Q13231 (CHIT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chitotriosidase-1
EC=3.2.1.14

Alternative name(s):
Chitinase-1

Gene names

Name:

CHIT1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	466 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Degrades chitin, chitotriose and chitobiose. May participate in the defense against nematodes and other pathogens. Isoform 3 has no enzymatic activity. Ref.1 Ref.5 Ref.6
Catalytic activity	Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. Ref.5 Ref.9 Ref.11
Subunit structure	Monomer.
Subcellular location	Secreted. Lysosome. Note: A small proportion is lysosomal. Ref.1 Ref.7 Ref.11
Tissue specificity	Detected in spleen. Secreted by cultured macrophages. Ref.5
Polymorphism	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 [MIM: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.
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.
Sequence similarities	Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily. Contains 1 chitin-binding type-2 domain.
Sequence caution	The sequence BAG51478.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Chitin degradation Polysaccharide degradation
Cellular component	Lysosome Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal
Ligand	Chitin-binding
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	chitin catabolic process Inferred from direct assay Ref.11. Source: UniProtKB immune response Non-traceable author statement Ref.6. Source: UniProtKB polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW response to bacterium Traceable author statement PubMed 9402970. Source: ProtInc
Cellular_component	extracellular space Inferred from direct assay Ref.11. Source: UniProtKB lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	chitin binding Traceable author statement Ref.6. Source: UniProtKB endochitinase activity Inferred from direct assay Ref.11. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q13231-1)

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.

Isoform 2 (identifier: Q13231-2)

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

Isoform 3 (identifier: Q13231-3)

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.

Isoform 4 (identifier: Q13231-4)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Ref.5

Chain

22 – 466

445

Chitotriosidase-1

PRO_0000011941

Regions

Domain

417 – 466

50

Chitin-binding type-2

Region

70 – 71

2

Chitooligosaccharide binding

Region

97 – 100

4

Chitooligosaccharide binding

Region

210 – 213

4

Chitooligosaccharide binding

Sites

Active site

140

1

Proton donor By similarity

Binding site

269

1

Chitooligosaccharide

Binding site

358

1

Chitooligosaccharide

Amino acid modifications

Glycosylation

100

1

N-linked (GlcNAc...); in variant S-102 Ref.11

Disulfide bond

26 ↔ 51

Ref.7

Disulfide bond

307 ↔ 370

Ref.7

Disulfide bond

450 ↔ 463

By similarity

Natural variations

Alternative sequence

87 – 105

19

Missing in isoform 4.

VSP_044816

Alternative sequence

344 – 372

29

Missing in isoform 3.

VSP_008633

Alternative sequence

386 – 387

2

SL → NG in isoform 2.

VSP_008631

Alternative sequence

388 – 466

79

Missing in isoform 2.

VSP_008632

Natural variant

40

1

R → H.
Corresponds to variant rs35920428 [ dbSNP | Ensembl ].

VAR_049190

Natural variant

74

1

E → K Rare variant detected in patients with Gaucher disease type 1. Ref.10

VAR_065914

Natural variant

102

1

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. Ref.4 Ref.10 Ref.11
Corresponds to variant rs2297950 [ dbSNP | Ensembl ].

VAR_022138

Natural variant

171

1

Q → H.
Corresponds to variant rs12562058 [ dbSNP | Ensembl ].

VAR_049191

Natural variant

442

1

A → G. Ref.2 Ref.4
Corresponds to variant rs1065761 [ dbSNP | Ensembl ].

VAR_024458

Secondary structure

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466

Helix Strand Turn

Details...

Beta strand

23 – 29

7

Helix

32 – 34

3

Helix

37 – 39

3

Helix

43 – 45

3

Turn

48 – 50

3

Beta strand

52 – 62

11

Beta strand

65 – 67

3

Helix

73 – 82

10

Helix

83 – 85

3

Beta strand

91 – 97

7

Turn

99 – 101

3

Helix

104 – 110

7

Helix

113 – 129

17

Beta strand

134 – 138

5

Beta strand

144 – 146

3

Helix

151 – 173

23

Beta strand

179 – 184

6

Helix

188 – 194

7

Helix

197 – 203

7

Beta strand

205 – 209

5

Beta strand

219 – 221

3

Helix

236 – 240

5

Helix

243 – 252

10

Helix

257 – 259

3

Beta strand

260 – 274

15

Beta strand

284 – 288

5

Turn

293 – 295

3

Beta strand

300 – 302

3

Helix

303 – 306

4

Beta strand

313 – 317

5

Turn

318 – 321

4

Beta strand

322 – 327

6

Beta strand

330 – 333

4

Helix

337 – 349

13

Beta strand

354 – 358

5

Helix

360 – 362

3

Beta strand

368 – 372

5

Helix

376 – 384

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: B4312D1E885E386D	FASTA	466	51,681
	10 20 30 40 50 60 MVRSVAWAGF MVLLMIPWGS AAKLVCYFTN WAQYRQGEAR FLPKDLDPSL CTHLIYAFAG 70 80 90 100 110 120 MTNHQLSTTE WNDETLYQEF NGLKKMNPKL KTLLAIGGWN FGTQKFTDMV ATANNRQTFV 130 140 150 160 170 180 NSAIRFLRKY SFDGLDLDWE YPGSQGSPAV DKERFTTLVQ DLANAFQQEA QTSGKERLLL 190 200 210 220 230 240 SAAVPAGQTY VDAGYEVDKI AQNLDFVNLM AYDFHGSWEK VTGHNSPLYK RQEESGAAAS 250 260 270 280 290 300 LNVDAAVQQW LQKGTPASKL ILGMPTYGRS FTLASSSDTR VGAPATGSGT PGPFTKEGGM 310 320 330 340 350 360 LAYYEVCSWK GATKQRIQDQ KVPYIFRDNQ WVGFDDVESF KTKVSYLKQK GLGGAMVWAL 370 380 390 400 410 420 DLDDFAGFSC NQGRYPLIQT LRQELSLPYL PSGTPELEVP KPGQPSEPEH GPSPGQDTFC 430 440 450 460 QGKADGLYPN PRERSSFYSC AAGRLFQQSC PTGLVFSNSC KCCTWN
	Isoform 2 [UniParc]. Checksum: 03A272B8BC5E0D71	FASTA	387	43,133
	10 20 30 40 50 60 MVRSVAWAGF MVLLMIPWGS AAKLVCYFTN WAQYRQGEAR FLPKDLDPSL CTHLIYAFAG 70 80 90 100 110 120 MTNHQLSTTE WNDETLYQEF NGLKKMNPKL KTLLAIGGWN FGTQKFTDMV ATANNRQTFV 130 140 150 160 170 180 NSAIRFLRKY SFDGLDLDWE YPGSQGSPAV DKERFTTLVQ DLANAFQQEA QTSGKERLLL 190 200 210 220 230 240 SAAVPAGQTY VDAGYEVDKI AQNLDFVNLM AYDFHGSWEK VTGHNSPLYK RQEESGAAAS 250 260 270 280 290 300 LNVDAAVQQW LQKGTPASKL ILGMPTYGRS FTLASSSDTR VGAPATGSGT PGPFTKEGGM 310 320 330 340 350 360 LAYYEVCSWK GATKQRIQDQ KVPYIFRDNQ WVGFDDVESF KTKVSYLKQK GLGGAMVWAL 370 380 DLDDFAGFSC NQGRYPLIQT LRQELNG
	Isoform 3 [UniParc]. Checksum: 1A073A5F90A43717	FASTA	437	48,565
	10 20 30 40 50 60 MVRSVAWAGF MVLLMIPWGS AAKLVCYFTN WAQYRQGEAR FLPKDLDPSL CTHLIYAFAG 70 80 90 100 110 120 MTNHQLSTTE WNDETLYQEF NGLKKMNPKL KTLLAIGGWN FGTQKFTDMV ATANNRQTFV 130 140 150 160 170 180 NSAIRFLRKY SFDGLDLDWE YPGSQGSPAV DKERFTTLVQ DLANAFQQEA QTSGKERLLL 190 200 210 220 230 240 SAAVPAGQTY VDAGYEVDKI AQNLDFVNLM AYDFHGSWEK VTGHNSPLYK RQEESGAAAS 250 260 270 280 290 300 LNVDAAVQQW LQKGTPASKL ILGMPTYGRS FTLASSSDTR VGAPATGSGT PGPFTKEGGM 310 320 330 340 350 360 LAYYEVCSWK GATKQRIQDQ KVPYIFRDNQ WVGFDDVESF KTKGRYPLIQ TLRQELSLPY 370 380 390 400 410 420 LPSGTPELEV PKPGQPSEPE HGPSPGQDTF CQGKADGLYP NPRERSSFYS CAAGRLFQQS 430 CPTGLVFSNS CKCCTWN
	Isoform 4 [UniParc]. Checksum: 4C083E18D767C381	FASTA	447	49,613
	10 20 30 40 50 60 MVRSVAWAGF MVLLMIPWGS AAKLVCYFTN WAQYRQGEAR FLPKDLDPSL CTHLIYAFAG 70 80 90 100 110 120 MTNHQLSTTE WNDETLYQEF NGLKKMFTDM VATANNRQTF VNSAIRFLRK YSFDGLDLDW 130 140 150 160 170 180 EYPGSQGSPA VDKERFTTLV QDLANAFQQE AQTSGKERLL LSAAVPAGQT YVDAGYEVDK 190 200 210 220 230 240 IAQNLDFVNL MAYDFHGSWE KVTGHNSPLY KRQEESGAAA SLNVDAAVQQ WLQKGTPASK 250 260 270 280 290 300 LILGMPTYGR SFTLASSSDT RVGAPATGSG TPGPFTKEGG MLAYYEVCSW KGATKQRIQD 310 320 330 340 350 360 QKVPYIFRDN QWVGFDDVES FKTKVSYLKQ KGLGGAMVWA LDLDDFAGFS CNQGRYPLIQ 370 380 390 400 410 420 TLRQELSLPY LPSGTPELEV PKPGQPSEPE HGPSPGQDTF CQGKADGLYP NPRERSSFYS 430 440 CAAGRLFQQS CPTGLVFSNS CKCCTWN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"The human chitotriosidase gene. Nature of inherited enzyme deficiency." Boot R.G., Renkema G.H., Verhoek M., Strijland A., Bliek J., de Meulemeester T.M.A.M.O., Mannens M.M.A.M., Aerts J.M.F.G. J. Biol. Chem. 273:25680-25685(1998) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00375364.
IPI00478217.
IPI00852865.
IPI00966316.

RefSeq

NP_001243054.2. NM_001256125.1.
NP_003456.1. NM_003465.2.

UniGene

Hs.201688.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q13231.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000255427.

Protein family/group databases

CAZy

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

Polymorphism databases

DMDM

37999493.

Proteomic databases

PaxDb

Q13231.

PRIDE

Q13231.

Protocols and materials databases

DNASU

1118.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000255427; ENSP00000255427; ENSG00000133063.
ENST00000367229; ENSP00000356198; ENSG00000133063.
ENST00000491855; ENSP00000423778; ENSG00000133063.

GeneID

1118.

KEGG

hsa:1118.

UCSC

uc001gzn.2. human.
uc009xal.1. human.

Organism-specific databases

CTD

1118.

GeneCards

GC01M203181.

HGNC

HGNC:1936. CHIT1.

HPA

HPA010575.

MIM

600031. gene.
614122. phenotype.

neXtProt

NX_Q13231.

PharmGKB

PA26467.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG3325.

HOVERGEN

HBG011684.

InParanoid

Q13231.

KO

K01183.

OMA

PGQDTFC.

OrthoDB

EOG476K16.

Gene expression databases

ArrayExpress

Q13231.

Bgee

Q13231.

CleanEx

HS_CHIT1.

Genevestigator

Q13231.

GermOnline

ENSG00000133063. Homo sapiens.

Family and domain databases

Gene3D

2.170.140.10. 1 hit.
3.20.20.80. 2 hits.

InterPro

IPR002557. Chitin-bd_dom.
IPR011583. Chitinase_II.
IPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Pfam

PF01607. CBM_14. 1 hit.
PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]

SMART

SM00494. ChtBD2. 1 hit.
SM00636. Glyco_18. 1 hit.
[Graphical view]

SUPFAM

SSF57625. Chitin_bind_PerA. 1 hit.
SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS50940. CHIT_BIND_II. 1 hit.
PS01095. CHITINASE_18. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q13231.

ChEMBL

CHEMBL3080.

ChiTaRS

CHIT1. human.

EvolutionaryTrace

Q13231.

GenomeRNAi

1118.

NextBio

35534786.

SOURCE

Search...

Entry information

Entry name

CHIT1_HUMAN

Accession

Primary (citable) accession number: Q13231
Secondary accession number(s): B3KNW6 , J3KN09, Q0VGG5, Q0VGG6, Q3ZAR1, Q6ISC2, Q9H3V8, Q9UDJ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 24, 2003
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 130 of the entry and version 1 of the sequence. [Complete history]

Entry status

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.