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 binding248
Annotation ExtensionEvidenceWith/FromReference
GO Biological Process
Term NameCount
canonical glycolysis14
Annotation ExtensionEvidenceWith/FromReference
GO Cellular Component
Term NameCount
cytoplasm4206
Annotation ExtensionEvidenceWith/FromReference
cytosol2316
Annotation ExtensionEvidenceWith/FromReference
nucleus2697
Annotation ExtensionEvidenceWith/FromReference
Fission Yeast Phenotype Ontology
Gene Deletion Viability: Inviable

Population Phenotype

Term NameAlleleExpressionCount
inviable vegetative cell populationfba1ΔNull1428

Cell Phenotype

Term NameAlleleExpressionCount
inviable sporefba1ΔNull468
Target Of
OntologyRelationshipGeneProductReference
FYPO affected by mutation in lkh1 dual specificity protein kinase Lkh1 PMID:23956636
Transcript
Ensembl transcript structure with UTRs, exons and introns

Exons

Exon Start End
116883361689599

UTRs

Region Coordinates Reference
five_prime_UTR1688336..1688366AU011079
three_prime_UTR1689444..1689599AU007197
mRNA1688336..1689599
exon1688367..1689443
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 14 356 1
PS00806 Prosite Patterns IPR000771 Ketose-bisphosphate aldolase, class-II 170 181 1
PS00602 Prosite Patterns IPR000771 Ketose-bisphosphate aldolase, class-II 98 110 1
3.20.20.70 Gene3D IPR013785 Aldolase-type TIM barrel 10 356 35
SSF51569 SuperFamily 1 357 9
PIRSF001359 PIRSF IPR000771 Ketose-bisphosphate aldolase, class-II 11 358 1
TIGR01520 tigrfam IPR006411 Fructose-bisphosphate aldolase, class II, yeast/E. coli subtype 3 357 1
TIGR00167 tigrfam IPR000771 Ketose-bisphosphate aldolase, class-II 13 357 1

View domain organization at Pfam

Protein Properties

Ave. residue weight 110.53 Da
Charge -1.50
Isoelectric point 6.32
Molecular weight 39.57 kDa
Number of residues 358
Modifications

Protein Modifications

Term NameResidueCount
O-phospho-L-serine 1670
present during mitotic M phaseS267
Annotation ExtensionEvidenceResidueReference
present during mitotic M phase experimental evidence S267 PMID:21712547
O-phospho-L-threonine 694
present during mitotic M phaseT289
T289, T312
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 1923
Annotation ExtensionEvidenceResidueReference
IDA PMID:19547744
Sequence
Gene Expression

Qualitative Gene Expression

DescriptionLevelEvidenceReference
RNA levelpresent during GO:0072690Northern assay evidencePMID:8286404

Quantitative Gene Expression

Protein Level

Molecules/Cell (average)ExtensionConditionScaleEvidenceReference
1280537during GO:0000080PECO:0000126,
PECO:0000005
single cellmass spectrometry evidencePMID:24763107
1367471during GO:0000084PECO:0000126,
PECO:0000005
single cellmass spectrometry evidencePMID:24763107
1350680during GO:0000085PECO:0000126,
PECO:0000005
single cellmass spectrometry evidencePMID:24763107
1365804during GO:0000087PECO:0000126,
PECO:0000005
single cellmass spectrometry evidencePMID:24763107
1025542.06during GO:0072690PECO:0000005,
PECO:0000014
population wideexperimental evidencePMID:23101633
1376321during GO:0072690PECO:0000126,
PECO:0000005
single cellmass spectrometry evidencePMID:24763107
292133.4during cell quiescence following G1 arrest due to nitrogen limitationPECO:0000005,
PECO:0000014,
PECO:0000127
population wideexperimental evidencePMID:23101633

RNA Level

Molecules/Cell (average)ExtensionConditionScaleEvidenceReference
520during GO:0072690PECO:0000005,
PECO:0000014
population wideexperimental evidencePMID:23101633
66during cell quiescence following G1 arrest due to nitrogen limitationPECO:0000005,
PECO:0000014,
PECO:0000127
population wideexperimental evidencePMID:23101633
Species Distribution
DescriptionQualifierReferenceCount
conserved in fungi4604
conserved in eukaryotes4516
conserved in bacteria1000
Orthologs

Manually curated orthologous groups

SpeciesGeneDescriptionLinksCount

Orthologs in Compara


Physical Interactions

Source: BioGRID

View all interactions in esyN
View the HCPIN interactions in esyN

Gene Product Evidence Reference
affinity captured byair1zinc knuckle TRAMP complex subunit Air1 Affinity Capture-MSPMID:20403971
affinity captured byfar8SIP/FAR complex striatin subunit, Far8/Csc3 Affinity Capture-MSPMID:22119525
affinity captured byfic1C2 domain protein Fic1 Affinity Capture-MSPMID:19139265
affinity captured byhhp1serine/threonine protein kinase Hhp1 Affinity Capture-MSPMID:24055157
affinity captured byhhp2serine/threonine protein kinase Hhp2 Affinity Capture-MSPMID:24055157
binds DNA-binding domain construct withmoc3transcription factor Moc3 Two-hybridPMID:19682301
affinity captured bynak1PAK-related kinase Nak1 Affinity Capture-MSPMID:23462181
affinity captured bypaa1protein phosphatase regulatory subunit Paa1 Affinity Capture-MSPMID:22403715
affinity captured bypaa1protein phosphatase regulatory subunit Paa1 Affinity Capture-MSPMID:24634168
affinity captured bypaa1protein phosphatase regulatory subunit Paa1 Affinity Capture-MSPMID:22119525
binds DNA-binding domain construct withsds23PP2A-type phosphatase inhibitor Sds23/Moc1 Two-hybridPMID:19682301
affinity captured byslm9hira protein Slm9 Affinity Capture-MSPMID:20976105
affinity captured bysog2leucine-rich repeat protein Lrp1 Affinity Capture-MSPMID:23462181
binds DNA-binding domain construct withzfs1CCCH tandem zinc finger protein, human Tristetraprolin homolog Zfs1, involved in mRNA catabolism Two-hybridPMID:19682301
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)
Cyclebase SPBC19C2.07 Cell Cycle Data
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
SPD / RIKEN40/40C08Orfeome Localization Data
IntEnz4.1.2.13Integrated relational Enzyme database
Rhea4.1.2.13Annotated reactions database
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 ArchiveBAA04237.1ENA Protein Mapping
European Nucleotide ArchiveCAB52034.1ENA Protein Mapping
MetaCycPWY-1042Glycolysis IV (plant cytosol)
MetaCycPWY-1861Formaldehyde assimilation II (RuMP Cycle)
MetaCycPWY-5484Glycolysis II (from fructose-6P)
MetaCycPWY-6142Gluconeogenesis II (Methanobacterium thermoautotrophicum)
MetaCycPWY-73851,3-propanediol biosynthesis (engineered)
KEGG_Enzyme00010+4.1.2.13Glycolysis / Gluconeogenesis
KEGG_Enzyme00030+4.1.2.13Pentose phosphate pathway
KEGG_Enzyme00051+4.1.2.13Fructose and mannose metabolism
KEGG_Enzyme00680+4.1.2.13Methane metabolism
KEGG_Enzyme00710+4.1.2.13Carbon fixation in photosynthetic organisms
UniParcUPI0000125829UniProt Archive
UniPathwayUPA00109Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5

Literature for fba1

Search: Europe PMC or PubMed

Release Version: PomBase:25_49 - 02 Feb 2015