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Q91Y97 (ALDOB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fructose-bisphosphate aldolase B

EC=4.1.2.13
Alternative name(s):
Aldolase 2
Liver-type aldolase
Gene names
Name:Aldob
Synonyms:Aldo2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length364 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.

Subunit structure

Homotetramer By similarity. Interacts with BBS1, BBS2, BBS4 and BBS7 By similarity.

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriolar satellite By similarity.

Miscellaneous

In vertebrates, 3 forms of this ubiquitous glycolytic enzyme are found, aldolase A in muscle, aldolase B in liver and aldolase C in brain.

Sequence similarities

Belongs to the class I fructose-bisphosphate aldolase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 364363Fructose-bisphosphate aldolase B
PRO_0000216941

Sites

Active site1881Proton acceptor By similarity
Active site2301Schiff-base intermediate with dihydroxyacetone-P
Binding site561Substrate
Binding site1471Substrate
Site3641Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

Amino acid modifications

Modified residue21N-acetylalanine Ref.3
Modified residue131N6-succinyllysine Ref.5
Modified residue361Phosphoserine Ref.4
Modified residue391Phosphothreonine Ref.4
Modified residue1211N6-succinyllysine Ref.5
Modified residue3171N6-succinyllysine Ref.5

Experimental info

Sequence conflict811H → Y in AAH34173. Ref.2
Sequence conflict155 – 1562AD → DH in AAL06323. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q91Y97 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E6CD995D0073ED47

FASTA36439,507
        10         20         30         40         50         60 
MAHRFPALTP EQKKELSEIA QRIVANGKGI LAADESVGTM GNRLQRIKVE NTEENRRQFR 

        70         80         90        100        110        120 
ELLFSVDNSI SQSIGGVILF HETLYQKDSQ GNLFRNVLKE KGIVVGIKLD QGGAPLAGTN 

       130        140        150        160        170        180 
KETTIQGLDG LSERCAQYKK DGVDFGKWRA VLRIADQCPS SLAIQENANA LARYASICQQ 

       190        200        210        220        230        240 
NGLVPIVEPE VLPDGDHDLE HCQYVSEKVL AAVYKALNDH HVYLEGTLLK PNMVTAGHAC 

       250        260        270        280        290        300 
TKKYTPEQVA MATVTALHRT VPAAVPGICF LSGGMSEEDA TLNLNAINRC PLPRPWKLSF 

       310        320        330        340        350        360 
SYGRALQASA LAAWGGKAAN KKATQEAFMK RAMANCQAAQ GQYVHTGSSG AAATQSLFTA 


SYTY 

« Hide

References

« Hide 'large scale' references
[1]"Mouse aldolase B (aldo2) genomic sequence of the open reading frame including first poly A site and signals."
Funari V.A., Tolan D.R.
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/Sv.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Colon, Kidney and Liver.
[3]Kanor S., Quadroni M., Bienvenut W.V.
Submitted (MAR-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-12 AND 108-120, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6J.
Tissue: Skeletal muscle.
[4]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND THR-39, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[5]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-13; LYS-121 AND LYS-317, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF403567, AF403565, AF403566 Genomic DNA. Translation: AAL06323.1.
BC016435 mRNA. Translation: AAH16435.1.
BC022113 mRNA. Translation: AAH22113.1.
BC024056 mRNA. Translation: AAH24056.1.
BC024112 mRNA. Translation: AAH24112.1.
BC026577 mRNA. Translation: AAH26577.1.
BC030724 mRNA. Translation: AAH30724.1.
BC030725 mRNA. Translation: AAH30725.1.
BC034169 mRNA. Translation: AAH34169.1.
BC034171 mRNA. Translation: AAH34171.1.
BC034172 mRNA. Translation: AAH34172.1.
BC034173 mRNA. Translation: AAH34173.1.
BC036130 mRNA. Translation: AAH36130.1.
BC036131 mRNA. Translation: AAH36131.1.
BC036132 mRNA. Translation: AAH36132.1.
BC036133 mRNA. Translation: AAH36133.1.
CCDSCCDS18176.1.
RefSeqNP_659152.1. NM_144903.2.
UniGeneMm.482116.

3D structure databases

ProteinModelPortalQ91Y97.
SMRQ91Y97. Positions 2-349.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ91Y97. 5 interactions.
MINTMINT-1862169.
STRING10090.ENSMUSP00000029987.

PTM databases

PhosphoSiteQ91Y97.

Proteomic databases

MaxQBQ91Y97.
PaxDbQ91Y97.
PRIDEQ91Y97.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029987; ENSMUSP00000029987; ENSMUSG00000028307.
GeneID230163.
KEGGmmu:230163.
UCSCuc008svw.1. mouse.

Organism-specific databases

CTD229.
MGIMGI:87995. Aldob.

Phylogenomic databases

eggNOGCOG3588.
GeneTreeENSGT00390000010235.
HOGENOMHOG000220876.
HOVERGENHBG002386.
InParanoidQ91Y97.
KOK01623.
OMADMEHCQY.
OrthoDBEOG744T94.
PhylomeDBQ91Y97.
TreeFamTF314203.

Enzyme and pathway databases

UniPathwayUPA00109; UER00183.

Gene expression databases

BgeeQ91Y97.
CleanExMM_ALDOB.
GenevestigatorQ91Y97.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR000741. Aldolase_I.
IPR013785. Aldolase_TIM.
[Graphical view]
PANTHERPTHR11627. PTHR11627. 1 hit.
PfamPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSALDOB. mouse.
NextBio379836.
PROQ91Y97.
SOURCESearch...

Entry information

Entry nameALDOB_MOUSE
AccessionPrimary (citable) accession number: Q91Y97
Secondary accession number(s): Q8K034, Q91W73
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot