dbPTM

HMCS2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HMCS2_MOUSE
UniProt AC	P54869
Protein Name	Hydroxymethylglutaryl-CoA synthase, mitochondrial
Gene Name	Hmgcs2
Organism	Mus musculus (Mouse).
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	MQRLLAPARRVLQVKRAMQETSLTPAHLLSAAQQRFSTIPPAPLAKTDTWPKDVGILALEVYFPAQYVDQTDLEKFNNVEAGKYTVGLGQTRMGFCSVQEDINSLCLTVVQRLMERTKLPWDAVGRLEVGTETIIDKSKAVKTVLMELFQDSGNTDIEGIDTTNACYGGTASLFNAANWMESSYWDGRYALVVCGDIAVYPSGNARPTGGAGAVAMLIGPKAPLVLEQGLRGTHMENAYDFYKPNLASEYPLVDGKLSIQCYLRALDRCYAAYRKKIQNQWKQAGNNQPFTLDDVQYMIFHTPFCKMVQKSLARLMFNDFLSSSSDKQNNLYKGLEAFRGLKLEETYTNKDVDKALLKASLDMFNQKTKASLYLSTNNGNMYTSSLYGCLASLLSHHSAQELAGSRIGAFSYGSGLAASFFSFRVSKDASPGSPLEKLVSSVSDLPKRLDSRRRMSPEEFTEIMNQREQFYHKVNFSPPGDTSNLFPGTWYLERVDEMHRRKYARCPV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
38	Phosphorylation	AAQQRFSTIPPAPLA HHHHHHCCCCCCCCC	34.49	22942356
46	Acetylation	IPPAPLAKTDTWPKD CCCCCCCCCCCCCCC	55.40	23576753
46	Ubiquitination	IPPAPLAKTDTWPKD CCCCCCCCCCCCCCC	55.40	22790023
49	Phosphorylation	APLAKTDTWPKDVGI CCCCCCCCCCCCCEE	49.23	-
52	Acetylation	AKTDTWPKDVGILAL CCCCCCCCCCEEEEE	57.52	23806337
52	Succinylation	AKTDTWPKDVGILAL CCCCCCCCCCEEEEE	57.52	-
52	Succinylation	AKTDTWPKDVGILAL CCCCCCCCCCEEEEE	57.52	23806337
75	Acetylation	VDQTDLEKFNNVEAG CCHHCHHHHCCCCCC	61.77	23576753
83	Acetylation	FNNVEAGKYTVGLGQ HCCCCCCCEEEECCC	44.81	23576753
83	Glutarylation	FNNVEAGKYTVGLGQ HCCCCCCCEEEECCC	44.81	24703693
83	Malonylation	FNNVEAGKYTVGLGQ HCCCCCCCEEEECCC	44.81	26073543
83	Succinylation	FNNVEAGKYTVGLGQ HCCCCCCCEEEECCC	44.81	-
83	Succinylation	FNNVEAGKYTVGLGQ HCCCCCCCEEEECCC	44.81	23806337
83	Ubiquitination	FNNVEAGKYTVGLGQ HCCCCCCCEEEECCC	44.81	27667366
96	S-palmitoylation	GQTRMGFCSVQEDIN CCCCCCCCCHHHHHH	3.01	28526873
106	S-palmitoylation	QEDINSLCLTVVQRL HHHHHHHHHHHHHHH	2.76	28526873
118	Acetylation	QRLMERTKLPWDAVG HHHHHHCCCCHHHCC	59.79	23576753
118	Glutarylation	QRLMERTKLPWDAVG HHHHHHCCCCHHHCC	59.79	24703693
118	Malonylation	QRLMERTKLPWDAVG HHHHHHCCCCHHHCC	59.79	26073543
118	Succinylation	QRLMERTKLPWDAVG HHHHHHCCCCHHHCC	59.79	-
118	Succinylation	QRLMERTKLPWDAVG HHHHHHCCCCHHHCC	59.79	23806337
118	Ubiquitination	QRLMERTKLPWDAVG HHHHHHCCCCHHHCC	59.79	-
131	Phosphorylation	VGRLEVGTETIIDKS CCCEEECCEEECCHH	34.82	20469934
133	Phosphorylation	RLEVGTETIIDKSKA CEEECCEEECCHHHH	24.07	20469934
137	Acetylation	GTETIIDKSKAVKTV CCEEECCHHHHHHHH	43.37	23864654
137	Ubiquitination	GTETIIDKSKAVKTV CCEEECCHHHHHHHH	43.37	22790023
221	Acetylation	VAMLIGPKAPLVLEQ EEHHHCCCCCEEECC	58.38	23806337
221	Succinylation	VAMLIGPKAPLVLEQ EEHHHCCCCCEEECC	58.38	-
221	Succinylation	VAMLIGPKAPLVLEQ EEHHHCCCCCEEECC	58.38	23806337
221	Ubiquitination	VAMLIGPKAPLVLEQ EEHHHCCCCCEEECC	58.38	-
243	Acetylation	ENAYDFYKPNLASEY CCHHHHCCCCCCCCC	27.68	23576753
243	Succinylation	ENAYDFYKPNLASEY CCHHHHCCCCCCCCC	27.68	23806337
243	Ubiquitination	ENAYDFYKPNLASEY CCHHHHCCCCCCCCC	27.68	-
248	Phosphorylation	FYKPNLASEYPLVDG HCCCCCCCCCCCCCC	40.61	-
250	Phosphorylation	KPNLASEYPLVDGKL CCCCCCCCCCCCCCE	10.20	26032504
256	Acetylation	EYPLVDGKLSIQCYL CCCCCCCCEEHHHHH	34.30	23576753
256	Succinylation	EYPLVDGKLSIQCYL CCCCCCCCEEHHHHH	34.30	-
256	Succinylation	EYPLVDGKLSIQCYL CCCCCCCCEEHHHHH	34.30	23806337
261	S-palmitoylation	DGKLSIQCYLRALDR CCCEEHHHHHHHHHH	3.09	28526873
282	Acetylation	KKIQNQWKQAGNNQP HHHHHHHHHCCCCCC	22.10	23864654
305	S-palmitoylation	MIFHTPFCKMVQKSL HHHCCHHHHHHHHHH	2.68	28526873
306	Acetylation	IFHTPFCKMVQKSLA HHCCHHHHHHHHHHH	42.35	23576753
306	Succinylation	IFHTPFCKMVQKSLA HHCCHHHHHHHHHHH	42.35	24315375
310	Acetylation	PFCKMVQKSLARLMF HHHHHHHHHHHHHHH	35.71	23576753
310	Glutarylation	PFCKMVQKSLARLMF HHHHHHHHHHHHHHH	35.71	24703693
310	Malonylation	PFCKMVQKSLARLMF HHHHHHHHHHHHHHH	35.71	26320211
310	Succinylation	PFCKMVQKSLARLMF HHHHHHHHHHHHHHH	35.71	-
310	Succinylation	PFCKMVQKSLARLMF HHHHHHHHHHHHHHH	35.71	23806337
310	Ubiquitination	PFCKMVQKSLARLMF HHHHHHHHHHHHHHH	35.71	-
322	Phosphorylation	LMFNDFLSSSSDKQN HHHHHHHCCCCHHHC	28.32	29472430
323	Phosphorylation	MFNDFLSSSSDKQNN HHHHHHCCCCHHHCC	35.69	29472430
324	Phosphorylation	FNDFLSSSSDKQNNL HHHHHCCCCHHHCCH	38.90	29472430
325	Phosphorylation	NDFLSSSSDKQNNLY HHHHCCCCHHHCCHH	51.26	25195567
327	Acetylation	FLSSSSDKQNNLYKG HHCCCCHHHCCHHHH	57.80	23576753
327	Glutarylation	FLSSSSDKQNNLYKG HHCCCCHHHCCHHHH	57.80	24703693
327	Succinylation	FLSSSSDKQNNLYKG HHCCCCHHHCCHHHH	57.80	-
327	Succinylation	FLSSSSDKQNNLYKG HHCCCCHHHCCHHHH	57.80	23806337
327	Ubiquitination	FLSSSSDKQNNLYKG HHCCCCHHHCCHHHH	57.80	27667366
333	Acetylation	DKQNNLYKGLEAFRG HHHCCHHHHHHHHHC	61.25	23864654
333	Glutarylation	DKQNNLYKGLEAFRG HHHCCHHHHHHHHHC	61.25	24703693
333	Succinylation	DKQNNLYKGLEAFRG HHHCCHHHHHHHHHC	61.25	-
333	Succinylation	DKQNNLYKGLEAFRG HHHCCHHHHHHHHHC	61.25	23806337
333	Ubiquitination	DKQNNLYKGLEAFRG HHHCCHHHHHHHHHC	61.25	-
342	Acetylation	LEAFRGLKLEETYTN HHHHHCCCCEEEECC	57.59	23576753
342	Malonylation	LEAFRGLKLEETYTN HHHHHCCCCEEEECC	57.59	26320211
342	Succinylation	LEAFRGLKLEETYTN HHHHHCCCCEEEECC	57.59	-
342	Succinylation	LEAFRGLKLEETYTN HHHHHCCCCEEEECC	57.59	23806337
342	Ubiquitination	LEAFRGLKLEETYTN HHHHHCCCCEEEECC	57.59	27667366
346	Phosphorylation	RGLKLEETYTNKDVD HCCCCEEEECCCHHH	26.69	20469934
347	Phosphorylation	GLKLEETYTNKDVDK CCCCEEEECCCHHHH	16.17	22871156
348	Phosphorylation	LKLEETYTNKDVDKA CCCEEEECCCHHHHH	43.12	30352176
350	Acetylation	LEETYTNKDVDKALL CEEEECCCHHHHHHH	51.86	23576753
350	Glutarylation	LEETYTNKDVDKALL CEEEECCCHHHHHHH	51.86	24703693
350	Malonylation	LEETYTNKDVDKALL CEEEECCCHHHHHHH	51.86	26073543
350	Succinylation	LEETYTNKDVDKALL CEEEECCCHHHHHHH	51.86	-
350	Succinylation	LEETYTNKDVDKALL CEEEECCCHHHHHHH	51.86	23806337
350	Ubiquitination	LEETYTNKDVDKALL CEEEECCCHHHHHHH	51.86	27667366
354	Acetylation	YTNKDVDKALLKASL ECCCHHHHHHHHHHH	40.56	23576753
354	Glutarylation	YTNKDVDKALLKASL ECCCHHHHHHHHHHH	40.56	24703693
354	Malonylation	YTNKDVDKALLKASL ECCCHHHHHHHHHHH	40.56	26073543
354	Succinylation	YTNKDVDKALLKASL ECCCHHHHHHHHHHH	40.56	-
354	Succinylation	YTNKDVDKALLKASL ECCCHHHHHHHHHHH	40.56	23806337
354	Ubiquitination	YTNKDVDKALLKASL ECCCHHHHHHHHHHH	40.56	27667366
358	Acetylation	DVDKALLKASLDMFN HHHHHHHHHHHHHHC	36.46	23576753
358	Glutarylation	DVDKALLKASLDMFN HHHHHHHHHHHHHHC	36.46	24703693
358	Malonylation	DVDKALLKASLDMFN HHHHHHHHHHHHHHC	36.46	26320211
358	Succinylation	DVDKALLKASLDMFN HHHHHHHHHHHHHHC	36.46	-
358	Succinylation	DVDKALLKASLDMFN HHHHHHHHHHHHHHC	36.46	23806337
358	Ubiquitination	DVDKALLKASLDMFN HHHHHHHHHHHHHHC	36.46	-
367	Acetylation	SLDMFNQKTKASLYL HHHHHCCCCCEEEEE	53.77	23864654
367	Succinylation	SLDMFNQKTKASLYL HHHHHCCCCCEEEEE	53.77	23954790
367	Ubiquitination	SLDMFNQKTKASLYL HHHHHCCCCCEEEEE	53.77	27667366
389	S-palmitoylation	YTSSLYGCLASLLSH CHHHHHHHHHHHHCC	1.49	28526873
427	Acetylation	FFSFRVSKDASPGSP HEEEEECCCCCCCCH	55.23	23576753
427	Malonylation	FFSFRVSKDASPGSP HEEEEECCCCCCCCH	55.23	26320211
427	Ubiquitination	FFSFRVSKDASPGSP HEEEEECCCCCCCCH	55.23	27667366
430	Phosphorylation	FRVSKDASPGSPLEK EEECCCCCCCCHHHH	39.67	25521595
433	Phosphorylation	SKDASPGSPLEKLVS CCCCCCCCHHHHHHH	29.69	25521595
437	Acetylation	SPGSPLEKLVSSVSD CCCCHHHHHHHCHHH	62.97	23576753
437	Succinylation	SPGSPLEKLVSSVSD CCCCHHHHHHHCHHH	62.97	24315375
437	Ubiquitination	SPGSPLEKLVSSVSD CCCCHHHHHHHCHHH	62.97	-
440	Phosphorylation	SPLEKLVSSVSDLPK CHHHHHHHCHHHHCH	35.14	29472430
441	Phosphorylation	PLEKLVSSVSDLPKR HHHHHHHCHHHHCHH	20.40	29472430
443	Phosphorylation	EKLVSSVSDLPKRLD HHHHHCHHHHCHHHH	35.06	29472430
447	Acetylation	SSVSDLPKRLDSRRR HCHHHHCHHHHHCCC	73.26	23576753
447	Glutarylation	SSVSDLPKRLDSRRR HCHHHHCHHHHHCCC	73.26	24703693
447	Malonylation	SSVSDLPKRLDSRRR HCHHHHCHHHHHCCC	73.26	26073543
447	Succinylation	SSVSDLPKRLDSRRR HCHHHHCHHHHHCCC	73.26	-
447	Succinylation	SSVSDLPKRLDSRRR HCHHHHCHHHHHCCC	73.26	23806337
447	Ubiquitination	SSVSDLPKRLDSRRR HCHHHHCHHHHHCCC	73.26	-
456	Phosphorylation	LDSRRRMSPEEFTEI HHHCCCCCHHHHHHH	27.61	19060867
461	Phosphorylation	RMSPEEFTEIMNQRE CCCHHHHHHHHHHHH	28.07	23140645
473	Acetylation	QREQFYHKVNFSPPG HHHHHHHHCCCCCCC	27.74	23576753
473	Succinylation	QREQFYHKVNFSPPG HHHHHHHHCCCCCCC	27.74	-
473	Succinylation	QREQFYHKVNFSPPG HHHHHHHHCCCCCCC	27.74	23806337
473	Ubiquitination	QREQFYHKVNFSPPG HHHHHHHHCCCCCCC	27.74	-
477	Phosphorylation	FYHKVNFSPPGDTSN HHHHCCCCCCCCCCC	25.61	26643407
482	Phosphorylation	NFSPPGDTSNLFPGT CCCCCCCCCCCCCCC	25.98	23984901
483	Phosphorylation	FSPPGDTSNLFPGTW CCCCCCCCCCCCCCE	35.95	23984901

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_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
83	K	Succinylation	24315375
Succinylation, at least at Lys-83 and Lys-310, inhibits the enzymatic activity.
310	K	Succinylation	24315375
Succinylation, at least at Lys-83 and Lys-310, inhibits the enzymatic activity.
427	K	Acetylation	23576753
Acetylation of Lys-427 is observed in liver mitochondria from fasted mice but not from fed mice.

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of HMCS2_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of HMCS2_MOUSE

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-83; LYS-427 AND LYS-437, ANDMASS SPECTROMETRY.	16916647 [Abstract]
Phosphorylation
Reference	PubMed
"Mitochondrial phosphoproteome revealed by an improved IMAC method andMS/MS/MS."; Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.; Mol. Cell. Proteomics 6:669-676(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, AND MASSSPECTROMETRY.	17208939 [Abstract]

show

show

show