fba1 (SPBC19C2.07)

Gene Standard Namefba1 Characterisation Statuspublished
Systematic IDSPBC19C2.07 Feature Typeprotein coding
Synonyms Name Description
Productfructose-bisphosphate aldolase Fba1 Product Size358aa, 39.57 kDa
Genomic Location Chromosome II, 1688336-1689599 (1264nt); CDS:1688367-1689443 (1077nt)

Ensembl Gene Location
GO Molecular Function
Term NameCount
fructose-bisphosphate aldolase activity1
Annotation ExtensionEvidenceWith/FromReference
zinc ion binding238
Annotation ExtensionEvidenceWith/FromReference
GO Biological Process
Term NameCount
canonical glycolysis14
Annotation ExtensionEvidenceWith/FromReference
GO Cellular Component
Term NameCount
Annotation ExtensionEvidenceWith/FromReference
Annotation ExtensionEvidenceWith/FromReference
Annotation ExtensionEvidenceWith/FromReference
FYPO Single-Allele Phenotypes
Gene Deletion Viability: Inviable

Population Phenotype

Term NameGenotypesCount
inviable vegetative cell populationfba1Δ1450

Cell Phenotype

Term NameGenotypesCount
inviable sporefba1Δ475
Target Of
FYPO affected by mutation in lkh1 dual specificity protein kinase Lkh1
Ensembl transcript structure with UTRs, exons and introns

Transcript Structure

Region Coordinates Reference
5' UTR1688336..1688366AU011079
3' UTR1689444..1689599AU007197
Protein Features

Graphical View

Ensembl protein image with mapped locations of structural domains

Protein Families and Domains

Feature ID Database InterPro Description Start End Count
PF01116 Pfam IPR000771 Ketose-bisphosphate aldolase, class-II 16 356 1
PS00602 Prosite Patterns IPR000771 Ketose-bisphosphate aldolase, class-II 98 110 1
PS00806 Prosite Patterns IPR000771 Ketose-bisphosphate aldolase, class-II 170 181 1
PTHR30559 HMMPANTHER 1 358 1
PTHR30559:SF0 HMMPANTHER 1 358 1 Gene3D IPR013785 Aldolase-type TIM barrel 10 356 35
SSF51569 SuperFamily 1 357 9
PIRSF001359 PIRSF IPR000771 Ketose-bisphosphate aldolase, class-II 12 358 1
TIGR00167 tigrfam IPR000771 Ketose-bisphosphate aldolase, class-II 13 357 1
TIGR01520 tigrfam IPR006411 Fructose-bisphosphate aldolase, class II, yeast/E. coli subtype 3 357 1

View domain organization at Pfam

Protein Properties

Ave. residue weight 110.53 Da
Charge -1.50
Codon Adaptation Index 0.83
Isoelectric point 6.32
Molecular weight 39.57 kDa
Number of residues 358

Protein Modifications

Term NameResidueCount
O-phospho-L-serine 1675
present during mitotic M phaseS267
Annotation ExtensionEvidenceResidueReference
present during mitotic M phase experimental evidence S267 PMID:21712547
O-phospho-L-threonineT289, T312 700
present during mitotic M phaseT289
present during mitotic M phaseT312
Annotation ExtensionEvidenceResidueReference
experimental evidence T289 PMID:24763107
present during mitotic M phase experimental evidence T289 PMID:21712547
experimental evidence T312 PMID:24763107
present during mitotic M phase experimental evidence T312 PMID:21712547
phosphorylated residue 1930
Annotation ExtensionEvidenceResidueReference
IDA PMID:19547744
ubiquitinylated lysineK71, K79, K248, K252, K257, K279, K307 512
Annotation ExtensionEvidenceResidueReference
IDA PMID:26412298
mass spectrometry evidence K71 PMID:26412298
mass spectrometry evidence K79 PMID:26412298
mass spectrometry evidence K248 PMID:26412298
mass spectrometry evidence K252 PMID:26412298
mass spectrometry evidence K257 PMID:26412298
mass spectrometry evidence K279 PMID:26412298
mass spectrometry evidence K307 PMID:26412298
sumoylated lysine 173
Annotation ExtensionEvidenceResidueReference
IDA PMID:26404184
Gene Expression

Qualitative Gene Expression

RNA levelpresent during GO:0072690Northern assay evidencePMID:8286404

Quantitative Gene Expression

View graphical display of gene expression data for fba1 (SPBC19C2.07)

Protein Level

Molecules/Cell (average)ExtensionConditionScaleEvidenceReference
1280537during GO:0000080PECO:0000005,
single cellmass spectrometry evidencePMID:24763107
1367471during GO:0000084PECO:0000005,
single cellmass spectrometry evidencePMID:24763107
1350680during GO:0000085PECO:0000005,
single cellmass spectrometry evidencePMID:24763107
1365804during GO:0000087PECO:0000005,
single cellmass spectrometry evidencePMID:24763107
1025542.06during GO:0072690PECO:0000014,
population wideexperimental evidencePMID:23101633
1376321during GO:0072690PECO:0000005,
single cellmass spectrometry evidencePMID:24763107
292133.4during cell quiescence following G1 arrest due to nitrogen limitationPECO:0000127,
population wideexperimental evidencePMID:23101633

RNA Level

Molecules/Cell (average)ExtensionConditionScaleEvidenceReference
520during GO:0072690PECO:0000014,
population wideexperimental evidencePMID:23101633
66during cell quiescence following G1 arrest due to nitrogen limitationPECO:0000127,
population wideexperimental evidencePMID:23101633
Taxonomic Conservation
conserved in fungi4604
conserved in eukaryotes4514
conserved in bacteria1000

Manually curated orthologous groups


Orthologs in Compara

Physical Interactions

Source: BioGRID

Load gene that interact physically with SPBC19C2.07 into the Query Builder
View all interactions in esyN
View the HCPIN interactions in esyN

Gene Product Evidence Reference
binds DNA-binding domain construct withzfs1CCCH tandem zinc finger protein, human Tristetraprolin homolog Zfs1, involved in mRNA catabolism Two-hybridPMID:19682301
binds DNA-binding domain construct withmoc3transcription factor Moc3 Two-hybridPMID:19682301
binds DNA-binding domain construct withsds23PP2A-type phosphatase inhibitor Sds23/Moc1 Two-hybridPMID:19682301
affinity captured byfic1C2 domain protein Fic1 Affinity Capture-MSPMID:19139265
affinity captured bypaa1protein phosphatase regulatory subunit Paa1 Affinity Capture-MSPMID:22403715
affinity captured bysog2leucine-rich repeat protein Lrp1 Affinity Capture-MSPMID:23462181
affinity captured byfar8SIP/FAR complex striatin subunit, Far8/Csc3 Affinity Capture-MSPMID:22119525
affinity captured byslm9hira protein Slm9 Affinity Capture-MSPMID:20976105
affinity captured byair1zinc knuckle TRAMP complex subunit Air1 Affinity Capture-MSPMID:20403971
affinity captured bynak1PAK-related kinase Nak1 Affinity Capture-MSPMID:23462181
External References
Database Identifier Description
NBRP SPBC19C2.07 Fission yeast strain database, National BioResource Project (Japan)
YOGY SPBC19C2.07 Retrieval of eukaryotic orthologs (Bähler Lab)
BioGrid SPBC19C2.07 BioGRID Interaction Datasets
Expression Viewer SPBC19C2.07 Cell Cycle Expression Profile (Bähler Lab)
Expression Viewer SPBC19C2.07 Meiosis/Sporulation Expression Profies (Bähler Lab)
Expression Viewer SPBC19C2.07 Pheromone response/mating expression profiles (Bähler Lab)
Expression Viewer SPBC19C2.07 Environmental stress expression profiles (Bähler Lab)
Pomb(A) SPBC19C2.07 Polyadenylation Viewer (Gullerova lab)
pombeTV SPBC19C2.07 Transcriptome Viewer (Bähler Lab)
GEO SPBC19C2.07 GEO profiles
PInt SPBC19C2.07 Protein-Protein Interaction Predictor (Bähler Lab)
PeptideAtlas SPBC19C2.07 Peptides identified in tandem mass spectrometry proteomics experiments
SYSGRO SPBC19C2.07 Fission yeast phenotypic data & analysis
Cyclebase SPBC19C2.07.1 Cell Cycle Data
IntEnz4.1.2.13Integrated relational Enzyme database
Rhea4.1.2.13Annotated reactions database
SPD / RIKEN40/40C08Orfeome Localization Data
UniProtKB/SwissProtP36580Fructose-bisphosphate aldolase
ModBaseP36580Database of comparative protein structure models
STRINGP36580Network display of known and predicted interactions and functional associations
RefSeq PeptideNP_595692fructose-bisphosphate aldolase Fba1
RefSeq mRNANM_001021589972h- fructose-bisphosphate aldolase Fba1 (fba1), mRNA
European Nucleotide ArchiveCU329671ENA EMBL mapping
European Nucleotide ArchiveD17415ENA EMBL mapping
European Nucleotide ArchiveBAA04237ENA Protein Mapping
European Nucleotide ArchiveCAB52034ENA Protein Mapping
MetaCycPWY-1042Glycolysis IV (plant cytosol)
MetaCycPWY-1861Formaldehyde assimilation II (RuMP Cycle)
MetaCycPWY-5484Glycolysis II (from fructose 6-phosphate)
MetaCycPWY-6142Gluconeogenesis II (Methanobacterium thermoautotrophicum)
MetaCycPWY-73851,3-propanediol biosynthesis (engineered)
KEGG00010+ / Gluconeogenesis
KEGG00030+ phosphate pathway
KEGG00051+ and mannose metabolism
KEGG00680+ metabolism
KEGG00710+ fixation in photosynthetic organisms
UniParcUPI0000125829UniProt Archive
UniPathwayUPA00109Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4

Literature for fba1

Search: Europe PMC or PubMed

Release Version: PomBase:30_57 - 27 Jan 2016