DHRS4_HUMAN - dbPTM
DHRS4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DHRS4_HUMAN
UniProt AC Q9BTZ2
Protein Name Dehydrogenase/reductase SDR family member 4
Gene Name DHRS4
Organism Homo sapiens (Human).
Sequence Length 278
Subcellular Localization Peroxisome . Isoform 1 is peroxisomal, while isoform 4 is not.
Isoform 7: Nucleus .
Protein Description Reduces all-trans-retinal and 9-cis retinal. Can also catalyze the oxidation of all-trans-retinol with NADP as co-factor, but with much lower efficiency. Reduces alkyl phenyl ketones and alpha-dicarbonyl compounds with aromatic rings, such as pyrimidine-4-aldehyde, 3-benzoylpyridine, 4-benzoylpyridine, menadione and 4-hexanoylpyridine. Has no activity towards aliphatic aldehydes and ketones (By similarity)..
Protein Sequence MHKAGLLGLCARAWNSVRMASSGMTRRDPLANKVALVTASTDGIGFAIARRLAQDGAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVATAVKLHGGIDILVSNAAVNPFFGSIMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLGLTKTLAIELAPRNIRVNCLAPGLIKTSFSRMLWMDKEKEESMKETLRIRRLGEPEDCAGIVSFLCSEDASYITGETVVVGGGTPSRL
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
62PhosphorylationDGAHVVVSSRKQQNV
CCCEEEEECCCCCCH		16.8924275569
63PhosphorylationGAHVVVSSRKQQNVD
CCEEEEECCCCCCHH		31.7128857561
65MalonylationHVVVSSRKQQNVDQA
EEEEECCCCCCHHHH		59.1726320211
65UbiquitinationHVVVSSRKQQNVDQA
EEEEECCCCCCHHHH		59.17-
92AcetylationGTVCHVGKAEDRERL
EEEEECCCHHHHHHH		47.73-
92SuccinylationGTVCHVGKAEDRERL
EEEEECCCHHHHHHH		47.73-
92MalonylationGTVCHVGKAEDRERL
EEEEECCCHHHHHHH		47.7326320211
92SuccinylationGTVCHVGKAEDRERL
EEEEECCCHHHHHHH		47.73-
105AcetylationRLVATAVKLHGGIDI
HHHHHHHHHCCCCCE		32.10-
116UbiquitinationGIDILVSNAAVNPFF
CCCEEEECCCCCHHH		25.1723000965
129 (in isoform 5)Phosphorylation-3.9318669648
140 (in isoform 5)Phosphorylation-7.7918669648
149PhosphorylationVKAPALMTKAVVPEM
CCCCHHHEEEHHHHH		19.3927362937
150UbiquitinationKAPALMTKAVVPEME
CCCHHHEEEHHHHHH		25.8123000965
160UbiquitinationVPEMEKRGGGSVVIV
HHHHHHCCCCEEEEE		56.7523000965
163PhosphorylationMEKRGGGSVVIVSSI
HHHCCCCEEEEEECE		19.2429083192
168PhosphorylationGGSVVIVSSIAAFSP
CCEEEEEECEEEECC		12.6129083192
169PhosphorylationGSVVIVSSIAAFSPS
CEEEEEECEEEECCC		12.8329083192
174PhosphorylationVSSIAAFSPSPGFSP
EECEEEECCCCCCCC		21.5329083192
182UbiquitinationPSPGFSPYNVSKTAL
CCCCCCCCCCCHHHH		27.3123000965
185PhosphorylationGFSPYNVSKTALLGL
CCCCCCCCHHHHHHH		22.20-
194UbiquitinationTALLGLTKTLAIELA
HHHHHHHHHHHHHCC		46.7323000965
216UbiquitinationCLAPGLIKTSFSRML
CCCCCCCHHCHHHHH		43.0623000965
216SuccinylationCLAPGLIKTSFSRML
CCCCCCCHHCHHHHH		43.06-
216AcetylationCLAPGLIKTSFSRML
CCCCCCCHHCHHHHH		43.06-
216SuccinylationCLAPGLIKTSFSRML
CCCCCCCHHCHHHHH		43.06-
220PhosphorylationGLIKTSFSRMLWMDK
CCCHHCHHHHHCCCH		19.29-
227SuccinylationSRMLWMDKEKEESMK
HHHHCCCHHHHHHHH		55.36-
227SuccinylationSRMLWMDKEKEESMK
HHHHCCCHHHHHHHH		55.36-
234SuccinylationKEKEESMKETLRIRR
HHHHHHHHHHHHHHH		57.75-
234SuccinylationKEKEESMKETLRIRR
HHHHHHHHHHHHHHH		57.75-
274PhosphorylationTVVVGGGTPSRL---
EEEECCCCCCCC---		22.74-
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 DHRS4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DHRS4_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 DHRS4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DHRS4_HUMANDHRS4physical
27499296
CLPB_HUMANCLPBphysical
27499296
NDUF5_HUMANNDUFAF5physical
27499296
NDUA5_HUMANNDUFA5physical
27499296
CHCH2_HUMANCHCHD2physical
27499296
RM13_HUMANMRPL13physical
27499296
MPPA_HUMANPMPCAphysical
27499296
NDUS2_HUMANNDUFS2physical
27499296
ECHP_HUMANEHHADHphysical
27499296
TBA8_HUMANEHHADHphysical
27499296
PREP_HUMANPITRM1physical
27499296
MPPB_HUMANPMPCBphysical
27499296
NDUF3_HUMANNDUFAF3physical
27499296
NDUS3_HUMANNDUFS3physical
27499296
PDIP2_HUMANPOLDIP2physical
27499296
NRDC_HUMANNRD1physical
27499296
ECH1_HUMANECH1physical
27499296
ODBA_HUMANBCKDHAphysical
27499296
ATP5E_HUMANATP5Ephysical
27499296
GLRX5_HUMANGLRX5physical
27499296
NDUF8_HUMANC17orf89physical
27499296
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
DB00162Vitamin A
Regulatory Network of DHRS4_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory