dbPTM

TRAP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TRAP1_HUMAN
UniProt AC	Q12931
Protein Name	Heat shock protein 75 kDa, mitochondrial
Gene Name	TRAP1
Organism	Homo sapiens (Human).
Sequence Length	704
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	MARELRALLLWGRRLRPLLRAPALAAVPGGKPILCPRRTTAQLGPRRNPAWSLQAGRLFSTQTAEDKEEPLHSIISSTESVQGSTSKHEFQAETKKLLDIVARSLYSEKEVFIRELISNASDALEKLRHKLVSDGQALPEMEIHLQTNAEKGTITIQDTGIGMTQEELVSNLGTIARSGSKAFLDALQNQAEASSKIIGQFGVGFYSAFMVADRVEVYSRSAAPGSLGYQWLSDGSGVFEIAEASGVRTGTKIIIHLKSDCKEFSSEARVRDVVTKYSNFVSFPLYLNGRRMNTLQAIWMMDPKDVREWQHEEFYRYVAQAHDKPRYTLHYKTDAPLNIRSIFYVPDMKPSMFDVSRELGSSVALYSRKVLIQTKATDILPKWLRFIRGVVDSEDIPLNLSRELLQESALIRKLRDVLQQRLIKFFIDQSKKDAEKYAKFFEDYGLFMREGIVTATEQEVKEDIAKLLRYESSALPSGQLTSLSEYASRMRAGTRNIYYLCAPNRHLAEHSPYYEAMKKKDTEVLFCFEQFDELTLLHLREFDKKKLISVETDIVVDHYKEEKFEDRSPAAECLSEKETEELMAWMRNVLGSRVTNVKVTLRLDTHPAMVTVLEMGAARHFLRMQQLAKTQEERAQLLQPTLEINPRHALIKKLNQLRASEPGLAQLLVDQIYENAMIAAGLVDDPRAMVGRLNELLVKALERH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
39	Phosphorylation	PILCPRRTTAQLGPR CCCCCCCCCCCCCCC	27.97	24732914
40	Phosphorylation	ILCPRRTTAQLGPRR CCCCCCCCCCCCCCC	15.59	-
56	Ubiquitination	PAWSLQAGRLFSTQT CCHHHHCCCCCCCCC	17.54	-
60	Phosphorylation	LQAGRLFSTQTAEDK HHCCCCCCCCCCCCC	24.97	22817901
61	Phosphorylation	QAGRLFSTQTAEDKE HCCCCCCCCCCCCCC	23.70	28787133
63	Phosphorylation	GRLFSTQTAEDKEEP CCCCCCCCCCCCCCC	31.91	28787133
73	Acetylation	DKEEPLHSIISSTES CCCCCHHHHHHCCCC	29.33	-
73	Phosphorylation	DKEEPLHSIISSTES CCCCCHHHHHHCCCC	29.33	26657352
76	Phosphorylation	EPLHSIISSTESVQG CCHHHHHHCCCCCCC	29.54	23312004
77	Phosphorylation	PLHSIISSTESVQGS CHHHHHHCCCCCCCC	26.28	25849741
78	Phosphorylation	LHSIISSTESVQGST HHHHHHCCCCCCCCC	26.03	25627689
80	Phosphorylation	SIISSTESVQGSTSK HHHHCCCCCCCCCCC	21.59	23312004
95	2-Hydroxyisobutyrylation	HEFQAETKKLLDIVA HHHHHHHHHHHHHHH	32.69	-
109	Ubiquitination	ARSLYSEKEVFIREL HHHCCCCHHHHHHHH	53.92	21890473
109	2-Hydroxyisobutyrylation	ARSLYSEKEVFIREL HHHCCCCHHHHHHHH	53.92	-
109	Acetylation	ARSLYSEKEVFIREL HHHCCCCHHHHHHHH	53.92	25825284
109	Ubiquitination	ARSLYSEKEVFIREL HHHCCCCHHHHHHHH	53.92	21890473
118	Phosphorylation	VFIRELISNASDALE HHHHHHHHCHHHHHH	38.68	20860994
121	Phosphorylation	RELISNASDALEKLR HHHHHCHHHHHHHHH	27.89	-
126	2-Hydroxyisobutyrylation	NASDALEKLRHKLVS CHHHHHHHHHHHHHC	52.23	-
126	Acetylation	NASDALEKLRHKLVS CHHHHHHHHHHHHHC	52.23	23749302
126	Succinylation	NASDALEKLRHKLVS CHHHHHHHHHHHHHC	52.23	27452117
130	2-Hydroxyisobutyrylation	ALEKLRHKLVSDGQA HHHHHHHHHHCCCCC	44.12	-
130	Acetylation	ALEKLRHKLVSDGQA HHHHHHHHHHCCCCC	44.12	25953088
147	Phosphorylation	EMEIHLQTNAEKGTI CEEEEEECCCCCCEE	42.63	27251275
153	Phosphorylation	QTNAEKGTITIQDTG ECCCCCCEEEEEECC	26.47	20068231
155	Phosphorylation	NAEKGTITIQDTGIG CCCCCEEEEEECCCC	16.66	24043423
159	Phosphorylation	GTITIQDTGIGMTQE CEEEEEECCCCCCHH	17.83	24043423
164	Phosphorylation	QDTGIGMTQEELVSN EECCCCCCHHHHHHH	27.84	24043423
170	Phosphorylation	MTQEELVSNLGTIAR CCHHHHHHHHHHHHH	38.67	24043423
174	Phosphorylation	ELVSNLGTIARSGSK HHHHHHHHHHHHCCH	18.03	20068231
178	Phosphorylation	NLGTIARSGSKAFLD HHHHHHHHCCHHHHH	38.09	23312004
180	Phosphorylation	GTIARSGSKAFLDAL HHHHHHCCHHHHHHH	23.27	23312004
181	Ubiquitination	TIARSGSKAFLDALQ HHHHHCCHHHHHHHH	46.84	-
194	Phosphorylation	LQNQAEASSKIIGQF HHHHHHHHHHHHHHH	24.54	25159151
195	Phosphorylation	QNQAEASSKIIGQFG HHHHHHHHHHHHHHC	34.62	30108239
221	Phosphorylation	RVEVYSRSAAPGSLG EEEEEECCCCCCCCC	23.89	28857561
223	Acetylation	EVYSRSAAPGSLGYQ EEEECCCCCCCCCCE	15.38	-
226	Phosphorylation	SRSAAPGSLGYQWLS ECCCCCCCCCCEECC	19.98	28857561
233	Phosphorylation	SLGYQWLSDGSGVFE CCCCEECCCCCCEEE	36.65	28857561
236	Phosphorylation	YQWLSDGSGVFEIAE CEECCCCCCEEEEHH	36.45	28857561
245	Phosphorylation	VFEIAEASGVRTGTK EEEEHHHHCCCCCCE	29.35	28857561
249	Phosphorylation	AEASGVRTGTKIIIH HHHHCCCCCCEEEEE	46.96	28857561
258	2-Hydroxyisobutyrylation	TKIIIHLKSDCKEFS CEEEEEECCCHHHCC	30.04	-
258	Acetylation	TKIIIHLKSDCKEFS CEEEEEECCCHHHCC	30.04	25953088
262	Acetylation	IHLKSDCKEFSSEAR EEECCCHHHCCCHHH	67.78	26051181
271	Acetylation	FSSEARVRDVVTKYS CCCHHHHHHHHHHHC	26.00	-
276	Acetylation	RVRDVVTKYSNFVSF HHHHHHHHHCCCCCC	34.76	23236377
279	Acetylation	DVVTKYSNFVSFPLY HHHHHHCCCCCCCEE	37.94	-
279	Ubiquitination	DVVTKYSNFVSFPLY HHHHHHCCCCCCCEE	37.94	-
282	Phosphorylation	TKYSNFVSFPLYLNG HHHCCCCCCCEEECC	19.60	19651622
317	Phosphorylation	QHEEFYRYVAQAHDK HHHHHHHHHHHHCCC	6.69	28152594
324	2-Hydroxyisobutyrylation	YVAQAHDKPRYTLHY HHHHHCCCCCEEEEE	22.87	-
324	Acetylation	YVAQAHDKPRYTLHY HHHHHCCCCCEEEEE	22.87	23749302
324	Succinylation	YVAQAHDKPRYTLHY HHHHHCCCCCEEEEE	22.87	27452117
324	Ubiquitination	YVAQAHDKPRYTLHY HHHHHCCCCCEEEEE	22.87	-
329	Ubiquitination	HDKPRYTLHYKTDAP CCCCCEEEEEECCCC	2.85	-
331	Phosphorylation	KPRYTLHYKTDAPLN CCCEEEEEECCCCCC	20.78	-
332	2-Hydroxyisobutyrylation	PRYTLHYKTDAPLNI CCEEEEEECCCCCCE	29.22	-
332	Acetylation	PRYTLHYKTDAPLNI CCEEEEEECCCCCCE	29.22	19608861
332	Malonylation	PRYTLHYKTDAPLNI CCEEEEEECCCCCCE	29.22	26320211
332	Succinylation	PRYTLHYKTDAPLNI CCEEEEEECCCCCCE	29.22	27452117
332	Ubiquitination	PRYTLHYKTDAPLNI CCEEEEEECCCCCCE	29.22	19608861
333	Phosphorylation	RYTLHYKTDAPLNIR CEEEEEECCCCCCEE	30.17	-
341	Phosphorylation	DAPLNIRSIFYVPDM CCCCCEEEEEECCCC	17.16	20068231
344	Phosphorylation	LNIRSIFYVPDMKPS CCEEEEEECCCCCHH	14.92	20068231
349	Acetylation	IFYVPDMKPSMFDVS EEECCCCCHHHHHHH	41.12	25953088
361	Phosphorylation	DVSRELGSSVALYSR HHHHHHCCHHHHHHC	33.97	21406692
362	Phosphorylation	VSRELGSSVALYSRK HHHHHCCHHHHHHCC	15.04	21406692
366	Phosphorylation	LGSSVALYSRKVLIQ HCCHHHHHHCCEEEE	9.19	21406692
367	Phosphorylation	GSSVALYSRKVLIQT CCHHHHHHCCEEEEC	26.86	24719451
369	2-Hydroxyisobutyrylation	SVALYSRKVLIQTKA HHHHHHCCEEEECCC	35.14	-
371	Acetylation	ALYSRKVLIQTKATD HHHHCCEEEECCCHH	2.42	-
375	2-Hydroxyisobutyrylation	RKVLIQTKATDILPK CCEEEECCCHHCHHH	32.67	-
375	Succinylation	RKVLIQTKATDILPK CCEEEECCCHHCHHH	32.67	27452117
377	Phosphorylation	VLIQTKATDILPKWL EEEECCCHHCHHHHH	25.73	24505115
378	Acetylation	LIQTKATDILPKWLR EEECCCHHCHHHHHH	45.33	-
382	2-Hydroxyisobutyrylation	KATDILPKWLRFIRG CCHHCHHHHHHHHHC	56.25	-
382	Acetylation	KATDILPKWLRFIRG CCHHCHHHHHHHHHC	56.25	19608861
382	Ubiquitination	KATDILPKWLRFIRG CCHHCHHHHHHHHHC	56.25	19608861
388	Methylation	PKWLRFIRGVVDSED HHHHHHHHCCCCCCC	29.19	115479779
393	Phosphorylation	FIRGVVDSEDIPLNL HHHCCCCCCCCCCCC	26.09	23911959
401	Phosphorylation	EDIPLNLSRELLQES CCCCCCCCHHHHHHH	23.72	30278072
408	Acetylation	SRELLQESALIRKLR CHHHHHHHHHHHHHH	18.53	-
408	Phosphorylation	SRELLQESALIRKLR CHHHHHHHHHHHHHH	18.53	26471730
424	2-Hydroxyisobutyrylation	VLQQRLIKFFIDQSK HHHHHHHHHHHCCCH	38.52	-
424	Acetylation	VLQQRLIKFFIDQSK HHHHHHHHHHHCCCH	38.52	19608861
424	Malonylation	VLQQRLIKFFIDQSK HHHHHHHHHHHCCCH	38.52	26320211
424	Succinylation	VLQQRLIKFFIDQSK HHHHHHHHHHHCCCH	38.52	27452117
431	2-Hydroxyisobutyrylation	KFFIDQSKKDAEKYA HHHHCCCHHHHHHHH	49.38	-
431	Acetylation	KFFIDQSKKDAEKYA HHHHCCCHHHHHHHH	49.38	23954790
431	Malonylation	KFFIDQSKKDAEKYA HHHHCCCHHHHHHHH	49.38	26320211
432	Acetylation	FFIDQSKKDAEKYAK HHHCCCHHHHHHHHH	68.37	7705877
437	Phosphorylation	SKKDAEKYAKFFEDY CHHHHHHHHHHHHHH	13.41	25367160
444	Phosphorylation	YAKFFEDYGLFMREG HHHHHHHHCCHHHCC	14.45	29083192
461	Acetylation	TATEQEVKEDIAKLL CCCHHHHHHHHHHHH	49.25	26822725
461	Ubiquitination	TATEQEVKEDIAKLL CCCHHHHHHHHHHHH	49.25	-
466	Acetylation	EVKEDIAKLLRYESS HHHHHHHHHHHHHHC	48.68	19608861
470	Phosphorylation	DIAKLLRYESSALPS HHHHHHHHHHCCCCC	21.82	28152594
472	Phosphorylation	AKLLRYESSALPSGQ HHHHHHHHCCCCCCC	16.39	28152594
473	Phosphorylation	KLLRYESSALPSGQL HHHHHHHCCCCCCCC	23.14	28152594
481	Phosphorylation	ALPSGQLTSLSEYAS CCCCCCCCCHHHHHH	21.53	28152594
482	Phosphorylation	LPSGQLTSLSEYASR CCCCCCCCHHHHHHH	38.19	28152594
484	Phosphorylation	SGQLTSLSEYASRMR CCCCCCHHHHHHHHC	28.47	28152594
486	Phosphorylation	QLTSLSEYASRMRAG CCCCHHHHHHHHCCC	13.39	29759185
488	Phosphorylation	TSLSEYASRMRAGTR CCHHHHHHHHCCCCC	26.21	29759185
494	Phosphorylation	ASRMRAGTRNIYYLC HHHHCCCCCCEEEEE	21.40	18669648
498	Phosphorylation	RAGTRNIYYLCAPNR CCCCCCEEEEECCCH	8.24	27273156
499	Phosphorylation	AGTRNIYYLCAPNRH CCCCCEEEEECCCHH	7.48	28152594
501	S-nitrosocysteine	TRNIYYLCAPNRHLA CCCEEEEECCCHHHH	3.23	-
501	S-nitrosylation	TRNIYYLCAPNRHLA CCCEEEEECCCHHHH	3.23	19483679
505	Methylation	YYLCAPNRHLAEHSP EEEECCCHHHHHCCH	25.74	115479787
511	Phosphorylation	NRHLAEHSPYYEAMK CHHHHHCCHHHHHHH	13.20	26074081
513	Phosphorylation	HLAEHSPYYEAMKKK HHHHCCHHHHHHHHC	19.56	26074081
514	Phosphorylation	LAEHSPYYEAMKKKD HHHCCHHHHHHHHCC	10.70	26074081
518	2-Hydroxyisobutyrylation	SPYYEAMKKKDTEVL CHHHHHHHHCCCEEE	64.81	-
518	Acetylation	SPYYEAMKKKDTEVL CHHHHHHHHCCCEEE	64.81	23954790
545	Succinylation	HLREFDKKKLISVET EHHHCCCCCCEEEEE	55.44	23954790
560	2-Hydroxyisobutyrylation	DIVVDHYKEEKFEDR CEEECCCCHHCCCCC	56.85	-
567	Methylation	KEEKFEDRSPAAECL CHHCCCCCCCHHHHC	37.02	115479771
568	Phosphorylation	EEKFEDRSPAAECLS HHCCCCCCCHHHHCC	31.08	27050516
573	Glutathionylation	DRSPAAECLSEKETE CCCCHHHHCCHHHHH	4.31	22555962
577	Acetylation	AAECLSEKETEELMA HHHHCCHHHHHHHHH	67.57	25953088
592	Phosphorylation	WMRNVLGSRVTNVKV HHHHHHCCCCCCEEE	21.29	29214152
598	2-Hydroxyisobutyrylation	GSRVTNVKVTLRLDT CCCCCCEEEEEEECC	31.41	-
598	Acetylation	GSRVTNVKVTLRLDT CCCCCCEEEEEEECC	31.41	25953088
598	Succinylation	GSRVTNVKVTLRLDT CCCCCCEEEEEEECC	31.41	27452117
609	Sulfoxidation	RLDTHPAMVTVLEMG EECCCHHHHHHHHHH	2.82	21406390
629	2-Hydroxyisobutyrylation	LRMQQLAKTQEERAQ HHHHHHHHCHHHHHH	60.37	-
629	Acetylation	LRMQQLAKTQEERAQ HHHHHHHHCHHHHHH	60.37	26210075
646	Ubiquitination	QPTLEINPRHALIKK HHHHCCCHHHHHHHH	34.79	-
652	Acetylation	NPRHALIKKLNQLRA CHHHHHHHHHHHHHC	52.65	21339330
699	Ubiquitination	RLNELLVKALERH-- HHHHHHHHHHHHC--	47.42	21890473
699	2-Hydroxyisobutyrylation	RLNELLVKALERH-- HHHHHHHHHHHHC--	47.42	-
699	Ubiquitination	RLNELLVKALERH-- HHHHHHHHHHHHC--	47.42	21890473

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
511	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
511	S	Phosphorylation	Kinase	MAPK3	P27361	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TRAP1_HUMAN !!

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 TRAP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RB_HUMAN	RB1	physical	8756626
PRS6B_HUMAN	PSMC4	physical	21979464
A4_HUMAN	APP	physical	21832049
WDHD1_HUMAN	WDHD1	physical	22939629
VDAC2_HUMAN	VDAC2	physical	22939629
VAMP2_HUMAN	VAMP2	physical	22939629
IF4A1_HUMAN	EIF4A1	physical	24113185
EF1G_HUMAN	EEF1G	physical	24113185
EF1A1_HUMAN	EEF1A1	physical	24113185
GRP78_HUMAN	HSPA5	physical	24113185
G3P_HUMAN	GAPDH	physical	24113185
RS19_HUMAN	RPS19	physical	24113185
RL7A_HUMAN	RPL7A	physical	24113185
E2AK4_HUMAN	EIF2AK4	physical	24113185
FKBP5_HUMAN	FKBP5	physical	22863883
ALDOA_HUMAN	ALDOA	physical	26344197
ALDOC_HUMAN	ALDOC	physical	26344197
COQ3_HUMAN	COQ3	physical	26344197
CX6B1_HUMAN	COX6B1	physical	26344197
DUT_HUMAN	DUT	physical	26344197
G3P_HUMAN	GAPDH	physical	26344197
GLRX1_HUMAN	GLRX	physical	26344197
IQGA1_HUMAN	IQGAP1	physical	26344197
LKHA4_HUMAN	LTA4H	physical	26344197
PRDX5_HUMAN	PRDX5	physical	26344197
PDIA3_HUMAN	PDIA3	physical	27173435
PLST_HUMAN	PLS3	physical	27173435

Drug and Disease Associations

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

Regulatory Network of TRAP1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-332; LYS-382; LYS-424 ANDLYS-466, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401, AND MASSSPECTROMETRY.	19690332 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-494, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-366, AND MASSSPECTROMETRY.	17924679 [Abstract]