DHC24_HUMAN - dbPTM
DHC24_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DHC24_HUMAN
UniProt AC Q15392
Protein Name Delta(24)-sterol reductase
Gene Name DHCR24
Organism Homo sapiens (Human).
Sequence Length 516
Subcellular Localization Endoplasmic reticulum membrane
Single-pass membrane protein. Golgi apparatus membrane
Single-pass membrane protein.
Protein Description Catalyzes the reduction of the Delta-24 double bond of sterol intermediates. Protects cells from oxidative stress by reducing caspase 3 activity during apoptosis induced by oxidative stress. Also protects against amyloid-beta peptide-induced apoptosis..
Protein Sequence MEPAVSLAVCALLFLLWVRLKGLEFVLIHQRWVFVCLFLLPLSLIFDIYYYVRAWVVFKLSSAPRLHEQRVRDIQKQVREWKEQGSKTFMCTGRPGWLTVSLRVGKYKKTHKNIMINLMDILEVDTKKQIVRVEPLVTMGQVTALLTSIGWTLPVLPELDDLTVGGLIMGTGIESSSHKYGLFQHICTAYELVLADGSFVRCTPSENSDLFYAVPWSCGTLGFLVAAEIRIIPAKKYVKLRFEPVRGLEAICAKFTHESQRQENHFVEGLLYSLDEAVIMTGVMTDEAEPSKLNSIGNYYKPWFFKHVENYLKTNREGLEYIPLRHYYHRHTRSIFWELQDIIPFGNNPIFRYLFGWMVPPKISLLKLTQGETLRKLYEQHHVVQDMLVPMKCLQQALHTFQNDIHVYPIWLCPFILPSQPGLVHPKGNEAELYIDIGAYGEPRVKHFEARSCMRQLEKFVRSVHGFQMLYADCYMNREEFWEMFDGSLYHKLREKLGCQDAFPEVYDKICKAARH
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
46UbiquitinationLLPLSLIFDIYYYVR
HHHHHHHHHHHHHHH		5.92-
76UbiquitinationQRVRDIQKQVREWKE
HHHHHHHHHHHHHHH		51.6121906983
82UbiquitinationQKQVREWKEQGSKTF
HHHHHHHHHHCCCEE		35.0929967540
87UbiquitinationEWKEQGSKTFMCTGR
HHHHHCCCEEEECCC		53.2429901268
87AcetylationEWKEQGSKTFMCTGR
HHHHHCCCEEEECCC		53.2427452117
110PhosphorylationRVGKYKKTHKNIMIN
EEECCCCCCCCCEEE		33.6522817900
180PhosphorylationIESSSHKYGLFQHIC
CCCCCHHHCHHHHHH		17.40-
188PhosphorylationGLFQHICTAYELVLA
CHHHHHHHHHHHHHC		31.50-
190PhosphorylationFQHICTAYELVLADG
HHHHHHHHHHHHCCC		7.52-
198PhosphorylationELVLADGSFVRCTPS
HHHHCCCCEEECCCC		22.55-
213UbiquitinationENSDLFYAVPWSCGT
CCCCCEEECCCCCCH		8.12-
239UbiquitinationIPAKKYVKLRFEPVR
EECHHEEEEEEEECC		30.7524816145
254AcetylationGLEAICAKFTHESQR
CHHHHHHHCCCHHHH		46.5126051181
254UbiquitinationGLEAICAKFTHESQR
CHHHHHHHCCCHHHH		46.5123000965
260UbiquitinationAKFTHESQRQENHFV
HHCCCHHHHHHCCHH		48.36-
272PhosphorylationHFVEGLLYSLDEAVI
CHHHHHHHCCCHHHH		16.5424043423
272UbiquitinationHFVEGLLYSLDEAVI
CHHHHHHHCCCHHHH		16.54-
273PhosphorylationFVEGLLYSLDEAVIM
HHHHHHHCCCHHHHH		29.3424043423
281PhosphorylationLDEAVIMTGVMTDEA
CCHHHHHHCCCCCCC		18.5924043423
285PhosphorylationVIMTGVMTDEAEPSK
HHHHCCCCCCCCHHH		28.4324043423
291PhosphorylationMTDEAEPSKLNSIGN
CCCCCCHHHCCCCCC		41.0824043423
299PhosphorylationKLNSIGNYYKPWFFK
HCCCCCCCCCHHHHH		13.9822817900
300PhosphorylationLNSIGNYYKPWFFKH
CCCCCCCCCHHHHHH		17.9922817900
301UbiquitinationNSIGNYYKPWFFKHV
CCCCCCCCHHHHHHH		25.9722817900
306UbiquitinationYYKPWFFKHVENYLK
CCCHHHHHHHHHHHH		36.9522817900
311PhosphorylationFFKHVENYLKTNREG
HHHHHHHHHHHCCCC		8.9628152594
313AcetylationKHVENYLKTNREGLE
HHHHHHHHHCCCCCC		33.1327452117
313MethylationKHVENYLKTNREGLE
HHHHHHHHHCCCCCC		33.13-
313UbiquitinationKHVENYLKTNREGLE
HHHHHHHHHCCCCCC		33.1321906983
321PhosphorylationTNREGLEYIPLRHYY
HCCCCCCCCCHHHHC		16.9328152594
326UbiquitinationLEYIPLRHYYHRHTR
CCCCCHHHHCCHHCC		34.8821890473
335UbiquitinationYHRHTRSIFWELQDI
CCHHCCHHHEEHHHH		4.13-
362UbiquitinationFGWMVPPKISLLKLT
HCCCCCCCEEEEECC		38.5723000965
364PhosphorylationWMVPPKISLLKLTQG
CCCCCCEEEEECCCC		33.5024719451
367UbiquitinationPPKISLLKLTQGETL
CCCEEEEECCCCHHH		55.5723000965
373PhosphorylationLKLTQGETLRKLYEQ
EECCCCHHHHHHHHH		38.39-
376UbiquitinationTQGETLRKLYEQHHV
CCCHHHHHHHHHHCC		59.5422817900
418UbiquitinationWLCPFILPSQPGLVH
ECCCEECCCCCCCCC		26.54-
427UbiquitinationQPGLVHPKGNEAELY
CCCCCCCCCCEEEEE		60.53-
446SumoylationAYGEPRVKHFEARSC
CCCCCCCCHHHHHHH		43.80-
446AcetylationAYGEPRVKHFEARSC
CCCCCCCCHHHHHHH		43.8026051181
446UbiquitinationAYGEPRVKHFEARSC
CCCCCCCCHHHHHHH		43.8021890473
451UbiquitinationRVKHFEARSCMRQLE
CCCHHHHHHHHHHHH		24.1621890473
455UbiquitinationFEARSCMRQLEKFVR
HHHHHHHHHHHHHHH		42.11-
459UbiquitinationSCMRQLEKFVRSVHG
HHHHHHHHHHHHHHH		58.7224816145
459AcetylationSCMRQLEKFVRSVHG
HHHHHHHHHHHHHHH		58.7227452117
468UbiquitinationVRSVHGFQMLYADCY
HHHHHHHHHHEEECC		26.09-
484SulfoxidationNREEFWEMFDGSLYH
CHHHHHHHCCHHHHH		2.4328465586
492UbiquitinationFDGSLYHKLREKLGC
CCHHHHHHHHHHHCC		35.3723000965
4962-HydroxyisobutyrylationLYHKLREKLGCQDAF
HHHHHHHHHCCCCCC		43.69-
496MalonylationLYHKLREKLGCQDAF
HHHHHHHHHCCCCCC		43.6930639696
496UbiquitinationLYHKLREKLGCQDAF
HHHHHHHHHCCCCCC		43.6923000965
507PhosphorylationQDAFPEVYDKICKAA
CCCCHHHHHHHHHHH		15.1728796482
509UbiquitinationAFPEVYDKICKAARH
CCHHHHHHHHHHHCC		32.1124816145
512UbiquitinationEVYDKICKAARH---
HHHHHHHHHHCC---		48.8627667366
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 DHC24_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DHC24_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 DHC24_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P53_HUMANTP53physical
15577914
ACTA_HUMANACTA2physical
26186194
AT12A_HUMANATP12Aphysical
26186194
FUND2_HUMANFUNDC2physical
26186194
REEP5_HUMANREEP5physical
26186194
ERAP1_HUMANERAP1physical
26186194
RASH_HUMANHRASphysical
26186194
LUZP1_HUMANLUZP1physical
26186194
LUZP1_HUMANLUZP1physical
28514442
FUND2_HUMANFUNDC2physical
28514442
ERAP1_HUMANERAP1physical
28514442
AT12A_HUMANATP12Aphysical
28514442
ACTA_HUMANACTA2physical
28514442
RASH_HUMANHRASphysical
28514442
Drug and Disease Associations
Kegg Disease
H00617 Desmosterolosis
OMIM Disease
602398Desmosterolosis (DESMOS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DHC24_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-110, AND MASSSPECTROMETRY.

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