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P36222

- CH3L1_HUMAN

UniProt

P36222 - CH3L1_HUMAN

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Protein

Chitinase-3-like protein 1

Gene

CHI3L1

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

Functioni

Carbohydrate-binding lectin with a preference for chitin. Has no chitinase activity. May play a role in tissue remodeling and in the capacity of cells to respond to and cope with changes in their environment. Plays a role in T-helper cell type 2 (Th2) inflammatory response and IL-13-induced inflammation, regulating allergen sensitization, inflammatory cell apoptosis, dendritic cell accumulation and M2 macrophage differentiation. Facilitates invasion of pathogenic enteric bacteria into colonic mucosa and lymphoid organs. Mediates activation of AKT1 signaling pathway and subsequent IL8 production in colonic epithelial cells. Regulates antibacterial responses in lung by contributing to macrophage bacterial killing, controlling bacterial dissemination and augmenting host tolerance. Also regulates hyperoxia-induced injury, inflammation and epithelial apoptosis in lung.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei141 – 1411Chitooligosaccharide
Binding sitei263 – 2631Chitooligosaccharide
Binding sitei352 – 3521Chitooligosaccharide

GO - Molecular functioni

  1. carbohydrate binding Source: UniProtKB-KW
  2. chitin binding Source: UniProtKB
  3. extracellular matrix structural constituent Source: UniProtKB
  4. hydrolase activity, hydrolyzing O-glycosyl compounds Source: InterPro

GO - Biological processi

  1. activation of NF-kappaB-inducing kinase activity Source: UniProtKB
  2. apoptotic process Source: UniProtKB-KW
  3. carbohydrate metabolic process Source: InterPro
  4. cartilage development Source: UniProtKB
  5. cellular response to tumor necrosis factor Source: UniProtKB
  6. chitin catabolic process Source: InterPro
  7. inflammatory response Source: UniProtKB
  8. interleukin-8 secretion Source: UniProtKB
  9. lung development Source: UniProtKB
  10. positive regulation of angiogenesis Source: UniProtKB
  11. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  12. positive regulation of peptidyl-threonine phosphorylation Source: UniProtKB
  13. positive regulation of protein kinase B signaling Source: UniProtKB
  14. response to interleukin-1 Source: UniProtKB
  15. response to interleukin-6 Source: UniProtKB
  16. response to mechanical stimulus Source: UniProtKB
  17. response to tumor necrosis factor Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial

Keywords - Biological processi

Apoptosis, Inflammatory response

Keywords - Ligandi

Lectin

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.

Names & Taxonomyi

Protein namesi
Recommended name:
Chitinase-3-like protein 1
Alternative name(s):
39 kDa synovial protein
Cartilage glycoprotein 39
Short name:
CGP-39
Short name:
GP-39
Short name:
hCGP-39
YKL-40
Gene namesi
Name:CHI3L1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:1932. CHI3L1.

Subcellular locationi

Secretedextracellular space 1 Publication. Cytoplasm By similarity. Cytoplasmperinuclear region By similarity. Endoplasmic reticulum By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. endoplasmic reticulum Source: UniProtKB
  3. extracellular space Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProtKB
  5. proteinaceous extracellular matrix Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Secreted

Pathology & Biotechi

Involvement in diseasei

Asthma-related traits 7 (ASRT7) [MIM:611960]: Asthma-related traits include clinical symptoms of asthma, such as coughing, wheezing, dyspnea, bronchial hyperresponsiveness as assessed by methacholine challenge test, serum IgE levels, atopy and atopic dermatitis.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

Keywords - Diseasei

Asthma

Organism-specific databases

MIMi611960. phenotype.
PharmGKBiPA26463.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21212 PublicationsAdd
BLAST
Chaini22 – 383362Chitinase-3-like protein 1PRO_0000011965Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 51
Glycosylationi60 – 601N-linked (GlcNAc...)1 Publication
Disulfide bondi300 ↔ 364

Post-translational modificationi

Glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP36222.
PeptideAtlasiP36222.
PRIDEiP36222.

PTM databases

PhosphoSiteiP36222.

Expressioni

Tissue specificityi

Present in activated macrophages, articular chondrocytes, synovial cells as well as in liver. Very low or undetectable expression in non-inflammatory colon. Undetectable in muscle tissues, lung, pancreas, mononuclear cells, or fibroblasts.2 Publications

Inductioni

Up-regulated in colon under several inflammatory conditions. Down-regulated by hyperoxia in bronchial epithelial cells.2 Publications

Gene expression databases

BgeeiP36222.
CleanExiHS_CHI3L1.
ExpressionAtlasiP36222. baseline and differential.
GenevestigatoriP36222.

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

BioGridi107540. 3 interactions.
STRINGi9606.ENSP00000255409.

Structurei

Secondary structure

1
383
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 297Combined sources
Helixi30 – 345Combined 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
Turni99 – 1013Combined sources
Helixi103 – 1119Combined sources
Helixi113 – 13018Combined sources
Beta strandi133 – 1386Combined sources
Helixi144 – 1463Combined sources
Helixi147 – 16519Combined sources
Turni166 – 1683Combined sources
Beta strandi173 – 1797Combined sources
Helixi182 – 1887Combined sources
Helixi191 – 1977Combined sources
Beta strandi199 – 2046Combined sources
Helixi211 – 2133Combined sources
Helixi227 – 2293Combined sources
Beta strandi233 – 2364Combined sources
Helixi237 – 24711Combined sources
Helixi251 – 2533Combined sources
Beta strandi254 – 27017Combined sources
Beta strandi277 – 2815Combined sources
Turni286 – 2883Combined sources
Beta strandi293 – 2953Combined sources
Helixi296 – 3027Combined sources
Turni303 – 3053Combined sources
Beta strandi307 – 3104Combined sources
Turni312 – 3143Combined sources
Beta strandi317 – 3215Combined sources
Beta strandi324 – 3274Combined sources
Helixi331 – 34313Combined sources
Beta strandi347 – 3526Combined sources
Helixi354 – 3563Combined sources
Beta strandi359 – 3613Combined sources
Beta strandi363 – 3664Combined sources
Helixi371 – 38111Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HJVX-ray2.75A/B/C/D22-383[»]
1HJWX-ray2.30A/B22-383[»]
1HJXX-ray1.85A/B/C/D22-383[»]
1LA7model-A22-383[»]
1NWRX-ray2.70A/B/C/D22-383[»]
1NWSX-ray2.70A/B/C/D22-383[»]
1NWTX-ray2.50A/B/C/D22-383[»]
1NWUX-ray2.20A/B/C/D22-383[»]
ProteinModelPortaliP36222.
SMRiP36222. Positions 22-382.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36222.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni70 – 712Chitooligosaccharide binding
Regioni97 – 1004Chitooligosaccharide binding
Regioni204 – 2074Chitooligosaccharide binding
Regioni324 – 33815Important for AKT1 activation and IL8 productionBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 18 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3325.
GeneTreeiENSGT00550000074323.
HOGENOMiHOG000111109.
HOVERGENiHBG011684.
InParanoidiP36222.
KOiK17523.
OMAiSNDHIDT.
OrthoDBiEOG7ZGX3G.
PhylomeDBiP36222.
TreeFamiTF315610.

Family and domain databases

Gene3Di3.10.50.10. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR028538. CHI3L1.
IPR011583. Chitinase_II.
IPR029070. Chitinase_insertion.
IPR001223. Glyco_hydro18cat.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR11177:SF81. PTHR11177:SF81. 1 hit.
PfamiPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SMARTiSM00636. Glyco_18. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
SSF54556. SSF54556. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P36222-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGVKASQTGF VVLVLLQCCS AYKLVCYYTS WSQYREGDGS CFPDALDRFL
60 70 80 90 100
CTHIIYSFAN ISNDHIDTWE WNDVTLYGML NTLKNRNPNL KTLLSVGGWN
110 120 130 140 150
FGSQRFSKIA SNTQSRRTFI KSVPPFLRTH GFDGLDLAWL YPGRRDKQHF
160 170 180 190 200
TTLIKEMKAE FIKEAQPGKK QLLLSAALSA GKVTIDSSYD IAKISQHLDF
210 220 230 240 250
ISIMTYDFHG AWRGTTGHHS PLFRGQEDAS PDRFSNTDYA VGYMLRLGAP
260 270 280 290 300
ASKLVMGIPT FGRSFTLASS ETGVGAPISG PGIPGRFTKE AGTLAYYEIC
310 320 330 340 350
DFLRGATVHR ILGQQVPYAT KGNQWVGYDD QESVKSKVQY LKDRQLAGAM
360 370 380
VWALDLDDFQ GSFCGQDLRF PLTNAIKDAL AAT
Length:383
Mass (Da):42,625
Last modified:December 20, 2005 - v2
Checksum:i6C9EF133BDC7C2D1
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti145 – 1451R → G.2 Publications
Corresponds to variant rs880633 [ dbSNP | Ensembl ].
VAR_019838
Natural varianti311 – 3111I → T.2 Publications
Corresponds to variant rs1049407 [ dbSNP | Ensembl ].
VAR_019839

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80927 mRNA. Translation: AAA16074.1.
Y08374
, Y08375, Y08376, Y08377, Y08378 Genomic DNA. Translation: CAA69661.1.
BT007223 mRNA. Translation: AAP35887.1.
AK312911 mRNA. Translation: BAG35757.1.
CH471067 Genomic DNA. Translation: EAW91467.1.
BC008568 mRNA. Translation: AAH08568.1.
BC038354 mRNA. Translation: AAH38354.1.
BC039132 mRNA. Translation: AAH39132.1.
CCDSiCCDS1435.1.
PIRiA49562.
RefSeqiNP_001267.2. NM_001276.2.
UniGeneiHs.382202.
Hs.733359.

Genome annotation databases

EnsembliENST00000255409; ENSP00000255409; ENSG00000133048.
GeneIDi1116.
KEGGihsa:1116.
UCSCiuc001gzi.2. human.

Polymorphism databases

DMDMi84028186.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80927 mRNA. Translation: AAA16074.1 .
Y08374
, Y08375 , Y08376 , Y08377 , Y08378 Genomic DNA. Translation: CAA69661.1 .
BT007223 mRNA. Translation: AAP35887.1 .
AK312911 mRNA. Translation: BAG35757.1 .
CH471067 Genomic DNA. Translation: EAW91467.1 .
BC008568 mRNA. Translation: AAH08568.1 .
BC038354 mRNA. Translation: AAH38354.1 .
BC039132 mRNA. Translation: AAH39132.1 .
CCDSi CCDS1435.1.
PIRi A49562.
RefSeqi NP_001267.2. NM_001276.2.
UniGenei Hs.382202.
Hs.733359.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HJV X-ray 2.75 A/B/C/D 22-383 [» ]
1HJW X-ray 2.30 A/B 22-383 [» ]
1HJX X-ray 1.85 A/B/C/D 22-383 [» ]
1LA7 model - A 22-383 [» ]
1NWR X-ray 2.70 A/B/C/D 22-383 [» ]
1NWS X-ray 2.70 A/B/C/D 22-383 [» ]
1NWT X-ray 2.50 A/B/C/D 22-383 [» ]
1NWU X-ray 2.20 A/B/C/D 22-383 [» ]
ProteinModelPortali P36222.
SMRi P36222. Positions 22-382.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107540. 3 interactions.
STRINGi 9606.ENSP00000255409.

Protein family/group databases

CAZyi GH18. Glycoside Hydrolase Family 18.

PTM databases

PhosphoSitei P36222.

Polymorphism databases

DMDMi 84028186.

Proteomic databases

PaxDbi P36222.
PeptideAtlasi P36222.
PRIDEi P36222.

Protocols and materials databases

DNASUi 1116.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000255409 ; ENSP00000255409 ; ENSG00000133048 .
GeneIDi 1116.
KEGGi hsa:1116.
UCSCi uc001gzi.2. human.

Organism-specific databases

CTDi 1116.
GeneCardsi GC01M203148.
HGNCi HGNC:1932. CHI3L1.
MIMi 601525. gene.
611960. phenotype.
neXtProti NX_P36222.
PharmGKBi PA26463.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3325.
GeneTreei ENSGT00550000074323.
HOGENOMi HOG000111109.
HOVERGENi HBG011684.
InParanoidi P36222.
KOi K17523.
OMAi SNDHIDT.
OrthoDBi EOG7ZGX3G.
PhylomeDBi P36222.
TreeFami TF315610.

Miscellaneous databases

ChiTaRSi CHI3L1. human.
EvolutionaryTracei P36222.
GeneWikii CHI3L1.
GenomeRNAii 1116.
NextBioi 4626.
PROi P36222.
SOURCEi Search...

Gene expression databases

Bgeei P36222.
CleanExi HS_CHI3L1.
ExpressionAtlasi P36222. baseline and differential.
Genevestigatori P36222.

Family and domain databases

Gene3Di 3.10.50.10. 1 hit.
3.20.20.80. 2 hits.
InterProi IPR028538. CHI3L1.
IPR011583. Chitinase_II.
IPR029070. Chitinase_insertion.
IPR001223. Glyco_hydro18cat.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
PANTHERi PTHR11177:SF81. PTHR11177:SF81. 1 hit.
Pfami PF00704. Glyco_hydro_18. 1 hit.
[Graphical view ]
SMARTi SM00636. Glyco_18. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 2 hits.
SSF54556. SSF54556. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human cartilage gp-39, a major secretory product of articular chondrocytes and synovial cells, is a mammalian member of a chitinase protein family."
    Hakala B.E., White C., Recklies A.D.
    J. Biol. Chem. 268:25803-25810(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT THR-311.
    Tissue: Cartilage.
  2. "Molecular characterization of the gene for human cartilage gp-39 (CHI3L1), a member of the chitinase protein family and marker for late stages of macrophage differentiation."
    Rehli M., Krause S.W., Andressen R.
    Genomics 43:221-225(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-311.
    Tissue: Blood.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLY-145.
  4. "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].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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], VARIANT GLY-145.
    Tissue: Brain.
  7. "Human synovial cells secrete a 39 kDa protein similar to a bovine mammary protein expressed during the non-lactating period."
    Nyirkos P., Golds E.E.
    Biochem. J. 269:265-268(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-45.
  8. "Chitotriosidase, a chitinase, and the 39-kDa human cartilage glycoprotein, a chitin-binding lectin, are homologues of family 18 glycosyl hydrolases secreted by human macrophages."
    Renkema G.H., Boot R.G., Au F.L., Donker-Koopman W.E., Strijland A., Muijsers A.O., Hrebicek M., Aerts J.M.F.G.
    Eur. J. Biochem. 251:504-509(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  9. "Chitinase 3-like-1 exacerbates intestinal inflammation by enhancing bacterial adhesion and invasion in colonic epithelial cells."
    Mizoguchi E.
    Gastroenterology 130:398-411(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.
  10. "Role of breast regression protein 39 (BRP-39)/chitinase 3-like-1 in Th2 and IL-13-induced tissue responses and apoptosis."
    Lee C.G., Hartl D., Lee G.R., Koller B., Matsuura H., Da Silva C.A., Sohn M.H., Cohn L., Homer R.J., Kozhich A.A., Humbles A., Kearley J., Coyle A., Chupp G., Reed J., Flavell R.A., Elias J.A.
    J. Exp. Med. 206:1149-1166(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "The chitinase-like proteins breast regression protein-39 and YKL-40 regulate hyperoxia-induced acute lung injury."
    Sohn M.H., Kang M.J., Matsuura H., Bhandari V., Chen N.Y., Lee C.G., Elias J.A.
    Am. J. Respir. Crit. Care Med. 182:918-928(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  12. "Structure and ligand-induced conformational change of the 39-kDa glycoprotein from human articular chondrocytes."
    Houston D.R., Recklies A.D., Krupa J.C., van Aalten D.M.F.
    J. Biol. Chem. 278:30206-30212(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 22-383 IN COMPLEX WITH CHITIN OLIGOMERS, DISULFIDE BONDS, GLYCOSYLATION AT ASN-60.
  13. "Crystal structure and carbohydrate-binding properties of the human cartilage glycoprotein-39."
    Fusetti F., Pijning T., Kalk K.H., Bos E., Dijkstra B.W.
    J. Biol. Chem. 278:37753-37760(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 22-383 IN COMPLEX WITH CHITIN OLIGOMERS, DISULFIDE BONDS.
  14. Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO ASTHMA-RELATED TRAITS.

Entry informationi

Entry nameiCH3L1_HUMAN
AccessioniPrimary (citable) accession number: P36222
Secondary accession number(s): B2R7B0
, P30923, Q8IVA4, Q96HI7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: December 20, 2005
Last modified: November 26, 2014
This is version 146 of the entry and version 2 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

Caution

Although it belongs to the glycosyl hydrolase 18 family, Leu-140 is present instead of the conserved Glu which is an active site residue. Therefore this protein lacks chitinase activity.Curated

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