ILVB_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ILVB_YEAST
• UniProt AC: P07342
• Protein Name: Acetolactate synthase catalytic subunit, mitochondrial
• Gene Name: ILV2
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 687
• Subcellular Localization: Mitochondrion.
• Protein Sequence: MIRQSTLKNFAIKRCFQHIAYRNTPAMRSVALAQRFYSSSSRYYSASPLPASKRPEPAPSFNVDPLEQPAEPSKLAKKLRAEPDMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSNALNQLTSRAQDEFVMQSINKAADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIPVTTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPEARRAAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMSKIFPVKERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKLSKVANDTGRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVDKKVPVLPMVAGGSGLDEFINFDPEVERQQTELRHKRTGGKH

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
60	Phosphorylation	KRPEPAPSFNVDPLE CCCCCCCCCCCCCCC	31.40	23749301
73	Phosphorylation	LEQPAEPSKLAKKLR CCCCCCHHHHHHHHH	31.63	21551504
74	Acetylation	EQPAEPSKLAKKLRA CCCCCHHHHHHHHHC	64.28	24489116
87	Phosphorylation	RAEPDMDTSFVGLTG HCCCCCCCCCCCCCH	19.89	22369663
88	Phosphorylation	AEPDMDTSFVGLTGG CCCCCCCCCCCCCHH	17.42	22369663
93	Phosphorylation	DTSFVGLTGGQIFNE CCCCCCCCHHHHHHH	33.08	22369663
103	Phosphorylation	QIFNEMMSRQNVDTV HHHHHHHHHCCCCCC	29.42	22369663
137	Acetylation	KFNFVLPKHEQGAGH CCEEEECCCCCCCCH	56.46	24489116
215	Acetylation	GISRSCTKWNVMVKS EECCCCCCCCEEEEE	40.89	24489116
251	Acetylation	PVLVDLPKDVTAAIL CEEEECCCCCCHHHH	72.61	24489116
265	Ubiquitination	LRNPIPTKTTLPSNA HCCCCCCCCCCCHHH	33.87	24961812
270	Phosphorylation	PTKTTLPSNALNQLT CCCCCCCHHHHHHHH	37.54	28889911
291	Acetylation	FVMQSINKAADLINL HHHHHHHHHHHHHHH	43.19	24489116
321	Acetylation	ADGPRLLKELSDRAQ CCHHHHHHHHHHHCC	62.29	25381059
382	Phosphorylation	ARFDDRVTGNISKFA CCCCHHCCCCHHHHC	25.96	22369663
386	Phosphorylation	DRVTGNISKFAPEAR HHCCCCHHHHCHHHH	26.22	22369663
387	Acetylation	RVTGNISKFAPEARR HCCCCHHHHCHHHHH	41.57	24489116
442	Acetylation	MSKIFPVKERSEWFA HHHHCCCHHHHHHHH	47.88	24489116
453	Acetylation	EWFAQINKWKKEYPY HHHHHHHHHHHHCCC	63.12	24489116
455	Acetylation	FAQINKWKKEYPYAY HHHHHHHHHHCCCCC	37.02	24489116
456	Acetylation	AQINKWKKEYPYAYM HHHHHHHHHCCCCCC	62.46	24489116
607	Ubiquitination	QLNPDFIKLAEAMGL CCCHHHHHHHHHCCC	41.46	15699485
607	Acetylation	QLNPDFIKLAEAMGL CCCHHHHHHHHHCCC	41.46	24489116
615	Succinylation	LAEAMGLKGLRVKKQ HHHHCCCCCCCCCCH	50.61	23954790
615	Acetylation	LAEAMGLKGLRVKKQ HHHHCCCCCCCCCCH	50.61	24489116
628	Acetylation	KQEELDAKLKEFVST CHHHHHHHHHHHHHC	60.81	24489116
630	Acetylation	EELDAKLKEFVSTKG HHHHHHHHHHHHCCC	48.69	22865919
636	Ubiquitination	LKEFVSTKGPVLLEV HHHHHHCCCCEEEEE	54.43	24961812
636	Acetylation	LKEFVSTKGPVLLEV HHHHHHCCCCEEEEE	54.43	24489116
659	Phosphorylation	LPMVAGGSGLDEFIN ECEECCCCCHHHHHC	34.95	30377154

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

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

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PEX19_YEAST	PEX19	physical	16554755
DHE2_YEAST	GDH2	physical	16554755
ARD1_YEAST	ARD1	physical	16554755
UBA1_YEAST	UBA1	physical	16554755
SSB2_YEAST	SSB2	physical	16554755
YP247_YEAST	YPL247C	physical	16554755
ILVB_YEAST	ILV2	physical	11902841
BCA2_YEAST	BAT2	genetic	21798060
ILV6_YEAST	ILV6	genetic	21798060
PMP1_YEAST	PMP1	physical	26404137

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, AND MASSSPECTROMETRY.
PubMed: 18407956