HMDH_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HMDH_SCHPO
• UniProt AC: Q10283
• Protein Name: 3-hydroxy-3-methylglutaryl-coenzyme A reductase
• Gene Name: hmg1
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 1053
• Subcellular Localization: Endoplasmic reticulum membrane ; Multi-pass membrane protein . Nucleus envelope .
• Protein Description: Catalyzes the conversion of HMG-CoA to mevalonate. It is the rate-limiting enzyme of the sterol biosynthesis pathway. Involved in ergosterol biosynthesis..
• Protein Sequence: MIYKLAARYPIQVIAIVGILVSMAYFSFLEALTQEDFPVLIRALKRFGILDGFPNTRLPNEMILKLSSVQGEDASVWEQIPAAELGGEGFVDFDITQWYYPANAKVDVAQLVEPYRNDCIFHDASGACHFFFKEVGNWTVSSIALPSNLANPPIDYFLDSSSTVIQRILPAIREHGISWSWLLQLIARTWMNTLKIASQASKTELLIVGTAYACMLISIVSLYLKMRRLGSKFWLFFSVLLSTLFSVQFAMTLVRASGVRISLVSLIESLPFLINVVALDKAAELTRQVITRCSVSDSHSPMHEDIAKACRNAAPPILRHFSFGIVVLAIFSYCNFGIKQFFLFAAVMIYDLLLLFSFFVAILTLKLEMRRYNAKDDVRKVLIEEGLSESTARHVADGNDSSATTSAGSRYFKVRYGTKIILFIFIAFNLFELCSIPFKHYAATSAAAARLIPLVRSQYPDFKSQRLLDDGVFDDVLSAISSMSNIESPSVRLLPAVFYGAELSSTSFLSTIHSFINNWSHYISASFLSKWIVCALSLSIAVNVFLLNAARLNSIKEEPEKKVVEKVVEVVKYIPSSNSSSIDDIQKDEIAQESVVRSLEECITLYNNGQISTLNDEEVVQLTLAKKIPLYALERVLKDVTRAVVIRRTVVSRSSRTKTLESSNCPVYHYDYSRVLNACCENVIGYMPLPLGVAGPLIIDGKPFYIPMATTEGALVASTMRGCKAINAGGGAVTVLTRDQMSRGPCVAFPNLTRAGRAKIWLDSPEGQEVMKKAFNSTSRFARLQHIKTALAGTRLFIRFCTSTGDAMGMNMISKGVEHALVVMSNDAGFDDMQVISVSGNYCTDKKPAAINWIDGRGKSVIAEAIIPGDAVKSVLKTTVEDLVKLNVDKNLIGSAMAGSVGGFNAHAANIVTAVYLATGQDPAQNVESSNCITLMDNVDGNLQLSVSMPSIEVGTIGGGTVLEPQGAMLDLLGVRGAHMTSPGDNSRQLARVVAAAVMAGELSLCSALASGHLVKSHIGLNRSALNTPAMDSSAKKPATDALKSVNSRVPGR

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
137	N-linked_Glycosylation	FFFKEVGNWTVSSIA EEEEECCCEEEEEEE	36.10	-
518	N-linked_Glycosylation	TIHSFINNWSHYISA HHHHHHHCHHHHHCH	36.49	-
576	Phosphorylation	EVVKYIPSSNSSSID HHHHHCCCCCCCCCH	32.37	25720772
577	Phosphorylation	VVKYIPSSNSSSIDD HHHHCCCCCCCCCHH	35.06	21712547
579	Phosphorylation	KYIPSSNSSSIDDIQ HHCCCCCCCCCHHHC	27.66	21712547
580	Phosphorylation	YIPSSNSSSIDDIQK HCCCCCCCCCHHHCH	35.25	24763107
581	Phosphorylation	IPSSNSSSIDDIQKD CCCCCCCCCHHHCHH	29.83	24763107
1017	Phosphorylation	ASGHLVKSHIGLNRS HCCCHHHCCCCCCHH	16.92	21712547
1024	Phosphorylation	SHIGLNRSALNTPAM CCCCCCHHHHCCCCC	35.71	28889911
1028	Phosphorylation	LNRSALNTPAMDSSA CCHHHHCCCCCCCCC	17.18	28889911
1033	Phosphorylation	LNTPAMDSSAKKPAT HCCCCCCCCCCCCHH	21.07	21712547
1040	Phosphorylation	SSAKKPATDALKSVN CCCCCCHHHHHHHHH	30.27	28889911
1045	Phosphorylation	PATDALKSVNSRVPG CHHHHHHHHHHCCCC	27.64	28889911
1048	Phosphorylation	DALKSVNSRVPGR-- HHHHHHHHCCCCC--	32.28	19547744

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of HMDH_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of HMDH_SCHPO !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of HMDH_SCHPO !!

Protein-Protein Interaction

Oops, there are no PPI records of HMDH_SCHPO !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1024 AND THR-1028, ANDMASS SPECTROMETRY.
PubMed: 18257517