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P05062 (ALDOB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fructose-bisphosphate aldolase B

EC=4.1.2.13
Alternative name(s):
Liver-type aldolase
Gene names
Name:ALDOB
Synonyms:ALDB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. Interacts with BBS1, BBS2, BBS4 and BBS7. Ref.10

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriolar satellite Ref.10.

Involvement in disease

Hereditary fructose intolerance (HFI) [MIM:229600]: Autosomal recessive disease that results in an inability to metabolize fructose and related sugars. Complete exclusion of fructose results in dramatic recovery; however, if not treated properly, HFI subjects suffer episodes of hypoglycemia, general ill condition, and risk of death the remainder of life.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23

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.

Biophysicochemical properties

Kinetic parameters:

KM=1.6 µM for fructose 1,6-bisphosphate Ref.20

KM=2.3 mM for fructose 1-phosphate

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   LigandSchiff base
   Molecular functionLyase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processNADH oxidation

Inferred from direct assay PubMed 17576770. Source: BHF-UCL

fructose 1,6-bisphosphate metabolic process

Inferred from direct assay PubMed 10625657PubMed 9244396. Source: BHF-UCL

fructose catabolic process

Traceable author statement. Source: Reactome

gluconeogenesis

Traceable author statement. Source: Reactome

glycolysis

Inferred from direct assay PubMed 10625657. Source: BHF-UCL

positive regulation of ATPase activity

Inferred from genetic interaction PubMed 17576770. Source: BHF-UCL

vacuolar proton-transporting V-type ATPase complex assembly

Inferred from genetic interaction PubMed 17576770. Source: BHF-UCL

   Cellular_componentcentriolar satellite

Inferred from direct assay Ref.10. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

   Molecular_functionATPase binding

Inferred from direct assay PubMed 17576770. Source: BHF-UCL

cytoskeletal protein binding

Inferred from direct assay PubMed 9244396. Source: BHF-UCL

fructose binding

Inferred from mutant phenotype PubMed 10625657. Source: BHF-UCL

fructose-bisphosphate aldolase activity

Inferred from direct assay PubMed 10625657PubMed 17576770PubMed 9244396. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 364363Fructose-bisphosphate aldolase B
PRO_0000216940

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 By similarity
Modified residue131N6-succinyllysine By similarity
Modified residue361Phosphoserine By similarity
Modified residue391Phosphothreonine By similarity
Modified residue1211N6-succinyllysine By similarity
Modified residue3171N6-succinyllysine By similarity

Natural variations

Natural variant741I → T in HFI; affects proper folding. Ref.22
VAR_020822
Natural variant120 – 1212Missing in HFI.
VAR_020823
Natural variant1341R → S.
Corresponds to variant rs10123355 [ dbSNP | Ensembl ].
VAR_038429
Natural variant1351C → R in HFI; America; partial activity. Ref.15
VAR_000551
Natural variant1481W → R in one subject with fructose intolerance; rare variant; America. Ref.16
VAR_000552
Natural variant1501A → P in HFI; frequent mutation. Ref.13 Ref.19 Ref.21 Ref.22 Ref.23
Corresponds to variant rs1800546 [ dbSNP | Ensembl ].
VAR_000553
Natural variant1751A → D in HFI; frequent mutation. Ref.14 Ref.19 Ref.21 Ref.22 Ref.23
Corresponds to variant rs76917243 [ dbSNP | Ensembl ].
VAR_000554
Natural variant1781C → R in HFI. Ref.23
VAR_058211
Natural variant1851P → R in HFI. Ref.21
VAR_020824
Natural variant2071E → Q.
Corresponds to variant rs3739721 [ dbSNP | Ensembl ].
VAR_020825
Natural variant2221V → F in HFI; affects proper folding. Ref.22
VAR_020826
Natural variant2291L → P in HFI; affects proper folding. Ref.22
VAR_020827
Natural variant2571L → P in HFI; Italy. Ref.17 Ref.19 Ref.22
VAR_000555
Natural variant2681I → N.
Corresponds to variant rs10989495 [ dbSNP | Ensembl ].
VAR_038430
Natural variant2841L → P in HFI. Ref.23
VAR_058212
Natural variant3041R → Q in HFI; 100-fold decrease in catalytic efficiency for substrates FBP and F1P. Ref.20
Corresponds to variant rs145078268 [ dbSNP | Ensembl ].
VAR_020828
Natural variant3041R → W in HFI; Turkey; 4800-fold decrease in catalytic efficiency for FBP and inactive with F1P. Ref.19 Ref.20
VAR_000556
Natural variant3351N → K in HFI; frequent mutation. Ref.18 Ref.19 Ref.21 Ref.22 Ref.23
VAR_000557
Natural variant3381A → V in HFI; Turkey and South Europe. Ref.19 Ref.22
VAR_000558

Experimental info

Sequence conflict541E → D in AAA51691. Ref.5
Sequence conflict2501A → D in CAA25072. Ref.9
Sequence conflict2781E → D in BAA00125. Ref.4
Sequence conflict3091S → V no nucleotide entry Ref.3
Sequence conflict3481S → C in BAA00125. Ref.4

Secondary structure

............................................................ 364
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05062 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: DCE314E7AC5586CA

FASTA36439,473
        10         20         30         40         50         60 
MAHRFPALTQ EQKKELSEIA QSIVANGKGI LAADESVGTM GNRLQRIKVE NTEENRRQFR 

        70         80         90        100        110        120 
EILFSVDSSI NQSIGGVILF HETLYQKDSQ GKLFRNILKE KGIVVGIKLD QGGAPLAGTN 

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

       190        200        210        220        230        240 
NGLVPIVEPE VIPDGDHDLE HCQYVTEKVL AAVYKALNDH HVYLEGTLLK PNMVTAGHAC 

       250        260        270        280        290        300 
TKKYTPEQVA MATVTALHRT VPAAVPGICF LSGGMSEEDA TLNLNAINLC PLPKPWKLSF 

       310        320        330        340        350        360 
SYGRALQASA LAAWGGKAAN KEATQEAFMK RAMANCQAAK GQYVHTGSSG AASTQSLFTA 


CYTY 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and nucleotide sequence of a full-length cDNA coding for aldolase B from human liver."
Paolella G., Santamaria R., Izzo P., Costanzo P., Salvatore F.
Nucleic Acids Res. 12:7401-7410(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Human aldolase isozyme gene: the structure of multispecies aldolase B mRNAs."
Sakakibara M., Mukai T., Yatsuki H., Hori K.
Nucleic Acids Res. 13:5055-5069(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Complete amino acid sequence for human aldolase B derived from cDNA and genomic clones."
Rottmann W.H., Tolan D.R., Penhoet E.E.
Proc. Natl. Acad. Sci. U.S.A. 81:2738-2742(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[4]"Human aldolase B gene: characterization of the genomic aldolase B gene and analysis of sequences required for multiple polyadenylations."
Mukai T., Yatsuki H., Arai Y., Joh K., Matsuhashi S., Hori K.
J. Biochem. 102:1043-1051(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Characterization of the human aldolase B gene."
Tolan D.R., Penhoet E.E.
Mol. Biol. Med. 3:245-264(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"Construction and expression of human aldolase A and B expression plasmids in Escherichia coli host."
Sakakibara M., Takahashi I., Takasaki Y., Mukai T., Hori K.
Biochim. Biophys. Acta 1007:334-342(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-33 AND 357-364.
[9]"Nucleotide sequence of a cDNA clone for human aldolase B."
Besmond C., Dreyfus J.-C., Gregori C., Frain M., Zakin M.M., Sala Trepat J., Kahn A.
Biochem. Biophys. Res. Commun. 117:601-609(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 238-364.
[10]"Novel interaction partners of Bardet-Biedl syndrome proteins."
Oeffner F., Moch C., Neundorf A., Hofmann J., Koch M., Grzeschik K.H.
Cell Motil. Cytoskeleton 65:143-155(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BBS1; BBS2; BBS4 AND BBS7, SUBCELLULAR LOCATION.
[11]"The structure of human liver fructose-1,6-bisphosphate aldolase."
Dalby A.R., Tolan D.R., Littlechild J.A.
Acta Crystallogr. D 57:1526-1533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[12]"Molecular basis of hereditary fructose intolerance: mutations and polymorphisms in the human aldolase B gene."
Tolan D.R.
Hum. Mutat. 6:210-218(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[13]"Catalytic deficiency of human aldolase B in hereditary fructose intolerance caused by a common missense mutation."
Cross N.C.P., Tolan D.R., Cox T.M.
Cell 53:881-885(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HFI PRO-150.
[14]"Molecular analysis of aldolase B genes in hereditary fructose intolerance."
Cross N.C.P., de Franchis R., Sebastio G., Dazzo C., Tolan D.R., Gregori C., Odievre M., Vidailhet M., Romano V., Mascali G., Romano C., Musumeci S., Steinmann B., Gitzelmann R., Cox T.M.
Lancet 335:306-309(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HFI ASP-175.
[15]"A partially active mutant aldolase B from a patient with hereditary fructose intolerance."
Brooks C.C., Tolan D.R.
FASEB J. 8:107-113(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HFI ARG-135.
[16]"Diverse mutations in the aldolase B gene that underlie the prevalence of hereditary fructose intolerance."
Ali M., Cox T.M.
Am. J. Hum. Genet. 56:1002-1005(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARG-148.
[17]"Identification of a novel mutation (Leu 256-->Pro) in the human aldolase B gene associated with hereditary fructose intolerance."
Ali M., Sebastio G., Cox T.M.
Hum. Mol. Genet. 3:203-204(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HFI PRO-257.
[18]"A new aldolase B variant, N334K, is a common cause of hereditary fructose intolerance in Yugoslavia."
Cross N.C.P., Stojanov L.M., Cox T.M.
Nucleic Acids Res. 18:1925-1925(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HFI LYS-335.
[19]"Screening for hereditary fructose intolerance mutations by reverse dot-blot."
Lau J., Tolan D.R.
Mol. Cell. Probes 13:35-40(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HFI PRO-150; ASP-175; PRO-257; TRP-304; LYS-335 AND VAL-338.
[20]"Functional and molecular modelling studies of two hereditary fructose intolerance-causing mutations at arginine 303 in human liver aldolase."
Santamaria R., Esposito G., Vitagliano L., Race V., Paglionico I., Zancan L., Zagari A., Salvatore F.
Biochem. J. 350:823-828(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HFI GLN-304 AND TRP-304, CHARACTERIZATION OF VARIANTS HFI GLN-304 AND TRP-304, KINETIC PARAMETERS.
[21]"Molecular analysis of the aldolase B gene in patients with hereditary fructose intolerance from Spain."
Sanchez-Gutierrez J.C., Benlloch T., Leal M.A., Samper B., Garcia-Ripoll I., Feliu J.E.
J. Med. Genet. 39:E56-E56(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HFI PRO-150; ASP-175; ARG-185 AND LYS-335.
[22]"Six novel alleles identified in Italian hereditary fructose intolerance patients enlarge the mutation spectrum of the aldolase B gene."
Esposito G., Santamaria R., Vitagliano L., Ieno L., Viola A., Fiori L., Parenti G., Zancan L., Zagari A., Salvatore F.
Hum. Mutat. 24:534-534(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HFI THR-74; 120-ASN-LYS-121 DEL; PRO-150; ASP-175; PHE-222; PRO-229; PRO-257; LYS-335 AND VAL-338, CHARACTERIZATION OF VARIANTS HFI THR-74; PHE-222 AND PRO-229.
[23]"The spectrum of aldolase B (ALDOB) mutations and the prevalence of hereditary fructose intolerance in Central Europe."
Santer R., Rischewski J., von Weihe M., Niederhaus M., Schneppenheim S., Baerlocher K., Kohlschuetter A., Muntau A., Posselt H.-G., Steinmann B., Schneppenheim R.
Hum. Mutat. 25:594-594(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HFI PRO-150; ASP-175; ARG-178; PRO-284 AND LYS-335.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02747 mRNA. Translation: CAA26526.1.
D00183 Genomic DNA. Translation: BAA00125.1.
M15656, M15657 Genomic DNA. Translation: AAA51691.1.
AL353621 Genomic DNA. Translation: CAI14614.1.
CH471105 Genomic DNA. Translation: EAW58951.1.
X00270 mRNA. Translation: CAA25072.1.
X01098 mRNA. Translation: CAA25572.1.
PIRADHUB. A41505.
RefSeqNP_000026.2. NM_000035.3.
UniGeneHs.530274.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QO5X-ray2.50A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R2-364[»]
1XDLX-ray3.00A/B/C/D/W/X/Y/Z2-363[»]
1XDMX-ray3.00A/B/C/D/W/X/Y/Z2-363[»]
ProteinModelPortalP05062.
SMRP05062. Positions 2-361.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106730. 12 interactions.
IntActP05062. 14 interactions.
STRING9606.ENSP00000363988.

PTM databases

PhosphoSiteP05062.

Polymorphism databases

DMDM113611.

Proteomic databases

PaxDbP05062.
PeptideAtlasP05062.
PRIDEP05062.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374855; ENSP00000363988; ENSG00000136872.
GeneID229.
KEGGhsa:229.
UCSCuc004bbk.2. human.

Organism-specific databases

CTD229.
GeneCardsGC09M104182.
H-InvDBHIX0125611.
HGNCHGNC:417. ALDOB.
HPACAB020827.
HPA002198.
MIM229600. phenotype.
612724. gene.
neXtProtNX_P05062.
Orphanet469. Hereditary fructose intolerance.
PharmGKBPA24710.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3588.
HOGENOMHOG000220876.
HOVERGENHBG002386.
InParanoidP05062.
KOK01623.
OMADMEHCQY.
OrthoDBEOG744T94.
PhylomeDBP05062.
TreeFamTF314203.

Enzyme and pathway databases

BioCycMetaCyc:HS06234-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP05062.
UniPathwayUPA00109; UER00183.

Gene expression databases

BgeeP05062.
CleanExHS_ALDOB.
GenevestigatorP05062.

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. human.
EvolutionaryTraceP05062.
GeneWikiAldolase_B.
GenomeRNAi229.
NextBio930.
PROP05062.
SOURCESearch...

Entry information

Entry nameALDOB_HUMAN
AccessionPrimary (citable) accession number: P05062
Secondary accession number(s): Q13741, Q13742, Q5T7D6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM