YC021_YEAST - dbPTM
YC021_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YC021_YEAST
UniProt AC Q96VH3
Protein Name Putative uncharacterized protein YCL021W-A
Gene Name YCL021W-A
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 125
Subcellular Localization Membrane
Single-pass membrane protein .
Protein Description
Protein Sequence MVLTDAEELRSPVITSDMSFFDLESNHSSDSVHLLCEKYTHKLPIESESQTTFRLAPTKQRLYRQSTLYVPLSLKQRVFLFTERVKSIWAGLPRCKPNKYFKVAFALAVLTPLAIWIFYIDFRVH
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

Oops, there are no PTM records of YC021_YEAST !!

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 YC021_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YC021_YEAST !!

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 YC021_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HIS9_YEASTHIS2physical
18467557
SIR1_YEASTSIR1physical
18467557
ITC1_YEASTITC1physical
18467557
HDA3_YEASTHDA3physical
18467557
SEC62_YEASTSEC62physical
18719252

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YC021_YEAST

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Related Literatures of Post-Translational Modification

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