PRDX5_HUMAN - dbPTM
PRDX5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRDX5_HUMAN
UniProt AC P30044
Protein Name Peroxiredoxin-5, mitochondrial
Gene Name PRDX5
Organism Homo sapiens (Human).
Sequence Length 214
Subcellular Localization Isoform Mitochondrial: Mitochondrion .
Isoform Cytoplasmic+peroxisomal: Cytoplasm . Peroxisome matrix . Imported into peroxisomes via peroxisomal targeting signal 1 receptor PEX5.
Protein Description Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events..
Protein Sequence MGLAGVCALRRSAGYILVGGAGGQSAAAAARRYSEGEWASGGVRSFSRAAAAMAPIKVGDAIPAVEVFEGEPGNKVNLAELFKGKKGVLFGVPGAFTPGCSKTHLPGFVEQAEALKAKGVQVVACLSVNDAFVTGEWGRAHKAEGKVRLLADPTGAFGKETDLLLDDSLVSIFGNRRLKRFSMVVQDGIVKALNVEPDGTGLTCSLAPNIISQL
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
12PhosphorylationGVCALRRSAGYILVG
HHHHHHHCCCEEEEE		21.4428555341
31 (in isoform 2)Ubiquitination-33.0921890473
31UbiquitinationQSAAAAARRYSEGEW
HHHHHHHHHHCCCCC		33.0933845483
34PhosphorylationAAAARRYSEGEWASG
HHHHHHHCCCCCCCC		37.0027251275
34UbiquitinationAAAARRYSEGEWASG
HHHHHHHCCCCCCCC		37.0033845483
45PhosphorylationWASGGVRSFSRAAAA
CCCCCHHHHHHHHHH		25.7632142685
47PhosphorylationSGGVRSFSRAAAAMA
CCCHHHHHHHHHHCC		23.4317081983
50 (in isoform 2)Ubiquitination-8.4721890473
50UbiquitinationVRSFSRAAAAMAPIK
HHHHHHHHHHCCCEE		8.4733845483
57UbiquitinationAAAMAPIKVGDAIPA
HHHCCCEECCCEECE		38.8223503661
64UbiquitinationKVGDAIPAVEVFEGE
ECCCEECEEEEECCC		12.1833845483
75AcetylationFEGEPGNKVNLAELF
ECCCCCCEEEHHHHH		38.11-
75UbiquitinationFEGEPGNKVNLAELF
ECCCCCCEEEHHHHH		38.1123503661
83AcetylationVNLAELFKGKKGVLF
EEHHHHHCCCCEEEE		80.5619608861
83 (in isoform 1)Ubiquitination-80.5621890473
83SuccinylationVNLAELFKGKKGVLF
EEHHHHHCCCCEEEE		80.56-
83UbiquitinationVNLAELFKGKKGVLF
EEHHHHHCCCCEEEE		80.5623000965
83UbiquitinationVNLAELFKGKKGVLF
EEHHHHHCCCCEEEE		80.5621890473
83UbiquitinationVNLAELFKGKKGVLF
EEHHHHHCCCCEEEE		80.5621890473
83SuccinylationVNLAELFKGKKGVLF
EEHHHHHCCCCEEEE		80.5623954790
85UbiquitinationLAELFKGKKGVLFGV
HHHHHCCCCEEEEEC		47.1223000965
86UbiquitinationAELFKGKKGVLFGVP
HHHHCCCCEEEEECC		64.0223000965
97UbiquitinationFGVPGAFTPGCSKTH
EECCCCCCCCCCCCC		20.4524816145
97PhosphorylationFGVPGAFTPGCSKTH
EECCCCCCCCCCCCC		20.4525159151
100S-nitrosocysteinePGAFTPGCSKTHLPG
CCCCCCCCCCCCCCC		3.87-
100GlutathionylationPGAFTPGCSKTHLPG
CCCCCCCCCCCCCCC		3.8722555962
100S-nitrosylationPGAFTPGCSKTHLPG
CCCCCCCCCCCCCCC		3.8722178444
100S-palmitoylationPGAFTPGCSKTHLPG
CCCCCCCCCCCCCCC		3.8729575903
101PhosphorylationGAFTPGCSKTHLPGF
CCCCCCCCCCCCCCH		46.6428450419
102UbiquitinationAFTPGCSKTHLPGFV
CCCCCCCCCCCCCHH		44.0021890473
102AcetylationAFTPGCSKTHLPGFV
CCCCCCCCCCCCCHH		44.0025953088
102 (in isoform 1)Ubiquitination-44.0021890473
116UbiquitinationVEQAEALKAKGVQVV
HHHHHHHHCCCCEEE		55.9133845483
116SuccinylationVEQAEALKAKGVQVV
HHHHHHHHCCCCEEE		55.91-
116MalonylationVEQAEALKAKGVQVV
HHHHHHHHCCCCEEE		55.9126320211
116AcetylationVEQAEALKAKGVQVV
HHHHHHHHCCCCEEE		55.9125038526
116SuccinylationVEQAEALKAKGVQVV
HHHHHHHHCCCCEEE		55.91-
118UbiquitinationQAEALKAKGVQVVAC
HHHHHHCCCCEEEEE		59.01-
142UbiquitinationGEWGRAHKAEGKVRL
CCCCCCCCCCCCEEE		47.3424816145
146UbiquitinationRAHKAEGKVRLLADP
CCCCCCCCEEEEECC		18.7129967540
159UbiquitinationDPTGAFGKETDLLLD
CCCCCCCCHHCEECC		51.4929967540
159AcetylationDPTGAFGKETDLLLD
CCCCCCCCHHCEECC		51.4925038526
161PhosphorylationTGAFGKETDLLLDDS
CCCCCCHHCEECCCH		35.1220873877
168PhosphorylationTDLLLDDSLVSIFGN
HCEECCCHHHHHHCC		30.2728258704
171PhosphorylationLLDDSLVSIFGNRRL
ECCCHHHHHHCCCCH		19.9325693802
182PhosphorylationNRRLKRFSMVVQDGI
CCCHHHEEEEEECCC		18.0728450419
183SulfoxidationRRLKRFSMVVQDGIV
CCHHHEEEEEECCCE		2.9221406390
204GlutathionylationPDGTGLTCSLAPNII
CCCCCEEEECCHHHH		3.6422555962
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 PRDX5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRDX5_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 PRDX5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CC90B_HUMANCCDC90Bphysical
16169070
A4_HUMANAPPphysical
21832049
STAM1_HUMANSTAMphysical
22939629
SODC_HUMANSOD1physical
22939629
VAMP2_HUMANVAMP2physical
22939629
PRDX6_HUMANPRDX6physical
22939629
SUMO1_HUMANSUMO1physical
22939629
SC24A_HUMANSEC24Aphysical
22939629
PTN23_HUMANPTPN23physical
22939629
SLD5_HUMANGINS4physical
22939629
RS12_HUMANRPS12physical
22939629
RD23B_HUMANRAD23Bphysical
22939629
TOM40_HUMANTOMM40physical
22939629
UBE2B_HUMANUBE2Bphysical
22939629
UBAP2_HUMANUBAP2physical
22939629
PTMS_HUMANPTMSphysical
22939629
IFT27_HUMANIFT27physical
22939629
PTGR1_HUMANPTGR1physical
22939629
UBE2A_HUMANUBE2Aphysical
22939629
SSA27_HUMANSSSCA1physical
22939629
ANCHR_HUMANZFYVE19physical
22939629
PSRC1_HUMANPSRC1physical
22939629
DUT_HUMANDUTphysical
26344197
NDKA_HUMANNME1physical
26344197
PARK7_HUMANPARK7physical
26344197
PRDX1_HUMANPRDX1physical
26344197
PRDX2_HUMANPRDX2physical
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 PRDX5_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-83, AND MASS SPECTROMETRY.

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