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Q13231

- CHIT1_HUMAN

UniProt

Q13231 - CHIT1_HUMAN

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Protein

Chitotriosidase-1

Gene

CHIT1

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

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
Complete GO annotation...

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-KW
Complete GO annotation...

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

BgeeiQ13231.
CleanExiHS_CHIT1.
ExpressionAtlasiQ13231. baseline and differential.
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.
GeneTreeiENSGT00550000074323.
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

        10         20         30         40         50
MVRSVAWAGF MVLLMIPWGS AAKLVCYFTN WAQYRQGEAR FLPKDLDPSL
60 70 80 90 100
CTHLIYAFAG MTNHQLSTTE WNDETLYQEF NGLKKMNPKL KTLLAIGGWN
110 120 130 140 150
FGTQKFTDMV ATANNRQTFV NSAIRFLRKY SFDGLDLDWE YPGSQGSPAV
160 170 180 190 200
DKERFTTLVQ DLANAFQQEA QTSGKERLLL SAAVPAGQTY VDAGYEVDKI
210 220 230 240 250
AQNLDFVNLM AYDFHGSWEK VTGHNSPLYK RQEESGAAAS LNVDAAVQQW
260 270 280 290 300
LQKGTPASKL ILGMPTYGRS FTLASSSDTR VGAPATGSGT PGPFTKEGGM
310 320 330 340 350
LAYYEVCSWK GATKQRIQDQ KVPYIFRDNQ WVGFDDVESF KTKVSYLKQK
360 370 380 390 400
GLGGAMVWAL DLDDFAGFSC NQGRYPLIQT LRQELSLPYL PSGTPELEVP
410 420 430 440 450
KPGQPSEPEH GPSPGQDTFC QGKADGLYPN PRERSSFYSC AAGRLFQQSC
460
PTGLVFSNSC KCCTWN
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.
GeneTreei ENSGT00550000074323.
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

Bgeei Q13231.
CleanExi HS_CHIT1.
ExpressionAtlasi Q13231. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 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

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