RDH11_HUMAN - dbPTM
RDH11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RDH11_HUMAN
UniProt AC Q8TC12
Protein Name Retinol dehydrogenase 11
Gene Name RDH11
Organism Homo sapiens (Human).
Sequence Length 318
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type II membrane protein .
Protein Description Exhibits an oxidoreductive catalytic activity towards retinoids. Most efficient as an NADPH-dependent retinal reductase. Displays high activity towards 9-cis and all-trans-retinol. Also involved in the metabolism of short-chain aldehydes. No steroid dehydrogenase activity detected..
Protein Sequence MVELMFPLLLLLLPFLLYMAAPQIRKMLSSGVCTSTVQLPGKVVVVTGANTGIGKETAKELAQRGARVYLACRDVEKGELVAKEIQTTTGNQQVLVRKLDLSDTKSIRAFAKGFLAEEKHLHVLINNAGVMMCPYSKTADGFEMHIGVNHLGHFLLTHLLLEKLKESAPSRIVNVSSLAHHLGRIHFHNLQGEKFYNAGLAYCHSKLANILFTQELARRLKGSGVTTYSVHPGTVQSELVRHSSFMRWMWWLFSFFIKTPQQGAQTSLHCALTEGLEILSGNHFSDCHVAWVSAQARNETIARRLWDVSCDLLGLPID
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
18PhosphorylationLLLPFLLYMAAPQIR
HHHHHHHHHHHHHHH		6.20-
26UbiquitinationMAAPQIRKMLSSGVC
HHHHHHHHHHHCCCC		45.91-
29PhosphorylationPQIRKMLSSGVCTST
HHHHHHHHCCCCCEE		22.8820068231
30PhosphorylationQIRKMLSSGVCTSTV
HHHHHHHCCCCCEEE		31.1420068231
34PhosphorylationMLSSGVCTSTVQLPG
HHHCCCCCEEEECCC		25.6520068231
35PhosphorylationLSSGVCTSTVQLPGK
HHCCCCCEEEECCCE		22.8120068231
36PhosphorylationSSGVCTSTVQLPGKV
HCCCCCEEEECCCEE		8.3020068231
47PhosphorylationPGKVVVVTGANTGIG
CCEEEEEECCCCCCC		20.9720068231
51PhosphorylationVVVTGANTGIGKETA
EEEECCCCCCCHHHH		29.6420068231
55UbiquitinationGANTGIGKETAKELA
CCCCCCCHHHHHHHH		50.3921906983
55UbiquitinationGANTGIGKETAKELA
CCCCCCCHHHHHHHH		50.3921890473
55 (in isoform 1)Ubiquitination-50.3921890473
59UbiquitinationGIGKETAKELAQRGA
CCCHHHHHHHHHCCC		61.76-
70 (in isoform 2)Ubiquitination-3.1221890473
77AcetylationLACRDVEKGELVAKE
EEECCHHHCCEEEEE		58.4926051181
77UbiquitinationLACRDVEKGELVAKE
EEECCHHHCCEEEEE		58.49-
83 (in isoform 1)Ubiquitination-48.1221890473
83UbiquitinationEKGELVAKEIQTTTG
HHCCEEEEEEEECCC		48.1222053931
83UbiquitinationEKGELVAKEIQTTTG
HHCCEEEEEEEECCC		48.1221890473
87PhosphorylationLVAKEIQTTTGNQQV
EEEEEEEECCCCCEE		31.8022817900
88PhosphorylationVAKEIQTTTGNQQVL
EEEEEEECCCCCEEE		19.1422817900
89PhosphorylationAKEIQTTTGNQQVLV
EEEEEECCCCCEEEE		37.2122817900
92 (in isoform 2)Ubiquitination-35.7821890473
98UbiquitinationNQQVLVRKLDLSDTK
CCEEEEEECCCCCCH		38.58-
99 (in isoform 2)Ubiquitination-5.8521890473
104PhosphorylationRKLDLSDTKSIRAFA
EECCCCCCHHHHHHH		24.2623312004
105MalonylationKLDLSDTKSIRAFAK
ECCCCCCHHHHHHHH		49.2130639696
105UbiquitinationKLDLSDTKSIRAFAK
ECCCCCCHHHHHHHH		49.2121890473
105UbiquitinationKLDLSDTKSIRAFAK
ECCCCCCHHHHHHHH		49.2121890473
105UbiquitinationKLDLSDTKSIRAFAK
ECCCCCCHHHHHHHH		49.2121890473
1052-HydroxyisobutyrylationKLDLSDTKSIRAFAK
ECCCCCCHHHHHHHH		49.21-
105 (in isoform 1)Ubiquitination-49.2121890473
106PhosphorylationLDLSDTKSIRAFAKG
CCCCCCHHHHHHHHH		21.2823312004
112 (in isoform 1)Ubiquitination-43.6821890473
112UbiquitinationKSIRAFAKGFLAEEK
HHHHHHHHHHHHCCC		43.6821890473
112UbiquitinationKSIRAFAKGFLAEEK
HHHHHHHHHHHHCCC		43.6821890473
112UbiquitinationKSIRAFAKGFLAEEK
HHHHHHHHHHHHCCC		43.6821890473
112AcetylationKSIRAFAKGFLAEEK
HHHHHHHHHHHHCCC		43.6819608861
1652-HydroxyisobutyrylationHLLLEKLKESAPSRI
HHHHHHHHHHCCCCE		61.77-
165UbiquitinationHLLLEKLKESAPSRI
HHHHHHHHHHCCCCE		61.77-
176PhosphorylationPSRIVNVSSLAHHLG
CCCEEEHHHHHHHHC		17.9027251275
177PhosphorylationSRIVNVSSLAHHLGR
CCEEEHHHHHHHHCC		25.8728857561
194UbiquitinationFHNLQGEKFYNAGLA
EECCCCCHHHCCCHH		61.03-
196PhosphorylationNLQGEKFYNAGLAYC
CCCCCHHHCCCHHHH		18.3822817900
205PhosphorylationAGLAYCHSKLANILF
CCHHHHHHHHHHHHH		26.2928857561
206UbiquitinationGLAYCHSKLANILFT
CHHHHHHHHHHHHHH		28.14-
208 (in isoform 2)Ubiquitination-12.5421890473
221UbiquitinationQELARRLKGSGVTTY
HHHHHHHCCCCCCEE		49.582190698
221 (in isoform 1)Ubiquitination-49.5821890473
244PhosphorylationSELVRHSSFMRWMWW
HHHHHHHHHHHHHHH		19.5524719451
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 RDH11_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RDH11_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 RDH11_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ROBO2_HUMANROBO2physical
21900206
CAH12_HUMANCA12physical
21900206
BL1S2_HUMANBLOC1S2physical
21900206
RDH11_HUMANRDH11physical
21900206
UBAC1_HUMANUBAC1physical
26186194
UBAC1_HUMANUBAC1physical
28514442
CCHL_HUMANHCCSphysical
27173435
COMT_HUMANCOMTphysical
27173435
ESYT1_HUMANESYT1physical
27173435
TMX1_HUMANTMX1physical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
616108Retinal dystrophy, juvenile cataracts, and short stature syndrome (RDJCSS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00162Vitamin A
Regulatory Network of RDH11_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-112, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-89, AND MASSSPECTROMETRY.

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