO:0006800 - decreased centromere clustering at nuclear periphery during mitotic interphase

References:

Genotypes:

FYPO:0003217 - decreased chromatin silencing at centromere central core

References:

Genotypes:

FYPO:0003411 - decreased chromatin silencing at centromere inner repeat

References:

Genotypes:

FYPO:0003412 - decreased chromatin silencing at centromere outer repeat

References:

Genotypes:

FYPO:0002827 - decreased chromatin silencing at silent mating-type cassette

References:

Genotypes:

FYPO:0002775 - decreased level of sumoylated protein in cell

References:

Genotypes:

FYPO:0000485 - decreased meiotic recombination

References:

Genotypes:

FYPO:0002778 - decreased protein sumoylation during vegetative growth

References:

Genotypes:

FYPO:0001645 - decreased protein-protein interaction

References:

Genotypes:

FYPO:0007532 - decreased replication fork colocalization with nuclear pore complex

References:

Genotypes:

FYPO:0000584 - decreased sporulation frequency

References:

Genotypes:

FYPO:0004003 - delayed onset of replication fork processing

References:

Genotypes:

FYPO:0002019 - elongated telomeres during vegetative growth

References:

Genotypes:

FYPO:0005261 - increased cell population growth on galactose carbon source

References:

Genotypes:

FYPO:0009094 - increased cell population growth on lysine and proline nitrogen source

References:

Genotypes:

FYPO:0009098 - increased cell population growth on mannitol carbon source

References:

Genotypes:

FYPO:0009028 - increased cell population growth on proline nitrogen source

References:

Genotypes:

FYPO:0009074 - increased cell population growth on serine nitrogen source

References:

Genotypes:

FYPO:0009096 - increased cell population growth on xylose carbon source

References:

Genotypes:

FYPO:0005629 - increased cellular HMW SUMO conjugate level

References:

Genotypes:

FYPO:0004251 - increased DNA resection during replication fork processing

References:

Genotypes:

FYPO:0000614 - increased duration of mitotic S phase

References:

Genotypes:

FYPO:0005619 - increased level of sumoylated protein in cell

References:

Genotypes:

FYPO:0001840 - increased minichromosome loss during vegetative growth

References:

Genotypes:

FYPO:0000473 - increased mitotic recombination

References:

Genotypes:

FYPO:0006518 - loss of viability in G0

References:

Genotypes:

FYPO:0000245 - loss of viability in stationary phase

References:

Genotypes:

FYPO:0004295 - multiseptate cell

References:

Genotypes:

FYPO:0006995 - normal chromatin silencing at centromere inner repeat

References:

Genotypes:

FYPO:0003555 - normal chromatin silencing at subtelomere

References:

Genotypes:

FYPO:0007553 - normal G1 to G0 transition

References:

Genotypes:

FYPO:0001690 - normal growth on camptothecin

References:

Genotypes:

FYPO:0000963 - normal growth on hydroxyurea

References:

Genotypes:

FYPO:0000957 - normal growth on methyl methanesulfonate

References:

Genotypes:

FYPO:0000964 - normal growth on thiabendazole

References:

Genotypes:

FYPO:0006033 - normal protein localization to chromatin during mitotic DNA replication

References:

Genotypes:

FYPO:0006320 - normal replication slippage during replication fork processing

References:

Genotypes:

FYPO:0000067 - resistance to brefeldin A

References:

Genotypes:

FYPO:0000764 - resistance to cycloheximide

References:

Genotypes:

FYPO:0001453 - resistance to ethanol

References:

Genotypes:

FYPO:0001034 - resistance to tunicamycin

References:

Genotypes:

FYPO:0007808 - resistance to valproic acid

References:

Genotypes:

FYPO:0007921 - sensitive to benzamidine

References:

Genotypes:

FYPO:0001701 - sensitive to bortezomib

References:

Genotypes:

FYPO:0006930 - sensitive to butylated hydroxyanisole

References:

Genotypes:

FYPO:0000085 - sensitive to camptothecin

References:

Genotypes:

FYPO:0000102 - sensitive to cisplatin

References:

Genotypes:

FYPO:0002640 - sensitive to clotrimazole

References:

Genotypes:

FYPO:0003559 - sensitive to doxorubicin

References:

Genotypes:

FYPO:0007931 - sensitive to egtazic acid

References:

Genotypes:

FYPO:0000842 - sensitive to ethanol during vegetative growth

References:

Genotypes:

FYPO:0000088 - sensitive to hydroxyurea

References:

Genotypes:

FYPO:0006149 - sensitive to idarubicin

References:

Genotypes:

FYPO:0001719 - sensitive to lithium

References:

Genotypes:

FYPO:0009086 - sensitive to lithium chloride and sodium dodecyl sulfate

References:

Genotypes:

FYPO:0009088 - sensitive to magnesium chloride and sodium dodecyl sulfate

References:

Genotypes:

FYPO:0000089 - sensitive to methyl methanesulfonate

References:

Genotypes:

FYPO:0007924 - sensitive to potassium chloride and sodium dodecyl sulfate

References:

Genotypes:

FYPO:0002328 - sensitive to terbinafine

References:

Genotypes:

FYPO:0000091 - sensitive to thiabendazole

References:

Genotypes:

FYPO:0009063 - sensitive to X-rays during vegetative growth

References:

Genotypes:

FYPO:0002060 - viable vegetative cell population

References:

Genotypes:

FYPO:0002177 - viable vegetative cell with normal cell morphology

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

Protein features

IDNameInterPro nameDB name
PF02037SAPSAP_domPFAM
PF02891zf-MIZZnf_MIZPFAM
PF14324PINITPINITPFAM
cd16792SP-RING_Siz-likeSIZ1/2_SP-RINGCDD
PS50800SAPSAP_domPROSITE_PROFILES
PS51466PINITPINITPROSITE_PROFILES
PS51044ZF_SP_RINGZnf_MIZPROSITE_PROFILES
SM00513sap_9SAP_domSMART
G3DSA:3.30.40.10:FF:000247FUNFAM
SSF68906SAP domainSAP_dom_sfSUPERFAMILY
G3DSA:2.60.120.780PINIT domainPINIT_sfGENE3D
G3DSA:3.30.40.10Zinc/RING finger domain, C3HC4 (zinc finger)Znf_RING/FYVE/PHDGENE3D
G3DSA:1.10.720.30SAP domainSAP_dom_sfGENE3D
PTHR10782ZINC FINGER MIZ DOMAIN-CONTAINING PROTEINPANTHER
mobidb-lite-Disorderdisorder_predictionMOBIDB-Disorder
mobidb-lite-Low-complexitydisorder_predictionMOBIDB-Low-complexity
mobidb-lite-Polardisorder_predictionMOBIDB-Polar

Orthologs

References / Literature

PMID:17209013 - Role of SUMO in the dynamics of telomere maintenance in fission yeast.
Xhemalce B et al. Proc Natl Acad Sci U S A 2007 Jan 16;104(3):893-8
PMID:41330900 - PolySUMOylation of PCNA and Rad52 restricts centromeric recombination in fission yeast.
Markowska K et al. Nat Commun 2025 Dec 02;16(1):10837
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:27298342 - Identification of S-phase DNA damage-response targets in fission yeast reveals conservation of damage-response networks.
Willis NA et al. Proc Natl Acad Sci U S A 2016 Jun 28;113(26):E3676-85
PMID:31072933 - Suppressor screening reveals common kleisin-hinge interaction in condensin and cohesin, but different modes of regulation.
Xu X et al. Proc Natl Acad Sci U S A 2019 May 28;116(22):10889-10898
PMID:23936535 - Slx8 removes Pli1-dependent protein-SUMO conjugates including SUMOylated topoisomerase I to promote genome stability.
Steinacher R et al. PLoS One 2013;8(8):e71960
PMID:26221037 - Pli1(PIAS1) SUMO ligase protected by the nuclear pore-associated SUMO protease Ulp1SENP1/2.
Nie M et al. J Biol Chem 2015 Sep 11;290(37):22678-85
PMID:28475613 - SUMO-targeted ubiquitin ligase activity can either suppress or promote genome instability, depending on the nature of the DNA lesion.
Nie M et al. PLoS Genet 2017 May;13(5):e1006776
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:27398807 - Functional Crosstalk between the PP2A and SUMO Pathways Revealed by Analysis of STUbL Suppressor, razor 1-1.
Nie M et al. PLoS Genet 2016 Jul;12(7):e1006165
PMID:21215368 - The Cul4-Ddb1(Cdt)² ubiquitin ligase inhibits invasion of a boundary-associated antisilencing factor into heterochromatin.
Braun S et al. Cell 2011 Jan 07;144(1):41-54
PMID:33260998 - High-Throughput Flow Cytometry Combined with Genetic Analysis Brings New Insights into the Understanding of Chromatin Regulation of Cellular Quiescence.
Zahedi Y et al. Int J Mol Sci 2020 Nov 27;21(23)
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:21511999 - Comparative functional genomics of the fission yeasts.
Rhind N et al. Science 2011 May 20;332(6032):930-6
PMID:28410370 - A systematic screen for morphological abnormalities during fission yeast sexual reproduction identifies a mechanism of actin aster formation for cell fusion.
Dudin O et al. PLoS Genet 2017 Apr;13(4):e1006721
PMID:18257517 - Phosphoproteome analysis of fission yeast.
Wilson-Grady JT et al. J Proteome Res 2008 Mar;7(3):1088-97
PMID:18031226 - The role of Schizosaccharomyces pombe SUMO ligases in genome stability.
Watts FZ et al. Biochem Soc Trans 2007 Dec;35(Pt 6):1379-84
PMID:21444718 - DNA repair and global sumoylation are regulated by distinct Ubc9 noncovalent complexes.
Prudden J et al. Mol Cell Biol 2011 Jun;31(11):2299-310
PMID:18931302 - Significant conservation of synthetic lethal genetic interaction networks between distantly related eukaryotes.
Dixon SJ et al. Proc Natl Acad Sci U S A 2008 Oct 28;105(43):16653-8
PMID:33159083 - The nuclear pore primes recombination-dependent DNA synthesis at arrested forks by promoting SUMO removal.
Kramarz K et al. Nat Commun 2020 Nov 06;11(1):5643
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:28481910 - PCNA ubiquitylation ensures timely completion of unperturbed DNA replication in fission yeast.
Daigaku Y et al. PLoS Genet 2017 May;13(5):e1006789
PMID:28552615 - SUMO-Targeted DNA Translocase Rrp2 Protects the Genome from Top2-Induced DNA Damage.
Wei Y et al. Mol Cell 2017 Jun 01;66(5):581-596.e6
PMID:21712547 - Mitotic substrates of the kinase aurora with roles in chromatin regulation identified through quantitative phosphoproteomics of fission yeast.
Koch A et al. Sci Signal 2011 Jun 28;4(179):rs6
PMID:19363481 - Molecular mimicry of SUMO promotes DNA repair.
Prudden J et al. Nat Struct Mol Biol 2009 May;16(5):509-16
PMID:35820914 - Antagonistic effects of mitochondrial matrix and intermembrane space proteases on yeast aging.
Vega M et al. BMC Biol 2022 Jul 12;20(1):160
PMID:37787768 - Broad functional profiling of fission yeast proteins using phenomics and machine learning.
Rodríguez-López M et al. Elife 2023 Oct 03;12
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:30824696 - Systematic analysis reveals the prevalence and principles of bypassable gene essentiality.
Li J et al. Nat Commun 2019 Mar 01;10(1):1002
GO_REF:0000002 - Comments
PMID:17515930 - Rad3-dependent phosphorylation of the checkpoint clamp regulates repair-pathway choice.
Kai M et al. Nat Cell Biol 2007 Jun;9(6):691-7
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:24265825 - Concerted action of the ubiquitin-fusion degradation protein 1 (Ufd1) and Sumo-targeted ubiquitin ligases (STUbLs) in the DNA-damage response.
Køhler JB et al. PLoS One 2013;8(11):e80442
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:23628481 - A proteome-wide visual screen identifies fission yeast proteins localizing to DNA double-strand breaks.
Yu Y et al. DNA Repair (Amst) 2013 Jun 01;12(6):433-43
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:15359282 - Role of the fission yeast SUMO E3 ligase Pli1p in centromere and telomere maintenance.
Xhemalce B et al. EMBO J 2004 Oct 01;23(19):3844-53
PMID:22252817 - A genomewide screen in Schizosaccharomyces pombe for genes affecting the sensitivity of antifungal drugs that target ergosterol biosynthesis.
Fang Y et al. Antimicrob Agents Chemother 2012 Apr;56(4):1949-59
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:24192486 - The conserved Fanconi anemia nuclease Fan1 and the SUMO E3 ligase Pli1 act in two novel Pso2-independent pathways of DNA interstrand crosslink repair in yeast.
Fontebasso Y et al. DNA Repair (Amst) 2013 Dec;12(12):1011-23
PMID:37970674 - SUMOylation regulates Lem2 function in centromere clustering and silencing.
Strachan J et al. J Cell Sci 2023 Dec 01;136(23)
PMID:30647105 - Comparative Genomic Screen in Two Yeasts Reveals Conserved Pathways in the Response Network to Phenol Stress.
Alhoch B et al. G3 (Bethesda) 2019 Mar 07;9(3):639-650
PMID:21760946 - Identification of genes affecting the toxicity of anti-cancer drug bortezomib by genome-wide screening in S. pombe.
Takeda K et al. PLoS One 2011;6(7):e22021
PMID:29996109 - Quantitative Phosphoproteomics Reveals the Signaling Dynamics of Cell-Cycle Kinases in the Fission Yeast Schizosaccharomyces pombe.
Swaffer MP et al. Cell Rep 2018 Jul 10;24(2):503-514
PMID:18818364 - Conservation and rewiring of functional modules revealed by an epistasis map in fission yeast.
Roguev A et al. Science 2008 Oct 17;322(5900):405-10
PMID:39786922 - The fission yeast SUMO-targeted ubiquitin ligase Slx8 functionally associates with clustered centromeres and the silent mating-type region at the nuclear periphery.
Chakraborty S et al. Biol Open 2024 Dec 15;13(12)
PMID:19547744 - Evolution of phosphoregulation: comparison of phosphorylation patterns across yeast species.
Beltrao P et al. PLoS Biol 2009 Jun 16;7(6):e1000134
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:19756689 - SUMOylation is required for normal development of linear elements and wild-type meiotic recombination in Schizosaccharomyces pombe.
Spirek M et al. Chromosoma 2010 Feb;119(1):59-72
PMID:31563844 - The roles of fission yeast exonuclease 5 in nuclear and mitochondrial genome stability.
Sparks JL et al. DNA Repair (Amst) 2019 Nov;83:102720
PMID:34250083 - Barcode sequencing and a high-throughput assay for chronological lifespan uncover ageing-associated genes in fission yeast.
Romila CA et al. Microb Cell 2021 Jul 05;8(7):146-160
PMID:11751918 - The fission yeast ES2 homologue, Bis1, interacts with the Ish1 stress-responsive nuclear envelope protein.
Taricani L et al. J Biol Chem 2002 Mar 22;277(12):10562-72
PMID:17762865 - SUMO-targeted ubiquitin ligases in genome stability.
Prudden J et al. EMBO J 2007 Sep 19;26(18):4089-101
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:39476757 - Characterization of Ksg1 protein kinase-dependent phosphoproteome in the fission yeast S. pombe.
Cipak L et al. Biochem Biophys Res Commun 2024 Oct 25;736:150895
PMID:26537787 - Targeting of SUMO substrates to a Cdc48-Ufd1-Npl4 segregase and STUbL pathway in fission yeast.
Køhler JB et al. Nat Commun 2015 Nov 05;6:8827
PMID:24925530 - Tpz1TPP1 SUMOylation reveals evolutionary conservation of SUMO-dependent Stn1 telomere association.
Garg M et al. EMBO Rep 2014 Aug;15(8):871-7