Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Exoglucanase 2  

UniProtKB / Swiss-Prot ID :  GUX2_HYPJE

Gene Name (Synonyms) : 
cbh2  

Species :  Hypocrea jecorina (Trichoderma reesei). 

Subcellular Localization :  Secreted. 

Protein Function :  The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4- glucosidases which hydrolyze the cellobiose and other short cello- oligosaccharides to glucose. 

Protein Sequence MIVGILTTLATLATLAASVPLEERQACSSVWGQCGGQNWSGPTCCASGSTCVYSNDYYSQCLPGAASSSS...
Predicted Secondary Structure  -
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
111O-linked (Man)SGTATYSGN
20.32OGlycBase
Link
111O-linked (Man...).SGTATYSGN
20.32UniProtKB
Link
121O-linked (Man)FVGVTPWAN
13.74OGlycBase
Link
121O-linked (Man...).FVGVTPWAN
13.74UniProtKB
Link
130O-linked (Man)AYYASEVSS
23.55OGlycBase
Link
130O-linked (Man...).AYYASEVSS
23.55UniProtKB
Link
133O-linked (Man)ASEVSSLAI
18.64OGlycBase
Link
133O-linked (Man...).ASEVSSLAI
18.64UniProtKB
Link
134O-linked (Man)SEVSSLAIP
27.31OGlycBase
Link
134O-linked (Man...).SEVSSLAIP
27.31UniProtKB
Link
139O-linked (Man)LAIPSLTGA
32.24OGlycBase
Link
139O-linked (Man...).LAIPSLTGA
32.24UniProtKB
Link
146O-linked (Man...).GAMATAAAA
12.07UniProtKB
Link
313N-linked (Glc...)NVYKNASSP
27.63OGlycBase
Link
313N-linked (GlcNAc...).NVYKNASSP
27.63UniProtKB
Link
334N-linked (Glc...)YNGWNITSP
29.11OGlycBase
Link
334N-linked (GlcNAc...).YNGWNITSP
29.11UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"The active site of Trichoderma reesei cellobiohydrolase II: the roleof tyrosine 169.";
Koivula A., Reinikainen T., Ruohonen L., Valkeajaervi A.,Claeyssens M., Teleman O., Kleywegt G.J., Szardenings M., Rouvinen J.,Jones T.A., Teeri T.T.;
Protein Eng. 9:691-699(1996).
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), DISULFIDE BONDS, ANDGLYCOSYLATION AT THR-111; THR-121; SER-130; SER-133; SER-134; SER-139;THR-146; ASN-313 AND ASN-334.
O-linked Glycosylation
ReferencePubMed
"The active site of Trichoderma reesei cellobiohydrolase II: the roleof tyrosine 169.";
Koivula A., Reinikainen T., Ruohonen L., Valkeajaervi A.,Claeyssens M., Teleman O., Kleywegt G.J., Szardenings M., Rouvinen J.,Jones T.A., Teeri T.T.;
Protein Eng. 9:691-699(1996).
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), DISULFIDE BONDS, ANDGLYCOSYLATION AT THR-111; THR-121; SER-130; SER-133; SER-134; SER-139;THR-146; ASN-313 AND ASN-334.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures