THIOM_HUMAN - dbPTM
THIOM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID THIOM_HUMAN
UniProt AC Q99757
Protein Name Thioredoxin, mitochondrial
Gene Name TXN2
Organism Homo sapiens (Human).
Sequence Length 166
Subcellular Localization Mitochondrion .
Protein Description Important for the control of mitochondrial reactive oxygen species homeostasis, apoptosis regulation and cell viability. Possesses a dithiol-reducing activity..
Protein Sequence MAQRLLLRRFLASVISRKPSQGQWPPLTSRALQTPQCSPGGLTVTPNPARTIYTTRISLTTFNIQDGPDFQDRVVNSETPVVVDFHAQWCGPCKILGPRLEKMVAKQHGKVVMAKVDIDDHTDLAIEYEVSAVPTVLAMKNGDVVDKFVGIKDEDQLEAFLKKLIG
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
94AcetylationAQWCGPCKILGPRLE
CCCCCCCEEHHHHHH
44.0626051181
102AcetylationILGPRLEKMVAKQHG
EHHHHHHHHHHHHCC
43.1825953088
102UbiquitinationILGPRLEKMVAKQHG
EHHHHHHHHHHHHCC
43.1821890473
1022-HydroxyisobutyrylationILGPRLEKMVAKQHG
EHHHHHHHHHHHHCC
43.18-
1062-HydroxyisobutyrylationRLEKMVAKQHGKVVM
HHHHHHHHHCCCEEE
31.27-
128PhosphorylationHTDLAIEYEVSAVPT
CCCEEEEEEECCCCE
18.6028258704
131PhosphorylationLAIEYEVSAVPTVLA
EEEEEEECCCCEEEE
16.1728258704
133UbiquitinationIEYEVSAVPTVLAMK
EEEEECCCCEEEEEC
2.9621890473
152AcetylationVDKFVGIKDEDQLEA
EEEECCCCCHHHHHH
49.4919608861
152SuccinylationVDKFVGIKDEDQLEA
EEEECCCCCHHHHHH
49.49-
1522-HydroxyisobutyrylationVDKFVGIKDEDQLEA
EEEECCCCCHHHHHH
49.49-
152SuccinylationVDKFVGIKDEDQLEA
EEEECCCCCHHHHHH
49.4923954790
1622-HydroxyisobutyrylationDQLEAFLKKLIG---
HHHHHHHHHHHC---
38.80-
162AcetylationDQLEAFLKKLIG---
HHHHHHHHHHHC---
38.8025953088

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 THIOM_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of THIOM_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 THIOM_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TOM22_HUMANTOMM22physical
22939629
TPM4_HUMANTPM4physical
22939629
VIME_HUMANVIMphysical
21988832
GCR_HUMANNR3C1physical
19570036
TF65_HUMANRELAphysical
19570036
RABX5_HUMANRABGEF1physical
25416956
ATRAP_HUMANAGTRAPphysical
25416956
PACE1_HUMANSCYL3physical
25416956
COAC_HUMANPPCDCphysical
25416956
TIFA_HUMANTIFAphysical
25416956
REEP6_HUMANREEP6physical
25416956
CC114_HUMANCCDC114physical
25416956
MR1L1_HUMANMRFAP1L1physical
25416956
K1C40_HUMANKRT40physical
25416956
RBM45_HUMANRBM45physical
25416956
FAM9B_HUMANFAM9Bphysical
25416956
ANXA6_HUMANANXA6physical
26344197
FA98B_HUMANFAM98Bphysical
26344197
SODC_HUMANSOD1physical
26344197
THIO_HUMANTXNphysical
26344197
WDR12_HUMANWDR12physical
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 THIOM_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-152, AND MASS SPECTROMETRY.

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