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Protein

Acidic mammalian chitinase

Gene

CHIA

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

Functioni

Degrades chitin and chitotriose. May participate in the defense against nematodes, fungi and other pathogens. Plays a role in T-helper cell type 2 (Th2) immune response. Contributes to the response to IL-13 and inflammation in response to IL-13. Stimulates chemokine production by pulmonary epithelial cells. Protects lung epithelial cells against apoptosis and promotes phosphorylation of AKT1. Its function in the inflammatory response and in protecting cells against apoptosis is inhibited by allosamidin, suggesting that the function of this protein depends on carbohydrate binding.4 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 donorCurated
Binding sitei141 – 1411ChitooligosaccharideBy similarity
Binding sitei360 – 3601ChitooligosaccharideBy similarity

GO - Molecular functioni

  • carbohydrate binding Source: UniProtKB
  • chitinase activity Source: UniProtKB
  • chitin binding Source: UniProtKB
  • kinase binding Source: UniProtKB
  • lysozyme activity Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • cell wall chitin metabolic process Source: UniProtKB
  • chitin catabolic process Source: UniProtKB
  • chitin metabolic process Source: UniProtKB
  • digestion Source: UniProtKB
  • immune response Source: UniProtKB
  • polysaccharide catabolic process Source: UniProtKB-KW
  • positive regulation of chemokine secretion Source: UniProtKB
  • production of molecular mediator involved in inflammatory response Source: UniProtKB
  • response to fungus Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Apoptosis, Carbohydrate metabolism, Chitin degradation, Immunity, Inflammatory response, Polysaccharide degradation

Keywords - Ligandi

Chitin-binding

Enzyme and pathway databases

BRENDAi3.2.1.14. 2681.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Acidic mammalian chitinase (EC:3.2.1.14)
Short name:
AMCase
Alternative name(s):
Lung-specific protein TSA1902
Gene namesi
Name:CHIA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:17432. CHIA.

Subcellular locationi

Isoform 1 :
  • Secreted

  • Note: Secretion depends on EGFR activity.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular region Source: GO_Central
  • extracellular space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi138 – 1381D → A: Loss of chitinase activity. No effect on protection against apoptosis or on AKT1 activation. 1 Publication

Organism-specific databases

PharmGKBiPA142672117.

Polymorphism and mutation databases

BioMutaiCHIA.
DMDMi37999771.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121By similarityAdd
BLAST
Chaini22 – 476455Acidic mammalian chitinasePRO_0000011944Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 51PROSITE-ProRule annotation1 Publication
Disulfide bondi49 ↔ 394PROSITE-ProRule annotation1 Publication
Disulfide bondi307 ↔ 372PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ9BZP6.
PaxDbiQ9BZP6.
PRIDEiQ9BZP6.

PTM databases

PhosphoSiteiQ9BZP6.

Expressioni

Tissue specificityi

Detected in lung epithelial cells from asthma patients (at protein level). Highly expressed in stomach. Detected at lower levels in lung.2 Publications

Inductioni

Up-regulated in lung epithelial cells from asthma patients.1 Publication

Gene expression databases

BgeeiQ9BZP6.
ExpressionAtlasiQ9BZP6. baseline and differential.
GenevisibleiQ9BZP6. HS.

Organism-specific databases

HPAiHPA059193.

Interactioni

Subunit structurei

Interacts with EGFR.2 Publications

Protein-protein interaction databases

BioGridi118039. 10 interactions.

Structurei

Secondary structure

1
476
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 297Combined sources
Helixi32 – 343Combined sources
Helixi37 – 393Combined sources
Helixi43 – 453Combined sources
Turni48 – 503Combined sources
Beta strandi52 – 6211Combined sources
Beta strandi65 – 673Combined sources
Helixi73 – 8210Combined sources
Helixi83 – 853Combined sources
Beta strandi91 – 977Combined sources
Helixi99 – 1013Combined sources
Helixi104 – 1107Combined sources
Helixi113 – 13018Combined sources
Beta strandi133 – 1386Combined sources
Helixi151 – 17323Combined sources
Beta strandi179 – 1846Combined sources
Helixi188 – 1947Combined sources
Helixi197 – 2037Combined sources
Beta strandi205 – 2095Combined sources
Helixi217 – 2193Combined sources
Helixi236 – 2405Combined sources
Helixi243 – 25210Combined sources
Helixi257 – 2593Combined sources
Beta strandi260 – 27516Combined sources
Beta strandi284 – 2885Combined sources
Turni293 – 2953Combined sources
Beta strandi300 – 3023Combined sources
Helixi303 – 3119Combined sources
Beta strandi315 – 3195Combined sources
Turni320 – 3234Combined sources
Beta strandi324 – 3296Combined sources
Beta strandi332 – 3354Combined sources
Helixi339 – 35113Combined sources
Beta strandi355 – 3606Combined sources
Helixi362 – 3643Combined sources
Beta strandi367 – 3693Combined sources
Turni370 – 3723Combined sources
Helixi378 – 3869Combined sources
Helixi392 – 3943Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YBTX-ray2.22A/B/C/D/E/F21-398[»]
2YBUX-ray2.25A/B/C/D/E/F21-398[»]
3FXYX-ray2.00A/B/C/D22-408[»]
3FY1X-ray1.70A/B22-408[»]
3RM4X-ray1.90A/B22-408[»]
3RM8X-ray1.80A/B22-408[»]
3RM9X-ray2.10A/B22-408[»]
3RMEX-ray1.80A/B22-408[»]
ProteinModelPortaliQ9BZP6.
SMRiQ9BZP6. Positions 21-397.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BZP6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini427 – 47650Chitin-binding type-2PROSITE-ProRule annotationAdd
BLAST

Region

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi415 – 4206Poly-Ser

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3325.
GeneTreeiENSGT00550000074323.
HOVERGENiHBG011684.
InParanoidiQ9BZP6.
KOiK01183.
OMAiCANGITY.
PhylomeDBiQ9BZP6.
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 (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BZP6-1) [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
MTKLILLTGL VLILNLQLGS AYQLTCYFTN WAQYRPGLGR FMPDNIDPCL
60 70 80 90 100
CTHLIYAFAG RQNNEITTIE WNDVTLYQAF NGLKNKNSQL KTLLAIGGWN
110 120 130 140 150
FGTAPFTAMV STPENRQTFI TSVIKFLRQY EFDGLDFDWE YPGSRGSPPQ
160 170 180 190 200
DKHLFTVLVQ EMREAFEQEA KQINKPRLMV TAAVAAGISN IQSGYEIPQL
210 220 230 240 250
SQYLDYIHVM TYDLHGSWEG YTGENSPLYK YPTDTGSNAY LNVDYVMNYW
260 270 280 290 300
KDNGAPAEKL IVGFPTYGHN FILSNPSNTG IGAPTSGAGP AGPYAKESGI
310 320 330 340 350
WAYYEICTFL KNGATQGWDA PQEVPYAYQG NVWVGYDNIK SFDIKAQWLK
360 370 380 390 400
HNKFGGAMVW AIDLDDFTGT FCNQGKFPLI STLKKALGLQ SASCTAPAQP
410 420 430 440 450
IEPITAAPSG SGNGSGSSSS GGSSGGSGFC AVRANGLYPV ANNRNAFWHC
460 470
VNGVTYQQNC QAGLVFDTSC DCCNWA
Length:476
Mass (Da):52,271
Last modified:June 1, 2001 - v1
Checksum:i92B27BAD2F7EB4CC
GO
Isoform 2 (identifier: Q9BZP6-2) [UniParc]FASTAAdd to basket

Also known as: TSA1902-L

The sequence of this isoform differs from the canonical sequence as follows:
     1-108: Missing.

Show »
Length:368
Mass (Da):40,139
Checksum:iFC2558C4CEA48609
GO
Isoform 3 (identifier: Q9BZP6-3) [UniParc]FASTAAdd to basket

Also known as: TSA1902-S

The sequence of this isoform differs from the canonical sequence as follows:
     1-161: Missing.

Show »
Length:315
Mass (Da):33,906
Checksum:i61D614709B577CAD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti203 – 2031Y → C in AAX81431 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti45 – 451N → D Increased chitinase activity; when associated with N-47 and M-61. 1 Publication
Corresponds to variant rs41282492 [ dbSNP | Ensembl ].
VAR_063030
Natural varianti47 – 471D → N Increased chitinase activity; when associated with N-47 and M-61. 1 Publication
Corresponds to variant rs41282494 [ dbSNP | Ensembl ].
VAR_063031
Natural varianti61 – 611R → M Increased chitinase activity; when associated with N-47 and M-61. 1 Publication
Corresponds to variant rs41282496 [ dbSNP | Ensembl ].
VAR_063032
Natural varianti102 – 1021G → R.1 Publication
Corresponds to variant rs3818822 [ dbSNP | Ensembl ].
VAR_049192
Natural varianti125 – 1251K → R.1 Publication
Corresponds to variant rs61756687 [ dbSNP | Ensembl ].
VAR_063033
Natural varianti324 – 3241V → G.
Corresponds to variant rs2256721 [ dbSNP | Ensembl ].
VAR_033730
Natural varianti339 – 3391I → V.2 Publications
Corresponds to variant rs2275253 [ dbSNP | Ensembl ].
VAR_049193
Natural varianti354 – 3541F → S.1 Publication
Corresponds to variant rs2275254 [ dbSNP | Ensembl ].
VAR_049194
Natural varianti377 – 3771F → L.
Corresponds to variant rs36011905 [ dbSNP | Ensembl ].
VAR_049195
Natural varianti432 – 4321V → G.2 Publications
Corresponds to variant rs2256721 [ dbSNP | Ensembl ].
VAR_049196

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 161161Missing in isoform 3. 2 PublicationsVSP_008634Add
BLAST
Alternative sequencei1 – 108108Missing in isoform 2. 3 PublicationsVSP_008635Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB025008 mRNA. Translation: BAA86980.1.
AB025009 mRNA. Translation: BAA86981.1.
AF290004 mRNA. Translation: AAG60019.1.
AY789444 mRNA. Translation: AAX81431.1.
AY789445 mRNA. Translation: AAX81432.1.
AL513202, AL356387 Genomic DNA. Translation: CAH70803.1.
AL356387, AL513202 Genomic DNA. Translation: CAI19265.1.
BC047336 mRNA. Translation: AAH47336.2.
BC036339 mRNA. Translation: AAH36339.2.
BC106910 mRNA. Translation: AAI06911.1.
CCDSiCCDS41368.1. [Q9BZP6-1]
CCDS58017.1. [Q9BZP6-3]
CCDS832.1. [Q9BZP6-2]
RefSeqiNP_001035713.1. NM_001040623.2. [Q9BZP6-3]
NP_001244930.1. NM_001258001.1. [Q9BZP6-2]
NP_001244931.1. NM_001258002.1. [Q9BZP6-3]
NP_001244932.1. NM_001258003.1. [Q9BZP6-2]
NP_001244933.1. NM_001258004.1. [Q9BZP6-3]
NP_001244934.1. NM_001258005.1. [Q9BZP6-3]
NP_068569.2. NM_021797.3. [Q9BZP6-2]
NP_970615.2. NM_201653.3. [Q9BZP6-1]
XP_006710640.1. XM_006710577.2. [Q9BZP6-3]
UniGeneiHs.128814.

Genome annotation databases

EnsembliENST00000343320; ENSP00000341828; ENSG00000134216. [Q9BZP6-1]
ENST00000353665; ENSP00000338970; ENSG00000134216. [Q9BZP6-3]
ENST00000369740; ENSP00000358755; ENSG00000134216. [Q9BZP6-1]
ENST00000430615; ENSP00000391132; ENSG00000134216. [Q9BZP6-2]
ENST00000451398; ENSP00000390476; ENSG00000134216. [Q9BZP6-3]
ENST00000483391; ENSP00000436946; ENSG00000134216. [Q9BZP6-3]
GeneIDi27159.
KEGGihsa:27159.
UCSCiuc001eaq.4. human. [Q9BZP6-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB025008 mRNA. Translation: BAA86980.1.
AB025009 mRNA. Translation: BAA86981.1.
AF290004 mRNA. Translation: AAG60019.1.
AY789444 mRNA. Translation: AAX81431.1.
AY789445 mRNA. Translation: AAX81432.1.
AL513202, AL356387 Genomic DNA. Translation: CAH70803.1.
AL356387, AL513202 Genomic DNA. Translation: CAI19265.1.
BC047336 mRNA. Translation: AAH47336.2.
BC036339 mRNA. Translation: AAH36339.2.
BC106910 mRNA. Translation: AAI06911.1.
CCDSiCCDS41368.1. [Q9BZP6-1]
CCDS58017.1. [Q9BZP6-3]
CCDS832.1. [Q9BZP6-2]
RefSeqiNP_001035713.1. NM_001040623.2. [Q9BZP6-3]
NP_001244930.1. NM_001258001.1. [Q9BZP6-2]
NP_001244931.1. NM_001258002.1. [Q9BZP6-3]
NP_001244932.1. NM_001258003.1. [Q9BZP6-2]
NP_001244933.1. NM_001258004.1. [Q9BZP6-3]
NP_001244934.1. NM_001258005.1. [Q9BZP6-3]
NP_068569.2. NM_021797.3. [Q9BZP6-2]
NP_970615.2. NM_201653.3. [Q9BZP6-1]
XP_006710640.1. XM_006710577.2. [Q9BZP6-3]
UniGeneiHs.128814.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YBTX-ray2.22A/B/C/D/E/F21-398[»]
2YBUX-ray2.25A/B/C/D/E/F21-398[»]
3FXYX-ray2.00A/B/C/D22-408[»]
3FY1X-ray1.70A/B22-408[»]
3RM4X-ray1.90A/B22-408[»]
3RM8X-ray1.80A/B22-408[»]
3RM9X-ray2.10A/B22-408[»]
3RMEX-ray1.80A/B22-408[»]
ProteinModelPortaliQ9BZP6.
SMRiQ9BZP6. Positions 21-397.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118039. 10 interactions.

Chemistry

BindingDBiQ9BZP6.
ChEMBLiCHEMBL1293197.

Protein family/group databases

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

PTM databases

PhosphoSiteiQ9BZP6.

Polymorphism and mutation databases

BioMutaiCHIA.
DMDMi37999771.

Proteomic databases

MaxQBiQ9BZP6.
PaxDbiQ9BZP6.
PRIDEiQ9BZP6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000343320; ENSP00000341828; ENSG00000134216. [Q9BZP6-1]
ENST00000353665; ENSP00000338970; ENSG00000134216. [Q9BZP6-3]
ENST00000369740; ENSP00000358755; ENSG00000134216. [Q9BZP6-1]
ENST00000430615; ENSP00000391132; ENSG00000134216. [Q9BZP6-2]
ENST00000451398; ENSP00000390476; ENSG00000134216. [Q9BZP6-3]
ENST00000483391; ENSP00000436946; ENSG00000134216. [Q9BZP6-3]
GeneIDi27159.
KEGGihsa:27159.
UCSCiuc001eaq.4. human. [Q9BZP6-1]

Organism-specific databases

CTDi27159.
GeneCardsiGC01P111833.
HGNCiHGNC:17432. CHIA.
HPAiHPA059193.
MIMi606080. gene.
neXtProtiNX_Q9BZP6.
PharmGKBiPA142672117.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG3325.
GeneTreeiENSGT00550000074323.
HOVERGENiHBG011684.
InParanoidiQ9BZP6.
KOiK01183.
OMAiCANGITY.
PhylomeDBiQ9BZP6.
TreeFamiTF315610.

Enzyme and pathway databases

BRENDAi3.2.1.14. 2681.

Miscellaneous databases

EvolutionaryTraceiQ9BZP6.
GenomeRNAii27159.
NextBioi49937.
PROiQ9BZP6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BZP6.
ExpressionAtlasiQ9BZP6. baseline and differential.
GenevisibleiQ9BZP6. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and mapping of a human lung-specific gene, TSA1902, encoding a novel chitinase family member."
    Saito A., Ozaki K., Fujiwara T., Nakamura Y., Tanigami A.
    Gene 239:325-331(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), VARIANTS VAL-339 AND GLY-432.
    Tissue: Lung.
  2. "Identification of a novel acidic mammalian chitinase distinct from chitotriosidase."
    Boot R.G., Blommaart E.F.C., Swart E., Ghauharali-van der Vlugt K., Bijl N., Moe C., Place A., Aerts J.M.F.G.
    J. Biol. Chem. 276:6770-6778(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
  3. "A novel chitinase family member."
    Chen X.H., Cai G.P.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
    Tissue: Kidney.
  4. "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].
  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 2).
  6. "Acidic mammalian chitinase in asthmatic Th2 inflammation and IL-13 pathway activation."
    Zhu Z., Zheng T., Homer R.J., Kim Y.K., Chen N.Y., Cohn L., Hamid Q., Elias J.A.
    Science 304:1678-1682(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, TISSUE SPECIFICITY.
  7. "Acidic mammalian chitinase is secreted via an ADAM17/epidermal growth factor receptor-dependent pathway and stimulates chemokine production by pulmonary epithelial cells."
    Hartl D., He C.H., Koller B., Da Silva C.A., Homer R., Lee C.G., Elias J.A.
    J. Biol. Chem. 283:33472-33482(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH EGFR, SUBCELLULAR LOCATION.
  8. "Acidic mammalian chitinase regulates epithelial cell apoptosis via a chitinolytic-independent mechanism."
    Hartl D., He C.H., Koller B., Da Silva C.A., Kobayashi Y., Lee C.G., Flavell R.A., Elias J.A.
    J. Immunol. 182:5098-5106(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-138.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 22-408 IN COMPLEX WITH METHYLALLOSAMIDIN, CATALYTIC ACTIVITY, DISULFIDE BONDS.
  10. Cited for: VARIANTS ASP-45; ASN-47; MET-61; ARG-102; ARG-125; VAL-339; SER-354 AND GLY-432, CATALYTIC ACTIVITY, FUNCTION, CHARACTERIZATION OF VARIANTS ASP-45; ASN-47 AND MET-61.

Entry informationi

Entry nameiCHIA_HUMAN
AccessioniPrimary (citable) accession number: Q9BZP6
Secondary accession number(s): Q32W79
, Q32W80, Q3B866, Q5U5Z5, Q5VUV4, Q86UD8, Q9ULY3, Q9ULY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: June 1, 2001
Last modified: June 24, 2015
This is version 137 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. 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.