DHCR7_HUMAN - dbPTM
DHCR7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DHCR7_HUMAN
UniProt AC Q9UBM7
Protein Name 7-dehydrocholesterol reductase
Gene Name DHCR7
Organism Homo sapiens (Human).
Sequence Length 475
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description Production of cholesterol by reduction of C7-C8 double bond of 7-dehydrocholesterol (7-DHC)..
Protein Sequence MAAKSQPNIPKAKSLDGVTNDRTASQGQWGRAWEVDWFSLASVIFLLLFAPFIVYYFIMACDQYSCALTGPVVDIVTGHARLSDIWAKTPPITRKAAQLYTLWVTFQVLLYTSLPDFCHKFLPGYVGGIQEGAVTPAGVVNKYQINGLQAWLLTHLLWFANAHLLSWFSPTIIFDNWIPLLWCANILGYAVSTFAMVKGYFFPTSARDCKFTGNFFYNYMMGIEFNPRIGKWFDFKLFFNGRPGIVAWTLINLSFAAKQRELHSHVTNAMVLVNVLQAIYVIDFFWNETWYLKTIDICHDHFGWYLGWGDCVWLPYLYTLQGLYLVYHPVQLSTPHAVGVLLLGLVGYYIFRVANHQKDLFRRTDGRCLIWGRKPKVIECSYTSADGQRHHSKLLVSGFWGVARHFNYVGDLMGSLAYCLACGGGHLLPYFYIIYMAILLTHRCLRDEHRCASKYGRDWERYTAAVPYRLLPGIF
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
4Ubiquitination----MAAKSQPNIPK
----CCCCCCCCCCC		39.83-
5Phosphorylation---MAAKSQPNIPKA
---CCCCCCCCCCCC		46.2524719451
13UbiquitinationQPNIPKAKSLDGVTN
CCCCCCCCCCCCCCC		58.6421890473
14PhosphorylationPNIPKAKSLDGVTND
CCCCCCCCCCCCCCC		36.2329255136
19PhosphorylationAKSLDGVTNDRTASQ
CCCCCCCCCCCCCCC		36.6123927012
23PhosphorylationDGVTNDRTASQGQWG
CCCCCCCCCCCCCCC		33.2623090842
25PhosphorylationVTNDRTASQGQWGRA
CCCCCCCCCCCCCCC		33.9423090842
88UbiquitinationRLSDIWAKTPPITRK
EHHHHHHHCCCCCHH		46.7121890473
88UbiquitinationRLSDIWAKTPPITRK
EHHHHHHHCCCCCHH		46.7121890473
135PhosphorylationGIQEGAVTPAGVVNK
CCCCCCCCCCCCCCC		13.59-
205PhosphorylationKGYFFPTSARDCKFT
CCEECCCCHHCCEEE		22.88-
231UbiquitinationEFNPRIGKWFDFKLF
EECCCCCCEEEEEEE		42.1721890473
254PhosphorylationAWTLINLSFAAKQRE
HHHHHHHHHHHHHHH		14.3527174698
358UbiquitinationFRVANHQKDLFRRTD
HHHHHCCHHHHHCCC		49.1721890473
358UbiquitinationFRVANHQKDLFRRTD
HHHHHCCHHHHHCCC		49.1721890473
374UbiquitinationRCLIWGRKPKVIECS
CEEEECCCCCEEEEE		45.30-
376UbiquitinationLIWGRKPKVIECSYT
EEECCCCCEEEEEEE		59.90-
381PhosphorylationKPKVIECSYTSADGQ
CCCEEEEEEECCCCC		20.7528152594
382PhosphorylationPKVIECSYTSADGQR
CCEEEEEEECCCCCC		19.1728152594
383PhosphorylationKVIECSYTSADGQRH
CEEEEEEECCCCCCH		10.9328152594
384PhosphorylationVIECSYTSADGQRHH
EEEEEEECCCCCCHH		19.0128152594
397PhosphorylationHHSKLLVSGFWGVAR
HHHHHHHHCHHHHHH		28.39-
453PhosphorylationRDEHRCASKYGRDWE
HCCCCHHHHHCCCHH		30.0030387612
454UbiquitinationDEHRCASKYGRDWER
CCCCHHHHHCCCHHH		32.9521890473
454AcetylationDEHRCASKYGRDWER
CCCCHHHHHCCCHHH		32.9525953088
455PhosphorylationEHRCASKYGRDWERY
CCCHHHHHCCCHHHH		18.2030387612
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 DHCR7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DHCR7_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 DHCR7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of DHCR7_HUMAN !!
Drug and Disease Associations
Kegg Disease
H00161 Smith-Lemli-Opitz syndrome
H00608 46,XY disorders of sex development (Disorders in androgen synthesis or action), including: Congenita
OMIM Disease
270400Smith-Lemli-Opitz syndrome (SLOS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DHCR7_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASSSPECTROMETRY.

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