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Protein

Chitinase-3-like protein 2

Gene

CHI3L2

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

Functioni

Lectin that binds chitooligosaccharides and other glycans with high affinity, but not heparin. Has no chitinase activity.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei104Chitooligosaccharide1 Publication1
Binding sitei146Chitooligosaccharide1 Publication1
Binding sitei213Chitooligosaccharide1 Publication1
Binding sitei360Chitooligosaccharide1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Chitin-binding, Lectin

Enzyme and pathway databases

BioCyciZFISH:ENSG00000064886-MONOMER.

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.

Names & Taxonomyi

Protein namesi
Recommended name:
Chitinase-3-like protein 2
Alternative name(s):
Chondrocyte protein 39
YKL-39
Gene namesi
Name:CHI3L2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:1933. CHI3L2.

Subcellular locationi

GO - Cellular componenti

  • extracellular space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi143S → D: Confers chitinase activity; when associated with E-145. 1 Publication1
Mutagenesisi145I → E: Confers chitinase activity; when associated with D-143. 1 Publication1

Organism-specific databases

DisGeNETi1117.
OpenTargetsiENSG00000064886.
PharmGKBiPA26464.

Polymorphism and mutation databases

BioMutaiCHI3L2.
DMDMi13124005.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Add BLAST26
ChainiPRO_000001196927 – 390Chitinase-3-like protein 2Add BLAST364

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi31 ↔ 56By similarity
Glycosylationi35N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ15782.
PaxDbiQ15782.
PeptideAtlasiQ15782.
PRIDEiQ15782.

PTM databases

iPTMnetiQ15782.
PhosphoSitePlusiQ15782.

Expressioni

Tissue specificityi

Highest expression in chondrocytes, followed by synoviocytes, lung and heart. Not detected in spleen, pancreas, and liver. May also be expressed in developing brain and placenta.1 Publication

Gene expression databases

BgeeiENSG00000064886.
CleanExiHS_CHI3L2.
ExpressionAtlasiQ15782. baseline and differential.
GenevisibleiQ15782. HS.

Organism-specific databases

HPAiHPA005443.

Interactioni

Protein-protein interaction databases

BioGridi107541. 3 interactors.
IntActiQ15782. 3 interactors.
STRINGi9606.ENSP00000358763.

Structurei

Secondary structure

1390
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi28 – 36Combined sources9
Helixi37 – 39Combined sources3
Helixi48 – 50Combined sources3
Turni53 – 55Combined sources3
Beta strandi57 – 67Combined sources11
Beta strandi70 – 72Combined sources3
Helixi78 – 91Combined sources14
Beta strandi96 – 103Combined sources8
Turni104 – 108Combined sources5
Helixi109 – 111Combined sources3
Helixi114 – 116Combined sources3
Helixi118 – 134Combined sources17
Beta strandi139 – 145Combined sources7
Helixi148 – 171Combined sources24
Beta strandi179 – 185Combined sources7
Helixi188 – 194Combined sources7
Helixi197 – 203Combined sources7
Beta strandi205 – 210Combined sources6
Helixi238 – 242Combined sources5
Helixi245 – 254Combined sources10
Helixi259 – 261Combined sources3
Beta strandi262 – 278Combined sources17
Beta strandi285 – 289Combined sources5
Turni294 – 296Combined sources3
Beta strandi301 – 303Combined sources3
Helixi304 – 310Combined sources7
Turni311 – 313Combined sources3
Beta strandi315 – 319Combined sources5
Turni320 – 323Combined sources4
Beta strandi324 – 329Combined sources6
Beta strandi332 – 335Combined sources4
Helixi339 – 351Combined sources13
Beta strandi355 – 360Combined sources6
Helixi362 – 364Combined sources3
Turni370 – 372Combined sources3
Helixi378 – 388Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4AY1X-ray1.95A/B/C/D/E/F/G/H/I/J/K/L26-390[»]
4P8UX-ray2.40A27-390[»]
4P8VX-ray1.64A27-390[»]
4P8WX-ray1.87A27-390[»]
4P8XX-ray2.48A27-390[»]
ProteinModelPortaliQ15782.
SMRiQ15782.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 18 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2806. Eukaryota.
COG3325. LUCA.
GeneTreeiENSGT00550000074323.
HOGENOMiHOG000111109.
HOVERGENiHBG011684.
InParanoidiQ15782.
KOiK17523.
OMAiESMETKV.
OrthoDBiEOG091G014W.
PhylomeDBiQ15782.
TreeFamiTF315610.

Family and domain databases

Gene3Di3.10.50.10. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR028541. CHI3L2.
IPR011583. Chitinase_II.
IPR029070. Chitinase_insertion.
IPR001223. Glyco_hydro18_cat.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR11177:SF82. PTHR11177:SF82. 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.

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: Q15782-4) [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
MGATTMDQKS LWAGVVVLLL LQGGSAYKLV CYFTNWSQDR QEPGKFTPEN
60 70 80 90 100
IDPFLCSHLI YSFASIENNK VIIKDKSEVM LYQTINSLKT KNPKLKILLS
110 120 130 140 150
IGGYLFGSKG FHPMVDSSTS RLEFINSIIL FLRNHNFDGL DVSWIYPDQK
160 170 180 190 200
ENTHFTVLIH ELAEAFQKDF TKSTKERLLL TAGVSAGRQM IDNSYQVEKL
210 220 230 240 250
AKDLDFINLL SFDFHGSWEK PLITGHNSPL SKGWQDRGPS SYYNVEYAVG
260 270 280 290 300
YWIHKGMPSE KVVMGIPTYG HSFTLASAET TVGAPASGPG AAGPITESSG
310 320 330 340 350
FLAYYEICQF LKGAKITRLQ DQQVPYAVKG NQWVGYDDVK SMETKVQFLK
360 370 380 390
NLNLGGAMIW SIDMDDFTGK SCNQGPYPLV QAVKRSLGSL
Length:390
Mass (Da):43,501
Last modified:November 1, 1996 - v1
Checksum:i97B86A2F3AA35677
GO
Isoform 2 (identifier: Q15782-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-79: Missing.

Show »
Length:311
Mass (Da):34,633
Checksum:i07D3831B311EB6AA
GO
Isoform 3 (identifier: Q15782-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     14-23: Missing.

Show »
Length:380
Mass (Da):42,508
Checksum:iF3BDD03CABDAF681
GO

Sequence cautioni

The sequence AAB04534 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAC50597 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_049198182A → V.2 PublicationsCorresponds to variant rs11556868dbSNPEnsembl.1
Natural variantiVAR_033731184V → I.Corresponds to variant rs34049547dbSNPEnsembl.1
Natural variantiVAR_061189318R → W.Corresponds to variant rs13721dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0442621 – 79Missing in isoform 2. 2 PublicationsAdd BLAST79
Alternative sequenceiVSP_04724514 – 23Missing in isoform 3. Curated10

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58515 mRNA. Translation: AAB04534.1. Different initiation.
U58514 mRNA. Translation: AAB04533.1.
U49835 mRNA. Translation: AAC50597.1. Different initiation.
BT006767 mRNA. Translation: AAP35413.1.
AK298466 mRNA. Translation: BAG60679.1.
AL355816 Genomic DNA. No translation available.
AL513202 Genomic DNA. No translation available.
CH471122 Genomic DNA. Translation: EAW56481.1.
BC011460 mRNA. Translation: AAH11460.1.
CCDSiCCDS30802.1. [Q15782-4]
CCDS30803.1. [Q15782-6]
CCDS41367.1. [Q15782-5]
RefSeqiNP_001020368.1. NM_001025197.1. [Q15782-6]
NP_001020370.1. NM_001025199.1. [Q15782-5]
NP_003991.2. NM_004000.2. [Q15782-4]
UniGeneiHs.514840.

Genome annotation databases

EnsembliENST00000369744; ENSP00000358759; ENSG00000064886. [Q15782-6]
ENST00000369748; ENSP00000358763; ENSG00000064886. [Q15782-4]
ENST00000445067; ENSP00000437082; ENSG00000064886. [Q15782-4]
ENST00000466741; ENSP00000437086; ENSG00000064886. [Q15782-5]
ENST00000524472; ENSP00000432049; ENSG00000064886. [Q15782-5]
GeneIDi1117.
KEGGihsa:1117.
UCSCiuc001eam.4. human. [Q15782-4]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58515 mRNA. Translation: AAB04534.1. Different initiation.
U58514 mRNA. Translation: AAB04533.1.
U49835 mRNA. Translation: AAC50597.1. Different initiation.
BT006767 mRNA. Translation: AAP35413.1.
AK298466 mRNA. Translation: BAG60679.1.
AL355816 Genomic DNA. No translation available.
AL513202 Genomic DNA. No translation available.
CH471122 Genomic DNA. Translation: EAW56481.1.
BC011460 mRNA. Translation: AAH11460.1.
CCDSiCCDS30802.1. [Q15782-4]
CCDS30803.1. [Q15782-6]
CCDS41367.1. [Q15782-5]
RefSeqiNP_001020368.1. NM_001025197.1. [Q15782-6]
NP_001020370.1. NM_001025199.1. [Q15782-5]
NP_003991.2. NM_004000.2. [Q15782-4]
UniGeneiHs.514840.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4AY1X-ray1.95A/B/C/D/E/F/G/H/I/J/K/L26-390[»]
4P8UX-ray2.40A27-390[»]
4P8VX-ray1.64A27-390[»]
4P8WX-ray1.87A27-390[»]
4P8XX-ray2.48A27-390[»]
ProteinModelPortaliQ15782.
SMRiQ15782.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107541. 3 interactors.
IntActiQ15782. 3 interactors.
STRINGi9606.ENSP00000358763.

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.

PTM databases

iPTMnetiQ15782.
PhosphoSitePlusiQ15782.

Polymorphism and mutation databases

BioMutaiCHI3L2.
DMDMi13124005.

Proteomic databases

MaxQBiQ15782.
PaxDbiQ15782.
PeptideAtlasiQ15782.
PRIDEiQ15782.

Protocols and materials databases

DNASUi1117.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369744; ENSP00000358759; ENSG00000064886. [Q15782-6]
ENST00000369748; ENSP00000358763; ENSG00000064886. [Q15782-4]
ENST00000445067; ENSP00000437082; ENSG00000064886. [Q15782-4]
ENST00000466741; ENSP00000437086; ENSG00000064886. [Q15782-5]
ENST00000524472; ENSP00000432049; ENSG00000064886. [Q15782-5]
GeneIDi1117.
KEGGihsa:1117.
UCSCiuc001eam.4. human. [Q15782-4]

Organism-specific databases

CTDi1117.
DisGeNETi1117.
GeneCardsiCHI3L2.
HGNCiHGNC:1933. CHI3L2.
HPAiHPA005443.
MIMi601526. gene.
neXtProtiNX_Q15782.
OpenTargetsiENSG00000064886.
PharmGKBiPA26464.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2806. Eukaryota.
COG3325. LUCA.
GeneTreeiENSGT00550000074323.
HOGENOMiHOG000111109.
HOVERGENiHBG011684.
InParanoidiQ15782.
KOiK17523.
OMAiESMETKV.
OrthoDBiEOG091G014W.
PhylomeDBiQ15782.
TreeFamiTF315610.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000064886-MONOMER.

Miscellaneous databases

GenomeRNAii1117.
PROiQ15782.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000064886.
CleanExiHS_CHI3L2.
ExpressionAtlasiQ15782. baseline and differential.
GenevisibleiQ15782. HS.

Family and domain databases

Gene3Di3.10.50.10. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR028541. CHI3L2.
IPR011583. Chitinase_II.
IPR029070. Chitinase_insertion.
IPR001223. Glyco_hydro18_cat.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR11177:SF82. PTHR11177:SF82. 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.
ProtoNetiSearch...

Entry informationi

Entry nameiCH3L2_HUMAN
AccessioniPrimary (citable) accession number: Q15782
Secondary accession number(s): A6NNY3
, B4DPR7, Q15749, Q15783, Q5VUV7, Q96F97
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 150 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

Caution

Lacks the conserved sequence motif DxxDxDxE that is essential for the catalytic activity of chitinases of the glycosyl hydrolase 18 family, and therefore has no 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

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 one 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.