HMCS2_HUMAN - dbPTM
HMCS2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HMCS2_HUMAN
UniProt AC P54868
Protein Name Hydroxymethylglutaryl-CoA synthase, mitochondrial
Gene Name HMGCS2
Organism Homo sapiens (Human).
Sequence Length 508
Subcellular Localization Mitochondrion.
Protein Description This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase..
Protein Sequence MQRLLTPVKRILQLTRAVQETSLTPARLLPVAHQRFSTASAVPLAKTDTWPKDVGILALEVYFPAQYVDQTDLEKYNNVEAGKYTVGLGQTRMGFCSVQEDINSLCLTVVQRLMERIQLPWDSVGRLEVGTETIIDKSKAVKTVLMELFQDSGNTDIEGIDTTNACYGGTASLFNAANWMESSSWDGRYAMVVCGDIAVYPSGNARPTGGAGAVAMLIGPKAPLALERGLRGTHMENVYDFYKPNLASEYPIVDGKLSIQCYLRALDRCYTSYRKKIQNQWKQAGSDRPFTLDDLQYMIFHTPFCKMVQKSLARLMFNDFLSASSDTQTSLYKGLEAFGGLKLEDTYTNKDLDKALLKASQDMFDKKTKASLYLSTHNGNMYTSSLYGCLASLLSHHSAQELAGSRIGAFSYGSGLAASFFSFRVSQDAAPGSPLDKLVSSTSDLPKRLASRKCVSPEEFTEIMNQREQFYHKVNFSPPGDTNSLFPGTWYLERVDEQHRRKYARRPV
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
37PhosphorylationPVAHQRFSTASAVPL
HHHHHCCCCCCCCCC
25.8326657352
38PhosphorylationVAHQRFSTASAVPLA
HHHHCCCCCCCCCCC
23.1724275569
52SuccinylationAKTDTWPKDVGILAL
CCCCCCCCCCCEEEE
57.52-
52SuccinylationAKTDTWPKDVGILAL
CCCCCCCCCCCEEEE
57.52-
76PhosphorylationDQTDLEKYNNVEAGK
CHHHHHHHCCCCCCC
11.55-
83AcetylationYNNVEAGKYTVGLGQ
HCCCCCCCEEEECCC
44.8120167786
83SuccinylationYNNVEAGKYTVGLGQ
HCCCCCCCEEEECCC
44.81-
83SuccinylationYNNVEAGKYTVGLGQ
HCCCCCCCEEEECCC
44.81-
97PhosphorylationQTRMGFCSVQEDINS
CCCCCCCCHHHHHHH
25.2828258704
131PhosphorylationVGRLEVGTETIIDKS
CCCEEECCEEECCHH
34.8223401153
133PhosphorylationRLEVGTETIIDKSKA
CEEECCEEECCHHHH
24.0724275569
137UbiquitinationGTETIIDKSKAVKTV
CCEEECCHHHHHHHH
43.3721906983
137AcetylationGTETIIDKSKAVKTV
CCEEECCHHHHHHHH
43.3725953088
166S-palmitoylationGIDTTNACYGGTASL
CCCCCCCCCCCHHHH
3.3520124434
221SuccinylationVAMLIGPKAPLALER
EEHHHCCCCCHHHHC
58.38-
221SuccinylationVAMLIGPKAPLALER
EEHHHCCCCCHHHHC
58.38-
239PhosphorylationGTHMENVYDFYKPNL
CCCCCHHHHHCCCCC
16.36-
243AcetylationENVYDFYKPNLASEY
CHHHHHCCCCCCCCC
27.68-
248PhosphorylationFYKPNLASEYPIVDG
HCCCCCCCCCCEECC
40.61-
250PhosphorylationKPNLASEYPIVDGKL
CCCCCCCCCEECCEE
8.8621253578
256AcetylationEYPIVDGKLSIQCYL
CCCEECCEEEHHHHH
34.3024889763
256SuccinylationEYPIVDGKLSIQCYL
CCCEECCEEEHHHHH
34.30-
256SuccinylationEYPIVDGKLSIQCYL
CCCEECCEEEHHHHH
34.30-
262PhosphorylationGKLSIQCYLRALDRC
CEEEHHHHHHHHHHH
5.26-
276TrimethylationCYTSYRKKIQNQWKQ
HHHHHHHHHHHHHHH
40.29-
276MethylationCYTSYRKKIQNQWKQ
HHHHHHHHHHHHHHH
40.2923644510
305S-nitrosylationMIFHTPFCKMVQKSL
HHHCCHHHHHHHHHH
2.6825040305
305S-palmitoylationMIFHTPFCKMVQKSL
HHHCCHHHHHHHHHH
2.6820124434
306AcetylationIFHTPFCKMVQKSLA
HHCCHHHHHHHHHHH
42.35-
310SuccinylationPFCKMVQKSLARLMF
HHHHHHHHHHHHHHH
35.71-
310AcetylationPFCKMVQKSLARLMF
HHHHHHHHHHHHHHH
35.712401891
310SuccinylationPFCKMVQKSLARLMF
HHHHHHHHHHHHHHH
35.71-
322PhosphorylationLMFNDFLSASSDTQT
HHHHHHHCCCCCCHH
26.5421406692
324PhosphorylationFNDFLSASSDTQTSL
HHHHHCCCCCCHHHH
25.9321406692
325PhosphorylationNDFLSASSDTQTSLY
HHHHCCCCCCHHHHH
44.3821406692
327PhosphorylationFLSASSDTQTSLYKG
HHCCCCCCHHHHHHH
35.3821406692
329PhosphorylationSASSDTQTSLYKGLE
CCCCCCHHHHHHHHH
23.8521406692
330PhosphorylationASSDTQTSLYKGLEA
CCCCCHHHHHHHHHH
21.6421406692
332PhosphorylationSDTQTSLYKGLEAFG
CCCHHHHHHHHHHCC
11.6321406692
333SuccinylationDTQTSLYKGLEAFGG
CCHHHHHHHHHHCCC
63.41-
333SuccinylationDTQTSLYKGLEAFGG
CCHHHHHHHHHHCCC
63.41-
342SuccinylationLEAFGGLKLEDTYTN
HHHCCCCCCEECCCC
53.78-
342SuccinylationLEAFGGLKLEDTYTN
HHHCCCCCCEECCCC
53.78-
342AcetylationLEAFGGLKLEDTYTN
HHHCCCCCCEECCCC
53.78-
346PhosphorylationGGLKLEDTYTNKDLD
CCCCCEECCCCCHHH
23.9123312004
347PhosphorylationGLKLEDTYTNKDLDK
CCCCEECCCCCHHHH
22.1923312004
348PhosphorylationLKLEDTYTNKDLDKA
CCCEECCCCCHHHHH
37.5723312004
350AcetylationLEDTYTNKDLDKALL
CEECCCCCHHHHHHH
52.4427178108
350SuccinylationLEDTYTNKDLDKALL
CEECCCCCHHHHHHH
52.44-
350SuccinylationLEDTYTNKDLDKALL
CEECCCCCHHHHHHH
52.44-
354SuccinylationYTNKDLDKALLKASQ
CCCCHHHHHHHHHCH
48.51-
354SuccinylationYTNKDLDKALLKASQ
CCCCHHHHHHHHHCH
48.51-
354AcetylationYTNKDLDKALLKASQ
CCCCHHHHHHHHHCH
48.5127178108
358SuccinylationDLDKALLKASQDMFD
HHHHHHHHHCHHHHC
47.01-
358SuccinylationDLDKALLKASQDMFD
HHHHHHHHHCHHHHC
47.01-
358AcetylationDLDKALLKASQDMFD
HHHHHHHHHCHHHHC
47.0127178108
366AcetylationASQDMFDKKTKASLY
HCHHHHCHHHCEEEE
51.5927178108
367AcetylationSQDMFDKKTKASLYL
CHHHHCHHHCEEEEE
58.047666167
398PhosphorylationASLLSHHSAQELAGS
HHHHCCCCHHHHCCC
26.65-
414PhosphorylationIGAFSYGSGLAASFF
CCEEECCCCCHHHHH
23.54-
419PhosphorylationYGSGLAASFFSFRVS
CCCCCHHHHHEEEEC
22.63-
422PhosphorylationGLAASFFSFRVSQDA
CCHHHHHEEEECCCC
15.3324719451
426PhosphorylationSFFSFRVSQDAAPGS
HHHEEEECCCCCCCC
20.3422798277
433PhosphorylationSQDAAPGSPLDKLVS
CCCCCCCCCHHHHHH
22.6426657352
437AcetylationAPGSPLDKLVSSTSD
CCCCCHHHHHHCCCC
59.48-
440PhosphorylationSPLDKLVSSTSDLPK
CCHHHHHHCCCCCCH
38.0322798277
441PhosphorylationPLDKLVSSTSDLPKR
CHHHHHHCCCCCCHH
25.1725072903
442PhosphorylationLDKLVSSTSDLPKRL
HHHHHHCCCCCCHHH
20.8225072903
443PhosphorylationDKLVSSTSDLPKRLA
HHHHHCCCCCCHHHH
38.8125072903
447SuccinylationSSTSDLPKRLASRKC
HCCCCCCHHHHCCCC
68.30-
447SuccinylationSSTSDLPKRLASRKC
HCCCCCCHHHHCCCC
68.30-
447AcetylationSSTSDLPKRLASRKC
HCCCCCCHHHHCCCC
68.302380825
456PhosphorylationLASRKCVSPEEFTEI
HHCCCCCCHHHHHHH
35.7428348404
473SuccinylationQREQFYHKVNFSPPG
HHHHHHHHCCCCCCC
27.74-
473SuccinylationQREQFYHKVNFSPPG
HHHHHHHHCCCCCCC
27.74-
473AcetylationQREQFYHKVNFSPPG
HHHHHHHHCCCCCCC
27.742380229
477PhosphorylationFYHKVNFSPPGDTNS
HHHHCCCCCCCCCCC
25.61-

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 HMCS2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
83KSuccinylation

-
310KSuccinylation

-

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 HMCS2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
605911HMG-CoA synthase deficiency (HMGCS deficiency)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HMCS2_HUMAN

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Related Literatures of Post-Translational Modification

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