Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Hydroxymethylglutaryl-CoA synthase, cytoplasmic  

UniProtKB / Swiss-Prot ID :  HMCS1_HUMAN

Gene Name (Synonyms) : 
HMGCS1, HMGCS  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. 

Protein Function :  This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase. 

Protein Sequence MPGSLPLNAEACWPKDVGIVALEIYFPSQYVDQAELEKYDGVDAGKYTIGLGQAKMGFCTDREDINSLCM...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCEEEEECCCCCCCCCHHHHHHHHCCCHHHHEECCCEEEEECCCCCCHHHHHHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
4Phosphoserine-MPGSLPLN
-CCCCCCCC
22.42HPRD
Link-
4Phosphoserine-MPGSLPLN
-CCCCCCCC
22.42Phosphositeplus
Link-
4Phosphoserine.-MPGSLPLN
-CCCCCCCC
22.42UniProtKB
Link-
46Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VDAGKYTIG
CCHHHHEEC
40.72Phosphositeplus
Link
46N6-acetyllysineVDAGKYTIG
CCHHHHEEC
40.72HPRD
Link
46N6-acetyllysineVDAGKYTIG
CCHHHHEEC
40.72Phosphositeplus
Link
46N6-acetyllysine.VDAGKYTIG
CCHHHHEEC
40.72UniProtKB
Link
206Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YDFYKPDML
CHHCCCCCC
34.24Phosphositeplus
Link
246Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AQWQKEGND
HHHHHHHHH
65.71Phosphositeplus
Link
246N6-acetyllysineAQWQKEGND
HHHHHHHHH
65.71HPRD
Link
246N6-acetyllysineAQWQKEGND
HHHHHHHHH
65.71Phosphositeplus
Link
246N6-acetyllysine.AQWQKEGND
HHHHHHHHH
65.71UniProtKB
Link
273Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KLVQKSLAR
HHHHHHHHH
39.70Phosphositeplus
Link
273N6-acetyllysineKLVQKSLAR
HHHHHHHHH
39.70HPRD
Link
273N6-acetyllysineKLVQKSLAR
HHHHHHHHH
39.70Phosphositeplus
Link
273N6-acetyllysine.KLVQKSLAR
HHHHHHHHH
39.70UniProtKB
Link
291Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QNRDKNSIY
HCCCCCCHH
49.73Phosphositeplus
Link
317Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RDVEKAFMK
HHHHHHHHH
46.93Phosphositeplus
Link
321Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KAFMKASSE
HHHHHHHHH
38.37Phosphositeplus
Link
321N6-acetyllysineKAFMKASSE
HHHHHHHHH
38.37HPRD
Link
321N6-acetyllysineKAFMKASSE
HHHHHHHHH
38.37Phosphositeplus
Link
321N6-acetyllysine.KAFMKASSE
HHHHHHHHH
38.37UniProtKB
Link
330Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LFSQKTKAS
HHHHHHCCC
51.28Phosphositeplus
Link
400Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SALDKITAS
CCHHHHHHH
42.69Phosphositeplus
Link
409Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LCDLKSRLD
HHCCHHHHH
21.93Phosphositeplus
Link
414PhosphoserineSRLDSRTGV
HHHHHHEEE
36.01HPRD
Link
428Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AENMKLRED
HHHHHHHHH
56.85Phosphositeplus
Link
471PhosphothreonineARRPTPNDD
CCCCCCCCC
32.67HPRD
Link-
471PhosphothreonineARRPTPNDD
CCCCCCCCC
32.67PhosphoELM
Link-
476PhosphothreoninePNDDTLDEG
CCCCCHHHC
38.68HPRD
Link-
476PhosphothreoninePNDDTLDEG
CCCCCHHHC
38.68PhosphoELM
Link-
476PhosphothreoninePNDDTLDEG
CCCCCHHHC
38.68Phosphositeplus
Link-
476PhosphothreoninePNDDTLDEG
CCCCCHHHC
38.68SysPTM
Link-
476Phosphothreonine.PNDDTLDEG
CCCCCHHHC
38.68UniProtKB
Link-
486PhosphoserineGLVHSNIAT
EEECCCCCC
23.58Phosphositeplus
Link-
490PhosphothreonineSNIATEHIP
CCCCCCCCC
25.05HPRD
Link-
495PhosphoserineEHIPSPAKK
CCCCCCHHH
36.57HPRD
Link-
495PhosphoserineEHIPSPAKK
CCCCCCHHH
36.57PhosphoELM
Link-
495PhosphoserineEHIPSPAKK
CCCCCCHHH
36.57Phosphositeplus
Link-
495PhosphoserineEHIPSPAKK
CCCCCCHHH
36.57SysPTM
Link-
495Phosphoserine.EHIPSPAKK
CCCCCCHHH
36.57UniProtKB
Link-
498Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PSPAKKVPR
CCCHHHCCC
58.65Phosphositeplus
Link-
516PhosphoserineAAVISNGEH
EEEECCCCC
31.98HPRD
Link-
516PhosphoserineAAVISNGEH
EEEECCCCC
31.98Phosphositeplus
Link-
516PhosphoserineAAVISNGEH
EEEECCCCC
31.98SysPTM
Link-
516Phosphoserine.AAVISNGEH
EEEECCCCC
31.98UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
HCD2_HUMANENSP00000322706STRING
SCOT_HUMANENSP00000322706STRING
ECHP_HUMANENSP00000322706STRING
LDLR_HUMANENSP00000322706STRING
DHB4_HUMANENSP00000322706STRING
THIL_HUMANENSP00000322706STRING
THIM_HUMANENSP00000322706STRING
HMDH_HUMANENSP00000322706STRING
AACS_HUMANENSP00000322706STRING
AACS_HUMANENSP00000322706STRING
AACS_HUMANENSP00000322706STRING
AACS_HUMANENSP00000322706STRING
AACS_HUMANENSP00000322706STRING
AACS_HUMANENSP00000322706STRING
AACS_HUMANENSP00000322706STRING
ECHB_HUMANENSP00000322706STRING
THIK_HUMANENSP00000322706STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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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.
"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.
"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.
"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.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures