GAS2_SCHPO - dbPTM
GAS2_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GAS2_SCHPO
UniProt AC Q9USU5
Protein Name 1,3-beta-glucanosyltransferase gas2
Gene Name gas2
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 459
Subcellular Localization Endoplasmic reticulum lumen . Secreted .
Protein Description Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall..
Protein Sequence MVSFTKFTLQLLSASAAFAYFEPLTIKGRKFFKNDTQFYIKGVAYQPAVDAEETSTIVDPLAEVNYKNCTEDAKIISNLGANVIRVYAVNASLNHDKCMEAFRNESIYVFLDLANPKTGIDRDTPTWNTDQFSSYQSVIDTFQKYNNTGAFFAGNEVVNNASNAPAVAYVRAAVRDSKNYIKSKKYRTIPVGYAGADIPVVRTELAAYLSCNATKLNNDTNSETDFLGYNMYEWCGHSDFYTSGYAARTQELENFTIPIFLSEFGCNKVTPRVFTEVQAIYSDNMTNVWSGGIVYEYSQEVNDYGLVNVSSTGERVLTTDYNNLKKQWASISPNITYKHSYNPNGTIPECPSRNKTSWAVSANAFPVTPNTTICSNAVKNLKCSANGTPSGSKISQVLSELCYYDNKACSSISSDPYEGTYGNYTGCTGVQQLSIALNAYTQDHGADSCSWGGVGELKA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
34N-linked_GlycosylationKGRKFFKNDTQFYIK
CCEECCCCCCEEEEE
53.02-
68N-linked_GlycosylationLAEVNYKNCTEDAKI
CHHCCCCCCCHHHHH
27.81-
90N-linked_GlycosylationVIRVYAVNASLNHDK
EEEEEEEECCCCCHH
18.68-
104N-linked_GlycosylationKCMEAFRNESIYVFL
HHHHHHCCCCEEEEE
40.70-
146N-linked_GlycosylationIDTFQKYNNTGAFFA
HHHHHHHCCCCCEEC
46.77-
160N-linked_GlycosylationAGNEVVNNASNAPAV
CCCHHCCCCCCCCHH
32.89-
212N-linked_GlycosylationLAAYLSCNATKLNND
HHHHHHCCCEECCCC
47.47-
218N-linked_GlycosylationCNATKLNNDTNSETD
CCCEECCCCCCCCCC
68.84-
254N-linked_GlycosylationARTQELENFTIPIFL
HCHHHHHCCCCEEEH
52.57-
284N-linked_GlycosylationVQAIYSDNMTNVWSG
EEEEECCCCCCCCCC
32.98-
308N-linked_GlycosylationVNDYGLVNVSSTGER
CCCCCCEECCCCCCE
32.75-
334N-linked_GlycosylationQWASISPNITYKHSY
HHEECCCCCEEECCC
32.23-
344N-linked_GlycosylationYKHSYNPNGTIPECP
EECCCCCCCCCCCCC
57.51-
354N-linked_GlycosylationIPECPSRNKTSWAVS
CCCCCCCCCCEEEEE
57.18-
370N-linked_GlycosylationNAFPVTPNTTICSNA
CCCCCCCCCEECCCH
40.25-
423N-linked_GlycosylationPYEGTYGNYTGCTGV
CCCCCCCCCCCCCCC
22.30-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of GAS2_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GAS2_SCHPO !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of GAS2_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of GAS2_SCHPO !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GAS2_SCHPO

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Related Literatures of Post-Translational Modification

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