RDH12_HUMAN - dbPTM
RDH12_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RDH12_HUMAN
UniProt AC Q96NR8
Protein Name Retinol dehydrogenase 12
Gene Name RDH12
Organism Homo sapiens (Human).
Sequence Length 316
Subcellular Localization
Protein Description Exhibits an oxidoreductive catalytic activity towards retinoids. Most efficient as an NADPH-dependent retinal reductase. Displays high activity toward 9-cis and all-trans-retinol. Also involved in the metabolism of short-chain aldehydes. No steroid dehydrogenase activity detected. Might be the key enzyme in the formation of 11-cis-retinal from 11-cis-retinol during regeneration of the cone visual pigments..
Protein Sequence MLVTLGLLTSFFSFLYMVAPSIRKFFAGGVCRTNVQLPGKVVVITGANTGIGKETARELASRGARVYIACRDVLKGESAASEIRVDTKNSQVLVRKLDLSDTKSIRAFAEGFLAEEKQLHILINNAGVMMCPYSKTADGFETHLGVNHLGHFLLTYLLLERLKVSAPARVVNVSSVAHHIGKIPFHDLQSEKRYSRGFAYCHSKLANVLFTRELAKRLQGTGVTTYAVHPGVVRSELVRHSSLLCLLWRLFSPFVKTAREGAQTSLHCALAEGLEPLSGKYFSDCKRTWVSPRARNNKTAERLWNVSCELLGIRWE
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
4Phosphorylation----MLVTLGLLTSF
----CCHHHHHHHHH
15.9024043423
9PhosphorylationLVTLGLLTSFFSFLY
CHHHHHHHHHHHHHH
28.6424043423
10PhosphorylationVTLGLLTSFFSFLYM
HHHHHHHHHHHHHHH
25.0224043423
13PhosphorylationGLLTSFFSFLYMVAP
HHHHHHHHHHHHHCH
16.6024043423
16PhosphorylationTSFFSFLYMVAPSIR
HHHHHHHHHHCHHHH
6.3724043423
21PhosphorylationFLYMVAPSIRKFFAG
HHHHHCHHHHHHHCC
25.8624043423
45PhosphorylationPGKVVVITGANTGIG
CCCEEEEECCCCCCC
20.7324719451
49PhosphorylationVVITGANTGIGKETA
EEEECCCCCCCHHHH
29.6424719451
61PhosphorylationETARELASRGARVYI
HHHHHHHHCCCEEEE
43.8224719451
78PhosphorylationRDVLKGESAASEIRV
HHHHCCCCCCCEEEE
37.4923403867
81PhosphorylationLKGESAASEIRVDTK
HCCCCCCCEEEEECC
33.0223403867
90PhosphorylationIRVDTKNSQVLVRKL
EEEECCCCEEEEEEC
24.1928857561
96UbiquitinationNSQVLVRKLDLSDTK
CCEEEEEECCCCCCH
38.58-
102PhosphorylationRKLDLSDTKSIRAFA
EECCCCCCHHHHHHH
24.2623312004
103UbiquitinationKLDLSDTKSIRAFAE
ECCCCCCHHHHHHHH
49.2121890473
103UbiquitinationKLDLSDTKSIRAFAE
ECCCCCCHHHHHHHH
49.2121890473
104PhosphorylationLDLSDTKSIRAFAEG
CCCCCCHHHHHHHHC
21.2823312004
165PhosphorylationLLERLKVSAPARVVN
HHHHHCCCCCCEEEE
27.2626437602
174PhosphorylationPARVVNVSSVAHHIG
CCEEEEHHHHHHHCC
17.5626437602
175PhosphorylationARVVNVSSVAHHIGK
CEEEEHHHHHHHCCC
21.0226437602
225PhosphorylationLQGTGVTTYAVHPGV
HCCCCCEEEEECCCC
13.69-

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 RDH12_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RDH12_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 RDH12_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AGFG1_HUMANAGFG1physical
26186194
UBE2T_HUMANUBE2Tphysical
26186194
RN123_HUMANRNF123physical
26186194
CCD25_HUMANCCDC25physical
26186194
UB2D2_HUMANUBE2D2physical
26186194
ARCH_HUMANZBTB8OSphysical
26186194
UB2E3_HUMANUBE2E3physical
26186194
LASP1_HUMANLASP1physical
26186194
ARPIN_HUMANARPINphysical
26186194
ARFG1_HUMANARFGAP1physical
26186194
TKFC_HUMANDAKphysical
26186194
UBAC1_HUMANUBAC1physical
26186194
TKFC_HUMANDAKphysical
28514442
LASP1_HUMANLASP1physical
28514442
4EBP2_HUMANEIF4EBP2physical
28514442
UB2E3_HUMANUBE2E3physical
28514442
ARPIN_HUMANARPINphysical
28514442
STABP_HUMANSTAMBPphysical
28514442
RN123_HUMANRNF123physical
28514442
TES_HUMANTESphysical
28514442
PMVK_HUMANPMVKphysical
28514442
CGL_HUMANCTHphysical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612712Leber congenital amaurosis 13 (LCA13)
612712Retinitis pigmentosa 53 (RP53)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00162Vitamin A
Regulatory Network of RDH12_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP