Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q03154

- ACY1_HUMAN

UniProt

Q03154 - ACY1_HUMAN

Protein

Aminoacylase-1

Gene

ACY1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate).1 Publication

    Catalytic activityi

    An N-acyl-aliphatic-L-amino acid + H2O = an aliphatic L-amino acid + a carboxylate.1 Publication
    An N-acetyl-L-cysteine-S-conjugate + H2O = an L-cysteine-S-conjugate + acetate.1 Publication

    Cofactori

    Binds 2 zinc ions per subunit.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi80 – 801Zinc 1
    Active sitei82 – 821By similarity
    Metal bindingi113 – 1131Zinc 1
    Metal bindingi113 – 1131Zinc 2
    Active sitei147 – 1471Proton acceptor1 Publication
    Metal bindingi148 – 1481Zinc 2
    Metal bindingi175 – 1751Zinc 1
    Metal bindingi373 – 3731Zinc 2

    GO - Molecular functioni

    1. aminoacylase activity Source: ProtInc
    2. metal ion binding Source: UniProtKB-KW
    3. metallopeptidase activity Source: InterPro

    GO - Biological processi

    1. cellular amino acid metabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03800-MONOMER.
    BRENDAi3.5.1.14. 2681.
    SABIO-RKQ03154.

    Protein family/group databases

    MEROPSiM20.973.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aminoacylase-1 (EC:3.5.1.14)
    Short name:
    ACY-1
    Alternative name(s):
    N-acyl-L-amino-acid amidohydrolase
    Gene namesi
    Name:ACY1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:177. ACY1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: ProtInc
    2. extracellular vesicular exosome Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Aminoacylase-1 deficiency (ACY1D) [MIM:609924]: An enzymatic deficiency resulting in encephalopathy, unspecific psychomotor delay, psychomotor delay with atrophy of the vermis and syringomyelia, marked muscular hypotonia or normal clinical features. Epileptic seizures are a frequent feature. All affected individuals exhibit markedly increased urinary excretion of several N-acetylated amino acids.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti197 – 1971R → W in ACY1D; loss of activity. 1 Publication
    VAR_043113
    Natural varianti233 – 2331E → D in ACY1D; loss of activity. 1 Publication
    VAR_026104
    Natural varianti353 – 3531R → C in ACY1D; loss of activity. 3 Publications
    Corresponds to variant rs121912698 [ dbSNP | Ensembl ].
    VAR_026105
    Natural varianti378 – 3781R → Q in ACY1D. 1 Publication
    VAR_065562
    Natural varianti378 – 3781R → W in ACY1D; slightly reduced activity. 1 Publication
    VAR_065563
    Natural varianti386 – 3861R → C in ACY1D; loss of activity. 1 Publication
    Corresponds to variant rs2229152 [ dbSNP | Ensembl ].
    VAR_020452
    Natural varianti393 – 3931R → H in ACY1D. 1 Publication
    Corresponds to variant rs121912701 [ dbSNP | Ensembl ].
    VAR_043114

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi80 – 801H → A: Almost abolishes enzyme activity. 1 Publication
    Mutagenesisi113 – 1131D → A: Almost abolishes enzyme activity. 1 Publication
    Mutagenesisi147 – 1471E → A or Q: Almost abolishes enzyme activity. 1 Publication
    Mutagenesisi147 – 1471E → D: Decreased protein stability. Loss of enzyme activity. 1 Publication
    Mutagenesisi148 – 1481E → A: Almost abolishes enzyme activity. 1 Publication
    Mutagenesisi175 – 1751E → A: Almost abolishes enzyme activity. 1 Publication
    Mutagenesisi206 – 2061H → N: Almost abolishes enzyme activity. 1 Publication
    Mutagenesisi373 – 3731H → A: Almost abolishes enzyme activity. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi609924. phenotype.
    Orphaneti137754. Neurological conditions associated with aminoacylase 1 deficiency.
    PharmGKBiPA24497.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 408407Aminoacylase-1PRO_0000185236Add
    BLAST

    Proteomic databases

    MaxQBiQ03154.
    PaxDbiQ03154.
    PeptideAtlasiQ03154.
    PRIDEiQ03154.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00009268.

    PTM databases

    PhosphoSiteiQ03154.

    Expressioni

    Tissue specificityi

    Expression is highest in kidney, strong in brain and weaker in placenta and spleen.1 Publication

    Gene expression databases

    BgeeiQ03154.
    CleanExiHS_ACY1.
    GenevestigatoriQ03154.

    Organism-specific databases

    HPAiCAB003695.
    HPA036174.
    HPA036175.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with SPHK1 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi106610. 9 interactions.
    IntActiQ03154. 5 interactions.
    MINTiMINT-4999851.
    STRINGi9606.ENSP00000232907.

    Structurei

    Secondary structure

    1
    408
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi11 – 2010
    Helixi31 – 4515
    Beta strandi48 – 558
    Beta strandi58 – 658
    Beta strandi74 – 807
    Helixi88 – 903
    Turni95 – 973
    Beta strandi104 – 1074
    Turni109 – 1146
    Helixi115 – 13016
    Beta strandi139 – 1457
    Helixi147 – 1493
    Turni152 – 1543
    Helixi155 – 1584
    Helixi162 – 1654
    Beta strandi169 – 1746
    Beta strandi180 – 1889
    Helixi194 – 1963
    Helixi322 – 33312
    Beta strandi338 – 3425
    Helixi348 – 3547
    Beta strandi359 – 3624
    Beta strandi378 – 3803
    Helixi381 – 39919
    Helixi405 – 4073

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Q7LX-ray1.40A/C1-198[»]
    B/D321-408[»]
    ProteinModelPortaliQ03154.
    SMRiQ03154. Positions 7-408.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ03154.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M20A family.Curated

    Phylogenomic databases

    eggNOGiCOG0624.
    HOGENOMiHOG000021196.
    HOVERGENiHBG000982.
    InParanoidiQ03154.
    KOiK14677.
    PhylomeDBiQ03154.
    TreeFamiTF313693.

    Family and domain databases

    Gene3Di3.30.70.360. 1 hit.
    InterProiIPR001261. ArgE/DapE_CS.
    IPR010159. N-acyl_aa_amidohydrolase.
    IPR002933. Peptidase_M20.
    IPR011650. Peptidase_M20_dimer.
    [Graphical view]
    PfamiPF07687. M20_dimer. 1 hit.
    PF01546. Peptidase_M20. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036696. ACY-1. 1 hit.
    SUPFAMiSSF55031. SSF55031. 1 hit.
    TIGRFAMsiTIGR01880. Ac-peptdase-euk. 1 hit.
    PROSITEiPS00758. ARGE_DAPE_CPG2_1. 1 hit.
    PS00759. ARGE_DAPE_CPG2_2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q03154-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MTSKGPEEEH PSVTLFRQYL RIRTVQPKPD YGAAVAFFEE TARQLGLGCQ    50
    KVEVAPGYVV TVLTWPGTNP TLSSILLNSH TDVVPVFKEH WSHDPFEAFK 100
    DSEGYIYARG AQDMKCVSIQ YLEAVRRLKV EGHRFPRTIH MTFVPDEEVG 150
    GHQGMELFVQ RPEFHALRAG FALDEGIANP TDAFTVFYSE RSPWWVRVTS 200
    TGRPGHASRF MEDTAAEKLH KVVNSILAFR EKEWQRLQSN PHLKEGSVTS 250
    VNLTKLEGGV AYNVIPATMS ASFDFRVAPD VDFKAFEEQL QSWCQAAGEG 300
    VTLEFAQKWM HPQVTPTDDS NPWWAAFSRV CKDMNLTLEP EIMPAATDNR 350
    YIRAVGVPAL GFSPMNRTPV LLHDHDERLH EAVFLRGVDI YTRLLPALAS 400
    VPALPSDS 408
    Length:408
    Mass (Da):45,885
    Last modified:February 1, 1994 - v1
    Checksum:i293350CD7759826C
    GO
    Isoform 2 (identifier: Q03154-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         103-174: Missing.

    Note: Gene prediction based on EST data.

    Show »
    Length:336
    Mass (Da):37,597
    Checksum:i68C1E4266A8CBE70
    GO
    Isoform 3 (identifier: Q03154-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         220-284: Missing.

    Note: Gene prediction based on EST data.

    Show »
    Length:343
    Mass (Da):38,629
    Checksum:i75F9FBDC8348189E
    GO
    Isoform 4 (identifier: Q03154-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         32-66: Missing.

    Note: Gene prediction based on EST data.

    Show »
    Length:373
    Mass (Da):42,195
    Checksum:i343DC089BDBDC22F
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti179 – 1791N → S.
    Corresponds to variant rs887540 [ dbSNP | Ensembl ].
    VAR_051805
    Natural varianti197 – 1971R → W in ACY1D; loss of activity. 1 Publication
    VAR_043113
    Natural varianti233 – 2331E → D in ACY1D; loss of activity. 1 Publication
    VAR_026104
    Natural varianti353 – 3531R → C in ACY1D; loss of activity. 3 Publications
    Corresponds to variant rs121912698 [ dbSNP | Ensembl ].
    VAR_026105
    Natural varianti378 – 3781R → Q in ACY1D. 1 Publication
    VAR_065562
    Natural varianti378 – 3781R → W in ACY1D; slightly reduced activity. 1 Publication
    VAR_065563
    Natural varianti381 – 3811E → D in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036076
    Natural varianti386 – 3861R → C in ACY1D; loss of activity. 1 Publication
    Corresponds to variant rs2229152 [ dbSNP | Ensembl ].
    VAR_020452
    Natural varianti393 – 3931R → H in ACY1D. 1 Publication
    Corresponds to variant rs121912701 [ dbSNP | Ensembl ].
    VAR_043114

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei32 – 6635Missing in isoform 4. CuratedVSP_046876Add
    BLAST
    Alternative sequencei103 – 17472Missing in isoform 2. CuratedVSP_046877Add
    BLAST
    Alternative sequencei220 – 28465Missing in isoform 3. CuratedVSP_046878Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L07548 mRNA. Translation: AAA02852.1.
    D14524 mRNA. Translation: BAA03397.1.
    D16307 mRNA. Translation: BAA03814.1.
    AC115284 Genomic DNA. No translation available.
    BC000545 mRNA. Translation: AAH00545.1.
    BC003023 mRNA. Translation: AAH03023.1.
    BC014112 mRNA. Translation: AAH14112.1.
    CCDSiCCDS2844.1. [Q03154-1]
    CCDS56261.1. [Q03154-2]
    CCDS56262.1. [Q03154-3]
    CCDS56263.1. [Q03154-4]
    PIRiA47488.
    RefSeqiNP_000657.1. NM_000666.2. [Q03154-1]
    NP_001185824.1. NM_001198895.1. [Q03154-1]
    NP_001185825.1. NM_001198896.1. [Q03154-2]
    NP_001185826.1. NM_001198897.1. [Q03154-3]
    NP_001185827.1. NM_001198898.1. [Q03154-4]
    UniGeneiHs.334707.

    Genome annotation databases

    EnsembliENST00000404366; ENSP00000384296; ENSG00000243989. [Q03154-1]
    ENST00000476351; ENSP00000417056; ENSG00000243989. [Q03154-4]
    ENST00000476854; ENSP00000419262; ENSG00000243989. [Q03154-3]
    ENST00000494103; ENSP00000417618; ENSG00000243989. [Q03154-2]
    GeneIDi95.
    KEGGihsa:95.
    UCSCiuc003dcp.3. human. [Q03154-1]

    Polymorphism databases

    DMDMi461466.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L07548 mRNA. Translation: AAA02852.1 .
    D14524 mRNA. Translation: BAA03397.1 .
    D16307 mRNA. Translation: BAA03814.1 .
    AC115284 Genomic DNA. No translation available.
    BC000545 mRNA. Translation: AAH00545.1 .
    BC003023 mRNA. Translation: AAH03023.1 .
    BC014112 mRNA. Translation: AAH14112.1 .
    CCDSi CCDS2844.1. [Q03154-1 ]
    CCDS56261.1. [Q03154-2 ]
    CCDS56262.1. [Q03154-3 ]
    CCDS56263.1. [Q03154-4 ]
    PIRi A47488.
    RefSeqi NP_000657.1. NM_000666.2. [Q03154-1 ]
    NP_001185824.1. NM_001198895.1. [Q03154-1 ]
    NP_001185825.1. NM_001198896.1. [Q03154-2 ]
    NP_001185826.1. NM_001198897.1. [Q03154-3 ]
    NP_001185827.1. NM_001198898.1. [Q03154-4 ]
    UniGenei Hs.334707.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Q7L X-ray 1.40 A/C 1-198 [» ]
    B/D 321-408 [» ]
    ProteinModelPortali Q03154.
    SMRi Q03154. Positions 7-408.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106610. 9 interactions.
    IntActi Q03154. 5 interactions.
    MINTi MINT-4999851.
    STRINGi 9606.ENSP00000232907.

    Chemistry

    DrugBanki DB00128. L-Aspartic Acid.

    Protein family/group databases

    MEROPSi M20.973.

    PTM databases

    PhosphoSitei Q03154.

    Polymorphism databases

    DMDMi 461466.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00009268.

    Proteomic databases

    MaxQBi Q03154.
    PaxDbi Q03154.
    PeptideAtlasi Q03154.
    PRIDEi Q03154.

    Protocols and materials databases

    DNASUi 95.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000404366 ; ENSP00000384296 ; ENSG00000243989 . [Q03154-1 ]
    ENST00000476351 ; ENSP00000417056 ; ENSG00000243989 . [Q03154-4 ]
    ENST00000476854 ; ENSP00000419262 ; ENSG00000243989 . [Q03154-3 ]
    ENST00000494103 ; ENSP00000417618 ; ENSG00000243989 . [Q03154-2 ]
    GeneIDi 95.
    KEGGi hsa:95.
    UCSCi uc003dcp.3. human. [Q03154-1 ]

    Organism-specific databases

    CTDi 95.
    GeneCardsi GC03P052017.
    HGNCi HGNC:177. ACY1.
    HPAi CAB003695.
    HPA036174.
    HPA036175.
    MIMi 104620. gene.
    609924. phenotype.
    neXtProti NX_Q03154.
    Orphaneti 137754. Neurological conditions associated with aminoacylase 1 deficiency.
    PharmGKBi PA24497.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0624.
    HOGENOMi HOG000021196.
    HOVERGENi HBG000982.
    InParanoidi Q03154.
    KOi K14677.
    PhylomeDBi Q03154.
    TreeFami TF313693.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS03800-MONOMER.
    BRENDAi 3.5.1.14. 2681.
    SABIO-RK Q03154.

    Miscellaneous databases

    ChiTaRSi ACY1. human.
    EvolutionaryTracei Q03154.
    GeneWikii ACY1.
    GenomeRNAii 95.
    NextBioi 361.
    PROi Q03154.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q03154.
    CleanExi HS_ACY1.
    Genevestigatori Q03154.

    Family and domain databases

    Gene3Di 3.30.70.360. 1 hit.
    InterProi IPR001261. ArgE/DapE_CS.
    IPR010159. N-acyl_aa_amidohydrolase.
    IPR002933. Peptidase_M20.
    IPR011650. Peptidase_M20_dimer.
    [Graphical view ]
    Pfami PF07687. M20_dimer. 1 hit.
    PF01546. Peptidase_M20. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036696. ACY-1. 1 hit.
    SUPFAMi SSF55031. SSF55031. 1 hit.
    TIGRFAMsi TIGR01880. Ac-peptdase-euk. 1 hit.
    PROSITEi PS00758. ARGE_DAPE_CPG2_1. 1 hit.
    PS00759. ARGE_DAPE_CPG2_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The nucleotide sequence of human aminoacylase-1."
      Mitta M., Kato I., Tsunasawa S.
      Biochim. Biophys. Acta 1174:201-203(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Human aminoacylase-1. Cloning, sequence, and expression analysis of a chromosome 3p21 gene inactivated in small cell lung cancer."
      Cook R.M., Burke B.J., Buchhagen D.L., Minna J.D., Miller Y.E.
      J. Biol. Chem. 268:17010-17017(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    3. Iwaki K., Tanaka Y., Ohta T., Fukuda S., Kurimoto M.
      Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1).
      Tissue: Brain, Lung and Skin.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Essential roles of zinc ligation and enzyme dimerization for catalysis in the aminoacylase-1/M20 family."
      Lindner H.A., Lunin V.V., Alary A., Hecker R., Cygler M., Menard R.
      J. Biol. Chem. 278:44496-44504(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH ZINC IONS, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF HIS-80; ASP-113; GLU-147; GLU-148; GLU-175; HIS-206 AND HIS-373.
    8. Cited for: VARIANT ACY1D CYS-353.
    9. Cited for: VARIANTS ACY1D ASP-233 AND CYS-353, TISSUE SPECIFICITY.
    10. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-381.
    11. Cited for: VARIANTS ACY1D TRP-197; CYS-353 AND HIS-393.
    12. Cited for: VARIANTS ACY1D GLN-378; TRP-378 AND CYS-386, CHARACTERIZATION OF VARIANTS ACY1D TRP-197; ASP-233; CYS-353; TRP-378 AND CYS-386.

    Entry informationi

    Entry nameiACY1_HUMAN
    AccessioniPrimary (citable) accession number: Q03154
    Secondary accession number(s): C9J6I6, C9J9D8, C9JWD4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 1, 1994
    Last modified: October 1, 2014
    This is version 146 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 3
      Human chromosome 3: 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. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3