GLRX1_HUMAN - dbPTM
GLRX1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GLRX1_HUMAN
UniProt AC P35754
Protein Name Glutaredoxin-1
Gene Name GLRX
Organism Homo sapiens (Human).
Sequence Length 106
Subcellular Localization Cytoplasm.
Protein Description Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins..
Protein Sequence MAQEFVNCKIQPGKVVVFIKPTCPYCRRAQEILSQLPIKQGLLEFVDITATNHTNEIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSLQQSGELLTRLKQIGALQ
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------MAQEFVNCK
------CCCCCCCCE
20.0119413330
8S-nitrosocysteineMAQEFVNCKIQPGKV
CCCCCCCCEECCCCE
3.27-
8S-nitrosylationMAQEFVNCKIQPGKV
CCCCCCCCEECCCCE
3.2722178444
9SuccinylationAQEFVNCKIQPGKVV
CCCCCCCEECCCCEE
38.89-
9UbiquitinationAQEFVNCKIQPGKVV
CCCCCCCEECCCCEE
38.89-
9SuccinylationAQEFVNCKIQPGKVV
CCCCCCCEECCCCEE
38.89-
9AcetylationAQEFVNCKIQPGKVV
CCCCCCCEECCCCEE
38.8923749302
20UbiquitinationGKVVVFIKPTCPYCR
CCEEEEECCCCHHHH
23.8621890473
20AcetylationGKVVVFIKPTCPYCR
CCEEEEECCCCHHHH
23.8623749302
20MalonylationGKVVVFIKPTCPYCR
CCEEEEECCCCHHHH
23.8626320211
22PhosphorylationVVVFIKPTCPYCRRA
EEEEECCCCHHHHHH
22.5528152594
23GlutathionylationVVFIKPTCPYCRRAQ
EEEECCCCHHHHHHH
2.839860827
25PhosphorylationFIKPTCPYCRRAQEI
EECCCCHHHHHHHHH
10.7528152594
34PhosphorylationRRAQEILSQLPIKQG
HHHHHHHHCCCCCCC
35.0226437602
65O-linked_GlycosylationQDYLQQLTGARTVPR
HHHHHHHHCCCCCCE
25.1829351928
79S-nitrosocysteineRVFIGKDCIGGCSDL
EEEECCCCCCCHHHH
3.38-
79S-nitrosylationRVFIGKDCIGGCSDL
EEEECCCCCCCHHHH
3.3822178444
83S-nitrosylationGKDCIGGCSDLVSLQ
CCCCCCCHHHHHHHH
2.1122178444
83S-nitrosocysteineGKDCIGGCSDLVSLQ
CCCCCCCHHHHHHHH
2.11-
84PhosphorylationKDCIGGCSDLVSLQQ
CCCCCCHHHHHHHHH
36.9428258704
100MalonylationGELLTRLKQIGALQ-
HHHHHHHHHHCCCC-
36.2626320211
100UbiquitinationGELLTRLKQIGALQ-
HHHHHHHHHHCCCC-
36.26-

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 GLRX1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GLRX1_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 GLRX1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATP7A_HUMANATP7Aphysical
16884690
ATP7B_HUMANATP7Bphysical
16884690
M3K5_HUMANMAP3K5physical
12244106
AATM_HUMANGOT2physical
21900206
MMP23_HUMANMMP23Bphysical
21988832
NIT1_HUMANNIT1physical
26344197

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 GLRX1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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