[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; PubMed=3840020 [NCBI, ExPASy, EBI, Israel, Japan] Sakakibara M., Mukai T., Hori K.; "Nucleotide sequence of a cDNA clone for human aldolase: a messenger RNA in the liver."; Biochem. Biophys. Res. Commun. 131:413-420(1985).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Fibroblast; DOI=10.1111/j.1432-1033.1987.tb10984.x; PubMed=3030757 [NCBI, ExPASy, EBI, Israel, Japan] Izzo P., Costanzo P., Lupo A., Rippa E., Borghese A.M., Paolella G., Salvatore F.; "A new human species of aldolase A mRNA from fibroblasts."; Eur. J. Biochem. 164:9-13(1987).
[3]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1111/j.1432-1033.1988.tb14136.x; PubMed=3391172 [NCBI, ExPASy, EBI, Israel, Japan] Izzo P., Costanzo P., Lupo A., Rippa E., Paolella G., Salvatore F.; "Human aldolase A gene. Structural organization and tissue-specific expression by multiple promoters and alternate mRNA processing."; Eur. J. Biochem. 174:569-578(1988).
[4]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1111/j.1432-1033.1991.tb15766.x; PubMed=1999195 [NCBI, ExPASy, EBI, Israel, Japan] Mukai T., Arai Y., Yatsuki H., Joh K., Hori K.; "An additional promoter functions in the human aldolase A gene, but not in rat."; Eur. J. Biochem. 195:781-787(1991).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."; Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Cervix, Eye, Lung, Testis, and Uterus; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[7]	PROTEIN SEQUENCE OF 2-364. PubMed=3355497 [NCBI, ExPASy, EBI, Israel, Japan] Freemont P.S., Dunbar B., Fothergill-Gilmore L.A.; "The complete amino acid sequence of human skeletal-muscle fructose-bisphosphate aldolase."; Biochem. J. 249:779-788(1988).
[8]	PROTEIN SEQUENCE OF 2-63 AND 148-358. DOI=10.1016/0003-9861(84)90075-4; PubMed=6696436 [NCBI, ExPASy, EBI, Israel, Japan] Freemont P.S., Dunbar B., Fothergill L.A.; "Human skeletal-muscle aldolase: N-terminal sequence analysis of CNBr- and o-iodosobenzoic acid-cleavage fragments."; Arch. Biochem. Biophys. 228:342-352(1984).
[9]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-108. DOI=10.1016/0022-2836(87)90556-0; PubMed=3441006 [NCBI, ExPASy, EBI, Israel, Japan] Maire P., Gautron S., Hakim V., Gregori C., Mennecier F., Kahn A.; "Characterization of three optional promoters in the 5' region of the human aldolase A gene."; J. Mol. Biol. 197:425-438(1987).
[10]	PROTEIN SEQUENCE OF 2-22. TISSUE=Platelet; DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan] Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.; "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."; Nat. Biotechnol. 21:566-569(2003).
[11]	PROTEIN SEQUENCE OF 88-99 AND 244-258, AND MASS SPECTROMETRY. TISSUE=Brain, and Cajal-Retzius cell; Lubec G., Vishwanath V.; Submitted (MAR-2007) to UniProtKB.
[12]	NUCLEOTIDE SEQUENCE [MRNA] OF 139-364. PubMed=3674018 [NCBI, ExPASy, EBI, Israel, Japan] Tolan D.R., Niclas J., Bruce B.D., Lebo R.V.; "Evolutionary implications of the human aldolase-A, -B, -C, and - pseudogene chromosome locations."; Am. J. Hum. Genet. 41:907-924(1987).
[13]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-204, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan] Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.; "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; Nat. Biotechnol. 23:94-101(2005).
[14]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-65, AND MASS SPECTROMETRY. TISSUE=Hepatocyte; DOI=10.1002/pmic.200401217; PubMed=16097034 [NCBI, ExPASy, EBI, Israel, Japan] Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K., Demol H., Martens L., Goethals M., Vandekerckhove J.; "Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC."; Proteomics 5:3589-3599(2005).
[15]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."; Cell 127:635-648(2006).
[16]	ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-13 AND LYS-42, AND MASS SPECTROMETRY. DOI=10.1016/j.molcel.2006.06.026; PubMed=16916647 [NCBI, ExPASy, EBI, Israel, Japan] Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; "Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."; Mol. Cell 23:607-618(2006).
[17]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-3; TYR-5 AND TYR-223, AND MASS SPECTROMETRY. DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan] Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; "Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."; Cell 131:1190-1203(2007).
[18]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-235; THR-241; SER-354 AND SER-356, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan] Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; "Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[19]	X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). DOI=10.1016/0014-5793(90)80211-Z; PubMed=2335208 [NCBI, ExPASy, EBI, Israel, Japan] Gamblin S.J., Cooper B., Millar J.R., Davies G.J., Littlechild J.A., Watson H.C.; "The crystal structure of human muscle aldolase at 3.0-A resolution."; FEBS Lett. 262:282-286(1990).
[20]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). DOI=10.1016/0022-2836(91)90650-U; PubMed=2056525 [NCBI, ExPASy, EBI, Israel, Japan] Gamblin S.J., Davies G.J., Grimes J.M., Jackson R.M., Littlechild J.A., Watson H.C.; "Activity and specificity of human aldolases."; J. Mol. Biol. 219:573-576(1991).
[21]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). PubMed=10048322 [NCBI, ExPASy, EBI, Israel, Japan] Dalby A., Dauter Z., Littlechild J.A.; "Crystal structure of human muscle aldolase complexed with fructose 1,6-bisphosphate: mechanistic implications."; Protein Sci. 8:291-297(1999).
[22]	VARIANT ALDOLASE A DEFICIENCY GLY-129, AND CHARACTERIZATION OF VARIANT ALDOLASE A DEFICIENCY GLY-129. PubMed=2825199 [NCBI, ExPASy, EBI, Israel, Japan] Kishi H., Mukai T., Hirono A., Fujii H., Miwa S., Hori K.; "Human aldolase A deficiency associated with a hemolytic anemia: thermolabile aldolase due to a single base mutation."; Proc. Natl. Acad. Sci. U.S.A. 84:8623-8627(1987).
[23]	CHARACTERIZATION OF VARIANT ALDOLASE A DEFICIENCY GLY-129. PubMed=2229018 [NCBI, ExPASy, EBI, Israel, Japan] Takasaki Y., Takahashi I., Mukai T., Hori K.; "Human aldolase A of a hemolytic anemia patient with Asp-128-->Gly substitution: characteristics of an enzyme generated in E. coli transfected with the expression plasmid pHAAD128G."; J. Biochem. 108:153-157(1990).
[24]	VARIANT ALDOLASE A DEFICIENCY LYS-207. DOI=10.1056/NEJM199604253341705; PubMed=8598869 [NCBI, ExPASy, EBI, Israel, Japan] Kreuder J., Borkhardt A., Repp R., Pekrun A., Goettsche B., Gottschalk U., Reichmann H., Schachenmayr W., Schlegel K., Lampert F.; "Brief report: inherited metabolic myopathy and hemolysis due to a mutation in aldolase A."; N. Engl. J. Med. 334:1100-1104(1996).
[25]	VARIANT ALDOLASE A DEFICIENCY TYR-339. DOI=10.1182/blood-2003-09-3160; PubMed=14615364 [NCBI, ExPASy, EBI, Israel, Japan] Yao D.C., Tolan D.R., Murray M.F., Harris D.J., Darras B.T., Geva A., Neufeld E.J.; "Hemolytic anemia and severe rhabdomyolysis caused by compound heterozygous mutations of the gene for erythrocyte/muscle isozyme of aldolase, ALDOA(Arg303X/Cys338Tyr)."; Blood 103:2401-2403(2004).
[26]	VARIANT ALDOLASE A DEFICIENCY SER-347, BIOPHYSICOCHEMICAL PROPERTIES, AND CHARACTERIZATION OF VARIANTS ALDOLASE A DEFICIENCY LYS-207 AND SER-347. DOI=10.1042/BJ20031941; PubMed=14766013 [NCBI, ExPASy, EBI, Israel, Japan] Esposito G., Vitagliano L., Costanzo P., Borrelli L., Barone R., Pavone L., Izzo P., Zagari A., Salvatore F.; "Human aldolase A natural mutants: relationship between flexibility of the C-terminal region and enzyme function."; Biochem. J. 380:51-56(2004).

Comments

CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters: K_M=52 µM for fructose 1,6-bisphosphate (at 30 degrees Celsius);
Temperature dependence: Thermal denaturation midpoint (Tm) is 54.4 degrees Celsius;
PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4 .
SUBUNIT: Homotetramer.
INTERACTION:
Q8IZH2:XRN1; NbExp=1; IntAct=EBI-709613, EBI-372406;
DISEASE: Defects in ALDOA are the cause of aldolase A deficiency [MIM:611881]; also known as aldoA deficiency or red cell aldolase deficiency. Aldolase A deficiency is an autosomal recessive disorder associated with hereditary hemolytic anemia.
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.
SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase family.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=ALDOA";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M11560; AAA51690.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X05236; CAA28861.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X12447; CAA30979.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR541880; CAG46678.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000367; AAH00367.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC004333; AAH04333.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010660; AAH10660.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012880; AAH12880.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC013614; AAH13614.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC015888; AAH15888.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC016170; AAH16170.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC016800; AAH16800.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M21190; AAA51697.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S14084; ADHUA.

RefSeq

NP_000025.1; -.
NP_001121089.1; -.
NP_908930.1; -.
NP_908932.1; -.

UniGene

Hs.513490

3D structure databases

PDB

1ALD; X-ray; 2.00 A; A=1-364.	[ExPASy / RCSB / EBI]
2ALD; X-ray; 2.10 A; A=1-364.	[ExPASy / RCSB / EBI]
4ALD; X-ray; 2.80 A; A=1-364.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1ALD; -.
2ALD; -.
4ALD; -.

ModBase

P04075.

Protein-protein interaction databases

IntAct

P04075; -.

PTM databases

PhosphoSite

P04075; -.

Enzyme and pathway databases

Reactome

REACT_1709; Metabolism of small molecules.

2D gel databases

P04075; -.

1302; NEPHGE.

P04075; -.

P04075; -.

IPI00465439; -.
P04075; -.

Siena-2DPAGE

P04075; -.

Organism-specific databases

HIX0012935; -.

HGNC:414; ALDOA.

CAB006252; -.
HPA004177; -.

MIM

103850; gene. [NCBI / EBI]
611881; phenotype. [NCBI / EBI]

Orphanet

57; Aldolase A deficiency.

PharmGKB

PA24707; -.

GeneCards

P04075.

Gene expression databases

ArrayExpress

P04075; -.

CleanEx

HS_ALDOA; -.

GermOnline

ENSG00000149925; Homo sapiens.

Ontologies

GO:0015629;	Cellular component: actin cytoskeleton (inferred from direct assay from UniProtKB).
GO:0070062;	Cellular component: extracellular vesicular exosome (inferred from direct assay from UniProtKB).
GO:0031674;	Cellular component: I band (traceable author statement from UniProtKB).
GO:0005634;	Cellular component: nucleus (inferred from direct assay from HPA).
GO:0003779;	Molecular function: actin binding (traceable author statement from UniProtKB).
GO:0070061;	Molecular function: fructose binding (inferred from direct assay from UniProtKB).
GO:0004332;	Molecular function: fructose-bisphosphate aldolase activity (inferred from direct assay from UniProtKB).
GO:0042802;	Molecular function: identical protein binding (traceable author statement from UniProtKB).
GO:0015631;	Molecular function: tubulin binding (traceable author statement from UniProtKB).
GO:0007015;	Biological process: actin filament organization (traceable author statement from UniProtKB).
GO:0006754;	Biological process: ATP biosynthetic process (inferred from mutant phenotype from UniProtKB).
GO:0030388;	Biological process: fructose 1,6-bisphosphate metabolic process (inferred from direct assay from UniProtKB).
GO:0006096;	Biological process: glycolysis (inferred from mutant phenotype from UniProtKB).
GO:0046716;	Biological process: muscle maintenance (inferred from mutant phenotype from UniProtKB).
GO:0008360;	Biological process: regulation of cell shape (inferred from direct assay from UniProtKB).
GO:0006941;	Biological process: striated muscle contraction (inferred from mutant phenotype from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR000741; Aldolase_I.
IPR013785; Aldolase_TIM.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.70; Aldolase_TIM; 1.

PANTHER

PTHR11627; Aldolase_I; 1.

Pfam

PF00274; Glycolytic; 1.
Pfam graphical view of domain structure.

ProDom

PD001128; Aldolase_I; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00158; ALDOLASE_CLASS_I; 1.

Other

Genome annotation databases

Ensembl

ENSG00000149925; Homo sapiens. [Contig view]

GeneID

226; -.

KEGG

hsa:226; -.

Phylogenomic databases

HOGENOM

P04075; -.

HOVERGEN

P04075; -.

Other

P04075; -.

920; -.

ALDOA; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; Direct protein sequencing; Disease mutation; Glycolysis; Hereditary hemolytic anemia; Lyase; Phosphoprotein; Schiff base.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 364`	`363`	`Fructose-bisphosphate aldolase A.`	`PRO_0000216936`
`ACT_SITE`	`188 188`		`Proton acceptor (By similarity).`
`ACT_SITE`	`230 230`		`Schiff-base intermediate with dihydroxyacetone-P.`
`BINDING`	`56 56`		`Substrate.`
`BINDING`	`147 147`		`Substrate.`
`SITE`	`364 364`	`1`	`Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate.`
`MOD_RES`	`3 3`		`Phosphotyrosine.`
`MOD_RES`	`5 5`		`Phosphotyrosine.`
`MOD_RES`	`13 13`		`N6-acetyllysine.`
`MOD_RES`	`36 36`		`Phosphoserine (By similarity).`
`MOD_RES`	`39 39`		`Phosphoserine (By similarity).`
`MOD_RES`	`42 42`		`N6-acetyllysine.`
`MOD_RES`	`46 46`		`Phosphoserine.`
`MOD_RES`	`65 65`		`Phosphothreonine.`
`MOD_RES`	`204 204`		`Phosphotyrosine.`
`MOD_RES`	`223 223`		`Phosphotyrosine.`
`MOD_RES`	`235 235`		`Phosphothreonine.`
`MOD_RES`	`241 241`		`Phosphothreonine.`
`MOD_RES`	`354 354`		`Phosphoserine.`
`MOD_RES`	`356 356`		`Phosphoserine.`
`VARIANT`	`129 129`	`1`	`D -> G (in aldolase A deficiency; thermolabile).`	`VAR_000550 [3D]`
`VARIANT`	`207 207`	`1`	`E -> K (in aldolase A deficiency; reduces thermal stability; 3-fold decrease in catalytic efficiency mostly due to reduced substrate affinity).`	`VAR_044142 [3D]`
`VARIANT`	`339 339`	`1`	`C -> Y (in aldolase A deficiency).`	`VAR_044143 [3D]`
`VARIANT`	`347 347`	`1`	`G -> S (in aldolase A deficiency; does not affect thermal stability; 4-fold decrease in catalytic efficiency due to reduced enzyme activity).`	`VAR_044144 [3D]`
`CONFLICT`	`180 180`		`Q -> R (in Ref. 5; CAG46678).`
`HELIX`	`10 23`	`14`
`STRAND`	`29 33`	`5`
`HELIX`	`37 46`	`10`
`HELIX`	`53 64`	`12`
`HELIX`	`68 73`	`6`
`STRAND`	`74 79`	`6`
`HELIX`	`83 85`	`3`
`HELIX`	`94 100`	`7`
`STRAND`	`104 108`	`5`
`STRAND`	`113 115`	`3`
`STRAND`	`119 121`	`3`
`STRAND`	`123 125`	`3`
`HELIX`	`131 140`	`10`
`STRAND`	`145 152`	`8`
`HELIX`	`161 179`	`19`
`TURN`	`180 182`	`3`
`STRAND`	`184 191`	`8`
`HELIX`	`199 219`	`21`
`HELIX`	`224 226`	`3`
`HELIX`	`246 258`	`13`
`STRAND`	`267 270`	`4`
`HELIX`	`277 289`	`13`
`STRAND`	`296 303`	`8`
`HELIX`	`304 314`	`11`
`HELIX`	`318 320`	`3`
`HELIX`	`321 338`	`18`
`TURN`	`339 341`	`3`
`STRAND`	`348 350`	`3`

Sequence information

Length: 364 AA [This is the length of the unprocessed precursor]

Molecular weight: 39420 Da [This is the MW of the unprocessed precursor]

CRC64: 0AAED80F755A7BE8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPYQYPALTP EQKKELSDIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE NTEENRRFYR 

        70         80         90        100        110        120 
QLLLTADDRV NPCIGGVILF HETLYQKADD GRPFPQVIKS KGGVVGIKVD KGVVPLAGTN 

       130        140        150        160        170        180 
GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKIGEHTPS ALAIMENANV LARYASICQQ 

       190        200        210        220        230        240 
NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HIYLEGTLLK PNMVTPGHAC 

       250        260        270        280        290        300 
TQKFSHEEIA MATVTALRRT VPPAVTGITF LSGGQSEEEA SINLNAINKC PLLKPWALTF 

       310        320        330        340        350        360 
SYGRALQASA LKAWGGKKEN LKAAQEEYVK RALANSLACQ GKYTPSGQAG AAASESLFVS 


NHAY

P04075 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL