GDIR_YEAST - dbPTM
GDIR_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GDIR_YEAST
UniProt AC Q12434
Protein Name Rho GDP-dissociation inhibitor
Gene Name RDI1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 202
Subcellular Localization Cytoplasm.
Protein Description Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them..
Protein Sequence MAEESTDFSQFEEERNNDQYKVSAKKTVDEYKNLDAEDESLAKWKESLGLSSDVLPLEFPGDKRKVVVQKIQLLVNTEPNPITFDLTNEKTIKELASKRYKIKENSIYKLKIVFKVQHEIITGLRYVQYIKKAGIAVDKIDDHLGSYAPNTKTKPFYEVELPESEAPSGFLARGNYSAVSKFIDDDKTNHLTLNWGVEIVKK
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
2Acetylation------MAEESTDFS
------CCCCCCCHH		29.3022814378
5Phosphorylation---MAEESTDFSQFE
---CCCCCCCHHHHH		25.4522369663
6Phosphorylation--MAEESTDFSQFEE
--CCCCCCCHHHHHH		44.3222369663
9PhosphorylationAEESTDFSQFEEERN
CCCCCCHHHHHHHHC		36.4522369663
20PhosphorylationEERNNDQYKVSAKKT
HHHCCCCCEEEEECC		19.0722369663
21AcetylationERNNDQYKVSAKKTV
HHCCCCCEEEEECCH		24.8724489116
26UbiquitinationQYKVSAKKTVDEYKN
CCEEEEECCHHHHHC		54.2022106047
26AcetylationQYKVSAKKTVDEYKN
CCEEEEECCHHHHHC		54.2024489116
27PhosphorylationYKVSAKKTVDEYKNL
CEEEEECCHHHHHCC		32.2725521595
32UbiquitinationKKTVDEYKNLDAEDE
ECCHHHHHCCCHHHH		49.3223749301
32AcetylationKKTVDEYKNLDAEDE
ECCHHHHHCCCHHHH		49.3224489116
40PhosphorylationNLDAEDESLAKWKES
CCCHHHHHHHHHHHH		46.0422369663
43AcetylationAEDESLAKWKESLGL
HHHHHHHHHHHHHCC		65.1824489116
47PhosphorylationSLAKWKESLGLSSDV
HHHHHHHHHCCCCCE		24.8219779198
51PhosphorylationWKESLGLSSDVLPLE
HHHHHCCCCCEECCC		23.7722369663
52PhosphorylationKESLGLSSDVLPLEF
HHHHCCCCCEECCCC		36.4622369663
63AcetylationPLEFPGDKRKVVVQK
CCCCCCCHHHEEEEE		61.0924489116
93UbiquitinationLTNEKTIKELASKRY
CCCHHHHHHHHHCCC		52.4823749301
106PhosphorylationRYKIKENSIYKLKIV
CCCCCCCCEEEEEEE		28.5228889911
131AcetylationLRYVQYIKKAGIAVD
HHHHHHHHHCCCEEE		31.4722865919
139AcetylationKAGIAVDKIDDHLGS
HCCCEEEECCCCCCC		41.2424489116
177PhosphorylationFLARGNYSAVSKFID
EECCCCCEEEEECCC		26.6228889911
181AcetylationGNYSAVSKFIDDDKT
CCCEEEEECCCCCCC		39.4824489116
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 GDIR_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GDIR_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 GDIR_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBX1_YEASTSHP1genetic
17314980
TPO3_YEASTTPO3physical
18467557
AGP2_YEASTAGP2genetic
20093466
BEM1_YEASTBEM1genetic
20093466
YCV1_YEASTYCR061Wgenetic
20093466
FUB1_YEASTFUB1genetic
20093466
PST1_YEASTPST1genetic
20093466
SWF1_YEASTSWF1genetic
20093466
HNT2_YEASTHNT2genetic
20093466
YD338_YEASTYDR338Cgenetic
20093466
AP2_YEASTCAD1genetic
20093466
DOT1_YEASTDOT1genetic
20093466
STP1_YEASTSTP1genetic
20093466
PUS2_YEASTPUS2genetic
20093466
TOS2_YEASTTOS2genetic
20093466
BIOB_YEASTBIO2genetic
20093466
YHK5_YEASTYHR045Wgenetic
20093466
LIN1_YEASTLIN1genetic
20093466
F26_YEASTFBP26genetic
20093466
SIP4_YEASTSIP4genetic
20093466
CBF1_YEASTCBF1genetic
20093466
SFC1_YEASTSFC1genetic
20093466
DAN1_YEASTDAN1genetic
20093466
GST2_YEASTGTT2genetic
20093466
SRL2_YEASTSRL2genetic
20093466
HMX1_YEASTHMX1genetic
20093466
PO152_YEASTPOM152genetic
20093466
YM79_YEASTYMR244Wgenetic
20093466
KC12_YEASTYCK2genetic
20093466
CARME_YEASTYNL092Wgenetic
20093466
YN95_YEASTYNR066Cgenetic
20093466
AB140_YEASTABP140genetic
20093466
BEM4_YEASTBEM4genetic
20093466
AXL1_YEASTAXL1genetic
20093466
KAR3_YEASTKAR3genetic
20093466
RHO1_YEASTRHO1physical
21171963
CDC42_YEASTCDC42physical
21171963
LEM3_YEASTLEM3genetic
22344035
TPO3_YEASTTPO3physical
22615397
RHO4_YEASTRHO4genetic
23264647
BEM2_YEASTBEM2genetic
27476596
MSN4_YEASTMSN4genetic
27708008
AGP2_YEASTAGP2genetic
27708008
SWF1_YEASTSWF1genetic
27708008
UME6_YEASTUME6genetic
27708008
MTH1_YEASTMTH1genetic
27708008
HNT2_YEASTHNT2genetic
27708008
YD338_YEASTYDR338Cgenetic
27708008
DOT1_YEASTDOT1genetic
27708008
STP1_YEASTSTP1genetic
27708008
PT122_YEASTPET122genetic
27708008
BEM2_YEASTBEM2genetic
27708008
ACOX_YEASTPOX1genetic
27708008
ASK10_YEASTASK10genetic
27708008
BIOB_YEASTBIO2genetic
27708008
YHK5_YEASTYHR045Wgenetic
27708008
LIN1_YEASTLIN1genetic
27708008
ASF1_YEASTASF1genetic
27708008
F26_YEASTFBP26genetic
27708008
YJU6_YEASTYJL206Cgenetic
27708008
3HAO_YEASTBNA1genetic
27708008
NU133_YEASTNUP133genetic
27708008
AVL9_YEASTAVL9genetic
27708008
RL31B_YEASTRPL31Bgenetic
27708008
MSC1_YEASTMSC1genetic
27708008
CLU_YEASTCLU1genetic
27708008
PO152_YEASTPOM152genetic
27708008
YM79_YEASTYMR244Wgenetic
27708008
YN95_YEASTYNR066Cgenetic
27708008
YVC1_YEASTYVC1genetic
27708008
YORA4_YEASTYOR114Wgenetic
27708008
AIM44_YEASTAIM44genetic
27708008
BEM4_YEASTBEM4genetic
27708008
MED1_YEASTMED1genetic
27708008
YBF9_YEASTYBL059Wgenetic
29674565
CHO2_YEASTCHO2genetic
29674565
ICE2_YEASTICE2genetic
29674565
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GDIR_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-27 AND SER-40, AND MASSSPECTROMETRY.
"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-52, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-27 AND SER-40, AND MASSSPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-27, AND MASSSPECTROMETRY.

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