TRAP1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TRAP1_MOUSE
• UniProt AC: Q9CQN1
• Protein Name: Heat shock protein 75 kDa, mitochondrial
• Gene Name: Trap1
• Organism: Mus musculus (Mouse).
• Sequence Length: 706
• Subcellular Localization: Mitochondrion. Mitochondrion inner membrane. Mitochondrion matrix.
• Protein Description: Chaperone that expresses an ATPase activity. Involved in maintaining mitochondrial function and polarization, downstream of PINK1 and mitochondrial complex I. Is a negative regulator of mitochondrial respiration able to modulate the balance between oxidative phosphorylation and aerobic glycolysis. The impact of TRAP1 on mitochondrial respiration is probably mediated by modulation of mitochondrial SRC and inhibition of SDHA..
• Protein Sequence: MACELRAVLLWGRGLQTVLRAPALAGVRRGKPVLHLQKTTVQFRGPTQSLASGISAGQLYSTQAAEDKEEESLHSIISNTEAVRGSVSKHEFQAETKKLLDIVARSLYSEKEVFIRELISNASDALEKLRHKLVCEGQVLPEMEIHLQTDAKKGTITIQDTGIGMTQEELVSNLGTIARSGSKAFLEALQNQAETSSKIIGQFGVGFYSAFMVADKVEVYSRSAAPESPGYQWLSDGSGVFEIAEASGVRPGTKIIIHLKSDCKDFASESRVQDVVTKYSNFVSFPLYLNGKRINTLQAIWMMDPKDISEFQHEEFYRYIAQAYDKPRFTLHYKTDAPLNIRSIFYVPEMKPSMFDVSRELGSSVALYSRKVLIQTKAADILPKWLRFIRGVVDSEDIPLNLSRELLQESALIRKLRDVLQQRLIKFFIDQSKKDAEKYAKFFEDYGLFMREGIVTTAEQDIKEDIAKLLRYESSALPAGQLTSLPDYASRMQAGTRNIYYLCAPNRHLAEHSPYYEAMKQKHTEVLFCYEQFDELTLLHLREFDKKKLISVETDIVVDHYKEEKFEDTSPADERLSEKETEDLMAWMRNALGSRVTNVKVTFRLDTHPAMVTVLEMGAARHFLRMQQLAKTQEERAQLLQPTLEINPRHTLIKKLCQLRESEPELAQLLVDQIYENAMIAAGLVDDPRAMVGRLNDLLVKVLEKH

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
17	Phosphorylation	LWGRGLQTVLRAPAL HHCCCHHHHHHHHHH	26.93	21183079
61	Phosphorylation	ISAGQLYSTQAAEDK CCHHHCCCCCCCCCC	23.72	20495213
89	Acetylation	AVRGSVSKHEFQAET HHHCCCCHHHHHHHH	45.02	23576753
97	Acetylation	HEFQAETKKLLDIVA HHHHHHHHHHHHHHH	32.69	2394797
111	Acetylation	ARSLYSEKEVFIREL HHHCCCCHHHHHHHH	53.92	23201123
111	Succinylation	ARSLYSEKEVFIREL HHHCCCCHHHHHHHH	53.92	23954790
135	S-nitrosocysteine	KLRHKLVCEGQVLPE HHHHHHHHCCCCCCC	7.63	-
135	S-nitrosylation	KLRHKLVCEGQVLPE HHHHHHHHCCCCCCC	7.63	22178444
152	Acetylation	IHLQTDAKKGTITIQ EEEECCCCCCEEEEE	55.32	23201123
153	Acetylation	HLQTDAKKGTITIQD EEECCCCCCEEEEEE	64.11	15618559
172	Phosphorylation	MTQEELVSNLGTIAR CCHHHHHHHHHHHHH	38.67	-
176	Phosphorylation	ELVSNLGTIARSGSK HHHHHHHHHHHHCCH	18.03	-
180	Phosphorylation	NLGTIARSGSKAFLE HHHHHHHHCCHHHHH	38.09	21082442
182	Phosphorylation	GTIARSGSKAFLEAL HHHHHHCCHHHHHHH	23.27	21183079
195	Phosphorylation	ALQNQAETSSKIIGQ HHHHHHHHHHHHHHH	41.12	25521595
196	Phosphorylation	LQNQAETSSKIIGQF HHHHHHHHHHHHHHH	22.57	25521595
263	S-nitrosylation	IIHLKSDCKDFASES EEEECCCCHHHHCHH	6.18	22178444
263	S-nitrosocysteine	IIHLKSDCKDFASES EEEECCCCHHHHCHH	6.18	-
263	Glutathionylation	IIHLKSDCKDFASES EEEECCCCHHHHCHH	6.18	24333276
264	Acetylation	IHLKSDCKDFASESR EEECCCCHHHHCHHH	61.95	23576753
278	Acetylation	RVQDVVTKYSNFVSF HHHHHHHHHCCCCCC	34.76	23954790
292	Acetylation	FPLYLNGKRINTLQA CCEEECCEECCCEEE	49.37	2374215
306	Acetylation	AIWMMDPKDISEFQH EEEECCCCCHHHHCH	64.53	23954790
326	Succinylation	YIAQAYDKPRFTLHY HHHHHHCCCCEEEEE	25.97	23806337
326	Acetylation	YIAQAYDKPRFTLHY HHHHHHCCCCEEEEE	25.97	23576753
334	Ubiquitination	PRFTLHYKTDAPLNI CCEEEEEECCCCCCE	29.22	-
334	Succinylation	PRFTLHYKTDAPLNI CCEEEEEECCCCCCE	29.22	23954790
334	Acetylation	PRFTLHYKTDAPLNI CCEEEEEECCCCCCE	29.22	23864654
351	Acetylation	IFYVPEMKPSMFDVS EEECCCCCHHHHHHH	32.07	23864654
403	Phosphorylation	EDIPLNLSRELLQES CCCCCCCCHHHHHHH	23.72	25521595
426	Acetylation	VLQQRLIKFFIDQSK HHHHHHHHHHHCCCH	38.52	23576753
426	Succinylation	VLQQRLIKFFIDQSK HHHHHHHHHHHCCCH	38.52	23806337
432	Phosphorylation	IKFFIDQSKKDAEKY HHHHHCCCHHHHHHH	37.61	22817900
433	Succinylation	KFFIDQSKKDAEKYA HHHHCCCHHHHHHHH	49.38	23954790
433	Acetylation	KFFIDQSKKDAEKYA HHHHCCCHHHHHHHH	49.38	23576753
438	Acetylation	QSKKDAEKYAKFFED CCHHHHHHHHHHHHH	52.83	23201123
468	Acetylation	DIKEDIAKLLRYESS HHHHHHHHHHHHHHC	48.68	-
496	Phosphorylation	ASRMQAGTRNIYYLC HHHHCCCCCCEEEEE	24.45	-
500	Phosphorylation	QAGTRNIYYLCAPNR CCCCCCEEEEECCCH	8.24	22817900
503	S-palmitoylation	TRNIYYLCAPNRHLA CCCEEEEECCCHHHH	3.23	28526873
565	Acetylation	VDHYKEEKFEDTSPA ECCCCHHHCCCCCHH	55.96	23954790
569	Phosphorylation	KEEKFEDTSPADERL CHHHCCCCCHHHHHH	29.43	20469934
570	Phosphorylation	EEKFEDTSPADERLS HHHCCCCCHHHHHHC	30.34	20469934
577	Phosphorylation	SPADERLSEKETEDL CHHHHHHCHHHHHHH	53.49	26525534
579	Acetylation	ADERLSEKETEDLMA HHHHHCHHHHHHHHH	67.57	23864654
581	Phosphorylation	ERLSEKETEDLMAWM HHHCHHHHHHHHHHH	45.96	28059163
654	Acetylation	NPRHTLIKKLCQLRE CHHHHHHHHHHHHHC	42.69	23201123

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

Oops, there are no upstream regulatory protein records of TRAP1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TRAP1_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of TRAP1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of TRAP1_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Acetylation

"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-89, AND MASS SPECTROMETRY.
PubMed: 16916647