P05062 (ALDOB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fructose-bisphosphate aldolase B
EC=4.1.2.13

Alternative name(s):
Liver-type aldolase

Gene names

Name:	ALDOB
Synonyms:	ALDB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	364 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
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.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22
Miscellaneous	In vertebrates, three 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.19 KM=2.3 mM for fructose 1-phosphate

Ontologies

Keywords
Biological process	Glycolysis
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Ligand	Schiff base
Molecular function	Lyase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	NADH 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_component	centriolar satellite Inferred from direct assay PubMed 18000879. Source: BHF-UCL cytosol Traceable author statement. Source: Reactome
Molecular_function	ATPase 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BBS1	Q8NFJ9	4	EBI-1045507,EBI-1805484
BBS2	Q9BXC9	4	EBI-1045507,EBI-748297
BBS4	Q96RK4	4	EBI-1045507,EBI-1805814
BBS7	Q8IWZ6	4	EBI-1045507,EBI-1806001

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8

Chain

2 – 364

363

Fructose-bisphosphate aldolase B

PRO_0000216940

Sites

Active site

188

1

Proton acceptor By similarity

Active site

230

1

Schiff-base intermediate with dihydroxyacetone-P

Binding site

56

1

Substrate

Binding site

147

1

Substrate

Site

364

1

Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Modified residue

36

1

Phosphoserine By similarity

Natural variations

Natural variant

74

1

I → T in HFI; affects proper folding. Ref.21

VAR_020822

Natural variant

120 – 121

2

Missing in HFI.

VAR_020823

Natural variant

134

1

R → S.
Corresponds to variant rs10123355 [ dbSNP | Ensembl ].

VAR_038429

Natural variant

135

1

C → R in HFI; America; partial activity. Ref.14

VAR_000551

Natural variant

148

1

W → R in one subject with fructose intolerance; rare variant; America. Ref.15

VAR_000552

Natural variant

150

1

A → P in HFI; frequent mutation. Ref.12 Ref.18 Ref.20 Ref.21 Ref.22
Corresponds to variant rs1800546 [ dbSNP | Ensembl ].

VAR_000553

Natural variant

175

1

A → D in HFI; frequent mutation. Ref.13 Ref.18 Ref.20 Ref.21 Ref.22

VAR_000554

Natural variant

178

1

C → R in HFI. Ref.22

VAR_058211

Natural variant

185

1

P → R in HFI. Ref.20

VAR_020824

Natural variant

207

1

E → Q.
Corresponds to variant rs3739721 [ dbSNP | Ensembl ].

VAR_020825

Natural variant

222

1

V → F in HFI; affects proper folding. Ref.21

VAR_020826

Natural variant

229

1

L → P in HFI; affects proper folding. Ref.21

VAR_020827

Natural variant

257

1

L → P in HFI; Italy. Ref.16 Ref.18 Ref.21

VAR_000555

Natural variant

268

1

I → N.
Corresponds to variant rs10989495 [ dbSNP | Ensembl ].

VAR_038430

Natural variant

284

1

L → P in HFI. Ref.22

VAR_058212

Natural variant

304

1

R → Q in HFI; 100-fold decrease in catalytic efficiency for substrates FBP and F1P. Ref.19

VAR_020828

Natural variant

304

1

R → W in HFI; Turkey; 4800-fold decrease in catalytic efficiency for FBP and inactive with F1P. Ref.18 Ref.19

VAR_000556

Natural variant

335

1

N → K in HFI; frequent mutation. Ref.17 Ref.18 Ref.20 Ref.21 Ref.22

VAR_000557

Natural variant

338

1

A → V in HFI; Turkey and South Europe. Ref.18 Ref.21

VAR_000558

Experimental info

Sequence conflict

54

1

E → D in AAA51691. Ref.5

Sequence conflict

250

1

A → D in CAA25072. Ref.9

Sequence conflict

278

1

E → D in BAA00125. Ref.4

Sequence conflict

309

1

S → V no nucleotide entry Ref.3

Sequence conflict

348

1

S → C in BAA00125. Ref.4

Secondary structure

1

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364

Helix Strand Turn

Details...

Helix

10 – 23

14

Turn

25 – 27

3

Beta strand

29 – 33

5

Helix

37 – 46

10

Helix

53 – 64

12

Helix

68 – 72

5

Beta strand

74 – 79

6

Helix

83 – 85

3

Turn

89 – 91

3

Helix

94 – 100

7

Beta strand

104 – 108

5

Beta strand

113 – 115

3

Beta strand

119 – 121

3

Beta strand

123 – 125

3

Helix

131 – 140

10

Beta strand

145 – 152

8

Helix

161 – 179

19

Turn

180 – 182

3

Beta strand

184 – 191

8

Helix

199 – 219

21

Helix

224 – 226

3

Helix

246 – 260

15

Beta strand

267 – 271

5

Helix

277 – 289

13

Beta strand

290 – 292

3

Beta strand

296 – 303

8

Helix

304 – 306

3

Helix

308 – 314

7

Helix

318 – 320

3

Helix

321 – 338

18

Turn

339 – 341

3

Helix

351 – 354

4

Sequences

	Sequence		Length	Mass (Da)
	P05062 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: DCE314E7AC5586CA	FASTA	364	39,473
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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).
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

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.

IPI

IPI00218407.

PIR

ADHUB. A41505.

RefSeq

NP_000026.2. NM_000035.3.

UniGene

Hs.530274.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QO5	X-ray	2.50	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R	2-364	[»]
1XDL	X-ray	3.00	A/B/C/D/W/X/Y/Z	2-363	[»]
1XDM	X-ray	3.00	A/B/C/D/W/X/Y/Z	2-363	[»]

ProteinModelPortal

P05062.

ModBase

Search...

Protein-protein interaction databases

IntAct

P05062. 14 interactions.

STRING

9606.ENSP00000363988.

PTM databases

PhosphoSite

P05062.

Polymorphism databases

DMDM

113611.

Proteomic databases

PaxDb

P05062.

PeptideAtlas

P05062.

PRIDE

P05062.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000374855; ENSP00000363988; ENSG00000136872.

GeneID

229.

KEGG

hsa:229.

UCSC

uc004bbk.2. human.

Organism-specific databases

CTD

229.

GeneCards

GC09M104182.

H-InvDB

HIX0125611.

HGNC

HGNC:417. ALDOB.

HPA

CAB020827.
HPA002198.

MIM

229600. phenotype.
612724. gene.

neXtProt

NX_P05062.

Orphanet

469. Hereditary fructose intolerance.

PharmGKB

PA24710.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG3588.

HOGENOM

HOG000220876.

HOVERGEN

HBG002386.

InParanoid

P05062.

KO

K01623.

OMA

IDNQCPS.

OrthoDB

EOG444KKK.

PhylomeDB

P05062.

Enzyme and pathway databases

BioCyc

MetaCyc:HS06234-MONOMER.

Pathway_Interaction_DB

hnf3bpathway. FOXA2 and FOXA3 transcription factor networks.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P05062.

UniPathway

UPA00109; UER00183.

Gene expression databases

ArrayExpress

P05062.

Bgee

P05062.

CleanEx

HS_ALDOB.

Genevestigator

P05062.

GermOnline

ENSG00000136872. Homo sapiens.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

InterPro

IPR000741. Aldolase_I.
IPR013785. Aldolase_TIM.
[Graphical view]

PANTHER

PTHR11627. PTHR11627. 1 hit.

Pfam

PF00274. Glycolytic. 1 hit.
[Graphical view]

PROSITE

PS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ALDOB. human.

EvolutionaryTrace

P05062.

GenomeRNAi

229.

NextBio

930.

SOURCE

Search...

Entry information

Entry name

ALDOB_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 154 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.