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Q13231

- CHIT1_HUMAN

UniProt

Q13231 - CHIT1_HUMAN

Protein

Chitotriosidase-1

Gene

CHIT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Degrades chitin, chitotriose and chitobiose. May participate in the defense against nematodes and other pathogens. Isoform 3 has no enzymatic activity.2 Publications

    Catalytic activityi

    Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei140 – 1401Proton donorPROSITE-ProRule annotation
    Binding sitei269 – 2691Chitooligosaccharide
    Binding sitei358 – 3581Chitooligosaccharide

    GO - Molecular functioni

    1. chitinase activity Source: UniProtKB
    2. chitin binding Source: UniProtKB
    3. endochitinase activity Source: UniProtKB

    GO - Biological processi

    1. chitin catabolic process Source: UniProtKB
    2. immune response Source: UniProtKB
    3. polysaccharide catabolic process Source: UniProtKB-KW
    4. response to bacterium Source: ProtInc

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Chitin degradation, Polysaccharide degradation

    Keywords - Ligandi

    Chitin-binding

    Protein family/group databases

    CAZyiCBM14. Carbohydrate-Binding Module Family 14.
    GH18. Glycoside Hydrolase Family 18.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chitotriosidase-1 (EC:3.2.1.14)
    Alternative name(s):
    Chitinase-1
    Gene namesi
    Name:CHIT1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1936. CHIT1.

    Subcellular locationi

    Secreted. Lysosome
    Note: A small proportion is lysosomal.

    GO - Cellular componenti

    1. extracellular space Source: UniProtKB
    2. lysosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Lysosome, Secreted

    Pathology & Biotechi

    Organism-specific databases

    MIMi614122. phenotype.
    PharmGKBiPA26467.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 21211 PublicationAdd
    BLAST
    Chaini22 – 466445Chitotriosidase-1PRO_0000011941Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi26 ↔ 511 PublicationPROSITE-ProRule annotation
    Glycosylationi100 – 1001N-linked (GlcNAc...); in variant S-1021 Publication
    Disulfide bondi307 ↔ 3701 PublicationPROSITE-ProRule annotation
    Disulfide bondi450 ↔ 463PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ13231.
    PRIDEiQ13231.

    Expressioni

    Tissue specificityi

    Detected in spleen. Secreted by cultured macrophages.1 Publication

    Gene expression databases

    ArrayExpressiQ13231.
    BgeeiQ13231.
    CleanExiHS_CHIT1.
    GenevestigatoriQ13231.

    Organism-specific databases

    HPAiHPA010575.

    Interactioni

    Subunit structurei

    Monomer.3 Publications

    Protein-protein interaction databases

    STRINGi9606.ENSP00000255427.

    Structurei

    Secondary structure

    1
    466
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi23 – 297
    Helixi32 – 343
    Helixi37 – 393
    Helixi43 – 453
    Turni48 – 503
    Beta strandi52 – 6211
    Beta strandi65 – 673
    Helixi73 – 8210
    Helixi83 – 853
    Beta strandi91 – 977
    Turni99 – 1013
    Helixi104 – 1107
    Helixi113 – 12917
    Beta strandi134 – 1385
    Beta strandi144 – 1463
    Helixi151 – 17323
    Beta strandi179 – 1846
    Helixi188 – 1947
    Helixi197 – 2037
    Beta strandi205 – 2095
    Beta strandi219 – 2213
    Helixi236 – 2405
    Helixi243 – 25210
    Helixi257 – 2593
    Beta strandi260 – 27415
    Beta strandi284 – 2885
    Turni293 – 2953
    Beta strandi300 – 3023
    Helixi303 – 3064
    Beta strandi313 – 3175
    Turni318 – 3214
    Beta strandi322 – 3276
    Beta strandi330 – 3334
    Helixi337 – 34913
    Beta strandi354 – 3585
    Helixi360 – 3623
    Beta strandi368 – 3725
    Helixi376 – 3849

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GUVX-ray2.35A22-387[»]
    1HKIX-ray2.55A22-386[»]
    1HKJX-ray2.60A22-386[»]
    1HKKX-ray1.85A22-385[»]
    1HKMX-ray2.55A22-386[»]
    1LG1X-ray2.78A22-386[»]
    1LG2X-ray2.10A22-386[»]
    1LQ0X-ray2.20A22-386[»]
    1WAWX-ray1.75A22-466[»]
    1WB0X-ray1.65A22-466[»]
    ProteinModelPortaliQ13231.
    SMRiQ13231. Positions 22-385.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13231.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini417 – 46650Chitin-binding type-2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni70 – 712Chitooligosaccharide binding
    Regioni97 – 1004Chitooligosaccharide binding
    Regioni210 – 2134Chitooligosaccharide binding

    Sequence similaritiesi

    Contains 1 chitin-binding type-2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3325.
    HOVERGENiHBG011684.
    InParanoidiQ13231.
    KOiK01183.
    OMAiPGQDTFC.
    OrthoDBiEOG7ZGX3G.
    PhylomeDBiQ13231.
    TreeFamiTF315610.

    Family and domain databases

    Gene3Di2.170.140.10. 1 hit.
    3.10.50.10. 1 hit.
    3.20.20.80. 2 hits.
    InterProiIPR002557. Chitin-bd_dom.
    IPR011583. Chitinase_II.
    IPR029070. Chitinase_insertion.
    IPR001223. Glyco_hydro18cat.
    IPR001579. Glyco_hydro_18_chit_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF01607. CBM_14. 1 hit.
    PF00704. Glyco_hydro_18. 1 hit.
    [Graphical view]
    SMARTiSM00494. ChtBD2. 1 hit.
    SM00636. Glyco_18. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 2 hits.
    SSF54556. SSF54556. 1 hit.
    SSF57625. SSF57625. 1 hit.
    PROSITEiPS50940. CHIT_BIND_II. 1 hit.
    PS01095. CHITINASE_18. 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: Q13231-1) [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

    MVRSVAWAGF MVLLMIPWGS AAKLVCYFTN WAQYRQGEAR FLPKDLDPSL    50
    CTHLIYAFAG MTNHQLSTTE WNDETLYQEF NGLKKMNPKL KTLLAIGGWN 100
    FGTQKFTDMV ATANNRQTFV NSAIRFLRKY SFDGLDLDWE YPGSQGSPAV 150
    DKERFTTLVQ DLANAFQQEA QTSGKERLLL SAAVPAGQTY VDAGYEVDKI 200
    AQNLDFVNLM AYDFHGSWEK VTGHNSPLYK RQEESGAAAS LNVDAAVQQW 250
    LQKGTPASKL ILGMPTYGRS FTLASSSDTR VGAPATGSGT PGPFTKEGGM 300
    LAYYEVCSWK GATKQRIQDQ KVPYIFRDNQ WVGFDDVESF KTKVSYLKQK 350
    GLGGAMVWAL DLDDFAGFSC NQGRYPLIQT LRQELSLPYL PSGTPELEVP 400
    KPGQPSEPEH GPSPGQDTFC QGKADGLYPN PRERSSFYSC AAGRLFQQSC 450
    PTGLVFSNSC KCCTWN 466
    Length:466
    Mass (Da):51,681
    Last modified:November 1, 1996 - v1
    Checksum:iB4312D1E885E386D
    GO
    Isoform 2 (identifier: Q13231-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         386-387: SL → NG
         388-466: Missing.

    Show »
    Length:387
    Mass (Da):43,133
    Checksum:i03A272B8BC5E0D71
    GO
    Isoform 3 (identifier: Q13231-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         344-372: Missing.

    Note: Duplication of 24 bp in exon 10 leads to the use of a cryptic splice site. The normal splice site is still present but not used.

    Show »
    Length:437
    Mass (Da):48,565
    Checksum:i1A073A5F90A43717
    GO
    Isoform 4 (identifier: Q13231-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         87-105: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:447
    Mass (Da):49,613
    Checksum:i4C083E18D767C381
    GO

    Sequence cautioni

    The sequence BAG51478.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Polymorphismi

    A 24 bp duplication in exon 10 leads to the activation of an alternative splice site and the production of an inactive protein resulting in chitotriosidase deficiency [MIMi:614122]. About 6% of the population are deficient for CHIT1 activity, while 35% are carriers and show reduced enzyme levels. People with CHIT1 deficiency appear perfectly healthy.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti40 – 401R → H.
    Corresponds to variant rs35920428 [ dbSNP | Ensembl ].
    VAR_049190
    Natural varianti74 – 741E → K Rare variant detected in patients with Gaucher disease type 1. 1 Publication
    Corresponds to variant rs137852607 [ dbSNP | Ensembl ].
    VAR_065914
    Natural varianti102 – 1021G → S Common variant detected in patients with Gaucher disease type 1 as well as healthy individuals; slightly reduced activity towards 4-methylumbelliferyl-chitotrioside but no effect on activity towards 4-methylumbelliferyl-deoxychitobioside. 2 Publications
    Corresponds to variant rs2297950 [ dbSNP | Ensembl ].
    VAR_022138
    Natural varianti171 – 1711Q → H.
    Corresponds to variant rs12562058 [ dbSNP | Ensembl ].
    VAR_049191
    Natural varianti442 – 4421A → G.2 Publications
    Corresponds to variant rs1065761 [ dbSNP | Ensembl ].
    VAR_024458

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei87 – 10519Missing in isoform 4. 1 PublicationVSP_044816Add
    BLAST
    Alternative sequencei344 – 37229Missing in isoform 3. CuratedVSP_008633Add
    BLAST
    Alternative sequencei386 – 3872SL → NG in isoform 2. 1 PublicationVSP_008631
    Alternative sequencei388 – 46679Missing in isoform 2. 1 PublicationVSP_008632Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U29615 mRNA. Translation: AAC50246.1.
    U62662 mRNA. Translation: AAG10644.1.
    AK055165 mRNA. Translation: BAG51478.1. Different initiation.
    AC105940 Genomic DNA. No translation available.
    AL359090 Genomic DNA. No translation available.
    BC069614 mRNA. Translation: AAH69614.1.
    BC103695 mRNA. Translation: AAI03696.1.
    BC105680 mRNA. Translation: AAI05681.1.
    BC105681 mRNA. Translation: AAI05682.1.
    BC105682 mRNA. Translation: AAI05683.1.
    CCDSiCCDS1436.1. [Q13231-1]
    CCDS58057.1. [Q13231-4]
    RefSeqiNP_001243054.2. NM_001256125.1. [Q13231-4]
    NP_003456.1. NM_003465.2. [Q13231-1]
    UniGeneiHs.201688.

    Genome annotation databases

    EnsembliENST00000255427; ENSP00000255427; ENSG00000133063. [Q13231-4]
    ENST00000367229; ENSP00000356198; ENSG00000133063. [Q13231-1]
    ENST00000491855; ENSP00000423778; ENSG00000133063. [Q13231-2]
    GeneIDi1118.
    KEGGihsa:1118.
    UCSCiuc001gzn.2. human. [Q13231-1]
    uc009xal.2. human. [Q13231-3]

    Polymorphism databases

    DMDMi37999493.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U29615 mRNA. Translation: AAC50246.1 .
    U62662 mRNA. Translation: AAG10644.1 .
    AK055165 mRNA. Translation: BAG51478.1 . Different initiation.
    AC105940 Genomic DNA. No translation available.
    AL359090 Genomic DNA. No translation available.
    BC069614 mRNA. Translation: AAH69614.1 .
    BC103695 mRNA. Translation: AAI03696.1 .
    BC105680 mRNA. Translation: AAI05681.1 .
    BC105681 mRNA. Translation: AAI05682.1 .
    BC105682 mRNA. Translation: AAI05683.1 .
    CCDSi CCDS1436.1. [Q13231-1 ]
    CCDS58057.1. [Q13231-4 ]
    RefSeqi NP_001243054.2. NM_001256125.1. [Q13231-4 ]
    NP_003456.1. NM_003465.2. [Q13231-1 ]
    UniGenei Hs.201688.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GUV X-ray 2.35 A 22-387 [» ]
    1HKI X-ray 2.55 A 22-386 [» ]
    1HKJ X-ray 2.60 A 22-386 [» ]
    1HKK X-ray 1.85 A 22-385 [» ]
    1HKM X-ray 2.55 A 22-386 [» ]
    1LG1 X-ray 2.78 A 22-386 [» ]
    1LG2 X-ray 2.10 A 22-386 [» ]
    1LQ0 X-ray 2.20 A 22-386 [» ]
    1WAW X-ray 1.75 A 22-466 [» ]
    1WB0 X-ray 1.65 A 22-466 [» ]
    ProteinModelPortali Q13231.
    SMRi Q13231. Positions 22-385.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000255427.

    Chemistry

    BindingDBi Q13231.
    ChEMBLi CHEMBL3080.

    Protein family/group databases

    CAZyi CBM14. Carbohydrate-Binding Module Family 14.
    GH18. Glycoside Hydrolase Family 18.

    Polymorphism databases

    DMDMi 37999493.

    Proteomic databases

    PaxDbi Q13231.
    PRIDEi Q13231.

    Protocols and materials databases

    DNASUi 1118.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000255427 ; ENSP00000255427 ; ENSG00000133063 . [Q13231-4 ]
    ENST00000367229 ; ENSP00000356198 ; ENSG00000133063 . [Q13231-1 ]
    ENST00000491855 ; ENSP00000423778 ; ENSG00000133063 . [Q13231-2 ]
    GeneIDi 1118.
    KEGGi hsa:1118.
    UCSCi uc001gzn.2. human. [Q13231-1 ]
    uc009xal.2. human. [Q13231-3 ]

    Organism-specific databases

    CTDi 1118.
    GeneCardsi GC01M203181.
    HGNCi HGNC:1936. CHIT1.
    HPAi HPA010575.
    MIMi 600031. gene.
    614122. phenotype.
    neXtProti NX_Q13231.
    PharmGKBi PA26467.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3325.
    HOVERGENi HBG011684.
    InParanoidi Q13231.
    KOi K01183.
    OMAi PGQDTFC.
    OrthoDBi EOG7ZGX3G.
    PhylomeDBi Q13231.
    TreeFami TF315610.

    Miscellaneous databases

    ChiTaRSi CHIT1. human.
    EvolutionaryTracei Q13231.
    GenomeRNAii 1118.
    NextBioi 35534786.
    PROi Q13231.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13231.
    Bgeei Q13231.
    CleanExi HS_CHIT1.
    Genevestigatori Q13231.

    Family and domain databases

    Gene3Di 2.170.140.10. 1 hit.
    3.10.50.10. 1 hit.
    3.20.20.80. 2 hits.
    InterProi IPR002557. Chitin-bd_dom.
    IPR011583. Chitinase_II.
    IPR029070. Chitinase_insertion.
    IPR001223. Glyco_hydro18cat.
    IPR001579. Glyco_hydro_18_chit_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF01607. CBM_14. 1 hit.
    PF00704. Glyco_hydro_18. 1 hit.
    [Graphical view ]
    SMARTi SM00494. ChtBD2. 1 hit.
    SM00636. Glyco_18. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 2 hits.
    SSF54556. SSF54556. 1 hit.
    SSF57625. SSF57625. 1 hit.
    PROSITEi PS50940. CHIT_BIND_II. 1 hit.
    PS01095. CHITINASE_18. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of a cDNA encoding chitotriosidase, a human chitinase produced by macrophages."
      Boot R.G., Renkema G.H., Strijland A., van Zonneveld A.J., Aerts J.M.F.G.
      J. Biol. Chem. 270:26252-26256(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION.
      Tissue: Macrophage.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), VARIANT GLY-442.
    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. "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), VARIANTS SER-102 AND GLY-442.
    5. "Purification and characterization of human chitotriosidase, a novel member of the chitinase family of proteins."
      Renkema G.H., Boot R.G., Muijsers A.O., Donker-Koopman W.E., Aerts J.M.F.G.
      J. Biol. Chem. 270:2198-2202(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 22-43 AND 178-198, FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
      Tissue: Spleen.
    6. Cited for: POLYMORPHISM, FUNCTION (ISOFORM 3).
    7. "Structure of human chitotriosidase. Implications for specific inhibitor design and function of mammalian chitinase-like lectins."
      Fusetti F., von Moeller H., Houston D., Rozeboom H.J., Dijkstra B.W., Boot R.G., Aerts J.M.F.G., van Aalten D.M.F.
      J. Biol. Chem. 277:25537-25544(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 22-386 IN COMPLEX WITH CHITOBIOSE AND ALLOSAMIDIN, SUBCELLULAR LOCATION, DISULFIDE BONDS.
    8. "Crystal structures of allosamidin derivatives in complex with human macrophage chitinase."
      Rao F.V., Houston D.R., Boot R.G., Aerts J.M., Sakuda S., van Aalten D.M.
      J. Biol. Chem. 278:20110-20116(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 22-385 IN COMPLEX WITH ALLOSAMIDIN.
    9. "Specificity and affinity of natural product cyclopentapeptide inhibitors against A. fumigatus, human, and bacterial chitinases."
      Rao F.V., Houston D.R., Boot R.G., Aerts J.M., Hodkinson M., Adams D.J., Shiomi K., Omura S., van Aalten D.M.
      Chem. Biol. 12:65-76(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 22-466 IN COMPLEX WITH THE CYCLOPENTAPEPTIDE INHIBITOR ARGADIN, CATALYTIC ACTIVITY.
    10. "Type 1 Gaucher disease: null and hypomorphic novel chitotriosidase mutations-implications for diagnosis and therapeutic monitoring."
      Grace M.E., Balwani M., Nazarenko I., Prakash-Cheng A., Desnick R.J.
      Hum. Mutat. 28:866-873(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS LYS-74 AND SER-102.
    11. "Common G102S polymorphism in chitotriosidase differentially affects activity towards 4-methylumbelliferyl substrates."
      Bussink A.P., Verhoek M., Vreede J., Ghauharali-van der Vlugt K., Donker-Koopman W.E., Sprenger R.R., Hollak C.E., Aerts J.M., Boot R.G.
      FEBS J. 276:5678-5688(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT SER-102, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, GLYCOSYLATION AT ASN-100.

    Entry informationi

    Entry nameiCHIT1_HUMAN
    AccessioniPrimary (citable) accession number: Q13231
    Secondary accession number(s): B3KNW6
    , J3KN09, Q0VGG5, Q0VGG6, Q3ZAR1, Q6ISC2, Q9H3V8, Q9UDJ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 24, 2003
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 145 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

    Miscellaneous

    Very high plasma levels of CHIT1 are found in patients with Gaucher disease type 1 (GD I). Can be used as diagnostic aid and to evaluate the success of treatment that brings levels back to normal.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3