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Q01459

- DIAC_HUMAN

UniProt

Q01459 - DIAC_HUMAN

Protein

Di-N-acetylchitobiase

Gene

CTBS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      Previous versions | rss
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    Functioni

    Involved in the degradation of asparagine-linked glycoproteins. Hydrolyze of N-acetyl-beta-D-glucosamine (1-4)N-acetylglucosamine chitobiose core from the reducing end of the bond, it requires prior cleavage by glycosylasparaginase.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei143 – 1431Proton donorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. chitinase activity Source: Ensembl

    GO - Biological processi

    1. chitin catabolic process Source: Ensembl
    2. oligosaccharide catabolic process Source: Ensembl

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Protein family/group databases

    CAZyiGH18. Glycoside Hydrolase Family 18.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Di-N-acetylchitobiase (EC:3.2.1.-)
    Gene namesi
    Name:CTBS
    Synonyms:CTB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:2496. CTBS.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: UniProt
    2. extracellular vesicular exosome Source: UniProt
    3. lysosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26997.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3838By similarityAdd
    BLAST
    Chaini39 – 385347Di-N-acetylchitobiasePRO_0000011961Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi193 – 1931N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi228 – 2281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi262 – 2621N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi299 – 2991N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ01459.
    PaxDbiQ01459.
    PeptideAtlasiQ01459.
    PRIDEiQ01459.

    PTM databases

    PhosphoSiteiQ01459.

    Expressioni

    Gene expression databases

    ArrayExpressiQ01459.
    BgeeiQ01459.
    CleanExiHS_CTBS.
    GenevestigatoriQ01459.

    Organism-specific databases

    HPAiCAB017043.
    HPA023594.
    HPA048810.

    Interactioni

    Protein-protein interaction databases

    BioGridi107868. 2 interactions.
    IntActiQ01459. 3 interactions.
    STRINGi9606.ENSP00000359664.

    Structurei

    3D structure databases

    ProteinModelPortaliQ01459.
    SMRiQ01459. Positions 116-384.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 18 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3858.
    HOGENOMiHOG000007829.
    HOVERGENiHBG005486.
    InParanoidiQ01459.
    KOiK12310.
    OMAiDEQSQIW.
    OrthoDBiEOG7ZGX3G.
    PhylomeDBiQ01459.
    TreeFamiTF332677.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR011583. Chitinase_II.
    IPR001223. Glyco_hydro18cat.
    IPR001579. Glyco_hydro_18_chit_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00704. Glyco_hydro_18. 1 hit.
    [Graphical view]
    SMARTiSM00636. Glyco_18. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 2 hits.
    PROSITEiPS01095. CHITINASE_18. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q01459-1 [UniParc]FASTAAdd to Basket

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    MSRPQLRRWR LVSSPPSGVP GLALLALLAL LALRLAAGTD CPCPEPELCR    50
    PIRHHPDFEV FVFDVGQKTW KSYDWSQITT VATFGKYDSE LMCYAHSKGA 100
    RVVLKGDVSL KDIIDPAFRA SWIAQKLNLA KTQYMDGINI DIEQEVNCLS 150
    PEYDALTALV KETTDSFHRE IEGSQVTFDV AWSPKNIDRR CYNYTGIADA 200
    CDFLFVMSYD EQSQIWSECI AAANAPYNQT LTGYNDYIKM SINPKKLVMG 250
    VPWYGYDYTC LNLSEDHVCT IAKVPFRGAP CSDAAGRQVP YKTIMKQINS 300
    SISGNLWDKD QRAPYYNYKD PAGHFHQVWY DNPQSISLKA TYIQNYRLRG 350
    IGMWNANCLD YSGDAVAKQQ TEEMWEVLKP KLLQR 385
    Length:385
    Mass (Da):43,760
    Last modified:July 1, 1993 - v1
    Checksum:i0A9D14C8B26B52EE
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti274 – 2741V → I.
    Corresponds to variant rs15911 [ dbSNP | Ensembl ].
    VAR_049197
    Natural varianti310 – 3101D → Y.
    Corresponds to variant rs3768249 [ dbSNP | Ensembl ].
    VAR_020160

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M95767 mRNA. Translation: AAA35684.1.
    AF085706
    , AF085700, AF085701, AF085702, AF085703, AF085704, AF085705 Genomic DNA. Translation: AAC35852.1.
    AL359762 Genomic DNA. Translation: CAH70207.1.
    CH471097 Genomic DNA. Translation: EAW73232.1.
    CH471097 Genomic DNA. Translation: EAW73233.1.
    BC126333 mRNA. Translation: AAI26334.1.
    BC126335 mRNA. Translation: AAI26336.1.
    CCDSiCCDS698.1.
    PIRiA44102.
    RefSeqiNP_004379.1. NM_004388.2.
    UniGeneiHs.513557.

    Genome annotation databases

    EnsembliENST00000370630; ENSP00000359664; ENSG00000117151.
    GeneIDi1486.
    KEGGihsa:1486.
    UCSCiuc001dka.2. human.

    Polymorphism databases

    DMDMi399376.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M95767 mRNA. Translation: AAA35684.1 .
    AF085706
    , AF085700 , AF085701 , AF085702 , AF085703 , AF085704 , AF085705 Genomic DNA. Translation: AAC35852.1 .
    AL359762 Genomic DNA. Translation: CAH70207.1 .
    CH471097 Genomic DNA. Translation: EAW73232.1 .
    CH471097 Genomic DNA. Translation: EAW73233.1 .
    BC126333 mRNA. Translation: AAI26334.1 .
    BC126335 mRNA. Translation: AAI26336.1 .
    CCDSi CCDS698.1.
    PIRi A44102.
    RefSeqi NP_004379.1. NM_004388.2.
    UniGenei Hs.513557.

    3D structure databases

    ProteinModelPortali Q01459.
    SMRi Q01459. Positions 116-384.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107868. 2 interactions.
    IntActi Q01459. 3 interactions.
    STRINGi 9606.ENSP00000359664.

    Protein family/group databases

    CAZyi GH18. Glycoside Hydrolase Family 18.

    PTM databases

    PhosphoSitei Q01459.

    Polymorphism databases

    DMDMi 399376.

    Proteomic databases

    MaxQBi Q01459.
    PaxDbi Q01459.
    PeptideAtlasi Q01459.
    PRIDEi Q01459.

    Protocols and materials databases

    DNASUi 1486.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000370630 ; ENSP00000359664 ; ENSG00000117151 .
    GeneIDi 1486.
    KEGGi hsa:1486.
    UCSCi uc001dka.2. human.

    Organism-specific databases

    CTDi 1486.
    GeneCardsi GC01M085018.
    HGNCi HGNC:2496. CTBS.
    HPAi CAB017043.
    HPA023594.
    HPA048810.
    MIMi 600873. gene.
    neXtProti NX_Q01459.
    PharmGKBi PA26997.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3858.
    HOGENOMi HOG000007829.
    HOVERGENi HBG005486.
    InParanoidi Q01459.
    KOi K12310.
    OMAi DEQSQIW.
    OrthoDBi EOG7ZGX3G.
    PhylomeDBi Q01459.
    TreeFami TF332677.

    Miscellaneous databases

    GeneWikii CTBS.
    GenomeRNAii 1486.
    NextBioi 6101.
    PROi Q01459.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q01459.
    Bgeei Q01459.
    CleanExi HS_CTBS.
    Genevestigatori Q01459.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR011583. Chitinase_II.
    IPR001223. Glyco_hydro18cat.
    IPR001579. Glyco_hydro_18_chit_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00704. Glyco_hydro_18. 1 hit.
    [Graphical view ]
    SMARTi SM00636. Glyco_18. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 2 hits.
    PROSITEi PS01095. CHITINASE_18. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of the cDNA sequence encoding the lysosomal glycosidase di-N-acetylchitobiase."
      Fisher K.J., Aronson N.N. Jr.
      J. Biol. Chem. 267:19607-19616(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    2. "Structure of the human gene for lysosomal di-N-acetylchitobiase."
      Liu B., Ahmad W., Aronson N.N. Jr.
      Glycobiology 9:589-593(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. 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].
      Tissue: Brain.
    6. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-299.
      Tissue: Liver.

    Entry informationi

    Entry nameiDIAC_HUMAN
    AccessioniPrimary (citable) accession number: Q01459
    Secondary accession number(s): Q5VX50
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 123 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

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3