dbPTM

HSP12_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HSP12_YEAST
UniProt AC	P22943
Protein Name	12 kDa heat shock protein
Gene Name	HSP12
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	109
Subcellular Localization
Protein Description	May play a role in a switch from carbohydrate utilizing metabolism to fatty acid utilizing metabolism..
Protein Sequence	MSDAGRKGFGEKASEALKPDSQKSYAEQGKEYITDKADKVAGKVQPEDNKGVFQGVHDSAEKGKDNAEGQGESLADQARDYMGAAKSKLNDAVEYVSGRVHGEEDPTKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSDAGRKGF ------CCHHHHCCC	35.85	24909858
12	Acetylation	GRKGFGEKASEALKP HHCCCCHHHHHHHCC	58.55	24489116
12	Ubiquitination	GRKGFGEKASEALKP HHCCCCHHHHHHHCC	58.55	23749301
12	2-Hydroxyisobutyrylation	GRKGFGEKASEALKP HHCCCCHHHHHHHCC	58.55	-
14	Phosphorylation	KGFGEKASEALKPDS CCCCHHHHHHHCCCC	34.17	22890988
18	2-Hydroxyisobutyrylation	EKASEALKPDSQKSY HHHHHHHCCCCHHHH	54.55	-
18	Acetylation	EKASEALKPDSQKSY HHHHHHHCCCCHHHH	54.55	24489116
18	Ubiquitination	EKASEALKPDSQKSY HHHHHHHCCCCHHHH	54.55	23749301
18	Succinylation	EKASEALKPDSQKSY HHHHHHHCCCCHHHH	54.55	23954790
21	Phosphorylation	SEALKPDSQKSYAEQ HHHHCCCCHHHHHHH	48.30	22369663
23	2-Hydroxyisobutyrylation	ALKPDSQKSYAEQGK HHCCCCHHHHHHHHH	49.76	-
23	Succinylation	ALKPDSQKSYAEQGK HHCCCCHHHHHHHHH	49.76	23954790
23	Ubiquitination	ALKPDSQKSYAEQGK HHCCCCHHHHHHHHH	49.76	23749301
23	Acetylation	ALKPDSQKSYAEQGK HHCCCCHHHHHHHHH	49.76	22865919
24	Phosphorylation	LKPDSQKSYAEQGKE HCCCCHHHHHHHHHH	23.18	22369663
25	Phosphorylation	KPDSQKSYAEQGKEY CCCCHHHHHHHHHHH	22.61	20377248
30	Acetylation	KSYAEQGKEYITDKA HHHHHHHHHHHHCHH	47.22	24489116
30	2-Hydroxyisobutyrylation	KSYAEQGKEYITDKA HHHHHHHHHHHHCHH	47.22	-
30	Succinylation	KSYAEQGKEYITDKA HHHHHHHHHHHHCHH	47.22	23954790
30	Ubiquitination	KSYAEQGKEYITDKA HHHHHHHHHHHHCHH	47.22	23749301
32	Phosphorylation	YAEQGKEYITDKADK HHHHHHHHHHCHHHH	16.77	19779198
34	Phosphorylation	EQGKEYITDKADKVA HHHHHHHHCHHHHHC	30.46	30377154
36	2-Hydroxyisobutyrylation	GKEYITDKADKVAGK HHHHHHCHHHHHCCC	50.24	-
36	Acetylation	GKEYITDKADKVAGK HHHHHHCHHHHHCCC	50.24	24489116
39	2-Hydroxyisobutyrylation	YITDKADKVAGKVQP HHHCHHHHHCCCCCC	38.55	-
39	Acetylation	YITDKADKVAGKVQP HHHCHHHHHCCCCCC	38.55	24489116
43	2-Hydroxyisobutyrylation	KADKVAGKVQPEDNK HHHHHCCCCCCCCCC	28.14	-
43	Acetylation	KADKVAGKVQPEDNK HHHHHCCCCCCCCCC	28.14	22865919
43	Ubiquitination	KADKVAGKVQPEDNK HHHHHCCCCCCCCCC	28.14	23749301
43	Succinylation	KADKVAGKVQPEDNK HHHHHCCCCCCCCCC	28.14	23954790
50	Ubiquitination	KVQPEDNKGVFQGVH CCCCCCCCCCCCCHH	69.63	17644757
50	Acetylation	KVQPEDNKGVFQGVH CCCCCCCCCCCCCHH	69.63	24489116
50	2-Hydroxyisobutyrylation	KVQPEDNKGVFQGVH CCCCCCCCCCCCCHH	69.63	-
59	Phosphorylation	VFQGVHDSAEKGKDN CCCCHHHCHHHCCCC	24.37	22369663
62	Acetylation	GVHDSAEKGKDNAEG CHHHCHHHCCCCCCC	71.61	24489116
62	2-Hydroxyisobutyrylation	GVHDSAEKGKDNAEG CHHHCHHHCCCCCCC	71.61	-
62	Ubiquitination	GVHDSAEKGKDNAEG CHHHCHHHCCCCCCC	71.61	17644757
64	Acetylation	HDSAEKGKDNAEGQG HHCHHHCCCCCCCCC	59.90	24489116
64	Ubiquitination	HDSAEKGKDNAEGQG HHCHHHCCCCCCCCC	59.90	23749301
64	2-Hydroxyisobutyrylation	HDSAEKGKDNAEGQG HHCHHHCCCCCCCCC	59.90	-
73	Phosphorylation	NAEGQGESLADQARD CCCCCCCCHHHHHHH	35.36	22369663
81	Phosphorylation	LADQARDYMGAAKSK HHHHHHHHHHHHHHH	7.59	22369663
86	Acetylation	RDYMGAAKSKLNDAV HHHHHHHHHHHHHHH	47.81	25381059
86	2-Hydroxyisobutyrylation	RDYMGAAKSKLNDAV HHHHHHHHHHHHHHH	47.81	-
86	Succinylation	RDYMGAAKSKLNDAV HHHHHHHHHHHHHHH	47.81	23954790
86	Ubiquitination	RDYMGAAKSKLNDAV HHHHHHHHHHHHHHH	47.81	23749301
87	Phosphorylation	DYMGAAKSKLNDAVE HHHHHHHHHHHHHHH	37.33	21082442
88	2-Hydroxyisobutyrylation	YMGAAKSKLNDAVEY HHHHHHHHHHHHHHH	51.07	-
88	Acetylation	YMGAAKSKLNDAVEY HHHHHHHHHHHHHHH	51.07	24489116
88	Ubiquitination	YMGAAKSKLNDAVEY HHHHHHHHHHHHHHH	51.07	23749301
95	Phosphorylation	KLNDAVEYVSGRVHG HHHHHHHHHHCCCCC	8.04	29136822
97	Phosphorylation	NDAVEYVSGRVHGEE HHHHHHHHCCCCCCC	21.71	22369663
108	Ubiquitination	HGEEDPTKK------ CCCCCCCCC------	62.97	17644757
108	Acetylation	HGEEDPTKK------ CCCCCCCCC------	62.97	24489116
108	Succinylation	HGEEDPTKK------ CCCCCCCCC------	62.97	23954790
109	Ubiquitination	GEEDPTKK------- CCCCCCCC-------	68.96	17644757

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
21	S	Phosphorylation	Kinase	ATM	P38110	Uniprot
21	S	Phosphorylation	Kinase	ATR	P38111	Uniprot
21	S	Phosphorylation	Kinase	ATM/ATR	-	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of HSP12_YEAST !!

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 HSP12_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CYPH_YEAST	CPR1	physical	11805837
CALM_YEAST	CMD1	physical	16554755
RFA2_YEAST	RFA2	physical	16554755
PEX19_YEAST	PEX19	genetic	27708008
UBCX_YEAST	PEX4	genetic	27708008
STE24_YEAST	STE24	genetic	27708008

Drug and Disease Associations

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

Regulatory Network of HSP12_YEAST

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-21; SER-24; SER-59;SER-73; SER-87 AND SER-97, AND MASS SPECTROMETRY.	18407956 [Abstract]
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-24; SER-59;SER-73 AND SER-87, AND MASS SPECTROMETRY.	17563356 [Abstract]
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-24, AND MASSSPECTROMETRY.	17287358 [Abstract]