GLRX3_HUMAN - dbPTM
GLRX3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GLRX3_HUMAN
UniProt AC O76003
Protein Name Glutaredoxin-3
Gene Name GLRX3
Organism Homo sapiens (Human).
Sequence Length 335
Subcellular Localization Cytoplasm, cytosol . Cytoplasm, cell cortex . Cytoplasm, myofibril, sarcomere, Z line . Under the plasma membrane (By similarity). After PMA stimulation, GLRX3 and PRKCQ/PKC-theta translocate to a more extended submembrane area (By similarity). In th
Protein Description Together with BOLA2, acts as a cytosolic iron-sulfur (Fe-S) cluster assembly factor that facilitates [2Fe-2S] cluster insertion into a subset of cytosolic proteins. [PubMed: 26613676]
Protein Sequence MAAGAAEAAVAAVEEVGSAGQFEELLRLKAKSLLVVHFWAPWAPQCAQMNEVMAELAKELPQVSFVKLEAEGVPEVSEKYEISSVPTFLFFKNSQKIDRLDGAHAPELTKKVQRHASSGSFLPSANEHLKEDLNLRLKKLTHAAPCMLFMKGTPQEPRCGFSKQMVEILHKHNIQFSSFDIFSDEEVRQGLKAYSSWPTYPQLYVSGELIGGLDIIKELEASEELDTICPKAPKLEERLKVLTNKASVMLFMKGNKQEAKCGFSKQILEILNSTGVEYETFDILEDEEVRQGLKAYSNWPTYPQLYVKGELVGGLDIVKELKENGELLPILRGEN
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------MAAGAAEAA
------CCCCHHHHH		18.0122223895
18PhosphorylationAAVEEVGSAGQFEEL
HHHHHHCCCCCHHHH		34.1125693802
32PhosphorylationLLRLKAKSLLVVHFW
HHHHHHCEEEEEEEE		31.62-
67UbiquitinationLPQVSFVKLEAEGVP
CCCCEEEEEEECCCC		38.30-
67SumoylationLPQVSFVKLEAEGVP
CCCCEEEEEEECCCC		38.30-
67SuccinylationLPQVSFVKLEAEGVP
CCCCEEEEEEECCCC		38.3023954790
79UbiquitinationGVPEVSEKYEISSVP
CCCCCCCCEEECCCC		40.45-
92AcetylationVPTFLFFKNSQKIDR
CCEEEEECCCHHCCC		48.6425953088
92UbiquitinationVPTFLFFKNSQKIDR
CCEEEEECCCHHCCC		48.6421906983
96UbiquitinationLFFKNSQKIDRLDGA
EEECCCHHCCCCCCC		46.53-
109PhosphorylationGAHAPELTKKVQRHA
CCCCHHHHHHHHHHH		27.4521406692
110AcetylationAHAPELTKKVQRHAS
CCCHHHHHHHHHHHH		64.6723749302
1102-HydroxyisobutyrylationAHAPELTKKVQRHAS
CCCHHHHHHHHHHHH		64.67-
110UbiquitinationAHAPELTKKVQRHAS
CCCHHHHHHHHHHHH		64.67-
111UbiquitinationHAPELTKKVQRHASS
CCHHHHHHHHHHHHC		38.06-
117PhosphorylationKKVQRHASSGSFLPS
HHHHHHHHCCCCCCC		29.1629255136
118PhosphorylationKVQRHASSGSFLPSA
HHHHHHHCCCCCCCH		38.9629255136
120PhosphorylationQRHASSGSFLPSANE
HHHHHCCCCCCCHHH		26.0929255136
124PhosphorylationSSGSFLPSANEHLKE
HCCCCCCCHHHHHHH		45.9628450419
130UbiquitinationPSANEHLKEDLNLRL
CCHHHHHHHHHHHHH		51.60-
139UbiquitinationDLNLRLKKLTHAAPC
HHHHHHHHHHHHCCE		64.31-
146GlutathionylationKLTHAAPCMLFMKGT
HHHHHCCEEEEECCC		2.9522555962
146S-nitrosylationKLTHAAPCMLFMKGT
HHHHHCCEEEEECCC		2.9524105792
151AcetylationAPCMLFMKGTPQEPR
CCEEEEECCCCCCCC		52.9125953088
151UbiquitinationAPCMLFMKGTPQEPR
CCEEEEECCCCCCCC		52.91-
151MalonylationAPCMLFMKGTPQEPR
CCEEEEECCCCCCCC		52.9126320211
153PhosphorylationCMLFMKGTPQEPRCG
EEEEECCCCCCCCCC		19.1124300666
163AcetylationEPRCGFSKQMVEILH
CCCCCCCHHHHHHHH		39.9025953088
163UbiquitinationEPRCGFSKQMVEILH
CCCCCCCHHHHHHHH		39.90-
165SulfoxidationRCGFSKQMVEILHKH
CCCCCHHHHHHHHHC		3.1630846556
177PhosphorylationHKHNIQFSSFDIFSD
HHCCCCCCEEECCCH		17.4530624053
178PhosphorylationKHNIQFSSFDIFSDE
HCCCCCCEEECCCHH		28.3830624053
183PhosphorylationFSSFDIFSDEEVRQG
CCEEECCCHHHHHHH		44.43-
196PhosphorylationQGLKAYSSWPTYPQL
HHHHHHHCCCCCCEE		25.13-
200PhosphorylationAYSSWPTYPQLYVSG
HHHCCCCCCEEEEEC		5.72-
229GlutathionylationSEELDTICPKAPKLE
HHCHHHHCCCCCCHH		2.8422555962
231UbiquitinationELDTICPKAPKLEER
CHHHHCCCCCCHHHH		73.28-
234AcetylationTICPKAPKLEERLKV
HHCCCCCCHHHHHHH		73.6825953088
234UbiquitinationTICPKAPKLEERLKV
HHCCCCCCHHHHHHH		73.68-
240UbiquitinationPKLEERLKVLTNKAS
CCHHHHHHHHHCCCC		41.2321890473
247PhosphorylationKVLTNKASVMLFMKG
HHHHCCCCEEEEECC		15.0730622161
253AcetylationASVMLFMKGNKQEAK
CCEEEEECCCCHHHC		52.5825953088
260AcetylationKGNKQEAKCGFSKQI
CCCCHHHCCCCHHHH		33.8525953088
296PhosphorylationVRQGLKAYSNWPTYP
HHHHHHHHHCCCCCC		10.8421406692
297PhosphorylationRQGLKAYSNWPTYPQ
HHHHHHHHCCCCCCE		36.9621406692
301PhosphorylationKAYSNWPTYPQLYVK
HHHHCCCCCCEEEEC		39.1721406692
302PhosphorylationAYSNWPTYPQLYVKG
HHHCCCCCCEEEECC		5.7221406692
306PhosphorylationWPTYPQLYVKGELVG
CCCCCEEEECCEEEC		8.5521406692
319UbiquitinationVGGLDIVKELKENGE
ECCHHHHHHHHHCCC		58.63-
322UbiquitinationLDIVKELKENGELLP
HHHHHHHHHCCCEEC		50.67-
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 GLRX3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GLRX3_HUMAN !!
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 GLRX3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NADK_HUMANNADKphysical
16189514
KR412_HUMANKRTAP4-12physical
16189514
FBLN4_HUMANEFEMP2physical
16189514
ATL4_HUMANADAMTSL4physical
16189514
CPIN1_HUMANCIAPIN1physical
16189514
KPCT_HUMANPRKCQphysical
10636891
GSH0_HUMANGCLMphysical
22863883
SGT1_HUMANSUGT1physical
22863883
FCL_HUMANTSTA3physical
22863883
GLRX3_HUMANGLRX3physical
25416956
MABP1_HUMANMAPKBP1physical
25416956
MOXD1_HUMANMOXD1physical
25416956
ZN544_HUMANZNF544physical
25416956
ZBT44_HUMANZBTB44physical
25416956
BOLA1_HUMANBOLA1physical
25416956
F118A_HUMANFAM118Aphysical
25416956
TRI36_HUMANTRIM36physical
25416956
CPIN1_HUMANCIAPIN1physical
25416956
GMCL1_HUMANGMCL1physical
25416956
ZN426_HUMANZNF426physical
25416956
SOX7_HUMANSOX7physical
25416956
KR412_HUMANKRTAP4-12physical
25416956
KRA92_HUMANKRTAP9-2physical
25416956
TMM25_HUMANTMEM25physical
25416956
KRA42_HUMANKRTAP4-2physical
25416956
NOE3_HUMANOLFM3physical
25416956
KR131_HUMANKRTAP13-1physical
25416956
ALKB3_HUMANALKBH3physical
25416956
TRI42_HUMANTRIM42physical
25416956
LCE2D_HUMANLCE2Dphysical
25416956
KR109_HUMANKRTAP10-9physical
25416956
KR101_HUMANKRTAP10-1physical
25416956
KR10B_HUMANKRTAP10-11physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
KRA56_HUMANKRTAP5-6physical
25416956
KR411_HUMANKRTAP4-11physical
25416956
KLRG2_HUMANKLRG2physical
26186194
BOLA1_HUMANBOLA1physical
26186194
API5_HUMANAPI5physical
26344197
INO1_HUMANISYNA1physical
26344197
PDIA1_HUMANP4HBphysical
26344197
PRPK_HUMANTP53RKphysical
26344197
GRN_HUMANGRNphysical
21516116
CPIN1_HUMANCIAPIN1physical
21516116
ZNF23_HUMANZNF23physical
21516116
BOLA1_HUMANBOLA1physical
28514442
AHNK2_HUMANAHNAK2physical
28514442
SRC_HUMANSRCphysical
28514442
GNAZ_HUMANGNAZphysical
28514442
DAAF1_HUMANDNAAF1physical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GLRX3_HUMAN

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