RGD2_YEAST - dbPTM
RGD2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RGD2_YEAST
UniProt AC P43556
Protein Name Rho-GTPase-activating protein RGD2
Gene Name RGD2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 714
Subcellular Localization
Protein Description Acts in signal transduction. Activates CDC42 and RHO5..
Protein Sequence MLSFCDYFWSEDLVSGLDVLFDRLYHGCEQCDLFIQLFASRMQFEVSHGRQLFGIEAGMDNLKAVQEDEDEGVTVSRALRGILQEMSQEGTHHLTIASNIESLVLQPFSKWCIEHRERIQYSEKTLLTNVNNFRKSKKYVGKLEKEYFNKCRQLEEFKRTHFNEDELANAMKSLKIQNKYEEDVAREKDHRFFNRIAGIDFDYKTMKETLQLLLTKLPKTDYKLPLISYSLSNTNNGGEITKFLLDHMSLKDIDQAETFGQDLLNLGFLKYCNGVGNTFVNSKKFQYQWKNTAYMFANVPMPGSEEPTTGESLISRFNNWDGSSAKEIIQSKIGNDQGAAKIQAPHISDNERTLFRMMDALAASDKKYYQECFKMDALRCSVEELLIDHLSFMEKCESDRLNAIKKATLDFCSTLGNKISSLRLCIDKMLTLENDIDPTADLLQLLVKYKTGSFKPQAIVYNNYYNPGSFQNFGVDLETRCRLDKKVVPLIISSIFSYMDKIYPDLPNDKVRTSIWTDSVKLSLTHQLRNLLNKQQFHNEGEIFDILSTSKLEPSTIASVVKIYLLELPDPLIPNDVSDILRVLYLDYPPLVETALQNSTSSPENQQDDDNEEGFDTKRIRGLYTTLSSLSKPHIATLDAITTHFYRLIKILKMGENGNEVADEFTVSISQEFANCIIQSKITDDNEIGFKIFYDLLTHKKQIFHELKRQNSKN
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
124AcetylationERIQYSEKTLLTNVN
HHHCCCHHHHHHCHH		38.2324489116
179UbiquitinationKSLKIQNKYEEDVAR
HHHCCCCHHHHHHHH		37.3523749301
204AcetylationAGIDFDYKTMKETLQ
CCCCCCHHHHHHHHH		43.9424489116
209PhosphorylationDYKTMKETLQLLLTK
CHHHHHHHHHHHHHC		17.8121440633
216AcetylationTLQLLLTKLPKTDYK
HHHHHHHCCCCCCCC		63.8624489116
216UbiquitinationTLQLLLTKLPKTDYK
HHHHHHHCCCCCCCC		63.8624961812
332AcetylationAKEIIQSKIGNDQGA
HHHHHHHHHCCCCCC		37.9525381059
332UbiquitinationAKEIIQSKIGNDQGA
HHHHHHHHHCCCCCC		37.9523749301
341UbiquitinationGNDQGAAKIQAPHIS
CCCCCCCCCCCCCCC		34.5123749301
555PhosphorylationSTSKLEPSTIASVVK
CCCCCCHHHHHHHEE		24.0717563356
559PhosphorylationLEPSTIASVVKIYLL
CCHHHHHHHEEEEEE		24.4817563356
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 RGD2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RGD2_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 RGD2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PIN2_YEASTPIN2physical
18467557
RGD2_YEASTRGD2physical
18467557
NNK1_YEASTNNK1physical
18719252
PIN2_YEASTPIN2physical
22615397
RPA14_YEASTRPA14genetic
27708008
ARO80_YEASTARO80genetic
27708008
RS10A_YEASTRPS10Agenetic
27708008
OSH1_YEASTSWH1genetic
27708008
ASF2_YEASTASF2genetic
27708008
TPS2_YEASTTPS2genetic
27708008
RT103_YEASTRTT103genetic
27708008
SUR2_YEASTSUR2genetic
27708008
RLA4_YEASTRPP2Bgenetic
27708008
HKR1_YEASTHKR1genetic
27708008
RAD4_YEASTRAD4genetic
27708008
MRM2_YEASTMRM2genetic
27708008
YIA6_YEASTYIA6genetic
27708008
NU133_YEASTNUP133genetic
27708008
APC9_YEASTAPC9genetic
27708008
SKY1_YEASTSKY1genetic
27708008
INO4_YEASTINO4genetic
27708008
DIA2_YEASTDIA2genetic
27708008
VAM3_YEASTVAM3genetic
27708008
GET4_YEASTGET4genetic
27708008
MTHR1_YEASTMET12genetic
27708008
YP027_YEASTYPR027Cgenetic
27708008
NAGK_HUMANNAGKphysical
27107014
TEKT4_HUMANTEKT4physical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RGD2_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-555 AND SER-559, ANDMASS SPECTROMETRY.

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