CHIT1

Functionⁱ

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

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.

Catalytic activityⁱ

Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
3 Publications
Manual assertion based on experiment inⁱ
- Ref.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.
- Ref.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.
- Ref.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.
EC:3.2.1.14

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	140	Proton donorPROSITE-ProRule annotation	1
Binding siteⁱ	141	ChitooligosaccharidePROSITE-ProRule annotation	1
Binding siteⁱ	358	ChitooligosaccharidePROSITE-ProRule annotation	1

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Glycosidase, Hydrolase
Biological process	Carbohydrate metabolism, Chitin degradation, Polysaccharide degradation
Ligand	Chitin-binding

Enzyme and pathway databases

Reactomeⁱ	R-HSA-189085 Digestion of dietary carbohydrate R-HSA-6798695 Neutrophil degranulation

Reactomeⁱ

R-HSA-189085 Digestion of dietary carbohydrate
R-HSA-6798695 Neutrophil degranulation

Protein family/group databases

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

CAZyⁱ

CBM14 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
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 1

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:1936 CHIT1
MIMⁱ	600031 gene
neXtProtⁱ	NX_Q13231

Keywords - Cellular componentⁱ

Lysosome, Secreted

Pathology & Biotechⁱ

Organism-specific databases

DisGeNET More...DisGeNETⁱ	1118
MalaCards human disease database More...MalaCardsⁱ	CHIT1
MIMⁱ	614122 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000133063
PharmGKBⁱ	PA26467

Miscellaneous databases

Pharosⁱ	Q13231 Tbio

Pharosⁱ

Q13231 Tbio

Chemistry databases

ChEMBLⁱ	CHEMBL3080
Drug and drug target database More...DrugBankⁱ	DB03539 2-(Acetylamino)-2-Deoxy-6-O-Methyl-Alpha-D-Allopyranose DB03109 2-acetylamino-2-deoxy-b-D-allopyranose DB04404 Allosamizoline DB04350 Argadin DB03632 Argifin DB02325 Isopropyl alcohol

Polymorphism and mutation databases

BioMutaⁱ	CHIT1
DMDMⁱ	37999493

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Signal peptideⁱ	1 – 21	1 PublicationAdd BLAST		21
ChainⁱPRO_0000011941	22 – 466	Chitotriosidase-1Add BLAST		445

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Disulfide bondⁱ	26 ↔ 51	PROSITE-ProRule annotation1 Publication
Glycosylationⁱ	100	N-linked (GlcNAc...) asparagine; in variant S-1021 Publication	1
Disulfide bondⁱ	307 ↔ 370	PROSITE-ProRule annotation1 Publication
Disulfide bondⁱ	450 ↔ 463	PROSITE-ProRule annotation

Keywords - PTMⁱ

Disulfide bond, Glycoprotein

Proteomic databases

jPOSTⁱ	Q13231
MassIVEⁱ	Q13231
PaxDbⁱ	Q13231
PeptideAtlas More...PeptideAtlasⁱ	Q13231
PRIDEⁱ	Q13231
ProteomicsDBⁱ	59236 [Q13231-1] 59237 [Q13231-2] 59238 [Q13231-3]

PTM databases

iPTMnetⁱ	Q13231
PhosphoSitePlusⁱ	Q13231

Expressionⁱ

Tissue specificityⁱ

Detected in spleen. Secreted by cultured macrophages.1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000133063 Expressed in lymph node and 85 other tissues
ExpressionAtlasⁱ	Q13231 baseline and differential
Genevisibleⁱ	Q13231 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000133063 Tissue enhanced (adipose tissue, lymphoid tissue)

HPAⁱ

ENSG00000133063 Tissue enhanced (adipose tissue, lymphoid tissue)

Interactionⁱ

Subunit structureⁱ

Monomer.

3 Publications

Protein-protein interaction databases

BioGridⁱ	107542, 4 interactors
IntActⁱ	Q13231, 5 interactors
STRINGⁱ	9606.ENSP00000356198

Chemistry databases

BindingDBⁱ

Q13231

Miscellaneous databases

RNActⁱ	Q13231 protein

RNActⁱ

Q13231 protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	23 – 29	Combined sources	7
Helixⁱ	32 – 34	Combined sources	3
Helixⁱ	37 – 39	Combined sources	3
Helixⁱ	43 – 45	Combined sources	3
Turnⁱ	48 – 50	Combined sources	3
Beta strandⁱ	52 – 62	Combined sources	11
Beta strandⁱ	65 – 67	Combined sources	3
Helixⁱ	73 – 86	Combined sources	14
Beta strandⁱ	91 – 97	Combined sources	7
Turnⁱ	99 – 101	Combined sources	3
Helixⁱ	104 – 110	Combined sources	7
Helixⁱ	113 – 130	Combined sources	18
Beta strandⁱ	133 – 138	Combined sources	6
Beta strandⁱ	144 – 146	Combined sources	3
Helixⁱ	151 – 173	Combined sources	23
Beta strandⁱ	179 – 185	Combined sources	7
Helixⁱ	188 – 194	Combined sources	7
Helixⁱ	197 – 201	Combined sources	5
Beta strandⁱ	205 – 210	Combined sources	6
Beta strandⁱ	219 – 221	Combined sources	3
Helixⁱ	236 – 240	Combined sources	5
Helixⁱ	243 – 252	Combined sources	10
Helixⁱ	257 – 259	Combined sources	3
Beta strandⁱ	260 – 274	Combined sources	15
Beta strandⁱ	284 – 288	Combined sources	5
Turnⁱ	293 – 295	Combined sources	3
Beta strandⁱ	300 – 302	Combined sources	3
Helixⁱ	303 – 306	Combined sources	4
Beta strandⁱ	313 – 317	Combined sources	5
Turnⁱ	318 – 321	Combined sources	4
Beta strandⁱ	322 – 327	Combined sources	6
Beta strandⁱ	330 – 333	Combined sources	4
Helixⁱ	337 – 349	Combined sources	13
Beta strandⁱ	353 – 358	Combined sources	6
Helixⁱ	360 – 362	Combined sources	3
Beta strandⁱ	367 – 372	Combined sources	6
Helixⁱ	376 – 384	Combined sources	9
Turnⁱ	419 – 422	Combined sources	4
Beta strandⁱ	425 – 430	Combined sources	6
Beta strandⁱ	433 – 441	Combined sources	9
Beta strandⁱ	444 – 449	Combined sources	6
Beta strandⁱ	455 – 457	Combined sources	3
Turnⁱ	458 – 461	Combined sources	4
Beta strandⁱ	462 – 464	Combined sources	3

Show more details

3D structure databases

SMRⁱ	Q13231
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q13231

EvolutionaryTraceⁱ

Q13231

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	22 – 388	GH18PROSITE-ProRule annotationAdd BLAST		367
Domainⁱ	417 – 466	Chitin-binding type-2PROSITE-ProRule annotationAdd BLAST		50

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	70 – 71	Chitooligosaccharide bindingPROSITE-ProRule annotation	2
Regionⁱ	97 – 100	Chitooligosaccharide bindingPROSITE-ProRule annotation	4
Regionⁱ	210 – 213	Chitooligosaccharide bindingPROSITE-ProRule annotation	4

Sequence similaritiesⁱ

Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily.Curated

Keywords - Domainⁱ

Signal

Phylogenomic databases

eggNOGⁱ	KOG2806 Eukaryota COG3325 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000161149
HOGENOMⁱ	CLU_002833_3_1_1
InParanoidⁱ	Q13231
KEGG Orthology (KO) More...KOⁱ	K01183
OMAⁱ	FYYCSGG
Database of Orthologous Groups More...OrthoDBⁱ	1289629at2759
PhylomeDBⁱ	Q13231
TreeFamⁱ	TF315610

Family and domain databases

Gene3Dⁱ	3.10.50.10, 1 hit
InterProⁱ	View protein in InterPro IPR002557 Chitin-bd_dom IPR036508 Chitin-bd_dom_sf IPR011583 Chitinase_II IPR029070 Chitinase_insertion_sf IPR001223 Glyco_hydro18_cat IPR001579 Glyco_hydro_18_chit_AS IPR017853 Glycoside_hydrolase_SF
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01607 CBM_14, 1 hit PF00704 Glyco_hydro_18, 1 hit
SMARTⁱ	View protein in SMART SM00494 ChtBD2, 1 hit SM00636 Glyco_18, 1 hit
SUPFAMⁱ	SSF51445 SSF51445, 1 hit SSF54556 SSF54556, 1 hit SSF57625 SSF57625, 1 hit
PROSITEⁱ	View protein in PROSITE PS50940 CHIT_BIND_II, 1 hit PS01095 GH18_1, 1 hit PS51910 GH18_2, 1 hit

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 Add to basket

This entry has 4 described isoforms and 1 potential isoform that is computationally mapped.Show all Align All

Isoform 1 (identifier: Q13231-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the canonicalⁱ 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]FASTA Add to basket

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

« 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 
GLGGAMVWAL DLDDFAGFSC NQGRYPLIQT LRQELNG

Show »

Length:387

Mass (Da):43,133

Checksum:ⁱ03A272B8BC5E0D71

GO

Isoform 3 (identifier: Q13231-3) [UniParc]FASTA Add to basket

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

« 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 KTKGRYPLIQ 
       360        370        380        390        400
TLRQELSLPY LPSGTPELEV PKPGQPSEPE HGPSPGQDTF CQGKADGLYP 
       410        420        430 
NPRERSSFYS CAAGRLFQQS CPTGLVFSNS CKCCTWN

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.Curated

Show »

Length:437

Mass (Da):48,565

Checksum:ⁱ1A073A5F90A43717

GO

Isoform 4 (identifier: Q13231-4) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MVRSVAWAGF MVLLMIPWGS AAKLVCYFTN WAQYRQGEAR FLPKDLDPSL 
        60         70         80         90        100
CTHLIYAFAG MTNHQLSTTE WNDETLYQEF NGLKKMFTDM VATANNRQTF 
       110        120        130        140        150
VNSAIRFLRK YSFDGLDLDW EYPGSQGSPA VDKERFTTLV QDLANAFQQE 
       160        170        180        190        200
AQTSGKERLL LSAAVPAGQT YVDAGYEVDK IAQNLDFVNL MAYDFHGSWE 
       210        220        230        240        250
KVTGHNSPLY KRQEESGAAA SLNVDAAVQQ WLQKGTPASK LILGMPTYGR 
       260        270        280        290        300
SFTLASSSDT RVGAPATGSG TPGPFTKEGG MLAYYEVCSW KGATKQRIQD 
       310        320        330        340        350
QKVPYIFRDN QWVGFDDVES FKTKVSYLKQ KGLGGAMVWA LDLDDFAGFS 
       360        370        380        390        400
CNQGRYPLIQ TLRQELSLPY LPSGTPELEV PKPGQPSEPE HGPSPGQDTF 
       410        420        430        440 
CQGKADGLYP NPRERSSFYS CAAGRLFQQS CPTGLVFSNS CKCCTWN

Show »

Length:447

Mass (Da):49,613

Checksum:ⁱ4C083E18D767C381

GO

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation

	D6REY1	D6REY1_HUMAN		Chitotriosidase-1 Chitotriosidase-1	CHIT1	361	Annotation score:

Sequence cautionⁱ

The sequence BAG51478 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

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.1 Publication

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_049190	40	R → H. Corresponds to variant dbSNP:rs35920428EnsemblClinVar.	1
Natural variantⁱVAR_065914	74	E → K Rare variant detected in patients with Gaucher disease type 1. 1 PublicationCorresponds to variant dbSNP:rs137852607EnsemblClinVar.	1
Natural variantⁱVAR_022138	102	G → 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. 3 PublicationsCorresponds to variant dbSNP:rs2297950EnsemblClinVar.	1
Natural variantⁱVAR_049191	171	Q → H. Corresponds to variant dbSNP:rs12562058Ensembl.	1
Natural variantⁱVAR_024458	442	A → G2 PublicationsCorresponds to variant dbSNP:rs1065761EnsemblClinVar.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Length
Alternative sequenceⁱVSP_044816	87 – 105	Missing in isoform 4. 1 PublicationAdd BLAST	19
Alternative sequenceⁱVSP_008633	344 – 372	Missing in isoform 3. CuratedAdd BLAST	29
Alternative sequenceⁱVSP_008631	386 – 387	SL → NG in isoform 2. 1 Publication	2
Alternative sequenceⁱVSP_008632	388 – 466	Missing in isoform 2. 1 PublicationAdd BLAST	79

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ 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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS1436.1 [Q13231-1] CCDS58057.1 [Q13231-4]
NCBI Reference Sequences More...RefSeqⁱ	NP_001243054.2, NM_001256125.1 [Q13231-4] NP_003456.1, NM_003465.2 [Q13231-1]

Genome annotation databases

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

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q13231	Chitinase 1		AOTNA		415	UniRef90_Q13231
CHIT1 isoform 7		PANTR		387
CHIT1 isoform 7		PONAB		387
Isoform 2 of Chitotriosidase-1		HUMAN		387
+8
Q13231-3	Isoform 4 of Chitotriosidase-1		HUMAN		447	UniRef90_Q13231-4
Chitinase 1		MACMU		481
Chitinase 1		MACFA		466
Chitinase 1		PAPAN		466
CHIT1 isoform 5		PONAB		466
+56

Protein	Similar proteins		Species	Score	Length	Source
Q13231	Acidic mammalian chitinase	)	HUMAN		476	UniRef50_Q13231
Acidic mammalian chitinase		BOVIN		472
Chitinase 1		AOTNA		415
CHIT1 isoform 7		PONAB		387
CHIT1 isoform 7		PANTR		387
+650
Q13231-3	Isoform 4 of Chitotriosidase-1		HUMAN		447	UniRef50_Q13231-4
Chitinase 1		MACMU		481
Chitinase 1		CERAT		466
Chitinase 1		MACNE		466
Chitin-binding type-2 domain-containing protein		MACFA		466
+95

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ 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]

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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	[»]
	4WJX	X-ray	1.00	A	22-387	[»]
	4WK9	X-ray	1.10	A	22-387	[»]
	4WKA	X-ray	0.95	A	22-386	[»]
	4WKF	X-ray	1.10	A	22-387	[»]
	4WKH	X-ray	1.05	A	22-387	[»]
	5HBF	X-ray	1.95	A/B	1-466	[»]
	5NR8	X-ray	1.35	A	22-387	[»]
	5NRA	X-ray	1.27	A	22-387	[»]
	5NRF	X-ray	1.45	A	22-387	[»]
	6SO0	NMR	-	A	418-466	[»]
SMRⁱ	Q13231
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	107542, 4 interactors
IntActⁱ	Q13231, 5 interactors
STRINGⁱ	9606.ENSP00000356198

Chemistry databases

BindingDBⁱ	Q13231
ChEMBLⁱ	CHEMBL3080
DrugBankⁱ	DB03539 2-(Acetylamino)-2-Deoxy-6-O-Methyl-Alpha-D-Allopyranose DB03109 2-acetylamino-2-deoxy-b-D-allopyranose DB04404 Allosamizoline DB04350 Argadin DB03632 Argifin DB02325 Isopropyl alcohol

Protein family/group databases

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

CAZyⁱ

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

PTM databases

iPTMnetⁱ	Q13231
PhosphoSitePlusⁱ	Q13231

Polymorphism and mutation databases

BioMutaⁱ	CHIT1
DMDMⁱ	37999493

Proteomic databases

jPOSTⁱ	Q13231
MassIVEⁱ	Q13231
PaxDbⁱ	Q13231
PeptideAtlasⁱ	Q13231
PRIDEⁱ	Q13231
ProteomicsDBⁱ	59236 [Q13231-1] 59237 [Q13231-2] 59238 [Q13231-3]

Protocols and materials databases

Antibodypediaⁱ	2441 231 antibodies
The DNASU plasmid repository More...DNASUⁱ	1118

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.3 human [Q13231-1]

Organism-specific databases

CTDⁱ	1118
DisGeNETⁱ	1118
GeneCardsⁱ	CHIT1
HGNCⁱ	HGNC:1936 CHIT1
HPAⁱ	ENSG00000133063 Tissue enhanced (adipose tissue, lymphoid tissue)
MalaCardsⁱ	CHIT1
MIMⁱ	600031 gene 614122 phenotype
neXtProtⁱ	NX_Q13231
OpenTargetsⁱ	ENSG00000133063
PharmGKBⁱ	PA26467
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG2806 Eukaryota COG3325 LUCA
GeneTreeⁱ	ENSGT00940000161149
HOGENOMⁱ	CLU_002833_3_1_1
InParanoidⁱ	Q13231
KOⁱ	K01183
OMAⁱ	FYYCSGG
OrthoDBⁱ	1289629at2759
PhylomeDBⁱ	Q13231
TreeFamⁱ	TF315610

Enzyme and pathway databases

Reactomeⁱ	R-HSA-189085 Digestion of dietary carbohydrate R-HSA-6798695 Neutrophil degranulation

Reactomeⁱ

R-HSA-189085 Digestion of dietary carbohydrate
R-HSA-6798695 Neutrophil degranulation

Miscellaneous databases

ChiTaRSⁱ	CHIT1 human
EvolutionaryTraceⁱ	Q13231
GenomeRNAiⁱ	1118
Pharosⁱ	Q13231 Tbio
Protein Ontology More...PROⁱ	PR:Q13231
RNActⁱ	Q13231 protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000133063 Expressed in lymph node and 85 other tissues
ExpressionAtlasⁱ	Q13231 baseline and differential
Genevisibleⁱ	Q13231 HS

Family and domain databases

Gene3Dⁱ	3.10.50.10, 1 hit
InterProⁱ	View protein in InterPro IPR002557 Chitin-bd_dom IPR036508 Chitin-bd_dom_sf IPR011583 Chitinase_II IPR029070 Chitinase_insertion_sf IPR001223 Glyco_hydro18_cat IPR001579 Glyco_hydro_18_chit_AS IPR017853 Glycoside_hydrolase_SF
Pfamⁱ	View protein in Pfam PF01607 CBM_14, 1 hit PF00704 Glyco_hydro_18, 1 hit
SMARTⁱ	View protein in SMART SM00494 ChtBD2, 1 hit SM00636 Glyco_18, 1 hit
SUPFAMⁱ	SSF51445 SSF51445, 1 hit SSF54556 SSF54556, 1 hit SSF57625 SSF57625, 1 hit
PROSITEⁱ	View protein in PROSITE PS50940 CHIT_BIND_II, 1 hit PS01095 GH18_1, 1 hit PS51910 GH18_2, 1 hit
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	CHIT1_HUMAN
Accessionⁱ	Q13231Primary (citable) accession number: Q13231 Secondary accession number(s): B3KNW6 Q9UDJ8
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 24, 2003
	Last sequence update:	November 1, 1996
	Last modified:	April 22, 2020
	This is version 191 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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, Direct protein sequencing, Reference proteome

Documents

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

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UniProtKB - Q13231 (CHIT1_HUMAN)

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Chitotriosidase-1

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

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Keywords - PTMi

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Keywords - Domaini

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<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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Sequence databases

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Keywords - Coding sequence diversityi

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ