HMCS1_HUMAN - dbPTM
HMCS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HMCS1_HUMAN
UniProt AC Q01581
Protein Name Hydroxymethylglutaryl-CoA synthase, cytoplasmic {ECO:0000305}
Gene Name HMGCS1 {ECO:0000312|HGNC:HGNC:5007}
Organism Homo sapiens (Human).
Sequence Length 520
Subcellular Localization Cytoplasm.
Protein Description This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase..
Protein Sequence MPGSLPLNAEACWPKDVGIVALEIYFPSQYVDQAELEKYDGVDAGKYTIGLGQAKMGFCTDREDINSLCMTVVQNLMERNNLSYDCIGRLEVGTETIIDKSKSVKTNLMQLFEESGNTDIEGIDTTNACYGGTAAVFNAVNWIESSSWDGRYALVVAGDIAVYATGNARPTGGVGAVALLIGPNAPLIFERGLRGTHMQHAYDFYKPDMLSEYPIVDGKLSIQCYLSALDRCYSVYCKKIHAQWQKEGNDKDFTLNDFGFMIFHSPYCKLVQKSLARMLLNDFLNDQNRDKNSIYSGLEAFGDVKLEDTYFDRDVEKAFMKASSELFSQKTKASLLVSNQNGNMYTSSVYGSLASVLAQYSPQQLAGKRIGVFSYGSGLAATLYSLKVTQDATPGSALDKITASLCDLKSRLDSRTGVAPDVFAENMKLREDTHHLVNYIPQGSIDSLFEGTWYLVRVDEKHRRTYARRPTPNDDTLDEGVGLVHSNIATEHIPSPAKKVPRLPATAAEPEAAVISNGEH
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
4Phosphorylation----MPGSLPLNAEA
----CCCCCCCCCCH		22.4226846344
12GlutathionylationLPLNAEACWPKDVGI
CCCCCCHHCCCCCEE		4.8722555962
46AcetylationYDGVDAGKYTIGLGQ
CCCCCCCCEEEEECC		40.7219608861
46UbiquitinationYDGVDAGKYTIGLGQ
CCCCCCCCEEEEECC		40.7221906983
67PhosphorylationTDREDINSLCMTVVQ
CCHHHHHHHHHHHHH		24.23-
84PhosphorylationMERNNLSYDCIGRLE
HHHCCCCCCCCEEEE		20.2825147952
94PhosphorylationIGRLEVGTETIIDKS
CEEEEECCEEEECCC		34.8223401153
96PhosphorylationRLEVGTETIIDKSKS
EEEECCEEEECCCHH		24.0726270265
100UbiquitinationGTETIIDKSKSVKTN
CCEEEECCCHHHHHH		49.7421890473
1002-HydroxyisobutyrylationGTETIIDKSKSVKTN
CCEEEECCCHHHHHH		49.74-
101PhosphorylationTETIIDKSKSVKTNL
CEEEECCCHHHHHHH		26.8126270265
103PhosphorylationTIIDKSKSVKTNLMQ
EEECCCHHHHHHHHH		35.6226270265
206UbiquitinationQHAYDFYKPDMLSEY
HHHHHCCCCCHHCCC		34.2421906983
206AcetylationQHAYDFYKPDMLSEY
HHHHHCCCCCHHCCC		34.2423954790
213PhosphorylationKPDMLSEYPIVDGKL
CCCHHCCCCEECCEE		8.5522817900
221PhosphorylationPIVDGKLSIQCYLSA
CEECCEEEHHHHHHH		17.6921712546
227PhosphorylationLSIQCYLSALDRCYS
EEHHHHHHHHHHHHH		10.5821712546
238UbiquitinationRCYSVYCKKIHAQWQ
HHHHHHHHHHHHHHH		36.76-
238AcetylationRCYSVYCKKIHAQWQ
HHHHHHHHHHHHHHH		36.7625953088
239UbiquitinationCYSVYCKKIHAQWQK
HHHHHHHHHHHHHHH		35.84-
246AcetylationKIHAQWQKEGNDKDF
HHHHHHHHHCCCCCC		65.7119608861
246UbiquitinationKIHAQWQKEGNDKDF
HHHHHHHHHCCCCCC		65.7121906983
273UbiquitinationPYCKLVQKSLARMLL
HHHHHHHHHHHHHHH		39.7021890473
273AcetylationPYCKLVQKSLARMLL
HHHHHHHHHHHHHHH		39.7019608861
273MalonylationPYCKLVQKSLARMLL
HHHHHHHHHHHHHHH		39.7026320211
291UbiquitinationLNDQNRDKNSIYSGL
HHCCCCCCCCCCHHH		49.7321906983
293PhosphorylationDQNRDKNSIYSGLEA
CCCCCCCCCCHHHHH		28.7530108239
295PhosphorylationNRDKNSIYSGLEAFG
CCCCCCCCHHHHHHC		9.1228796482
296PhosphorylationRDKNSIYSGLEAFGD
CCCCCCCHHHHHHCC		34.9228796482
305UbiquitinationLEAFGDVKLEDTYFD
HHHHCCCEEECCCCC		51.39-
305SumoylationLEAFGDVKLEDTYFD
HHHHCCCEEECCCCC		51.39-
310PhosphorylationDVKLEDTYFDRDVEK
CCEEECCCCCHHHHH		18.79-
313MethylationLEDTYFDRDVEKAFM
EECCCCCHHHHHHHH		39.72115478823
317UbiquitinationYFDRDVEKAFMKASS
CCCHHHHHHHHHHCH		46.9321906983
317AcetylationYFDRDVEKAFMKASS
CCCHHHHHHHHHHCH		46.9323749302
321UbiquitinationDVEKAFMKASSELFS
HHHHHHHHHCHHHHC		38.3721906983
321AcetylationDVEKAFMKASSELFS
HHHHHHHHHCHHHHC		38.3719608861
323PhosphorylationEKAFMKASSELFSQK
HHHHHHHCHHHHCCC		20.8730206219
324PhosphorylationKAFMKASSELFSQKT
HHHHHHCHHHHCCCC		43.0830206219
328PhosphorylationKASSELFSQKTKASL
HHCHHHHCCCCCEEE		43.3130206219
330AcetylationSSELFSQKTKASLLV
CHHHHCCCCCEEEEE		51.2825953088
330UbiquitinationSSELFSQKTKASLLV
CHHHHCCCCCEEEEE		51.2821906983
332UbiquitinationELFSQKTKASLLVSN
HHHCCCCCEEEEEEC		42.91-
361PhosphorylationASVLAQYSPQQLAGK
HHHHHHCCHHHHCCC		12.26-
368UbiquitinationSPQQLAGKRIGVFSY
CHHHHCCCEEEEEEC		34.92-
374PhosphorylationGKRIGVFSYGSGLAA
CCEEEEEECCCHHHH		26.6125262027
375PhosphorylationKRIGVFSYGSGLAAT
CEEEEEECCCHHHHH		12.1225262027
377PhosphorylationIGVFSYGSGLAATLY
EEEEECCCHHHHHHH		23.5425262027
382PhosphorylationYGSGLAATLYSLKVT
CCCHHHHHHHEEEEC		22.1825262027
384PhosphorylationSGLAATLYSLKVTQD
CHHHHHHHEEEECCC		13.9625262027
385PhosphorylationGLAATLYSLKVTQDA
HHHHHHHEEEECCCC		25.4824719451
400UbiquitinationTPGSALDKITASLCD
CCCCHHHHHHHHHCH		42.6921906983
409SuccinylationTASLCDLKSRLDSRT
HHHHCHHHHHHHHCC		21.9323954790
409UbiquitinationTASLCDLKSRLDSRT
HHHHCHHHHHHHHCC		21.9321890473
409AcetylationTASLCDLKSRLDSRT
HHHHCHHHHHHHHCC		21.9325953088
414PhosphorylationDLKSRLDSRTGVAPD
HHHHHHHHCCCCCCH		36.0120068231
416PhosphorylationKSRLDSRTGVAPDVF
HHHHHHCCCCCCHHH		39.7020068231
427SulfoxidationPDVFAENMKLREDTH
CHHHHHHCCCCCCHH		3.0521406390
428AcetylationDVFAENMKLREDTHH
HHHHHHCCCCCCHHH		56.8525953088
428UbiquitinationDVFAENMKLREDTHH
HHHHHHCCCCCCHHH		56.8521906983
461UbiquitinationYLVRVDEKHRRTYAR
EEEEECHHHHHHCCC		37.6421890473
465PhosphorylationVDEKHRRTYARRPTP
ECHHHHHHCCCCCCC		22.8421406692
466PhosphorylationDEKHRRTYARRPTPN
CHHHHHHCCCCCCCC		9.0421406692
471PhosphorylationRTYARRPTPNDDTLD
HHCCCCCCCCCCCCC		32.6723927012
476PhosphorylationRPTPNDDTLDEGVGL
CCCCCCCCCCCCCEE		38.6823927012
486PhosphorylationEGVGLVHSNIATEHI
CCCEEECCCCCCCCC		23.5829209046
490PhosphorylationLVHSNIATEHIPSPA
EECCCCCCCCCCCCC		25.0522167270
495PhosphorylationIATEHIPSPAKKVPR
CCCCCCCCCCCCCCC		36.5729255136
498UbiquitinationEHIPSPAKKVPRLPA
CCCCCCCCCCCCCCC		58.6521906983
498AcetylationEHIPSPAKKVPRLPA
CCCCCCCCCCCCCCC		58.6525953088
499UbiquitinationHIPSPAKKVPRLPAT
CCCCCCCCCCCCCCC		60.62-
506PhosphorylationKVPRLPATAAEPEAA
CCCCCCCCCCCCCEE		25.1826074081
516PhosphorylationEPEAAVISNGEH---
CCCEEEECCCCC---		31.9819664994
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
495SPhosphorylationKinaseCDK1P06493
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HMCS1_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 HMCS1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPDLY_HUMANSPDL1physical
22939629
SPG21_HUMANSPG21physical
22939629
PEG10_HUMANPEG10physical
22939629
SYDC_HUMANDARSphysical
22939629
PROF2_HUMANPFN2physical
22939629
SYIC_HUMANIARSphysical
22939629
SYK_HUMANKARSphysical
22939629
MK09_HUMANMAPK9physical
22939629
VATE1_HUMANATP6V1E1physical
26344197
IMDH1_HUMANIMPDH1physical
26344197
MVD1_HUMANMVDphysical
26344197
NEDD8_HUMANNEDD8physical
26344197
NMD3_HUMANNMD3physical
26344197
RD23B_HUMANRAD23Bphysical
26344197
NLTP_HUMANSCP2physical
26344197
UFM1_HUMANUFM1physical
26344197
XPP1_HUMANXPNPEP1physical
26344197
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
There are no disease associations of PTM sites.
Regulatory Network of HMCS1_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-46; LYS-246; LYS-273 ANDLYS-321, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND MASSSPECTROMETRY.
"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-495 AND SER-516, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-476 AND SER-495, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, AND MASSSPECTROMETRY.

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