HMDH_HUMAN - dbPTM
HMDH_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HMDH_HUMAN
UniProt AC P04035
Protein Name 3-hydroxy-3-methylglutaryl-coenzyme A reductase
Gene Name HMGCR {ECO:0000312|HGNC:HGNC:5006}
Organism Homo sapiens (Human).
Sequence Length 888
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein.
Protein Description Transmembrane glycoprotein that is the rate-limiting enzyme in cholesterol biosynthesis as well as in the biosynthesis of nonsterol isoprenoids that are essential for normal cell function including ubiquinone and geranylgeranyl proteins..
Protein Sequence MLSRLFRMHGLFVASHPWEVIVGTVTLTICMMSMNMFTGNNKICGWNYECPKFEEDVLSSDIIILTITRCIAILYIYFQFQNLRQLGSKYILGIAGLFTIFSSFVFSTVVIHFLDKELTGLNEALPFFLLLIDLSRASTLAKFALSSNSQDEVRENIARGMAILGPTFTLDALVECLVIGVGTMSGVRQLEIMCCFGCMSVLANYFVFMTFFPACVSLVLELSRESREGRPIWQLSHFARVLEEEENKPNPVTQRVKMIMSLGLVLVHAHSRWIADPSPQNSTADTSKVSLGLDENVSKRIEPSVSLWQFYLSKMISMDIEQVITLSLALLLAVKYIFFEQTETESTLSLKNPITSPVVTQKKVPDNCCRREPMLVRNNQKCDSVEEETGINRERKVEVIKPLVAETDTPNRATFVVGNSSLLDTSSVLVTQEPEIELPREPRPNEECLQILGNAEKGAKFLSDAEIIQLVNAKHIPAYKLETLMETHERGVSIRRQLLSKKLSEPSSLQYLPYRDYNYSLVMGACCENVIGYMPIPVGVAGPLCLDEKEFQVPMATTEGCLVASTNRGCRAIGLGGGASSRVLADGMTRGPVVRLPRACDSAEVKAWLETSEGFAVIKEAFDSTSRFARLQKLHTSIAGRNLYIRFQSRSGDAMGMNMISKGTEKALSKLHEYFPEMQILAVSGNYCTDKKPAAINWIEGRGKSVVCEAVIPAKVVREVLKTTTEAMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSNCITLMEASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQMLGVQGACKDNPGENARQLARIVCGTVMAGELSLMAALAAGHLVKSHMIHNRSKINLQDLQGACTKKTA
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
73UbiquitinationTITRCIAILYIYFQF
HHHHHHHHHHHHHHH		1.2021890473
89UbiquitinationNLRQLGSKYILGIAG
CHHHHCHHHHHHHHH		34.2214593114
142UbiquitinationSRASTLAKFALSSNS
HHHHHHHHHHHCCCC		33.9921890473
142 (in isoform 2)Ubiquitination-33.9921890473
142 (in isoform 1)Ubiquitination-33.9921890473
248UbiquitinationVLEEEENKPNPVTQR
HHHHHHCCCCCHHHH		49.8315247208
248 (in isoform 2)Ubiquitination-49.8321890473
248 (in isoform 1)Ubiquitination-49.8321890473
253PhosphorylationENKPNPVTQRVKMIM
HCCCCCHHHHHHHHH		16.3522210691
261PhosphorylationQRVKMIMSLGLVLVH
HHHHHHHHHCCHHHH		14.3624114839
271PhosphorylationLVLVHAHSRWIADPS
CHHHHHHHHCCCCCC		30.0522210691
278PhosphorylationSRWIADPSPQNSTAD
HHCCCCCCCCCCCCC		39.4021406692
281N-linked_GlycosylationIADPSPQNSTADTSK
CCCCCCCCCCCCCCC		44.72UniProtKB CARBOHYD
282PhosphorylationADPSPQNSTADTSKV
CCCCCCCCCCCCCCE		21.5221406692
283PhosphorylationDPSPQNSTADTSKVS
CCCCCCCCCCCCCEE		35.7821406692
286PhosphorylationPQNSTADTSKVSLGL
CCCCCCCCCCEECCC		28.1621406692
287PhosphorylationQNSTADTSKVSLGLD
CCCCCCCCCEECCCC		31.4421406692
288UbiquitinationNSTADTSKVSLGLDE
CCCCCCCCEECCCCC		37.6321906983
288 (in isoform 2)Ubiquitination-37.6321890473
288 (in isoform 1)Ubiquitination-37.6321890473
296N-linked_GlycosylationVSLGLDENVSKRIEP
EECCCCCCHHHCCCC		42.92UniProtKB CARBOHYD
299UbiquitinationGLDENVSKRIEPSVS
CCCCCHHHCCCCCHH		53.7821906983
299 (in isoform 2)Ubiquitination-53.7821890473
299 (in isoform 1)Ubiquitination-53.7821890473
351UbiquitinationTESTLSLKNPITSPV
CCCEECCCCCCCCCC		58.2521906983
351 (in isoform 1)Ubiquitination-58.2521890473
351 (in isoform 2)Ubiquitination-58.2521890473
355PhosphorylationLSLKNPITSPVVTQK
ECCCCCCCCCCCCCC		28.3830266825
356PhosphorylationSLKNPITSPVVTQKK
CCCCCCCCCCCCCCC		19.2030266825
360PhosphorylationPITSPVVTQKKVPDN
CCCCCCCCCCCCCCC		34.6030266825
362UbiquitinationTSPVVTQKKVPDNCC
CCCCCCCCCCCCCCC		46.5021906983
362 (in isoform 2)Ubiquitination-46.5021890473
362 (in isoform 1)Ubiquitination-46.5021890473
363UbiquitinationSPVVTQKKVPDNCCR
CCCCCCCCCCCCCCC		49.54-
363 (in isoform 2)Ubiquitination-49.54-
381UbiquitinationMLVRNNQKCDSVEEE
EEECCCCCCCCHHHH		41.9821906983
381 (in isoform 2)Ubiquitination-41.9821890473
381 (in isoform 1)Ubiquitination-41.9821890473
384PhosphorylationRNNQKCDSVEEETGI
CCCCCCCCHHHHHCC		40.6825072903
389PhosphorylationCDSVEEETGINRERK
CCCHHHHHCCCHHHC		46.79-
391UbiquitinationSVEEETGINRERKVE
CHHHHHCCCHHHCEE		6.0021890473
396UbiquitinationTGINRERKVEVIKPL
HCCCHHHCEEEECCC		37.6821906983
396 (in isoform 2)Ubiquitination-37.6821890473
396 (in isoform 1)Ubiquitination-37.6821890473
401UbiquitinationERKVEVIKPLVAETD
HHCEEEECCCEEECC		37.1621906983
401 (in isoform 2)Ubiquitination-37.1621890473
401 (in isoform 1)Ubiquitination-37.1621890473
405UbiquitinationEVIKPLVAETDTPNR
EEECCCEEECCCCCC		22.9621890473
407PhosphorylationIKPLVAETDTPNRAT
ECCCEEECCCCCCEE		35.1225850435
409PhosphorylationPLVAETDTPNRATFV
CCEEECCCCCCEEEE		29.8629496963
411UbiquitinationVAETDTPNRATFVVG
EEECCCCCCEEEEEC		48.5921890473
419N-linked_GlycosylationRATFVVGNSSLLDTS
CEEEEECCCHHCCCC		19.47UniProtKB CARBOHYD
420PhosphorylationATFVVGNSSLLDTSS
EEEEECCCHHCCCCC		19.2126657352
421PhosphorylationTFVVGNSSLLDTSSV
EEEECCCHHCCCCCE		36.6326074081
425PhosphorylationGNSSLLDTSSVLVTQ
CCCHHCCCCCEEEEC		23.9128348404
427PhosphorylationSSLLDTSSVLVTQEP
CHHCCCCCEEEECCC		22.89-
431PhosphorylationDTSSVLVTQEPEIEL
CCCCEEEECCCCCCC		24.05-
457UbiquitinationQILGNAEKGAKFLSD
HHHCCHHHHCCCCCH		62.85-
460UbiquitinationGNAEKGAKFLSDAEI
CCHHHHCCCCCHHHH		56.3521890473
460 (in isoform 2)Ubiquitination-56.3521890473
460 (in isoform 1)Ubiquitination-56.3521890473
463PhosphorylationEKGAKFLSDAEIIQL
HHHCCCCCHHHHHHH		37.60-
474UbiquitinationIIQLVNAKHIPAYKL
HHHHHCCCCCCCCHH		36.5421890473
474 (in isoform 2)Ubiquitination-36.5421890473
474 (in isoform 1)Ubiquitination-36.5421890473
480UbiquitinationAKHIPAYKLETLMET
CCCCCCCHHHHHHHH		41.7921890473
480 (in isoform 2)Ubiquitination-41.7921890473
480 (in isoform 1)Ubiquitination-41.7921890473
485SulfoxidationAYKLETLMETHERGV
CCHHHHHHHHHHHHH		7.9321406390
500PhosphorylationSIRRQLLSKKLSEPS
HHHHHHHHCCCCCCC		36.0124719451
502UbiquitinationRRQLLSKKLSEPSSL
HHHHHHCCCCCCCCC		54.6021906983
502 (in isoform 2)Ubiquitination-54.6021890473
502MalonylationRRQLLSKKLSEPSSL
HHHHHHCCCCCCCCC		54.6033225896
502 (in isoform 1)Ubiquitination-54.6021890473
504PhosphorylationQLLSKKLSEPSSLQY
HHHHCCCCCCCCCCC		57.2330631047
507PhosphorylationSKKLSEPSSLQYLPY
HCCCCCCCCCCCCCC		39.3630108239
508PhosphorylationKKLSEPSSLQYLPYR
CCCCCCCCCCCCCCC		30.1530108239
517 (in isoform 2)Phosphorylation-13.6520068231
518N-linked_GlycosylationYLPYRDYNYSLVMGA
CCCCCCCCCHHHHHC		24.98UniProtKB CARBOHYD
519 (in isoform 2)Phosphorylation-9.3520068231
520 (in isoform 2)Phosphorylation-15.7320068231
527 (in isoform 2)Phosphorylation-4.1720068231
528 (in isoform 2)Phosphorylation-55.1820068231
536 (in isoform 2)Phosphorylation-2.1720068231
553 (in isoform 2)Ubiquitination-4.20-
566 (in isoform 2)Ubiquitination-21.1421890473
580PhosphorylationIGLGGGASSRVLADG
ECCCCCHHHCCCCCC		23.1924043423
580 (in isoform 2)Ubiquitination-23.1921890473
581PhosphorylationGLGGGASSRVLADGM
CCCCCHHHCCCCCCC		26.3524043423
589PhosphorylationRVLADGMTRGPVVRL
CCCCCCCCCCCEEEC		37.6926074081
602PhosphorylationRLPRACDSAEVKAWL
ECCCCCCHHHHHHHH		26.6424719451
606UbiquitinationACDSAEVKAWLETSE
CCCHHHHHHHHHCCC		25.91-
609 (in isoform 2)Ubiquitination-6.5121890473
611PhosphorylationEVKAWLETSEGFAVI
HHHHHHHCCCCCHHH		29.8826074081
612PhosphorylationVKAWLETSEGFAVIK
HHHHHHCCCCCHHHH		26.7526074081
613 (in isoform 2)Ubiquitination-66.7921890473
617 (in isoform 2)Ubiquitination-6.32-
619UbiquitinationSEGFAVIKEAFDSTS
CCCCHHHHHHHHCCC		36.0721906983
619 (in isoform 1)Ubiquitination-36.0721890473
633UbiquitinationSRFARLQKLHTSIAG
CHHHHHHHHHHHHCC		46.9921906983
633 (in isoform 1)Ubiquitination-46.9921890473
637PhosphorylationRLQKLHTSIAGRNLY
HHHHHHHHHCCCCEE		10.33-
639 (in isoform 2)Ubiquitination-15.6221890473
644PhosphorylationSIAGRNLYIRFQSRS
HHCCCCEEEEEECCC		8.13-
651 (in isoform 2)Ubiquitination-46.3921890473
662UbiquitinationMGMNMISKGTEKALS
CCCEECCHHHHHHHH		59.9521906983
662 (in isoform 2)Ubiquitination-59.95-
662 (in isoform 1)Ubiquitination-59.9521890473
666UbiquitinationMISKGTEKALSKLHE
ECCHHHHHHHHHHHH		55.2421906983
666 (in isoform 1)Ubiquitination-55.2421890473
670UbiquitinationGTEKALSKLHEYFPE
HHHHHHHHHHHHCCC		55.50-
692SumoylationGNYCTDKKPAAINWI
CCCCCCCCCCCCEEC		42.57-
692UbiquitinationGNYCTDKKPAAINWI
CCCCCCCCCCCCEEC		42.5721906983
692SumoylationGNYCTDKKPAAINWI
CCCCCCCCCCCCEEC		42.57-
692 (in isoform 1)Ubiquitination-42.5721890473
704UbiquitinationNWIEGRGKSVVCEAV
EECCCCCCEEEEEEE		38.422190698
704 (in isoform 1)Ubiquitination-38.4221890473
705O-linked_GlycosylationWIEGRGKSVVCEAVI
ECCCCCCEEEEEEEE		23.7031373491
715UbiquitinationCEAVIPAKVVREVLK
EEEEEEHHHHHHHHH		35.59-
811 (in isoform 2)Ubiquitination-8.08-
820 (in isoform 2)Ubiquitination-1.96-
832 (in isoform 2)Ubiquitination-47.23-
833 (in isoform 2)Ubiquitination-49.31-
864UbiquitinationLAAGHLVKSHMIHNR
HHHHHHHHHHCCCCC		40.79-
870N-linked_GlycosylationVKSHMIHNRSKINLQ
HHHHCCCCCCCCCHH		38.71UniProtKB CARBOHYD
872PhosphorylationSHMIHNRSKINLQDL
HHCCCCCCCCCHHHH		43.1123401153
873UbiquitinationHMIHNRSKINLQDLQ
HCCCCCCCCCHHHHC		32.17-
884PhosphorylationQDLQGACTKKTA---
HHHCCHHCCCCC---		34.73-
885UbiquitinationDLQGACTKKTA----
HHCCHHCCCCC----		48.27-
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
-KUbiquitinationE3 ubiquitin ligaseAMFRQ9UKV5
PMID:16168377
-KUbiquitinationE3 ubiquitin ligaseSYVN1Q86TM6
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
248Kubiquitylation

19458199
872SPhosphorylation

24275569
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 HMDH_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
INSI1_HUMANINSIG1physical
20458442
UBC_HUMANUBCphysical
21343306
ERLN2_HUMANERLIN2physical
21343306
AMFR_HUMANAMFRphysical
21343306
TERA_HUMANVCPphysical
21343306
AUP1_HUMANAUP1physical
23223569
INSI1_HUMANINSIG1physical
23223569
INSI1_HUMANINSIG1physical
16168377
AMFR_HUMANAMFRphysical
16168377
INSI1_HUMANINSIG1physical
21343306
UBIA1_HUMANUBIAD1physical
23169578
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
D00359 Lovastatin (USP/INN); MK-803; ML-530B; Mevacor (TN)
D00434 Simvastatin (JP16/USP/INN); MK-733; Zocor (TN)
D00887 Atorvastatin calcium (USAN); Lipitor (TN)
D00889 Cerivastatin sodium (JAN/USAN); Baycol (TN)
D00892 Fluvastatin sodium (JAN/USAN); Lescol (TN)
D00893 Pravastatin sodium (JP16/USAN); CS-514; Pravachol (TN)
D01862 Pitavastatin calcium (JAN); NK 104; Livalo (TN)
D01915 Rosuvastatin calcium (JAN/USAN); ZD 4522; Crestor (TN)
D02258 Atorvastatin calcium hydrate (JP16); Lipitor (TN)
D03601 Crilvastatin (USAN/INN)
D03643 Dalvastatin (USAN/INN)
D03816 Tenivastatin calcium (USAN)
D07474 Atorvastatin (INN); Lipitor (TN); Sortis (TN)
D07661 Cerivastatin (INN)
D07983 Fluvastatin (INN); Fluvas (TN)
D08410 Pravastatin (INN); Pravator (TN)
D08492 Rosuvastatin (INN); Creston (TN)
DrugBank
DB01076Atorvastatin
DB01095Fluvastatin
DB00227Lovastatin
DB08860Pitavastatin
DB00175Pravastatin
DB01098Rosuvastatin
DB00641Simvastatin
Regulatory Network of HMDH_HUMAN

loading...

Related Literatures of Post-Translational Modification
Ubiquitylation
ReferencePubMed
"Dislocation of HMG-CoA reductase and Insig-1, two polytopicendoplasmic reticulum proteins, en route to proteasomal degradation.";
Leichner G.S., Avner R., Harats D., Roitelman J.;
Mol. Biol. Cell 20:3330-3341(2009).
Cited for: INTERACTION WITH INSIG1, UBIQUITINATION AT LYS-89 AND LYS-248,GLYCOSYLATION, AND MUTAGENESIS OF 75-TYR--TYR-77; LYS-89 AND LYS-248.

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