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Protein

Fructose-bisphosphate aldolase

Gene

ALDOC

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi: glycolysis

This protein is involved in step 4 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.UniRule annotationSAAS annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Glucose-6-phosphate isomerase, Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase, Glucose-6-phosphate isomerase (GPI)
  3. ATP-dependent 6-phosphofructokinase (PFKM), ATP-dependent 6-phosphofructokinase, liver type (PFKL), ATP-dependent 6-phosphofructokinase, muscle type (PFKM), ATP-dependent 6-phosphofructokinase, platelet type (PFKP)
  4. Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOB), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase C (ALDOC), Fructose-bisphosphate aldolase (HEL-S-87p), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOB), Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase B (ALDOB), Fructose-bisphosphate aldolase A (ALDOA), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOC)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotationSAAS annotation

Keywords - Biological processi

GlycolysisUniRule annotationSAAS annotation

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolaseUniRule annotationSAAS annotation (EC:4.1.2.13UniRule annotationSAAS annotation)
Gene namesi
Name:ALDOCImported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:418. ALDOC.

PTM / Processingi

Proteomic databases

EPDiA8MVZ9.
MaxQBiA8MVZ9.
PRIDEiA8MVZ9.

Expressioni

Gene expression databases

BgeeiA8MVZ9.
ExpressionAtlasiA8MVZ9. baseline and differential.

Structurei

3D structure databases

ProteinModelPortaliA8MVZ9.
SMRiA8MVZ9. Positions 3-316.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class I fructose-bisphosphate aldolase family.UniRule annotationSAAS annotation

Phylogenomic databases

GeneTreeiENSGT00390000010235.
HOGENOMiHOG000220876.
HOVERGENiHBG002386.
OrthoDBiEOG744T94.

Family and domain databases

Gene3Di3.20.20.70. 2 hits.
InterProiIPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR000741. FBA_I.
[Graphical view]
PfamiPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEiPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A8MVZ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPHSYPALSA EQKKELSDIA LRIVAPGKGI LAADESVGSM AKRLSQIGVE
60 70 80 90 100
NTEENRRLYR QVLFSADDRV KKCIGGVIFF HETLYQKDDN GVPFVRTIQD
110 120 130 140 150
KGIVVGIKVD KGVVPLAGTD GETTTQGLDG LSERCAQYKK DGADFAKWRC
160 170 180 190 200
VLKISERTPS ALAILENANV LARYASICQQ VLAAVYKALS DHHVYLEGTL
210 220 230 240 250
LKPNMVTPGH ACPIKYTPEE IAMATVTALR RTVPPAVPGV TFLSGGQSEE
260 270 280 290 300
EASFNLNAIN RCPLPRPWAL TFSYGRALQA SALNAWRGQR DNAGAATEEF
310 320 330
IKRAEVNGLA AQGKYEGSGE DGGAAAQSLY IANHAY
Length:336
Mass (Da):36,295
Last modified:December 4, 2007 - v1
Checksum:iB9BE86B2D31D2823
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC005726 Genomic DNA. No translation available.

Genome annotation databases

EnsembliENST00000395319; ENSP00000378729; ENSG00000109107.
UCSCiuc060czk.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC005726 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortaliA8MVZ9.
SMRiA8MVZ9. Positions 3-316.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

EPDiA8MVZ9.
MaxQBiA8MVZ9.
PRIDEiA8MVZ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000395319; ENSP00000378729; ENSG00000109107.
UCSCiuc060czk.1. human.

Organism-specific databases

HGNCiHGNC:418. ALDOC.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00390000010235.
HOGENOMiHOG000220876.
HOVERGENiHBG002386.
OrthoDBiEOG744T94.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.

Miscellaneous databases

ChiTaRSiALDOC. human.
NextBioi35464955.

Gene expression databases

BgeeiA8MVZ9.
ExpressionAtlasiA8MVZ9. baseline and differential.

Family and domain databases

Gene3Di3.20.20.70. 2 hits.
InterProiIPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR000741. FBA_I.
[Graphical view]
PfamiPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEiPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
  5. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "N-terminome analysis of the human mitochondrial proteome."
    Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.
    Proteomics 15:2519-2524(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiA8MVZ9_HUMAN
AccessioniPrimary (citable) accession number: A8MVZ9
Entry historyi
Integrated into UniProtKB/TrEMBL: December 4, 2007
Last sequence update: December 4, 2007
Last modified: May 11, 2016
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.