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P45381

- ACY2_HUMAN

UniProt

P45381 - ACY2_HUMAN

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Protein

Aspartoacylase

Gene

ASPA

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

Functioni

Catalyzes the deacetylation of N-acetylaspartic acid (NAA) to produce acetate and L-aspartate. NAA occurs in high concentration in brain and its hydrolysis NAA plays a significant part in the maintenance of intact white matter. In other tissues it act as a scavenger of NAA from body fluids.

Catalytic activityi

N-acyl-L-aspartate + H2O = a carboxylate + L-aspartate.1 Publication

Cofactori

Zn2+2 PublicationsNote: Binds 1 zinc ion per subunit.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi21 – 211Zinc
Metal bindingi24 – 241Zinc
Binding sitei63 – 631Substrate
Metal bindingi116 – 1161Zinc
Active sitei178 – 17811 Publication
Binding sitei178 – 1781Substrate
Binding sitei288 – 2881Substrate

GO - Molecular functioni

  1. aminoacylase activity Source: ProtInc
  2. aspartoacylase activity Source: UniProtKB-EC
  3. hydrolase activity, acting on ester bonds Source: InterPro
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. aspartate catabolic process Source: ProtInc
  2. central nervous system myelination Source: Ensembl
  3. positive regulation of oligodendrocyte differentiation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:HS03094-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartoacylase (EC:3.5.1.15)
Alternative name(s):
Aminoacylase-2
Short name:
ACY-2
Gene namesi
Name:ASPA
Synonyms:ACY2, ASP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:756. ASPA.

Subcellular locationi

Cytoplasm. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. extracellular vesicular exosome Source: UniProt
  3. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Canavan disease (CAND) [MIM:271900]: A rare neurodegenerative condition of infancy or childhood characterized by white matter vacuolization and demyelination that gives rise to a spongy appearance. The clinical features are onset in early infancy, atonia of neck muscles, hypotonia, hyperextension of legs and flexion of arms, blindness, severe mental defect, megalocephaly, and death by 18 months on the average.11 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti16 – 161I → T in CAND; <0.5% residual enzyme activity. 2 Publications
VAR_039079
Natural varianti21 – 211H → P in CAND. 1 Publication
VAR_016778
Natural varianti24 – 241E → G in CAND. 1 Publication
VAR_016782
Natural varianti27 – 271G → R in CAND; 3% residual enzyme activity. 2 Publications
VAR_039080
Natural varianti57 – 571A → T in CAND. 1 Publication
VAR_016779
Natural varianti68 – 681D → A in CAND. 1 Publication
VAR_016783
Natural varianti114 – 1141D → E in CAND; <0.5% residual enzyme activity. 1 Publication
VAR_039081
Natural varianti114 – 1141D → Y in CAND. 1 Publication
VAR_016784
Natural varianti123 – 1231G → E in CAND; about 25% residual enzyme activity. 1 Publication
VAR_039082
Natural varianti143 – 1431I → T in CAND; in a Japanese patient. 1 Publication
VAR_004995
Natural varianti152 – 1521C → R in CAND; loss of activity. 1 Publication
VAR_004996
Natural varianti152 – 1521C → W in CAND. 1 Publication
VAR_016785
Natural varianti152 – 1521C → Y in CAND; <0.5% residual enzyme activity. 1 Publication
VAR_039083
Natural varianti168 – 1681R → C in CAND; undetectable enzyme activity. 1 Publication
VAR_039084
Natural varianti168 – 1681R → H in CAND. 1 Publication
VAR_016780
Natural varianti176 – 1772Missing in CAND. 1 Publication
VAR_004997
Natural varianti181 – 1811P → T in CAND. 1 Publication
VAR_016781
Natural varianti183 – 1831P → H in CAND. 1 Publication
VAR_039085
Natural varianti186 – 1861V → F in CAND. 1 Publication
VAR_039086
Natural varianti195 – 1951M → R in CAND. 1 Publication
VAR_039087
Natural varianti231 – 2311Y → C in CAND. 1 Publication
VAR_016786
Natural varianti244 – 2441H → R in CAND. 1 Publication
VAR_016787
Natural varianti249 – 2491D → V in CAND. 2 Publications
VAR_016788
Natural varianti274 – 2741G → R in CAND. 2 Publications
VAR_004998
Natural varianti280 – 2801P → L in CAND. 1 Publication
VAR_039088
Natural varianti280 – 2801P → S in CAND. 1 Publication
VAR_039089
Natural varianti285 – 2851E → A in CAND; predominant mutation in Ashkenazi Jewish population; 99% loss of activity. 3 Publications
Corresponds to variant rs28940279 [ dbSNP | Ensembl ].
VAR_004999
Natural varianti287 – 2871A → T in CAND. 1 Publication
VAR_039090
Natural varianti295 – 2951F → S in CAND. 2 Publications
VAR_005000
Natural varianti305 – 3051A → E in CAND; loss of activity; pan-European origin; most prevalent among non-Jewish CAND patients; probably the most ancient mutation. 4 Publications
Corresponds to variant rs28940574 [ dbSNP | Ensembl ].
VAR_005001

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi71 – 711R → K: Reduces activity by 99%. 1 Publication
Mutagenesisi164 – 1641Y → F: Reduces activity by 99%. 1 Publication
Mutagenesisi168 – 1681R → K: Reduces activity by 99%. 1 Publication
Mutagenesisi178 – 1781E → A: Reduces activity by 99%. 2 Publications
Mutagenesisi178 – 1781E → D: Abolishes enzymatic activity. 2 Publications
Mutagenesisi178 – 1781E → Q: Abolishes enzymatic activity. 2 Publications
Mutagenesisi285 – 2851E → D: 5-fold decrease in activity. 1 Publication
Mutagenesisi288 – 2881Y → F: Reduces activity by 99%. 1 Publication

Keywords - Diseasei

Disease mutation, Leukodystrophy

Organism-specific databases

MIMi271900. phenotype.
Orphaneti314918. Mild Canavan disease.
314911. Severe Canavan disease.
PharmGKBiPA25055.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 313313AspartoacylasePRO_0000216871Add
BLAST

Proteomic databases

PaxDbiP45381.
PRIDEiP45381.

PTM databases

PhosphoSiteiP45381.

Expressioni

Tissue specificityi

Brain white matter, skeletal muscle, kidney, adrenal glands, lung and liver.

Gene expression databases

BgeeiP45381.
CleanExiHS_ASPA.
ExpressionAtlasiP45381. baseline and differential.
GenevestigatoriP45381.

Organism-specific databases

HPAiHPA022142.
HPA022145.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi106935. 1 interaction.
DIPiDIP-60793N.
MINTiMINT-1440951.
STRINGi9606.ENSP00000263080.

Structurei

Secondary structure

1
313
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 185Combined sources
Helixi25 – 3410Combined sources
Helixi39 – 413Combined sources
Beta strandi48 – 536Combined sources
Helixi55 – 595Combined sources
Beta strandi65 – 673Combined sources
Helixi69 – 713Combined sources
Helixi75 – 784Combined sources
Beta strandi84 – 863Combined sources
Helixi88 – 10013Combined sources
Beta strandi105 – 1084Combined sources
Beta strandi110 – 1178Combined sources
Beta strandi119 – 1213Combined sources
Beta strandi123 – 1297Combined sources
Helixi134 – 14714Combined sources
Beta strandi152 – 1565Combined sources
Beta strandi160 – 1623Combined sources
Helixi167 – 1704Combined sources
Beta strandi171 – 18111Combined sources
Helixi189 – 21022Combined sources
Beta strandi218 – 22912Combined sources
Beta strandi237 – 2393Combined sources
Beta strandi241 – 2433Combined sources
Turni245 – 2495Combined sources
Beta strandi259 – 2635Combined sources
Beta strandi269 – 2713Combined sources
Beta strandi274 – 2763Combined sources
Beta strandi278 – 2825Combined sources
Helixi286 – 2883Combined sources
Turni289 – 2924Combined sources
Beta strandi294 – 30512Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2I3CX-ray2.80A/B2-313[»]
2O4HX-ray2.70A/B1-313[»]
2O53X-ray2.70A/B1-313[»]
2Q51X-ray2.80A/B2-313[»]
4MRIX-ray2.80A/B1-313[»]
4MXUX-ray2.60A/B1-313[»]
4NFRX-ray3.00A/B1-313[»]
4TNUX-ray2.90A/B1-313[»]
ProteinModelPortaliP45381.
SMRiP45381. Positions 9-310.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP45381.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni70 – 712Substrate binding
Regioni164 – 1685Substrate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2988.
HOGENOMiHOG000232489.
HOVERGENiHBG004172.
InParanoidiP45381.
KOiK01437.
OMAiTTRSVAK.
PhylomeDBiP45381.
TreeFamiTF328708.

Family and domain databases

HAMAPiMF_00704. Aspartoacylase.
InterProiIPR016708. Aspartoacylase.
IPR007036. Aste_AspA.
[Graphical view]
PfamiPF04952. AstE_AspA. 1 hit.
[Graphical view]
PIRSFiPIRSF018001. Aspartoacylase. 1 hit.

Sequencei

Sequence statusi: Complete.

P45381-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTSCHIAEEH IQKVAIFGGT HGNELTGVFL VKHWLENGAE IQRTGLEVKP
60 70 80 90 100
FITNPRAVKK CTRYIDCDLN RIFDLENLGK KMSEDLPYEV RRAQEINHLF
110 120 130 140 150
GPKDSEDSYD IIFDLHNTTS NMGCTLILED SRNNFLIQMF HYIKTSLAPL
160 170 180 190 200
PCYVYLIEHP SLKYATTRSI AKYPVGIEVG PQPQGVLRAD ILDQMRKMIK
210 220 230 240 250
HALDFIHHFN EGKEFPPCAI EVYKIIEKVD YPRDENGEIA AIIHPNLQDQ
260 270 280 290 300
DWKPLHPGDP MFLTLDGKTI PLGGDCTVYP VFVNEAAYYE KKEAFAKTTK
310
LTLNAKSIRC CLH
Length:313
Mass (Da):35,735
Last modified:November 1, 1995 - v1
Checksum:i33C0B9B07839E7F5
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti16 – 161I → T in CAND; <0.5% residual enzyme activity. 2 Publications
VAR_039079
Natural varianti21 – 211H → P in CAND. 1 Publication
VAR_016778
Natural varianti24 – 241E → G in CAND. 1 Publication
VAR_016782
Natural varianti27 – 271G → R in CAND; 3% residual enzyme activity. 2 Publications
VAR_039080
Natural varianti57 – 571A → T in CAND. 1 Publication
VAR_016779
Natural varianti68 – 681D → A in CAND. 1 Publication
VAR_016783
Natural varianti114 – 1141D → E in CAND; <0.5% residual enzyme activity. 1 Publication
VAR_039081
Natural varianti114 – 1141D → Y in CAND. 1 Publication
VAR_016784
Natural varianti123 – 1231G → E in CAND; about 25% residual enzyme activity. 1 Publication
VAR_039082
Natural varianti143 – 1431I → T in CAND; in a Japanese patient. 1 Publication
VAR_004995
Natural varianti152 – 1521C → R in CAND; loss of activity. 1 Publication
VAR_004996
Natural varianti152 – 1521C → W in CAND. 1 Publication
VAR_016785
Natural varianti152 – 1521C → Y in CAND; <0.5% residual enzyme activity. 1 Publication
VAR_039083
Natural varianti168 – 1681R → C in CAND; undetectable enzyme activity. 1 Publication
VAR_039084
Natural varianti168 – 1681R → H in CAND. 1 Publication
VAR_016780
Natural varianti176 – 1772Missing in CAND. 1 Publication
VAR_004997
Natural varianti181 – 1811P → T in CAND. 1 Publication
VAR_016781
Natural varianti183 – 1831P → H in CAND. 1 Publication
VAR_039085
Natural varianti186 – 1861V → F in CAND. 1 Publication
VAR_039086
Natural varianti195 – 1951M → R in CAND. 1 Publication
VAR_039087
Natural varianti231 – 2311Y → C in CAND. 1 Publication
VAR_016786
Natural varianti244 – 2441H → R in CAND. 1 Publication
VAR_016787
Natural varianti249 – 2491D → V in CAND. 2 Publications
VAR_016788
Natural varianti274 – 2741G → R in CAND. 2 Publications
VAR_004998
Natural varianti280 – 2801P → L in CAND. 1 Publication
VAR_039088
Natural varianti280 – 2801P → S in CAND. 1 Publication
VAR_039089
Natural varianti285 – 2851E → A in CAND; predominant mutation in Ashkenazi Jewish population; 99% loss of activity. 3 Publications
Corresponds to variant rs28940279 [ dbSNP | Ensembl ].
VAR_004999
Natural varianti287 – 2871A → T in CAND. 1 Publication
VAR_039090
Natural varianti295 – 2951F → S in CAND. 2 Publications
VAR_005000
Natural varianti305 – 3051A → E in CAND; loss of activity; pan-European origin; most prevalent among non-Jewish CAND patients; probably the most ancient mutation. 4 Publications
Corresponds to variant rs28940574 [ dbSNP | Ensembl ].
VAR_005001
Natural varianti310 – 3101C → G.1 Publication
VAR_039091

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S67156 mRNA. Translation: AAB29190.1.
BC029128 mRNA. Translation: AAH29128.1.
CCDSiCCDS11028.1.
PIRiS38538.
RefSeqiNP_000040.1. NM_000049.2.
NP_001121557.1. NM_001128085.1.
XP_006721590.1. XM_006721527.1.
UniGeneiHs.171142.

Genome annotation databases

EnsembliENST00000263080; ENSP00000263080; ENSG00000108381.
ENST00000456349; ENSP00000409976; ENSG00000108381.
GeneIDi443.
KEGGihsa:443.
UCSCiuc002fvq.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S67156 mRNA. Translation: AAB29190.1 .
BC029128 mRNA. Translation: AAH29128.1 .
CCDSi CCDS11028.1.
PIRi S38538.
RefSeqi NP_000040.1. NM_000049.2.
NP_001121557.1. NM_001128085.1.
XP_006721590.1. XM_006721527.1.
UniGenei Hs.171142.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2I3C X-ray 2.80 A/B 2-313 [» ]
2O4H X-ray 2.70 A/B 1-313 [» ]
2O53 X-ray 2.70 A/B 1-313 [» ]
2Q51 X-ray 2.80 A/B 2-313 [» ]
4MRI X-ray 2.80 A/B 1-313 [» ]
4MXU X-ray 2.60 A/B 1-313 [» ]
4NFR X-ray 3.00 A/B 1-313 [» ]
4TNU X-ray 2.90 A/B 1-313 [» ]
ProteinModelPortali P45381.
SMRi P45381. Positions 9-310.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106935. 1 interaction.
DIPi DIP-60793N.
MINTi MINT-1440951.
STRINGi 9606.ENSP00000263080.

Chemistry

DrugBanki DB00128. L-Aspartic Acid.

PTM databases

PhosphoSitei P45381.

Proteomic databases

PaxDbi P45381.
PRIDEi P45381.

Protocols and materials databases

DNASUi 443.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000263080 ; ENSP00000263080 ; ENSG00000108381 .
ENST00000456349 ; ENSP00000409976 ; ENSG00000108381 .
GeneIDi 443.
KEGGi hsa:443.
UCSCi uc002fvq.3. human.

Organism-specific databases

CTDi 443.
GeneCardsi GC17P003376.
GeneReviewsi ASPA.
HGNCi HGNC:756. ASPA.
HPAi HPA022142.
HPA022145.
MIMi 271900. phenotype.
608034. gene.
neXtProti NX_P45381.
Orphaneti 314918. Mild Canavan disease.
314911. Severe Canavan disease.
PharmGKBi PA25055.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2988.
HOGENOMi HOG000232489.
HOVERGENi HBG004172.
InParanoidi P45381.
KOi K01437.
OMAi TTRSVAK.
PhylomeDBi P45381.
TreeFami TF328708.

Enzyme and pathway databases

BioCyci MetaCyc:HS03094-MONOMER.

Miscellaneous databases

EvolutionaryTracei P45381.
GenomeRNAii 443.
NextBioi 1855.
PROi P45381.
SOURCEi Search...

Gene expression databases

Bgeei P45381.
CleanExi HS_ASPA.
ExpressionAtlasi P45381. baseline and differential.
Genevestigatori P45381.

Family and domain databases

HAMAPi MF_00704. Aspartoacylase.
InterProi IPR016708. Aspartoacylase.
IPR007036. Aste_AspA.
[Graphical view ]
Pfami PF04952. AstE_AspA. 1 hit.
[Graphical view ]
PIRSFi PIRSF018001. Aspartoacylase. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the human aspartoacylase cDNA and a common missense mutation in Canavan disease."
    Kaul R., Gao G.P., Balamurugan K., Matalon R.
    Nat. Genet. 5:118-123(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT CAND ALA-285.
    Tissue: Kidney.
  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].
    Tissue: Brain.
  3. "Purification and preliminary characterization of brain aspartoacylase."
    Moore R.A., Le Coq J., Faehnle C.R., Viola R.E.
    Arch. Biochem. Biophys. 413:1-8(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, CHARACTERIZATION OF VARIANT CAND ALA-285, MUTAGENESIS OF GLU-285.
    Tissue: Brain.
  4. "Identification of the zinc binding ligands and the catalytic residue in human aspartoacylase, an enzyme involved in Canavan disease."
    Herga S., Berrin J.G., Perrier J., Puigserver A., Giardina T.
    FEBS Lett. 580:5899-5904(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, ZINC-BINDING SITES, ACTIVE SITE, MUTAGENESIS OF GLU-178.
  5. "Examination of the mechanism of human brain aspartoacylase through the binding of an intermediate analogue."
    Le Coq J., Pavlovsky A., Malik R., Sanishvili R., Xu C., Viola R.E.
    Biochemistry 47:3484-3492(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEXES WITH ZINC IONS; PHOSPHATE AND N-PHOSPHONOMETHYL-L-ASPARTATE, COFACTOR, SUBUNIT, MUTAGENESIS OF ARG-71; TYR-164; ARG-168; GLU-178 AND TYR-288.
  6. "Structure of aspartoacylase, the brain enzyme impaired in Canavan disease."
    Bitto E., Bingman C.A., Wesenberg G.E., McCoy J.G., Phillips G.N. Jr.
    Proc. Natl. Acad. Sci. U.S.A. 104:456-461(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH ZINC IONS, SUBUNIT, COFACTOR.
  7. "Canavan disease: mutations among Jewish and non-Jewish patients."
    Kaul R., Gao G.P., Aloya M., Balamurugan K., Petrosky A., Michals K., Matalon R.
    Am. J. Hum. Genet. 55:34-41(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CAND ALA-285 AND GLU-305.
  8. "The molecular basis of canavan (aspartoacylase deficiency) disease in European non-Jewish patients."
    Shaag A., Anikster Y., Christensen E., Glustein J.Z., Fois A., Michelakakis H., Nigro F., Pronicka E., Ribes A., Zabot M.-T., Elpeleg O.N.
    Am. J. Hum. Genet. 57:572-580(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CAND 176-GLY-ILE-177 DEL; ARG-274; SER-295 AND GLU-305.
  9. "Novel (Cys152 > Arg) missense mutation in an Arab patient with Canavan disease."
    Kaul R., Gao G.P., Michals K., Whelan D.T., Levin S., Matalon R.
    Hum. Mutat. 5:269-271(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CAND ARG-152.
  10. "Identification and expression of eight novel mutations among non-Jewish patients with Canavan disease."
    Kaul R., Gao G.P., Matalon R., Aloya M., Su Q., Jin M., Johnson A.B., Schutgens R.B.H., Clarke J.T.R.
    Am. J. Hum. Genet. 59:95-102(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CAND THR-16; ARG-27; GLU-114; GLU-123; TYR-152; CYS-168; ALA-285 AND GLU-305, VARIANT GLY-310, CHARACTERIZATION OF VARIANTS CAND THR-16; ARG-27; GLU-114; GLU-123; TYR-152 AND CYS-168.
  11. "Missense mutation (I143T) in a Japanese patient with Canavan disease."
    Kobayashi K., Tsujino S., Ezoe T., Hamaguchi H., Nihei K., Sakuragawa N.
    Hum. Mutat. Suppl. 1:S308-S309(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CAND THR-143.
  12. "Novel missense mutation (Y231C) in a Turkish patient with Canavan disease."
    Rady P.L., Vargas T., Tyring S.K., Matalon R., Langenbeck U.
    Am. J. Med. Genet. 87:273-275(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CAND CYS-231.
  13. "The spectrum of mutations of the aspartoacylase gene in Canavan disease in non-Jewish patients."
    Elpeleg O.N., Shaag A.
    J. Inherit. Metab. Dis. 22:531-534(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CAND THR-16; ARG-27; HIS-183; PHE-186; ARG-195; ARG-274; SER-280; LEU-280; THR-287; SER-295 AND GLU-305.
  14. "Mutation detection in the aspartoacylase gene in 17 patients with Canavan disease: four new mutations in the non-Jewish population."
    Sistermans E.A., de Coo R.F., van Beerendonk H.M., Poll-The B.T., Kleijer W.J., van Oost B.A.
    Eur. J. Hum. Genet. 8:557-560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CAND PRO-21; THR-57; HIS-168 AND THR-181.
  15. "Identification and characterization of novel mutations of the aspartoacylase gene in non-Jewish patients with Canavan disease."
    Zeng B.J., Wang Z.H., Ribeiro L.A., Leone P., De Gasperi R., Kim S.J., Raghavan S., Ong E., Pastores G.M., Kolodny E.H.
    J. Inherit. Metab. Dis. 25:557-570(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CAND GLY-24; ALA-68; TRP-152; ARG-244 AND VAL-249.
  16. "Two novel aspartoacylase gene (ASPA) missense mutations specific to Norwegian and Swedish patients with Canavan disease."
    Olsen T.R., Tranebjaerg L., Kvittingen E.A., Hagenfeldt L., Moller C., Nilssen O.
    J. Med. Genet. 39:E55-E55(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CAND TYR-114 AND VAL-249.

Entry informationi

Entry nameiACY2_HUMAN
AccessioniPrimary (citable) accession number: P45381
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 26, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3