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Protein

Chitinase domain-containing protein 1

Gene

CHID1

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

Functioni

Saccharide- and LPS-binding protein with possible roles in pathogen sensing and endotoxin neutralization. Ligand-binding specificity relates to the length of the oligosaccharides, with preference for chitotetraose (in vitro).1 Publication

GO - Molecular functioni

  • chitinase activity Source: GO_Central
  • chitin binding Source: GO_Central
  • oligosaccharide binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Immunity, Innate immunity

Enzyme and pathway databases

ReactomeiR-HSA-114608. Platelet degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Chitinase domain-containing protein 1
Alternative name(s):
Stabilin-1-interacting chitinase-like protein
Short name:
SI-CLP
Gene namesi
Name:CHID1
ORF Names:GL008, PSEC0104, SB139
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:28474. CHID1.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • late endosome Source: UniProtKB
  • lysosome Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleus Source: UniProtKB
  • trans-Golgi network Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi84Y → S: Significantly decreased carbohydrate binding. 1 Publication1
Mutagenesisi88W → A: Significantly decreased carbohydrate binding. 1 Publication1
Mutagenesisi110W → A: Significantly decreased carbohydrate binding. 1 Publication1
Mutagenesisi261Y → S: Significantly decreased carbohydrate binding. 1 Publication1
Mutagenesisi277W → A: No noticeable effect. 1 Publication1
Mutagenesisi302Y → S: Significantly decreased carbohydrate binding. 1 Publication1

Organism-specific databases

DisGeNETi66005.
OpenTargetsiENSG00000177830.
PharmGKBiPA142672118.

Polymorphism and mutation databases

BioMutaiCHID1.
DMDMi74733460.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000028060820 – 393Chitinase domain-containing protein 1Add BLAST374

Proteomic databases

EPDiQ9BWS9.
MaxQBiQ9BWS9.
PeptideAtlasiQ9BWS9.
PRIDEiQ9BWS9.
TopDownProteomicsiQ9BWS9-2. [Q9BWS9-2]

PTM databases

iPTMnetiQ9BWS9.
PhosphoSitePlusiQ9BWS9.

Expressioni

Tissue specificityi

Expressed in cells of monocytic, T, B and epithelial origin.2 Publications

Inductioni

Up-regulated by IL4/interleukin-4 and dexamethasone in the macrophages. Up-regulated by glucocorticoid.2 Publications

Gene expression databases

BgeeiENSG00000177830.
CleanExiHS_CHID1.
ExpressionAtlasiQ9BWS9. baseline and differential.
GenevisibleiQ9BWS9. HS.

Organism-specific databases

HPAiHPA039374.

Interactioni

Subunit structurei

Interacts with STAB1.1 Publication

Protein-protein interaction databases

BioGridi122451. 6 interactors.
IntActiQ9BWS9. 1 interactor.

Structurei

Secondary structure

1393
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi45 – 47Combined sources3
Helixi57 – 63Combined sources7
Turni70 – 73Combined sources4
Beta strandi81 – 86Combined sources6
Helixi91 – 99Combined sources9
Helixi100 – 102Combined sources3
Beta strandi104 – 108Combined sources5
Beta strandi111 – 117Combined sources7
Beta strandi120 – 124Combined sources5
Helixi126 – 128Combined sources3
Helixi131 – 140Combined sources10
Beta strandi141 – 143Combined sources3
Beta strandi149 – 152Combined sources4
Helixi157 – 164Combined sources8
Helixi167 – 184Combined sources18
Beta strandi188 – 192Combined sources5
Helixi194 – 196Combined sources3
Helixi202 – 218Combined sources17
Beta strandi222 – 227Combined sources6
Turni233 – 235Combined sources3
Beta strandi236 – 238Combined sources3
Helixi243 – 249Combined sources7
Turni250 – 252Combined sources3
Beta strandi254 – 258Combined sources5
Helixi275 – 285Combined sources11
Helixi292 – 294Combined sources3
Beta strandi295 – 307Combined sources13
Turni308 – 311Combined sources4
Beta strandi312 – 316Combined sources5
Helixi318 – 328Combined sources11
Beta strandi333 – 335Combined sources3
Turni336 – 339Combined sources4
Beta strandi340 – 347Combined sources8
Turni348 – 350Combined sources3
Beta strandi351 – 356Combined sources6
Helixi360 – 373Combined sources14
Beta strandi376 – 380Combined sources5
Helixi387 – 392Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BXWX-ray2.70A/B1-393[»]
ProteinModelPortaliQ9BWS9.
SMRiQ9BWS9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BWS9.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 18 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

GeneTreeiENSGT00390000012069.
HOVERGENiHBG055278.
InParanoidiQ9BWS9.
KOiK17525.
OMAiYSINERI.
OrthoDBiEOG091G0BSF.
PhylomeDBiQ9BWS9.
TreeFamiTF319271.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR011583. Chitinase_II.
IPR001223. Glyco_hydro18_cat.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SMARTiSM00636. Glyco_18. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.

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: Q9BWS9-1) [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
MRTLFNLLWL ALACSPVHTT LSKSDAKKAA SKTLLEKSQF SDKPVQDRGL
60 70 80 90 100
VVTDLKAESV VLEHRSYCSA KARDRHFAGD VLGYVTPWNS HGYDVTKVFG
110 120 130 140 150
SKFTQISPVW LQLKRRGREM FEVTGLHDVD QGWMRAVRKH AKGLHIVPRL
160 170 180 190 200
LFEDWTYDDF RNVLDSEDEI EELSKTVVQV AKNQHFDGFV VEVWNQLLSQ
210 220 230 240 250
KRVGLIHMLT HLAEALHQAR LLALLVIPPA ITPGTDQLGM FTHKEFEQLA
260 270 280 290 300
PVLDGFSLMT YDYSTAHQPG PNAPLSWVRA CVQVLDPKSK WRSKILLGLN
310 320 330 340 350
FYGMDYATSK DAREPVVGAR YIQTLKDHRP RMVWDSQASE HFFEYKKSRS
360 370 380 390
GRHVVFYPTL KSLQVRLELA RELGVGVSIW ELGQGLDYFY DLL
Length:393
Mass (Da):44,941
Last modified:June 1, 2001 - v1
Checksum:iFFD5E67C20AF69B4
GO
Isoform 2 (identifier: Q9BWS9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     37-37: K → KVKFCSCCPGWSAMARSWLTATSATQ

Show »
Length:418
Mass (Da):47,616
Checksum:iD8591C41BF31FB5D
GO
Isoform 3 (identifier: Q9BWS9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     204-234: Missing.

Show »
Length:362
Mass (Da):41,678
Checksum:i5C0F15F14D50CFF5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti335D → G in BAB55316 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_031173331R → Q.1 PublicationCorresponds to variant rs1127800dbSNPEnsembl.1
Natural variantiVAR_031174338A → V.3 PublicationsCorresponds to variant rs6682dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_02382537K → KVKFCSCCPGWSAMARSWLT ATSATQ in isoform 2. 1 Publication1
Alternative sequenceiVSP_023826204 – 234Missing in isoform 3. 1 PublicationAdd BLAST31

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BN000479 mRNA. Translation: CAF32458.1.
AF212229 mRNA. Translation: AAK14915.1.
AY037151 mRNA. Translation: AAK67632.1.
AK027711 mRNA. Translation: BAB55316.1.
AK075413 mRNA. Translation: BAC11603.1.
AK124697 mRNA. Translation: BAG54072.1.
BC000001 mRNA. Translation: AAH00001.1.
BC013642 mRNA. Translation: AAH13642.1.
BC095409 mRNA. Translation: AAH95409.1.
CCDSiCCDS44510.1. [Q9BWS9-3]
CCDS44511.1. [Q9BWS9-2]
CCDS7722.1. [Q9BWS9-1]
RefSeqiNP_001136146.1. NM_001142674.1. [Q9BWS9-1]
NP_001136147.1. NM_001142675.1. [Q9BWS9-1]
NP_001136148.1. NM_001142676.1. [Q9BWS9-2]
NP_001136149.1. NM_001142677.1. [Q9BWS9-3]
NP_076436.3. NM_023947.3. [Q9BWS9-1]
XP_005253130.1. XM_005253073.4. [Q9BWS9-3]
XP_006718345.1. XM_006718282.2. [Q9BWS9-1]
XP_016873655.1. XM_017018166.1. [Q9BWS9-1]
UniGeneiHs.144468.

Genome annotation databases

EnsembliENST00000323578; ENSP00000325055; ENSG00000177830. [Q9BWS9-1]
ENST00000429789; ENSP00000416034; ENSG00000177830. [Q9BWS9-3]
ENST00000436108; ENSP00000388156; ENSG00000177830. [Q9BWS9-1]
ENST00000449825; ENSP00000391255; ENSG00000177830. [Q9BWS9-1]
ENST00000454838; ENSP00000398722; ENSG00000177830. [Q9BWS9-2]
ENST00000528581; ENSP00000435503; ENSG00000177830. [Q9BWS9-2]
GeneIDi66005.
KEGGihsa:66005.
UCSCiuc001lsm.4. human. [Q9BWS9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BN000479 mRNA. Translation: CAF32458.1.
AF212229 mRNA. Translation: AAK14915.1.
AY037151 mRNA. Translation: AAK67632.1.
AK027711 mRNA. Translation: BAB55316.1.
AK075413 mRNA. Translation: BAC11603.1.
AK124697 mRNA. Translation: BAG54072.1.
BC000001 mRNA. Translation: AAH00001.1.
BC013642 mRNA. Translation: AAH13642.1.
BC095409 mRNA. Translation: AAH95409.1.
CCDSiCCDS44510.1. [Q9BWS9-3]
CCDS44511.1. [Q9BWS9-2]
CCDS7722.1. [Q9BWS9-1]
RefSeqiNP_001136146.1. NM_001142674.1. [Q9BWS9-1]
NP_001136147.1. NM_001142675.1. [Q9BWS9-1]
NP_001136148.1. NM_001142676.1. [Q9BWS9-2]
NP_001136149.1. NM_001142677.1. [Q9BWS9-3]
NP_076436.3. NM_023947.3. [Q9BWS9-1]
XP_005253130.1. XM_005253073.4. [Q9BWS9-3]
XP_006718345.1. XM_006718282.2. [Q9BWS9-1]
XP_016873655.1. XM_017018166.1. [Q9BWS9-1]
UniGeneiHs.144468.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BXWX-ray2.70A/B1-393[»]
ProteinModelPortaliQ9BWS9.
SMRiQ9BWS9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122451. 6 interactors.
IntActiQ9BWS9. 1 interactor.

PTM databases

iPTMnetiQ9BWS9.
PhosphoSitePlusiQ9BWS9.

Polymorphism and mutation databases

BioMutaiCHID1.
DMDMi74733460.

Proteomic databases

EPDiQ9BWS9.
MaxQBiQ9BWS9.
PeptideAtlasiQ9BWS9.
PRIDEiQ9BWS9.
TopDownProteomicsiQ9BWS9-2. [Q9BWS9-2]

Protocols and materials databases

DNASUi66005.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000323578; ENSP00000325055; ENSG00000177830. [Q9BWS9-1]
ENST00000429789; ENSP00000416034; ENSG00000177830. [Q9BWS9-3]
ENST00000436108; ENSP00000388156; ENSG00000177830. [Q9BWS9-1]
ENST00000449825; ENSP00000391255; ENSG00000177830. [Q9BWS9-1]
ENST00000454838; ENSP00000398722; ENSG00000177830. [Q9BWS9-2]
ENST00000528581; ENSP00000435503; ENSG00000177830. [Q9BWS9-2]
GeneIDi66005.
KEGGihsa:66005.
UCSCiuc001lsm.4. human. [Q9BWS9-1]

Organism-specific databases

CTDi66005.
DisGeNETi66005.
GeneCardsiCHID1.
HGNCiHGNC:28474. CHID1.
HPAiHPA039374.
MIMi615692. gene.
neXtProtiNX_Q9BWS9.
OpenTargetsiENSG00000177830.
PharmGKBiPA142672118.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00390000012069.
HOVERGENiHBG055278.
InParanoidiQ9BWS9.
KOiK17525.
OMAiYSINERI.
OrthoDBiEOG091G0BSF.
PhylomeDBiQ9BWS9.
TreeFamiTF319271.

Enzyme and pathway databases

ReactomeiR-HSA-114608. Platelet degranulation.

Miscellaneous databases

ChiTaRSiCHID1. human.
EvolutionaryTraceiQ9BWS9.
GenomeRNAii66005.
PROiQ9BWS9.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000177830.
CleanExiHS_CHID1.
ExpressionAtlasiQ9BWS9. baseline and differential.
GenevisibleiQ9BWS9. HS.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR011583. Chitinase_II.
IPR001223. Glyco_hydro18_cat.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SMARTiSM00636. Glyco_18. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiCHID1_HUMAN
AccessioniPrimary (citable) accession number: Q9BWS9
Secondary accession number(s): B3KWB0
, Q8NBM9, Q96CZ3, Q96S93, Q96SK0, Q9BY52
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: June 1, 2001
Last modified: November 2, 2016
This is version 121 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 11
    Human chromosome 11: 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.