PTGR3_HUMAN - dbPTM
PTGR3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTGR3_HUMAN
UniProt AC Q8N4Q0
Protein Name Prostaglandin reductase 3
Gene Name ZADH2 {ECO:0000312|HGNC:HGNC:28697}
Organism Homo sapiens (Human).
Sequence Length 377
Subcellular Localization Peroxisome .
Protein Description Functions as 15-oxo-prostaglandin 13-reductase and acts on 15-keto-PGE1, 15-keto-PGE2, 15-keto-PGE1-alpha and 15-keto-PGE2-alpha with highest efficienty towards 15-keto-PGE2-alpha. Overexpression represses transcriptional activity of PPARG and inhibits adipocyte differentiation..
Protein Sequence MLRLVPTGARAIVDMSYARHFLDFQGSAIPQAMQKLVVTRLSPNFREAVTLSRDCPVPLPGDGDLLVRNRFVGVNASDINYSAGRYDPSVKPPFDIGFEGIGEVVALGLSASARYTVGQAVAYMAPGSFAEYTVVPASIATPVPSVKPEYLTLLVSGTTAYISLKELGGLSEGKKVLVTAAAGGTGQFAMQLSKKAKCHVIGTCSSDEKSAFLKSLGCDRPINYKTEPVGTVLKQEYPEGVDVVYESVGGAMFDLAVDALATKGRLIVIGFISGYQTPTGLSPVKAGTLPAKLLKKSASVQGFFLNHYLSKYQAAMSHLLEMCVSGDLVCEVDLGDLSPEGRFTGLESIFRAVNYMYMGKNTGKIVVELPHSVNSKL
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
35AcetylationAIPQAMQKLVVTRLS
CHHHHHHHHHHHEEC
-
123PhosphorylationTVGQAVAYMAPGSFA
EHHCHHHHCCCCCCE
20068231
128PhosphorylationVAYMAPGSFAEYTVV
HHHCCCCCCEEEEEE
20068231
145PhosphorylationSIATPVPSVKPEYLT
CEECCCCCCCHHHEE
22496350
150PhosphorylationVPSVKPEYLTLLVSG
CCCCCHHHEEEEEEC
28111955
152PhosphorylationSVKPEYLTLLVSGTT
CCCHHHEEEEEECCE
28111955
156PhosphorylationEYLTLLVSGTTAYIS
HHEEEEEECCEEEEE
28111955
158PhosphorylationLTLLVSGTTAYISLK
EEEEEECCEEEEEHH
28111955
159PhosphorylationTLLVSGTTAYISLKE
EEEEECCEEEEEHHH
28111955
161PhosphorylationLVSGTTAYISLKELG
EEECCEEEEEHHHHC
28111955
163PhosphorylationSGTTAYISLKELGGL
ECCEEEEEHHHHCCC
28111955
174AcetylationLGGLSEGKKVLVTAA
HCCCCCCCEEEEEEC
30593455
174MethylationLGGLSEGKKVLVTAA
HCCCCCCCEEEEEEC
-
175AcetylationGGLSEGKKVLVTAAA
CCCCCCCEEEEEECC
19818077
179PhosphorylationEGKKVLVTAAAGGTG
CCCEEEEEECCCCHH
22210691
194AcetylationQFAMQLSKKAKCHVI
HHHHHHHHHCCCEEE
19818085
209UbiquitinationGTCSSDEKSAFLKSL
ECCCCHHHHHHHHHC
-
214UbiquitinationDEKSAFLKSLGCDRP
HHHHHHHHHCCCCCC
-
225AcetylationCDRPINYKTEPVGTV
CCCCCCCCCCCCCCE
25953088
225UbiquitinationCDRPINYKTEPVGTV
CCCCCCCCCCCCCCE
-
279PhosphorylationISGYQTPTGLSPVKA
ECCCCCCCCCCCCCC
28348404
282PhosphorylationYQTPTGLSPVKAGTL
CCCCCCCCCCCCCCC
24719451
299PhosphorylationKLLKKSASVQGFFLN
HHHHHCCCHHHHHHH
14702039
357PhosphorylationFRAVNYMYMGKNTGK
HHHHHHHHCCCCCCC
30257219

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 PTGR3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTGR3_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 PTGR3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
MD1L1_HUMANMAD1L1physical
28514442
CCNB1_HUMANCCNB1physical
28514442
CG043_HUMANC7orf43physical
28514442
ODB2_HUMANDBTphysical
28514442
TPC10_HUMANTRAPPC10physical
28514442
CKS2_HUMANCKS2physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PTGR3_HUMAN

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Related Literatures of Post-Translational Modification

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