GLRX2_YEAST - dbPTM
GLRX2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GLRX2_YEAST
UniProt AC P17695
Protein Name Glutaredoxin-2, mitochondrial
Gene Name GRX2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 143
Subcellular Localization Cytoplasm . Mitochondrion . Two forms, a long and a short one are found in the mitochondrion, but only the short one is detected in the cytoplasm.
Protein Description Component of the glutathione system which performs several activities such as glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage. GRX2 is more active as an oxidoreductase than GRX1..
Protein Sequence METNFSFDSNLIVIIIITLFATRIIAKRFLSTPKMVSQETVAHVKDLIGQKEVFVAAKTYCPYCKATLSTLFQELNVPKSKALVLELDEMSNGSEIQDALEEISGQKTVPNVYINGKHIGGNSDLETLKKNGKLAEILKPVFQ
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
31PhosphorylationIIAKRFLSTPKMVSQ
HHHHHHHCCCCCCCH		39.6919823750
32PhosphorylationIAKRFLSTPKMVSQE
HHHHHHCCCCCCCHH		29.1319823750
37PhosphorylationLSTPKMVSQETVAHV
HCCCCCCCHHHHHHH		20.8525752575
45AcetylationQETVAHVKDLIGQKE
HHHHHHHHHHHCCCC		36.6324489116
51AcetylationVKDLIGQKEVFVAAK
HHHHHCCCCCEEEEE		51.1124489116
51UbiquitinationVKDLIGQKEVFVAAK
HHHHHCCCCCEEEEE		51.1123749301
58UbiquitinationKEVFVAAKTYCPYCK
CCCEEEEECCCHHHH		30.2324961812
61GlutathionylationFVAAKTYCPYCKATL
EEEEECCCHHHHHHH		2.0418992757
67PhosphorylationYCPYCKATLSTLFQE
CCHHHHHHHHHHHHH		13.5121440633
69PhosphorylationPYCKATLSTLFQELN
HHHHHHHHHHHHHCC		20.7921440633
70PhosphorylationYCKATLSTLFQELNV
HHHHHHHHHHHHCCC		34.4024961812
79AcetylationFQELNVPKSKALVLE
HHHCCCCHHHEEEEE		61.3724489116
91PhosphorylationVLELDEMSNGSEIQD
EEEHHHHCCCHHHHH		35.6722369663
94PhosphorylationLDEMSNGSEIQDALE
HHHHCCCHHHHHHHH		35.4622369663
104PhosphorylationQDALEEISGQKTVPN
HHHHHHHHCCCCCCE		38.1522369663
107UbiquitinationLEEISGQKTVPNVYI
HHHHHCCCCCCEEEE		55.8224961812
108PhosphorylationEEISGQKTVPNVYIN
HHHHCCCCCCEEEEC		33.0522369663
113PhosphorylationQKTVPNVYINGKHIG
CCCCCEEEECCEECC		8.7022369663
117UbiquitinationPNVYINGKHIGGNSD
CEEEECCEECCCCCC		27.7924961812
117AcetylationPNVYINGKHIGGNSD
CEEEECCEECCCCCC		27.7924489116
123PhosphorylationGKHIGGNSDLETLKK
CEECCCCCCHHHHHH		47.0122369663
127PhosphorylationGGNSDLETLKKNGKL
CCCCCHHHHHHCCCH		51.6922369663
129AcetylationNSDLETLKKNGKLAE
CCCHHHHHHCCCHHH		52.1722865919
129SuccinylationNSDLETLKKNGKLAE
CCCHHHHHHCCCHHH		52.1723954790
133UbiquitinationETLKKNGKLAEILKP
HHHHHCCCHHHHHHH		54.6523749301
133AcetylationETLKKNGKLAEILKP
HHHHHCCCHHHHHHH		54.6524489116
139UbiquitinationGKLAEILKPVFQ---
CCHHHHHHHHCC---		44.8123749301
139AcetylationGKLAEILKPVFQ---
CCHHHHHHHHCC---		44.8124489116
139SuccinylationGKLAEILKPVFQ---
CCHHHHHHHHCC---		44.8123954790
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 GLRX2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GLRX2_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 GLRX2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GET3_YEASTGET3physical
18719252
TPS1_YEASTTPS1genetic
20093466
PCP1_YEASTPCP1genetic
20093466
COPE_YEASTSEC28genetic
20093466
SAC1_YEASTSAC1genetic
20093466
HMDH2_YEASTHMG2genetic
20093466
SIP18_YEASTSIP18genetic
20093466
PFKA2_YEASTPFK2genetic
20093466
SWS2_YEASTSWS2genetic
20093466
RCM1_YEASTRCM1genetic
20093466
COQ2_YEASTCOQ2genetic
20093466
SIN3_YEASTSIN3genetic
20093466
GLRX7_YEASTGRX7genetic
20522499
GLRX6_YEASTGRX6genetic
20522499
PRX1_YEASTPRX1genetic
21385868
HTD2_YEASTHTD2genetic
21623372
CEM1_YEASTCEM1genetic
21623372
FABD_YEASTMCT1genetic
21623372
RIB3_YEASTRIB3physical
21565288
GLRX2_YEASTGRX2physical
22940862
SSB1_YEASTSSB1physical
22940862
HSP71_YEASTSSA1physical
22940862
TPS1_YEASTTPS1genetic
27708008
ODPB_YEASTPDB1genetic
27708008
GPR1_YEASTGPR1genetic
27708008
OST4_YEASTOST4genetic
27708008
TPS2_YEASTTPS2genetic
27708008
UBP3_YEASTUBP3genetic
27708008
BEM2_YEASTBEM2genetic
27708008
BMH1_YEASTBMH1genetic
27708008
ODPA_YEASTPDA1genetic
27708008
MRM2_YEASTMRM2genetic
27708008
MED5_YEASTNUT1genetic
27708008
RTF1_YEASTRTF1genetic
27708008
DAL81_YEASTDAL81genetic
27708008
FABG_YEASTOAR1genetic
27708008
RL8B_YEASTRPL8Bgenetic
27708008
ICT1_YEASTICT1genetic
27708008
MID2_YEASTMID2genetic
27708008
HMDH2_YEASTHMG2genetic
27708008
SIP18_YEASTSIP18genetic
27708008
EOS1_YEASTEOS1genetic
27708008
SWS2_YEASTSWS2genetic
27708008
NOP12_YEASTNOP12genetic
27708008
RTC6_YEASTRTC6genetic
27708008
SGTB_HUMANSGTBphysical
27107014
SGTA_HUMANSGTAphysical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GLRX2_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 SER-37; SER-91; SER-94 ANDSER-123, AND MASS SPECTROMETRY.

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