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P45381

- ACY2_HUMAN

UniProt

P45381 - ACY2_HUMAN

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Protein
Aspartoacylase
Gene
ASPA, ACY2, ASP
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.UniRule annotation

Catalytic activityi

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

Cofactori

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 UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. extracellular vesicular exosome Source: UniProt
  3. nucleus Source: UniProtKB-SubCell
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.12 Publications
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.
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. 4 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 – 313313AspartoacylaseUniRule annotation
PRO_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

ArrayExpressiP45381.
BgeeiP45381.
CleanExiHS_ASPA.
GenevestigatoriP45381.

Organism-specific databases

HPAiHPA022142.
HPA022145.

Interactioni

Subunit structurei

Homodimer Inferred.2 Publications

Protein-protein interaction databases

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

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 186
Helixi25 – 3410
Helixi39 – 413
Beta strandi46 – 538
Helixi55 – 606
Beta strandi65 – 673
Helixi69 – 713
Helixi75 – 784
Helixi88 – 10013
Beta strandi105 – 1084
Beta strandi110 – 1178
Beta strandi119 – 1213
Beta strandi123 – 1297
Helixi134 – 14714
Beta strandi152 – 1565
Beta strandi160 – 1623
Helixi167 – 1704
Beta strandi171 – 18010
Helixi189 – 21022
Beta strandi218 – 22912
Beta strandi235 – 2373
Beta strandi241 – 2433
Turni245 – 2495
Beta strandi259 – 2635
Beta strandi269 – 2713
Beta strandi274 – 2763
Beta strandi278 – 2825
Helixi286 – 2883
Turni289 – 2924
Beta strandi294 – 30512

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortaliP45381.
SMRiP45381. Positions 9-310.

Miscellaneous databases

EvolutionaryTraceiP45381.

Family & Domainsi

Region

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

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

MTSCHIAEEH IQKVAIFGGT HGNELTGVFL VKHWLENGAE IQRTGLEVKP    50
FITNPRAVKK CTRYIDCDLN RIFDLENLGK KMSEDLPYEV RRAQEINHLF 100
GPKDSEDSYD IIFDLHNTTS NMGCTLILED SRNNFLIQMF HYIKTSLAPL 150
PCYVYLIEHP SLKYATTRSI AKYPVGIEVG PQPQGVLRAD ILDQMRKMIK 200
HALDFIHHFN EGKEFPPCAI EVYKIIEKVD YPRDENGEIA AIIHPNLQDQ 250
DWKPLHPGDP MFLTLDGKTI PLGGDCTVYP VFVNEAAYYE KKEAFAKTTK 300
LTLNAKSIRC CLH 313
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.
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. 4 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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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 [» ]
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 GC17P003326.
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

ArrayExpressi P45381.
Bgeei P45381.
CleanExi HS_ASPA.
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: September 3, 2014
This is version 135 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

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