HSP26_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HSP26_YEAST
• UniProt AC: P15992
• Protein Name: Heat shock protein 26
• Gene Name: HSP26
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 214
• Protein Description: Not known. One of the major polypeptides produced on heat shock..
• Protein Sequence: MSFNSPFFDFFDNINNEVDAFNRLLGEGGLRGYAPRRQLANTPAKDSTGKEVARPNNYAGALYDPRDETLDDWFDNDLSLFPSGFGFPRSVAVPVDILDHDNNYELKVVVPGVKSKKDIDIEYHQNKNQILVSGEIPSTLNEESKDKVKVKESSSGKFKRVITLPDYPGVDADNIKADYANGVLTLTVPKLKPQKDGKNHVKKIEVSSQESWGN

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
2	Acetylation	------MSFNSPFFD ------CCCCCCCHH	32.89	22814378
2	Phosphorylation	------MSFNSPFFD ------CCCCCCCHH	32.89	24909858
5	Phosphorylation	---MSFNSPFFDFFD ---CCCCCCCHHHHH	22.52	29136822
42	Phosphorylation	PRRQLANTPAKDSTG CHHHHCCCCCCCCCC	21.00	22369663
45	Acetylation	QLANTPAKDSTGKEV HHCCCCCCCCCCCCC	54.11	24489116
45	2-Hydroxyisobutyrylation	QLANTPAKDSTGKEV HHCCCCCCCCCCCCC	54.11	-
47	Phosphorylation	ANTPAKDSTGKEVAR CCCCCCCCCCCCCCC	38.05	22369663
48	Phosphorylation	NTPAKDSTGKEVARP CCCCCCCCCCCCCCC	63.51	22369663
50	2-Hydroxyisobutyrylation	PAKDSTGKEVARPNN CCCCCCCCCCCCCCC	49.45	-
50	Ubiquitination	PAKDSTGKEVARPNN CCCCCCCCCCCCCCC	49.45	24961812
90	Phosphorylation	SGFGFPRSVAVPVDI CCCCCCCCEEEEEEE	18.05	22369663
114	2-Hydroxyisobutyrylation	KVVVPGVKSKKDIDI EEEECCCCCCCCEEE	63.57	-
115	Phosphorylation	VVVPGVKSKKDIDIE EEECCCCCCCCEEEE	42.40	29136822
116	Acetylation	VVPGVKSKKDIDIEY EECCCCCCCCEEEEE	49.07	24489116
116	2-Hydroxyisobutyrylation	VVPGVKSKKDIDIEY EECCCCCCCCEEEEE	49.07	-
117	Acetylation	VPGVKSKKDIDIEYH ECCCCCCCCEEEEEE	67.99	24489116
117	2-Hydroxyisobutyrylation	VPGVKSKKDIDIEYH ECCCCCCCCEEEEEE	67.99	-
133	Phosphorylation	NKNQILVSGEIPSTL CCCEEEEECCCCCCC	27.54	24909858
138	Phosphorylation	LVSGEIPSTLNEESK EEECCCCCCCCHHHC	51.71	24909858
139	Phosphorylation	VSGEIPSTLNEESKD EECCCCCCCCHHHCC	28.40	22369663
144	Phosphorylation	PSTLNEESKDKVKVK CCCCCHHHCCCEEEE	39.72	22369663
145	Acetylation	STLNEESKDKVKVKE CCCCHHHCCCEEEEE	65.92	24489116
145	Ubiquitination	STLNEESKDKVKVKE CCCCHHHCCCEEEEE	65.92	18433149
147	2-Hydroxyisobutyrylation	LNEESKDKVKVKESS CCHHHCCCEEEEECC	47.92	-
147	Acetylation	LNEESKDKVKVKESS CCHHHCCCEEEEECC	47.92	24489116
153	Phosphorylation	DKVKVKESSSGKFKR CCEEEEECCCCCCEE	24.88	28889911
155	Phosphorylation	VKVKESSSGKFKRVI EEEEECCCCCCEEEE	56.11	28889911
157	2-Hydroxyisobutyrylation	VKESSSGKFKRVITL EEECCCCCCEEEEEC	50.05	-
159	Acetylation	ESSSGKFKRVITLPD ECCCCCCEEEEECCC	49.60	25381059
163	Phosphorylation	GKFKRVITLPDYPGV CCCEEEEECCCCCCC	29.40	22369663
167	Phosphorylation	RVITLPDYPGVDADN EEEECCCCCCCCHHH	10.43	22369663
192	2-Hydroxyisobutyrylation	TLTVPKLKPQKDGKN EEEECCCCCCCCCCC	52.08	-
195	Acetylation	VPKLKPQKDGKNHVK ECCCCCCCCCCCCCE	76.58	25381059
195	2-Hydroxyisobutyrylation	VPKLKPQKDGKNHVK ECCCCCCCCCCCCCE	76.58	-
207	Phosphorylation	HVKKIEVSSQESWGN CCEEEEECCCCCCCC	17.32	22369663
208	Phosphorylation	VKKIEVSSQESWGN- CEEEEECCCCCCCC-	43.04	22369663
211	Phosphorylation	IEVSSQESWGN---- EEECCCCCCCC----	32.42	22369663

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

Oops, there are no upstream regulatory protein records of HSP26_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of HSP26_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 HSP26_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HSP26_YEAST	HSP26	physical	11967834
HSP26_YEAST	HSP26	physical	10581247
VATB_YEAST	VMA2	physical	16554755
CUL8_YEAST	RTT101	physical	16554755
ADH3_YEAST	ADH3	physical	16554755
RUXE_YEAST	SME1	physical	16554755
TFB4_YEAST	TFB4	physical	16554755
HSP26_YEAST	HSP26	physical	18243115
HSP26_YEAST	HSP26	physical	18719252
RLA2_YEAST	RPP2A	physical	19536198
HSP72_YEAST	SSA2	physical	19536198
MAS5_YEAST	YDJ1	physical	19536198
HSP42_YEAST	HSP42	genetic	22723742
SIS1_YEAST	SIS1	genetic	22723742
MAS5_YEAST	YDJ1	genetic	22723742

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 THR-42; SER-90; THR-163;SER-208 AND SER-211, AND MASS SPECTROMETRY.
PubMed: 18407956

"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-42; SER-208 AND SER-211,AND MASS SPECTROMETRY.
PubMed: 11875433

"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 THR-42, AND MASSSPECTROMETRY.
PubMed: 17563356