dbPTM

GRP75_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GRP75_HUMAN
UniProt AC	P38646
Protein Name	Stress-70 protein, mitochondrial
Gene Name	HSPA9
Organism	Homo sapiens (Human).
Sequence Length	679
Subcellular Localization	Mitochondrion . Nucleus, nucleolus .
Protein Description	Chaperone protein which plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis. Interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU. [PubMed: 26702583 Regulates erythropoiesis via stabilization of ISC assembly]
Protein Sequence	MISASRAAAARLVGAAASRGPTAARHQDSWNGLSHEAFRLVSRRDYASEAIKGAVVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPEVQKDIKNVPFKIVRASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQISGLNVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIVKEFKRETGVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLTMDSSGPKHLNMKLTRAQFEGIVTDLIRRTIAPCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAGDVTDVLLLDVTPLSLGIETLGGVFTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMAGDNKLLGQFTLIGIPPAPRGVPQIEVTFDIDANGIVHVSAKDKGTGREQQIVIQSSGGLSKDDIENMVKNAEKYAEEDRRKKERVEAVNMAEGIIHDTETKMEEFKDQLPADECNKLKEEISKMRELLARKDSETGENIRQAASSLQQASLKLFEMAYKKMASEREGSGSSGTGEQKEDQKEEKQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MISASRAAAA -----CCCHHHHHHH	20.92	17855441
5	Phosphorylation	---MISASRAAAARL ---CCCHHHHHHHHH	18.70	25954137
22	Phosphorylation	AAASRGPTAARHQDS HHHHCCCCCCCCCCC	35.45	22817900
29	Phosphorylation	TAARHQDSWNGLSHE CCCCCCCCCCCCCHH	18.83	28857561
46	Phosphorylation	RLVSRRDYASEAIKG HHHHCHHHHHHHHCC	15.37	19702290
62	Phosphorylation	VVGIDLGTTNSCVAV EEEEECCCCCCEEEE	30.05	17573779
63	Phosphorylation	VGIDLGTTNSCVAVM EEEECCCCCCEEEEE	24.28	20068231
65	Phosphorylation	IDLGTTNSCVAVMEG EECCCCCCEEEEECC	14.10	17573779
76	2-Hydroxyisobutyrylation	VMEGKQAKVLENAEG EECCCCEEEECCCCC	44.87	-
76	Acetylation	VMEGKQAKVLENAEG EECCCCEEEECCCCC	44.87	26210075
76	Malonylation	VMEGKQAKVLENAEG EECCCCEEEECCCCC	44.87	26320211
76	Succinylation	VMEGKQAKVLENAEG EECCCCEEEECCCCC	44.87	27452117
76	Ubiquitination	VMEGKQAKVLENAEG EECCCCEEEECCCCC	44.87	-
86	Phosphorylation	ENAEGARTTPSVVAF CCCCCCCCCCCEEEE	42.39	25159151
87	Phosphorylation	NAEGARTTPSVVAFT CCCCCCCCCCEEEEE	14.17	25159151
89	Phosphorylation	EGARTTPSVVAFTAD CCCCCCCCEEEEECC	27.42	23927012
106	2-Hydroxyisobutyrylation	RLVGMPAKRQAVTNP EECCCCCCCCCCCCC	38.89	-
106	Succinylation	RLVGMPAKRQAVTNP EECCCCCCCCCCCCC	38.89	23954790
106	Ubiquitination	RLVGMPAKRQAVTNP EECCCCCCCCCCCCC	38.89	-
111	Phosphorylation	PAKRQAVTNPNNTFY CCCCCCCCCCCCCCC	48.23	28152594
116	Phosphorylation	AVTNPNNTFYATKRL CCCCCCCCCCCHHHH	25.35	28152594
118	Phosphorylation	TNPNNTFYATKRLIG CCCCCCCCCHHHHHC	16.01	28152594
120	Phosphorylation	PNNTFYATKRLIGRR CCCCCCCHHHHHCCC	12.81	28152594
121	2-Hydroxyisobutyrylation	NNTFYATKRLIGRRY CCCCCCHHHHHCCCC	36.72	-
121	Acetylation	NNTFYATKRLIGRRY CCCCCCHHHHHCCCC	36.72	26051181
121	Succinylation	NNTFYATKRLIGRRY CCCCCCHHHHHCCCC	36.72	23954790
121	Ubiquitination	NNTFYATKRLIGRRY CCCCCCHHHHHCCCC	36.72	-
128	Phosphorylation	KRLIGRRYDDPEVQK HHHHCCCCCCHHHHH	24.28	28152594
135	2-Hydroxyisobutyrylation	YDDPEVQKDIKNVPF CCCHHHHHHHCCCCE	67.60	-
135	Acetylation	YDDPEVQKDIKNVPF CCCHHHHHHHCCCCE	67.60	19608861
135	Malonylation	YDDPEVQKDIKNVPF CCCHHHHHHHCCCCE	67.60	26320211
135	Succinylation	YDDPEVQKDIKNVPF CCCHHHHHHHCCCCE	67.60	-
135	Succinylation	YDDPEVQKDIKNVPF CCCHHHHHHHCCCCE	67.60	-
135	Ubiquitination	YDDPEVQKDIKNVPF CCCHHHHHHHCCCCE	67.60	19608861
138	Acetylation	PEVQKDIKNVPFKIV HHHHHHHCCCCEEEE	63.12	19608861
138	Malonylation	PEVQKDIKNVPFKIV HHHHHHHCCCCEEEE	63.12	26320211
138	Succinylation	PEVQKDIKNVPFKIV HHHHHHHCCCCEEEE	63.12	-
138	Succinylation	PEVQKDIKNVPFKIV HHHHHHHCCCCEEEE	63.12	-
138	Ubiquitination	PEVQKDIKNVPFKIV HHHHHHHCCCCEEEE	63.12	21890473
143	2-Hydroxyisobutyrylation	DIKNVPFKIVRASNG HHCCCCEEEEECCCC	33.93	-
143	Acetylation	DIKNVPFKIVRASNG HHCCCCEEEEECCCC	33.93	19608861
143	Malonylation	DIKNVPFKIVRASNG HHCCCCEEEEECCCC	33.93	26320211
143	Ubiquitination	DIKNVPFKIVRASNG HHCCCCEEEEECCCC	33.93	19608861
148	Phosphorylation	PFKIVRASNGDAWVE CEEEEECCCCCCEEE	30.68	30108239
159	Acetylation	AWVEAHGKLYSPSQI CEEEECCEEECHHHH	34.09	23954790
161	Phosphorylation	VEAHGKLYSPSQIGA EEECCEEECHHHHHH	23.25	28152594
162	Phosphorylation	EAHGKLYSPSQIGAF EECCEEECHHHHHHH	28.63	28152594
164	Phosphorylation	HGKLYSPSQIGAFVL CCEEECHHHHHHHHH	28.61	30108239
173	Acetylation	IGAFVLMKMKETAEN HHHHHHHHCHHHHHH	42.53	25038526
175	2-Hydroxyisobutyrylation	AFVLMKMKETAENYL HHHHHHCHHHHHHHH	46.52	-
175	Acetylation	AFVLMKMKETAENYL HHHHHHCHHHHHHHH	46.52	25038526
175	Succinylation	AFVLMKMKETAENYL HHHHHHCHHHHHHHH	46.52	27452117
175	Ubiquitination	AFVLMKMKETAENYL HHHHHHCHHHHHHHH	46.52	-
177	Phosphorylation	VLMKMKETAENYLGH HHHHCHHHHHHHHCC	33.48	28152594
181	Phosphorylation	MKETAENYLGHTAKN CHHHHHHHHCCCCCC	12.93	28152594
185	Phosphorylation	AENYLGHTAKNAVIT HHHHHCCCCCCEEEE	37.21	28152594
187	Acetylation	NYLGHTAKNAVITVP HHHCCCCCCEEEEEE	46.74	25038526
187	Malonylation	NYLGHTAKNAVITVP HHHCCCCCCEEEEEE	46.74	26320211
187	Succinylation	NYLGHTAKNAVITVP HHHCCCCCCEEEEEE	46.74	27452117
187	Ubiquitination	NYLGHTAKNAVITVP HHHCCCCCCEEEEEE	46.74	-
192	Phosphorylation	TAKNAVITVPAYFND CCCCEEEEEECCCCH	17.53	28152594
196	Nitration	AVITVPAYFNDSQRQ EEEEEECCCCHHHHH	9.24	-
196	Phosphorylation	AVITVPAYFNDSQRQ EEEEEECCCCHHHHH	9.24	28152594
200	Phosphorylation	VPAYFNDSQRQATKD EECCCCHHHHHHCCC	28.50	17525332
205	Phosphorylation	NDSQRQATKDAGQIS CHHHHHHCCCCCCCC	22.56	22817900
206	N6-malonyllysine	DSQRQATKDAGQISG HHHHHHCCCCCCCCC	48.90	-
206	2-Hydroxyisobutyrylation	DSQRQATKDAGQISG HHHHHHCCCCCCCCC	48.90	-
206	Acetylation	DSQRQATKDAGQISG HHHHHHCCCCCCCCC	48.90	23954790
206	Malonylation	DSQRQATKDAGQISG HHHHHHCCCCCCCCC	48.90	26320211
206	Succinylation	DSQRQATKDAGQISG HHHHHHCCCCCCCCC	48.90	-
206	Ubiquitination	DSQRQATKDAGQISG HHHHHHCCCCCCCCC	48.90	-
212	Phosphorylation	TKDAGQISGLNVLRV CCCCCCCCCCCEEEE	29.37	20873877
218	Methylation	ISGLNVLRVINEPTA CCCCCEEEECCCHHH	24.00	115479953
224	Phosphorylation	LRVINEPTAAALAYG EEECCCHHHHHHHHC	23.81	27174698
230	Phosphorylation	PTAAALAYGLDKSED HHHHHHHHCCCCCCC	21.04	27174698
234	2-Hydroxyisobutyrylation	ALAYGLDKSEDKVIA HHHHCCCCCCCEEEE	61.87	-
234	Acetylation	ALAYGLDKSEDKVIA HHHHCCCCCCCEEEE	61.87	19608861
234	Malonylation	ALAYGLDKSEDKVIA HHHHCCCCCCCEEEE	61.87	26320211
234	Succinylation	ALAYGLDKSEDKVIA HHHHCCCCCCCEEEE	61.87	23954790
234	Ubiquitination	ALAYGLDKSEDKVIA HHHHCCCCCCCEEEE	61.87	19608861
235	Phosphorylation	LAYGLDKSEDKVIAV HHHCCCCCCCEEEEE	51.17	30622161
243	Phosphorylation	EDKVIAVYDLGGGTF CCEEEEEEECCCCEE	9.09	30622161
249	Phosphorylation	VYDLGGGTFDISILE EEECCCCEEEEEEEE	22.78	30622161
253	Phosphorylation	GGGTFDISILEIQKG CCCEEEEEEEEEECC	23.98	30622161
265	Ubiquitination	QKGVFEVKSTNGDTF ECCEEEEECCCCCCC	44.35	-
266	Phosphorylation	KGVFEVKSTNGDTFL CCEEEEECCCCCCCC	32.08	28060719
267	Phosphorylation	GVFEVKSTNGDTFLG CEEEEECCCCCCCCC	37.19	28060719
271	Phosphorylation	VKSTNGDTFLGGEDF EECCCCCCCCCCCCH	23.35	28060719
288	2-Hydroxyisobutyrylation	ALLRHIVKEFKRETG HHHHHHHHHHHHHHC	57.75	-
288	Acetylation	ALLRHIVKEFKRETG HHHHHHHHHHHHHHC	57.75	19608861
288	Malonylation	ALLRHIVKEFKRETG HHHHHHHHHHHHHHC	57.75	26320211
288	Succinylation	ALLRHIVKEFKRETG HHHHHHHHHHHHHHC	57.75	27452117
288	Ubiquitination	ALLRHIVKEFKRETG HHHHHHHHHHHHHHC	57.75	19608861
291	Acetylation	RHIVKEFKRETGVDL HHHHHHHHHHHCCCC	50.87	2402089
291	Succinylation	RHIVKEFKRETGVDL HHHHHHHHHHHCCCC	50.87	23954790
294	Phosphorylation	VKEFKRETGVDLTKD HHHHHHHHCCCCCHH	46.68	21406692
299	Phosphorylation	RETGVDLTKDNMALQ HHHCCCCCHHHHHHH	31.71	21406692
300	Acetylation	ETGVDLTKDNMALQR HHCCCCCHHHHHHHH	55.17	19608861
300	Malonylation	ETGVDLTKDNMALQR HHCCCCCHHHHHHHH	55.17	26320211
300	Succinylation	ETGVDLTKDNMALQR HHCCCCCHHHHHHHH	55.17	-
300	Succinylation	ETGVDLTKDNMALQR HHCCCCCHHHHHHHH	55.17	27452117
300	Ubiquitination	ETGVDLTKDNMALQR HHCCCCCHHHHHHHH	55.17	19608861
303	Sulfoxidation	VDLTKDNMALQRVRE CCCCHHHHHHHHHHH	5.89	28465586
307	Methylation	KDNMALQRVREAAEK HHHHHHHHHHHHHHH	30.25	115479961
316	2-Hydroxyisobutyrylation	REAAEKAKCELSSSV HHHHHHHCCCCCCCC	39.03	-
320	O-linked_Glycosylation	EKAKCELSSSVQTDI HHHCCCCCCCCCCCC	9.77	23301498
320	Phosphorylation	EKAKCELSSSVQTDI HHHCCCCCCCCCCCC	9.77	27080861
321	Phosphorylation	KAKCELSSSVQTDIN HHCCCCCCCCCCCCC	47.34	27080861
322	Phosphorylation	AKCELSSSVQTDINL HCCCCCCCCCCCCCC	18.18	27080861
325	Phosphorylation	ELSSSVQTDINLPYL CCCCCCCCCCCCCEE	36.37	27080861
331	Phosphorylation	QTDINLPYLTMDSSG CCCCCCCEEECCCCC	20.26	27080861
333	Phosphorylation	DINLPYLTMDSSGPK CCCCCEEECCCCCCC	17.06	21601212
336	Phosphorylation	LPYLTMDSSGPKHLN CCEEECCCCCCCCCC	26.77	28857561
337	Phosphorylation	PYLTMDSSGPKHLNM CEEECCCCCCCCCCC	55.65	28857561
345	2-Hydroxyisobutyrylation	GPKHLNMKLTRAQFE CCCCCCCHHHHHHHH	45.71	-
345	Acetylation	GPKHLNMKLTRAQFE CCCCCCCHHHHHHHH	45.71	25825284
345	Succinylation	GPKHLNMKLTRAQFE CCCCCCCHHHHHHHH	45.71	27452117
356	Phosphorylation	AQFEGIVTDLIRRTI HHHHHHHHHHHHHHC	24.14	22817900
360	Methylation	GIVTDLIRRTIAPCQ HHHHHHHHHHCHHHH	36.67	92461
362	Phosphorylation	VTDLIRRTIAPCQKA HHHHHHHHCHHHHHH	16.19	22817900
366	S-palmitoylation	IRRTIAPCQKAMQDA HHHHCHHHHHHHCCC	4.85	21044946
368	2-Hydroxyisobutyrylation	RTIAPCQKAMQDAEV HHCHHHHHHHCCCCC	53.17	-
368	Acetylation	RTIAPCQKAMQDAEV HHCHHHHHHHCCCCC	53.17	23954790
368	Malonylation	RTIAPCQKAMQDAEV HHCHHHHHHHCCCCC	53.17	26320211
368	Succinylation	RTIAPCQKAMQDAEV HHCHHHHHHHCCCCC	53.17	-
368	Succinylation	RTIAPCQKAMQDAEV HHCHHHHHHHCCCCC	53.17	-
368	Ubiquitination	RTIAPCQKAMQDAEV HHCHHHHHHHCCCCC	53.17	21890473
376	Phosphorylation	AMQDAEVSKSDIGEV HHCCCCCCHHHCCEE	20.25	20068231
377	2-Hydroxyisobutyrylation	MQDAEVSKSDIGEVI HCCCCCCHHHCCEEE	58.27	-
377	Acetylation	MQDAEVSKSDIGEVI HCCCCCCHHHCCEEE	58.27	23954790
377	Succinylation	MQDAEVSKSDIGEVI HCCCCCCHHHCCEEE	58.27	23954790
377	Ubiquitination	MQDAEVSKSDIGEVI HCCCCCCHHHCCEEE	58.27	-
378	Phosphorylation	QDAEVSKSDIGEVIL CCCCCCHHHCCEEEE	27.27	20068231
389	Sulfoxidation	EVILVGGMTRMPKVQ EEEEECCCCCCHHHH	1.44	21406390
390	Phosphorylation	VILVGGMTRMPKVQQ EEEECCCCCCHHHHH	27.39	20068231
394	2-Hydroxyisobutyrylation	GGMTRMPKVQQTVQD CCCCCCHHHHHHHHH	43.25	-
394	Acetylation	GGMTRMPKVQQTVQD CCCCCCHHHHHHHHH	43.25	25825284
394	Malonylation	GGMTRMPKVQQTVQD CCCCCCHHHHHHHHH	43.25	26320211
394	Succinylation	GGMTRMPKVQQTVQD CCCCCCHHHHHHHHH	43.25	-
394	Succinylation	GGMTRMPKVQQTVQD CCCCCCHHHHHHHHH	43.25	27452117
394	Ubiquitination	GGMTRMPKVQQTVQD CCCCCCHHHHHHHHH	43.25	-
398	Phosphorylation	RMPKVQQTVQDLFGR CCHHHHHHHHHHHCC	11.75	29888752
405	Methylation	TVQDLFGRAPSKAVN HHHHHHCCCCCCCCC	35.67	115479977
408	Phosphorylation	DLFGRAPSKAVNPDE HHHCCCCCCCCCHHH	32.06	25159151
462	Phosphorylation	TKLINRNTTIPTKKS HHHHHCCCCCCCCCH	23.90	20860994
463	Phosphorylation	KLINRNTTIPTKKSQ HHHHCCCCCCCCCHH	28.63	20860994
466	Phosphorylation	NRNTTIPTKKSQVFS HCCCCCCCCCHHHEE	47.45	20860994
467	2-Hydroxyisobutyrylation	RNTTIPTKKSQVFST CCCCCCCCCHHHEEE	45.10	-
467	Succinylation	RNTTIPTKKSQVFST CCCCCCCCCHHHEEE	45.10	23954790
473	Phosphorylation	TKKSQVFSTAADGQT CCCHHHEEECCCCCE	20.48	20860994
480	Phosphorylation	STAADGQTQVEIKVC EECCCCCEEEEEEEE	39.86	20860994
485	Acetylation	GQTQVEIKVCQGERE CCEEEEEEEECCCHH	24.37	26051181
487	S-nitrosocysteine	TQVEIKVCQGEREMA EEEEEEEECCCHHHC	3.50	-
487	S-nitrosylation	TQVEIKVCQGEREMA EEEEEEEECCCHHHC	3.50	22178444
498	Acetylation	REMAGDNKLLGQFTL HHHCCCCCCCCEEEE	50.24	23954790
504	Phosphorylation	NKLLGQFTLIGIPPA CCCCCEEEEEECCCC	15.02	22817900
513	Methylation	IGIPPAPRGVPQIEV EECCCCCCCCCEEEE	61.93	24129315
521	Phosphorylation	GVPQIEVTFDIDANG CCCEEEEEEEECCCC	11.64	15302935
533	Phosphorylation	ANGIVHVSAKDKGTG CCCEEEEEEECCCCC	18.09	-
555	Acetylation	QSSGGLSKDDIENMV ECCCCCCHHHHHHHH	65.54	26051181
555	Ubiquitination	QSSGGLSKDDIENMV ECCCCCCHHHHHHHH	65.54	-
561	Sulfoxidation	SKDDIENMVKNAEKY CHHHHHHHHHHHHHH	2.70	28465586
563	2-Hydroxyisobutyrylation	DDIENMVKNAEKYAE HHHHHHHHHHHHHHH	39.40	-
563	Acetylation	DDIENMVKNAEKYAE HHHHHHHHHHHHHHH	39.40	27452117
563	Succinylation	DDIENMVKNAEKYAE HHHHHHHHHHHHHHH	39.40	23954790
567	Acetylation	NMVKNAEKYAEEDRR HHHHHHHHHHHHHHH	47.56	19608861
567	Succinylation	NMVKNAEKYAEEDRR HHHHHHHHHHHHHHH	47.56	-
567	Succinylation	NMVKNAEKYAEEDRR HHHHHHHHHHHHHHH	47.56	23954790
568	Phosphorylation	MVKNAEKYAEEDRRK HHHHHHHHHHHHHHH	15.68	20068231
584	Sulfoxidation	ERVEAVNMAEGIIHD HHHHHHHHHHCCCCC	2.63	28465586
594	Phosphorylation	GIIHDTETKMEEFKD CCCCCHHHHHHHHHH	37.47	21601212
595	2-Hydroxyisobutyrylation	IIHDTETKMEEFKDQ CCCCHHHHHHHHHHH	37.77	-
595	Acetylation	IIHDTETKMEEFKDQ CCCCHHHHHHHHHHH	37.77	19608861
600	2-Hydroxyisobutyrylation	ETKMEEFKDQLPADE HHHHHHHHHHCCHHH	48.09	-
600	Acetylation	ETKMEEFKDQLPADE HHHHHHHHHHCCHHH	48.09	23954790
600	Malonylation	ETKMEEFKDQLPADE HHHHHHHHHHCCHHH	48.09	26320211
600	Succinylation	ETKMEEFKDQLPADE HHHHHHHHHHCCHHH	48.09	-
600	Succinylation	ETKMEEFKDQLPADE HHHHHHHHHHCCHHH	48.09	27452117
608	S-nitrosocysteine	DQLPADECNKLKEEI HHCCHHHHHHHHHHH	5.83	-
608	S-nitrosylation	DQLPADECNKLKEEI HHCCHHHHHHHHHHH	5.83	22178444
610	2-Hydroxyisobutyrylation	LPADECNKLKEEISK CCHHHHHHHHHHHHH	73.01	-
610	Acetylation	LPADECNKLKEEISK CCHHHHHHHHHHHHH	73.01	23954790
610	Succinylation	LPADECNKLKEEISK CCHHHHHHHHHHHHH	73.01	-
610	Succinylation	LPADECNKLKEEISK CCHHHHHHHHHHHHH	73.01	-
612	2-Hydroxyisobutyrylation	ADECNKLKEEISKMR HHHHHHHHHHHHHHH	55.71	-
612	Acetylation	ADECNKLKEEISKMR HHHHHHHHHHHHHHH	55.71	25825284
612	Malonylation	ADECNKLKEEISKMR HHHHHHHHHHHHHHH	55.71	26320211
612	Succinylation	ADECNKLKEEISKMR HHHHHHHHHHHHHHH	55.71	27452117
612	Ubiquitination	ADECNKLKEEISKMR HHHHHHHHHHHHHHH	55.71	-
616	Phosphorylation	NKLKEEISKMRELLA HHHHHHHHHHHHHHH	24.55	20068231
617	Acetylation	KLKEEISKMRELLAR HHHHHHHHHHHHHHC	47.87	25953088
617	Malonylation	KLKEEISKMRELLAR HHHHHHHHHHHHHHC	47.87	26320211
617	Succinylation	KLKEEISKMRELLAR HHHHHHHHHHHHHHC	47.87	27452117
624	Methylation	KMRELLARKDSETGE HHHHHHHCCCCHHCH	43.19	115479969
625	2-Hydroxyisobutyrylation	MRELLARKDSETGEN HHHHHHCCCCHHCHH	61.06	-
627	Phosphorylation	ELLARKDSETGENIR HHHHCCCCHHCHHHH	39.84	25849741
629	Phosphorylation	LARKDSETGENIRQA HHCCCCHHCHHHHHH	54.47	29083192
638	Phosphorylation	ENIRQAASSLQQASL HHHHHHHHHHHHHHH	34.30	20068231
639	Phosphorylation	NIRQAASSLQQASLK HHHHHHHHHHHHHHH	26.02	20068231
644	Phosphorylation	ASSLQQASLKLFEMA HHHHHHHHHHHHHHH	23.00	26074081
646	2-Hydroxyisobutyrylation	SLQQASLKLFEMAYK HHHHHHHHHHHHHHH	48.94	-
646	Acetylation	SLQQASLKLFEMAYK HHHHHHHHHHHHHHH	48.94	19608861
646	Succinylation	SLQQASLKLFEMAYK HHHHHHHHHHHHHHH	48.94	-
646	Succinylation	SLQQASLKLFEMAYK HHHHHHHHHHHHHHH	48.94	23954790
646	Ubiquitination	SLQQASLKLFEMAYK HHHHHHHHHHHHHHH	48.94	21890473
650	Sulfoxidation	ASLKLFEMAYKKMAS HHHHHHHHHHHHHHH	3.75	21406390
652	Nitration	LKLFEMAYKKMASER HHHHHHHHHHHHHHC	15.16	-
652	Phosphorylation	LKLFEMAYKKMASER HHHHHHHHHHHHHHC	15.16	25056879
653	2-Hydroxyisobutyrylation	KLFEMAYKKMASERE HHHHHHHHHHHHHCC	26.91	-
653	Acetylation	KLFEMAYKKMASERE HHHHHHHHHHHHHCC	26.91	25953088
653	Methylation	KLFEMAYKKMASERE HHHHHHHHHHHHHCC	26.91	2402095
653	Succinylation	KLFEMAYKKMASERE HHHHHHHHHHHHHCC	26.91	23954790
653	Ubiquitination	KLFEMAYKKMASERE HHHHHHHHHHHHHCC	26.91	-
657	Phosphorylation	MAYKKMASEREGSGS HHHHHHHHHCCCCCC	33.42	26074081
662	Phosphorylation	MASEREGSGSSGTGE HHHHCCCCCCCCCCC	30.65	26074081
664	Phosphorylation	SEREGSGSSGTGEQK HHCCCCCCCCCCCCC	27.56	28985074
665	Phosphorylation	EREGSGSSGTGEQKE HCCCCCCCCCCCCCH	43.85	26074081
667	Phosphorylation	EGSGSSGTGEQKEDQ CCCCCCCCCCCCHHH	39.22	26074081
671	Acetylation	SSGTGEQKEDQKEEK CCCCCCCCHHHHHHH	59.98	2402099
675	Acetylation	GEQKEDQKEEKQ--- CCCCHHHHHHHC---	78.96	129531
678	Acetylation	KEDQKEEKQ------ CHHHHHHHC------	63.50	2402101

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
62	T	Phosphorylation	Kinase	TTK	P33981	PSP
65	S	Phosphorylation	Kinase	TTK	P33981	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of GRP75_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 GRP75_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
P53_HUMAN	TP53	physical	11900485
DNLZ_HUMAN	DNLZ	physical	22162012
PRKN_HUMAN	PARK2	physical	21640711
DNJA3_HUMAN	DNAJA3	physical	22544056
TIM14_HUMAN	DNAJC19	physical	22544056
A4_HUMAN	APP	physical	21832049
RAI3_HUMAN	GPRC5A	physical	22939629
NDUS8_HUMAN	NDUFS8	physical	22939629
P73_HUMAN	TP73	physical	22340593
XPO1_HUMAN	XPO1	physical	21988832
LSM8_HUMAN	LSM8	physical	21988832
ABHEA_HUMAN	ABHD14A	physical	22863883
AIP_HUMAN	AIP	physical	22863883
BZW2_HUMAN	BZW2	physical	22863883
CNBP_HUMAN	CNBP	physical	22863883
ECHM_HUMAN	ECHS1	physical	22863883
IF4E_HUMAN	EIF4E	physical	22863883
IF6_HUMAN	EIF6	physical	22863883
G3P_HUMAN	GAPDH	physical	22863883
PSF3_HUMAN	GINS3	physical	22863883
OSGEP_HUMAN	OSGEP	physical	22863883
GDS1_HUMAN	RAP1GDS1	physical	22863883
CDN2A_HUMAN	CDKN2A	physical	19049976
ARF_HUMAN	CDKN2A	physical	19049976
YKT6_HUMAN	YKT6	physical	25416956
AHNK_HUMAN	AHNAK	physical	26344197
THOC4_HUMAN	ALYREF	physical	26344197
CCD58_HUMAN	CCDC58	physical	26344197
COF1_HUMAN	CFL1	physical	26344197
DNJA4_HUMAN	DNAJA4	physical	26344197
DNJB1_HUMAN	DNAJB1	physical	26344197
DNJB4_HUMAN	DNAJB4	physical	26344197
DNJC1_HUMAN	DNAJC1	physical	26344197
DNJC3_HUMAN	DNAJC3	physical	26344197
DNJC8_HUMAN	DNAJC8	physical	26344197
DNJC9_HUMAN	DNAJC9	physical	26344197
DUT_HUMAN	DUT	physical	26344197
G3BP1_HUMAN	G3BP1	physical	26344197
LYAG_HUMAN	GAA	physical	26344197
RACK1_HUMAN	GNB2L1	physical	26344197
GRPE1_HUMAN	GRPEL1	physical	26344197
HNRPD_HUMAN	HNRNPD	physical	26344197
HNRPU_HUMAN	HNRNPU	physical	26344197
HCD2_HUMAN	HSD17B10	physical	26344197
HSP72_HUMAN	HSPA2	physical	26344197
HSP74_HUMAN	HSPA4	physical	26344197
HS74L_HUMAN	HSPA4L	physical	26344197
HSP7C_HUMAN	HSPA8	physical	26344197
HS105_HUMAN	HSPH1	physical	26344197
ITPA_HUMAN	ITPA	physical	26344197
LDHA_HUMAN	LDHA	physical	26344197
LDHB_HUMAN	LDHB	physical	26344197
PDCD6_HUMAN	PDCD6	physical	26344197
OFUT1_HUMAN	POFUT1	physical	26344197
PTBP1_HUMAN	PTBP1	physical	26344197
STMN1_HUMAN	STMN1	physical	26344197
TIM44_HUMAN	TIMM44	physical	26344197
TKT_HUMAN	TKT	physical	26344197
DJC13_HUMAN	DNAJC13	physical	28514442
DNLZ_HUMAN	DNLZ	physical	28514442
SLAI1_HUMAN	SLAIN1	physical	28514442
MAVS_HUMAN	MAVS	physical	28514442
CKAP5_HUMAN	CKAP5	physical	28514442

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 GRP75_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-135; LYS-138; LYS-143;LYS-234; LYS-288; LYS-300; LYS-345; LYS-567 AND LYS-646, AND MASSSPECTROMETRY.	19608861 [Abstract]
Malonylation
Reference	PubMed
"The first identification of lysine malonylation substrates and itsregulatory enzyme."; Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.; Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011). Cited for: MALONYLATION AT LYS-206.	21908771 [Abstract]
N6-malonyllysine
Reference	PubMed
"The first identification of lysine malonylation substrates and itsregulatory enzyme."; Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.; Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011). Cited for: MALONYLATION AT LYS-206.	21908771 [Abstract]
Phosphorylation
Reference	PubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-568, AND MASSSPECTROMETRY.	18083107 [Abstract]