RETST_HUMAN - dbPTM
RETST_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RETST_HUMAN
UniProt AC Q6NUM9
Protein Name All-trans-retinol 13,14-reductase
Gene Name RETSAT
Organism Homo sapiens (Human).
Sequence Length 610
Subcellular Localization Endoplasmic reticulum membrane
Peripheral membrane protein .
Protein Description Catalyzes the saturation of all-trans-retinol to all-trans-13,14-dihydroretinol. Does not exhibit any activity toward all-trans-retinoic acid, nor 9-cis, 11-cis or 13-cis-retinol isomers. May play a role in the metabolism of vitamin A. Independently of retinol conversion, may regulate liver metabolism upstream of MLXIPL/ChREBP. May play a role in adipocyte differentiation..
Protein Sequence MWLPLVLLLAVLLLAVLCKVYLGLFSGSSPNPFSEDVKRPPAPLVTDKEARKKVLKQAFSANQVPEKLDVVVIGSGFGGLAAAAILAKAGKRVLVLEQHTKAGGCCHTFGKNGLEFDTGIHYIGRMEEGSIGRFILDQITEGQLDWAPLSSPFDIMVLEGPNGRKEYPMYSGEKAYIQGLKEKFPQEEAIIDKYIKLVKVVSSGAPHAILLKFLPLPVVQLLDRCGLLTRFSPFLQASTQSLAEVLQQLGASSELQAVLSYIFPTYGVTPNHSAFSMHALLVNHYMKGGFYPRGGSSEIAFHTIPVIQRAGGAVLTKATVQSVLLDSAGKACGVSVKKGHELVNIYCPIVVSNAGLFNTYEHLLPGNARCLPGVKQQLGTVRPGLGMTSVFICLRGTKEDLHLPSTNYYVYYDTDMDQAMERYVSMPREEAAEHIPLLFFAFPSAKDPTWEDRFPGRSTMIMLIPTAYEWFEEWQAELKGKRGSDYETFKNSFVEASMSVVLKLFPQLEGKVESVTAGSPLTNQFYLAAPRGACYGADHDLGRLHPCVMASLRAQSPIPNLYLTGQDIFTCGLVGALQGALLCSSAILKRNLYSDLKNLDSRIRAQKKKN
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
29PhosphorylationLGLFSGSSPNPFSED
HHHCCCCCCCCCCCC		32.02-
482-HydroxyisobutyrylationPAPLVTDKEARKKVL
CCCCCCCHHHHHHHH		43.86-
48UbiquitinationPAPLVTDKEARKKVL
CCCCCCCHHHHHHHH		43.8621906983
48MalonylationPAPLVTDKEARKKVL
CCCCCCCHHHHHHHH		43.8626320211
48 (in isoform 1)Ubiquitination-43.8621890473
48 (in isoform 2)Ubiquitination-43.8621890473
52UbiquitinationVTDKEARKKVLKQAF
CCCHHHHHHHHHHHH		55.0422817900
53UbiquitinationTDKEARKKVLKQAFS
CCHHHHHHHHHHHHH		47.4422817900
56UbiquitinationEARKKVLKQAFSANQ
HHHHHHHHHHHHCCC		42.4421906983
56MalonylationEARKKVLKQAFSANQ
HHHHHHHHHHHHCCC		42.4426320211
56 (in isoform 1)Ubiquitination-42.4421890473
56 (in isoform 2)Ubiquitination-42.4421890473
60PhosphorylationKVLKQAFSANQVPEK
HHHHHHHHCCCCCCC		29.3522985185
100PhosphorylationVLVLEQHTKAGGCCH
EEEEEECCCCCCCCC		23.4524667141
101AcetylationLVLEQHTKAGGCCHT
EEEEECCCCCCCCCC		42.8025953088
101MalonylationLVLEQHTKAGGCCHT
EEEEECCCCCCCCCC		42.8026320211
111AcetylationGCCHTFGKNGLEFDT
CCCCCCCCCCEEECC		43.5926051181
111UbiquitinationGCCHTFGKNGLEFDT
CCCCCCCCCCEEECC		43.5921963094
165 (in isoform 2)Ubiquitination-64.1021890473
165UbiquitinationLEGPNGRKEYPMYSG
EECCCCCCCCCCCCC		64.1022817900
165 (in isoform 1)Ubiquitination-64.1021890473
167PhosphorylationGPNGRKEYPMYSGEK
CCCCCCCCCCCCCCH		9.0626657352
170PhosphorylationGRKEYPMYSGEKAYI
CCCCCCCCCCCHHHH		14.7126657352
171PhosphorylationRKEYPMYSGEKAYIQ
CCCCCCCCCCHHHHH		33.9428060719
174UbiquitinationYPMYSGEKAYIQGLK
CCCCCCCHHHHHHHH		50.4423000965
174 (in isoform 1)Ubiquitination-50.4421890473
174 (in isoform 2)Ubiquitination-50.4421890473
176PhosphorylationMYSGEKAYIQGLKEK
CCCCCHHHHHHHHHH		12.5828060719
181UbiquitinationKAYIQGLKEKFPQEE
HHHHHHHHHHCCHHH		66.7321906983
181 (in isoform 2)Ubiquitination-66.7321890473
181 (in isoform 1)Ubiquitination-66.7321890473
183UbiquitinationYIQGLKEKFPQEEAI
HHHHHHHHCCHHHHH		61.8421906983
183 (in isoform 2)Ubiquitination-61.8421890473
183AcetylationYIQGLKEKFPQEEAI
HHHHHHHHCCHHHHH		61.8420167786
183 (in isoform 1)Ubiquitination-61.8421890473
193UbiquitinationQEEAIIDKYIKLVKV
HHHHHHHHHHHHHHH		38.1721906983
193 (in isoform 2)Ubiquitination-38.1721890473
193 (in isoform 1)Ubiquitination-38.1721890473
196UbiquitinationAIIDKYIKLVKVVSS
HHHHHHHHHHHHHCC		44.1022817900
199UbiquitinationDKYIKLVKVVSSGAP
HHHHHHHHHHCCCCC		47.5622817900
199 (in isoform 2)Ubiquitination-47.5621890473
199AcetylationDKYIKLVKVVSSGAP
HHHHHHHHHHCCCCC		47.5626051181
199 (in isoform 1)Ubiquitination-47.5621890473
212UbiquitinationAPHAILLKFLPLPVV
CCCCHHHHHCCCCHH		41.2233845483
293MethylationMKGGFYPRGGSSEIA
HCCCCCCCCCCCCEE		51.21115491139
296PhosphorylationGFYPRGGSSEIAFHT
CCCCCCCCCCEEEEC		27.85-
316PhosphorylationRAGGAVLTKATVQSV
ECCCEEECHHHHHHH		16.43-
317 (in isoform 2)Ubiquitination-37.5921890473
317 (in isoform 1)Ubiquitination-37.5921890473
317UbiquitinationAGGAVLTKATVQSVL
CCCEEECHHHHHHHH		37.5921906983
330UbiquitinationVLLDSAGKACGVSVK
HHHCCCCHHCCEEEC		39.9729967540
337UbiquitinationKACGVSVKKGHELVN
HHCCEEECCCCCEEE		45.6029967540
380PhosphorylationGVKQQLGTVRPGLGM
CHHHHCCCCCCCCCC		23.1823898821
388PhosphorylationVRPGLGMTSVFICLR
CCCCCCCEEEEEEEC		21.6823898821
389PhosphorylationRPGLGMTSVFICLRG
CCCCCCEEEEEEECC		13.2123898821
397PhosphorylationVFICLRGTKEDLHLP
EEEEECCCCCCCCCC		25.4823898821
408PhosphorylationLHLPSTNYYVYYDTD
CCCCCCCEEEEEECC		8.39-
412PhosphorylationSTNYYVYYDTDMDQA
CCCEEEEEECCHHHH		11.43-
423PhosphorylationMDQAMERYVSMPREE
HHHHHHHHHCCCHHH		5.42-
446UbiquitinationFFAFPSAKDPTWEDR
EEECCCCCCCCHHHC		69.4521963094
453MethylationKDPTWEDRFPGRSTM
CCCCHHHCCCCCCEE		28.30115491131
471 (in isoform 2)Phosphorylation-3.9929083192
474 (in isoform 2)Phosphorylation-8.7629083192
481UbiquitinationWQAELKGKRGSDYET
HHHHHCCCCCCCHHH		52.5829967540
484PhosphorylationELKGKRGSDYETFKN
HHCCCCCCCHHHHHH		40.8428355574
486PhosphorylationKGKRGSDYETFKNSF
CCCCCCCHHHHHHHH		20.6828796482
488PhosphorylationKRGSDYETFKNSFVE
CCCCCHHHHHHHHHH		33.4123927012
511UbiquitinationLFPQLEGKVESVTAG
HHHHHCCCEEEEECC		33.1921963094
519PhosphorylationVESVTAGSPLTNQFY
EEEEECCCCCCCCEE		17.8027050516
597 (in isoform 1)Ubiquitination-61.5321890473
597UbiquitinationRNLYSDLKNLDSRIR
CCHHHHHCCHHHHHH		61.5322817900
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 RETST_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RETST_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 RETST_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
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 RETST_HUMAN

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Related Literatures of Post-Translational Modification

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