dbPTM

CH60_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CH60_HUMAN
UniProt AC	P10809
Protein Name	60 kDa heat shock protein, mitochondrial
Gene Name	HSPD1
Organism	Homo sapiens (Human).
Sequence Length	573
Subcellular Localization	Mitochondrion matrix.
Protein Description	Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. [PubMed: 1346131]
Protein Sequence	MLRLPTVFRQMRPVSRVLAPHLTRAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEGLTLNLEDVQPHDLGKVGEVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALNATRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSEVGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKEEKDPGMGAMGGMGGGMGGGMF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Methylation	-----MLRLPTVFRQ -----CCCCCHHHHH	37.00	115384203
14	Sulfoxidation	VFRQMRPVSRVLAPH HHHHCCCHHHHHHHH	3.94	28465586
29	Sulfoxidation	LTRAYAKDVKFGADA HHHHHHCCCCCCHHH	40.44	28465586
31	Acetylation	RAYAKDVKFGADARA HHHHCCCCCCHHHHH	48.49	-
31	Ubiquitination	RAYAKDVKFGADARA HHHHCCCCCCHHHHH	48.49	21890473
31	2-Hydroxyisobutyrylation	RAYAKDVKFGADARA HHHHCCCCCCHHHHH	48.49	-
31	Acetylation	RAYAKDVKFGADARA HHHHCCCCCCHHHHH	48.49	25825284
31	Succinylation	RAYAKDVKFGADARA HHHHCCCCCCHHHHH	48.49	-
31	Succinylation	RAYAKDVKFGADARA HHHHCCCCCCHHHHH	48.49	23954790
31	Ubiquitination	RAYAKDVKFGADARA HHHHCCCCCCHHHHH	48.49	21890473
54	O-linked_Glycosylation	LADAVAVTMGPKGRT HHHEEEHHCCCCCCE	13.48	31373491
58	Ubiquitination	VAVTMGPKGRTVIIE EEHHCCCCCCEEEEE	56.12	21890473
58	2-Hydroxyisobutyrylation	VAVTMGPKGRTVIIE EEHHCCCCCCEEEEE	56.12	-
58	Ubiquitination	VAVTMGPKGRTVIIE EEHHCCCCCCEEEEE	56.12	21906983
61	Phosphorylation	TMGPKGRTVIIEQSW HCCCCCCEEEEEECC	25.40	23927012
67	Phosphorylation	RTVIIEQSWGSPKVT CEEEEEECCCCCCCC	22.18	30266825
70	Phosphorylation	IIEQSWGSPKVTKDG EEEECCCCCCCCCCC	18.45	19664994
72	Ubiquitination	EQSWGSPKVTKDGVT EECCCCCCCCCCCEE	65.32	21890473
72	2-Hydroxyisobutyrylation	EQSWGSPKVTKDGVT EECCCCCCCCCCCEE	65.32	-
72	Acetylation	EQSWGSPKVTKDGVT EECCCCCCCCCCCEE	65.32	25953088
72	Malonylation	EQSWGSPKVTKDGVT EECCCCCCCCCCCEE	65.32	26320211
72	Ubiquitination	EQSWGSPKVTKDGVT EECCCCCCCCCCCEE	65.32	21890473
74	Phosphorylation	SWGSPKVTKDGVTVA CCCCCCCCCCCEEEE	29.55	21949786
75	Ubiquitination	WGSPKVTKDGVTVAK CCCCCCCCCCEEEEE	56.31	21890473
75	2-Hydroxyisobutyrylation	WGSPKVTKDGVTVAK CCCCCCCCCCEEEEE	56.31	-
75	Acetylation	WGSPKVTKDGVTVAK CCCCCCCCCCEEEEE	56.31	-
75	Malonylation	WGSPKVTKDGVTVAK CCCCCCCCCCEEEEE	56.31	26320211
75	Ubiquitination	WGSPKVTKDGVTVAK CCCCCCCCCCEEEEE	56.31	21890473
79	Phosphorylation	KVTKDGVTVAKSIDL CCCCCCEEEEEECCC	21.92	20068231
82	Acetylation	KDGVTVAKSIDLKDK CCCEEEEEECCCHHH	43.54	-
82	Ubiquitination	KDGVTVAKSIDLKDK CCCEEEEEECCCHHH	43.54	21890473
82	Acetylation	KDGVTVAKSIDLKDK CCCEEEEEECCCHHH	43.54	19608861
82	Succinylation	KDGVTVAKSIDLKDK CCCEEEEEECCCHHH	43.54	-
82	Succinylation	KDGVTVAKSIDLKDK CCCEEEEEECCCHHH	43.54	23954790
82	Ubiquitination	KDGVTVAKSIDLKDK CCCEEEEEECCCHHH	43.54	21890473
83	Phosphorylation	DGVTVAKSIDLKDKY CCEEEEEECCCHHHH	16.17	29214152
87	Acetylation	VAKSIDLKDKYKNIG EEEECCCHHHHHHHH	48.72	-
87	Ubiquitination	VAKSIDLKDKYKNIG EEEECCCHHHHHHHH	48.72	-
87	2-Hydroxyisobutyrylation	VAKSIDLKDKYKNIG EEEECCCHHHHHHHH	48.72	-
87	Acetylation	VAKSIDLKDKYKNIG EEEECCCHHHHHHHH	48.72	23749302
87	Malonylation	VAKSIDLKDKYKNIG EEEECCCHHHHHHHH	48.72	26320211
87	Succinylation	VAKSIDLKDKYKNIG EEEECCCHHHHHHHH	48.72	27452117
87	Ubiquitination	VAKSIDLKDKYKNIG EEEECCCHHHHHHHH	48.72	-
89	Ubiquitination	KSIDLKDKYKNIGAK EECCCHHHHHHHHHH	57.44	-
89	Ubiquitination	KSIDLKDKYKNIGAK EECCCHHHHHHHHHH	57.44	-
90	Phosphorylation	SIDLKDKYKNIGAKL ECCCHHHHHHHHHHH	21.28	28464451
91	Acetylation	IDLKDKYKNIGAKLV CCCHHHHHHHHHHHH	48.07	-
91	2-Hydroxyisobutyrylation	IDLKDKYKNIGAKLV CCCHHHHHHHHHHHH	48.07	-
91	Acetylation	IDLKDKYKNIGAKLV CCCHHHHHHHHHHHH	48.07	23749302
91	Succinylation	IDLKDKYKNIGAKLV CCCHHHHHHHHHHHH	48.07	27452117
91	Ubiquitination	IDLKDKYKNIGAKLV CCCHHHHHHHHHHHH	48.07	-
96	Acetylation	KYKNIGAKLVQDVAN HHHHHHHHHHHHHHH	43.93	-
96	Ubiquitination	KYKNIGAKLVQDVAN HHHHHHHHHHHHHHH	43.93	21890473
96	2-Hydroxyisobutyrylation	KYKNIGAKLVQDVAN HHHHHHHHHHHHHHH	43.93	-
96	Acetylation	KYKNIGAKLVQDVAN HHHHHHHHHHHHHHH	43.93	23954790
96	Ubiquitination	KYKNIGAKLVQDVAN HHHHHHHHHHHHHHH	43.93	21906983
105	Phosphorylation	VQDVANNTNEEAGDG HHHHHHCCCCCCCCC	43.76	19664995
113	Phosphorylation	NEEAGDGTTTATVLA CCCCCCCHHHHHHHH	26.22	29396449
114	Phosphorylation	EEAGDGTTTATVLAR CCCCCCHHHHHHHHH	21.69	28102081
115	Phosphorylation	EAGDGTTTATVLARS CCCCCHHHHHHHHHH	21.84	28102081
119	Sulfoxidation	GTTTATVLARSIAKE CHHHHHHHHHHHHHH	2.59	21406390
125	Acetylation	VLARSIAKEGFEKIS HHHHHHHHHHHHHHH	57.61	-
125	Ubiquitination	VLARSIAKEGFEKIS HHHHHHHHHHHHHHH	57.61	21890473
125	Acetylation	VLARSIAKEGFEKIS HHHHHHHHHHHHHHH	57.61	19608861
125	Malonylation	VLARSIAKEGFEKIS HHHHHHHHHHHHHHH	57.61	26320211
125	Succinylation	VLARSIAKEGFEKIS HHHHHHHHHHHHHHH	57.61	-
125	Succinylation	VLARSIAKEGFEKIS HHHHHHHHHHHHHHH	57.61	-
125	Ubiquitination	VLARSIAKEGFEKIS HHHHHHHHHHHHHHH	57.61	21890473
130	Acetylation	IAKEGFEKISKGANP HHHHHHHHHHCCCCC	50.44	-
130	Ubiquitination	IAKEGFEKISKGANP HHHHHHHHHHCCCCC	50.44	-
130	2-Hydroxyisobutyrylation	IAKEGFEKISKGANP HHHHHHHHHHCCCCC	50.44	-
130	Acetylation	IAKEGFEKISKGANP HHHHHHHHHHCCCCC	50.44	19608861
130	Malonylation	IAKEGFEKISKGANP HHHHHHHHHHCCCCC	50.44	26320211
130	Succinylation	IAKEGFEKISKGANP HHHHHHHHHHCCCCC	50.44	23954790
130	Ubiquitination	IAKEGFEKISKGANP HHHHHHHHHHCCCCC	50.44	19608861
132	Phosphorylation	KEGFEKISKGANPVE HHHHHHHHCCCCCHH	35.78	27251275
133	Acetylation	EGFEKISKGANPVEI HHHHHHHCCCCCHHH	66.57	-
133	Ubiquitination	EGFEKISKGANPVEI HHHHHHHCCCCCHHH	66.57	21890473
133	N6-malonyllysine	EGFEKISKGANPVEI HHHHHHHCCCCCHHH	66.57	-
133	2-Hydroxyisobutyrylation	EGFEKISKGANPVEI HHHHHHHCCCCCHHH	66.57	-
133	Acetylation	EGFEKISKGANPVEI HHHHHHHCCCCCHHH	66.57	23749302
133	Malonylation	EGFEKISKGANPVEI HHHHHHHCCCCCHHH	66.57	26320211
133	Succinylation	EGFEKISKGANPVEI HHHHHHHCCCCCHHH	66.57	-
133	Ubiquitination	EGFEKISKGANPVEI HHHHHHHCCCCCHHH	66.57	21890473
141	Methylation	GANPVEIRRGVMLAV CCCCHHHHHHHHHHH	18.78	115479731
156	Acetylation	DAVIAELKKQSKPVT HHHHHHHHHCCCCCC	40.03	25825284
156	Succinylation	DAVIAELKKQSKPVT HHHHHHHHHCCCCCC	40.03	27452117
157	2-Hydroxyisobutyrylation	AVIAELKKQSKPVTT HHHHHHHHCCCCCCC	72.87	-
157	Acetylation	AVIAELKKQSKPVTT HHHHHHHHCCCCCCC	72.87	30583425
159	Phosphorylation	IAELKKQSKPVTTPE HHHHHHCCCCCCCHH	48.05	25850435
160	Ubiquitination	AELKKQSKPVTTPEE HHHHHCCCCCCCHHH	40.80	21906983
163	Phosphorylation	KKQSKPVTTPEEIAQ HHCCCCCCCHHHHHH	45.20	25850435
164	Phosphorylation	KQSKPVTTPEEIAQV HCCCCCCCHHHHHHH	29.01	25849741
164	Sulfoxidation	KQSKPVTTPEEIAQV HCCCCCCCHHHHHHH	29.01	21406390
173	Phosphorylation	EEIAQVATISANGDK HHHHHHHEEECCCCH	19.33	20363803
175	Phosphorylation	IAQVATISANGDKEI HHHHHEEECCCCHHH	16.01	20363803
180	Acetylation	TISANGDKEIGNIIS EEECCCCHHHHHHHH	53.26	23236377
187	Phosphorylation	KEIGNIISDAMKKVG HHHHHHHHHHHHHHC	18.60	21815630
191	Acetylation	NIISDAMKKVGRKGV HHHHHHHHHHCCCCE	46.13	23954790
191	Succinylation	NIISDAMKKVGRKGV HHHHHHHHHHCCCCE	46.13	-
191	Succinylation	NIISDAMKKVGRKGV HHHHHHHHHHCCCCE	46.13	27452117
191	Sulfoxidation	NIISDAMKKVGRKGV HHHHHHHHHHCCCCE	46.13	21406390
191	Ubiquitination	NIISDAMKKVGRKGV HHHHHHHHHHCCCCE	46.13	21890473
192	Acetylation	IISDAMKKVGRKGVI HHHHHHHHHCCCCEE	36.52	155891
196	2-Hydroxyisobutyrylation	AMKKVGRKGVITVKD HHHHHCCCCEEEEEC	52.15	-
196	Malonylation	AMKKVGRKGVITVKD HHHHHCCCCEEEEEC	52.15	26320211
196	Succinylation	AMKKVGRKGVITVKD HHHHHCCCCEEEEEC	52.15	27452117
196	Ubiquitination	AMKKVGRKGVITVKD HHHHHCCCCEEEEEC	52.15	-
200	Phosphorylation	VGRKGVITVKDGKTL HCCCCEEEEECCCCC	21.06	-
202	2-Hydroxyisobutyrylation	RKGVITVKDGKTLND CCCEEEEECCCCCCC	52.71	-
202	Acetylation	RKGVITVKDGKTLND CCCEEEEECCCCCCC	52.71	19608861
202	Succinylation	RKGVITVKDGKTLND CCCEEEEECCCCCCC	52.71	-
202	Succinylation	RKGVITVKDGKTLND CCCEEEEECCCCCCC	52.71	27452117
202	Ubiquitination	RKGVITVKDGKTLND CCCEEEEECCCCCCC	52.71	19608861
205	2-Hydroxyisobutyrylation	VITVKDGKTLNDELE EEEEECCCCCCCHHH	61.03	-
205	Acetylation	VITVKDGKTLNDELE EEEEECCCCCCCHHH	61.03	25038526
205	Malonylation	VITVKDGKTLNDELE EEEEECCCCCCCHHH	61.03	26320211
205	Succinylation	VITVKDGKTLNDELE EEEEECCCCCCCHHH	61.03	-
205	Succinylation	VITVKDGKTLNDELE EEEEECCCCCCCHHH	61.03	-
205	Ubiquitination	VITVKDGKTLNDELE EEEEECCCCCCCHHH	61.03	-
206	Phosphorylation	ITVKDGKTLNDELEI EEEECCCCCCCHHHH	36.00	20873877
218	2-Hydroxyisobutyrylation	LEIIEGMKFDRGYIS HHHEECCCCCCCCCC	55.78	-
218	Acetylation	LEIIEGMKFDRGYIS HHHEECCCCCCCCCC	55.78	19608861
218	Succinylation	LEIIEGMKFDRGYIS HHHEECCCCCCCCCC	55.78	-
218	Succinylation	LEIIEGMKFDRGYIS HHHEECCCCCCCCCC	55.78	23954790
218	Ubiquitination	LEIIEGMKFDRGYIS HHHEECCCCCCCCCC	55.78	21890473
221	Methylation	IEGMKFDRGYISPYF EECCCCCCCCCCCEE	42.84	115479723
223	Phosphorylation	GMKFDRGYISPYFIN CCCCCCCCCCCEEEE	10.10	28152594
225	Phosphorylation	KFDRGYISPYFINTS CCCCCCCCCEEEECC	12.69	28152594
227	Phosphorylation	DRGYISPYFINTSKG CCCCCCCEEEECCCC	15.42	27273156
231	Phosphorylation	ISPYFINTSKGQKCE CCCEEEECCCCCCCC	27.31	25159151
232	O-linked_Glycosylation	SPYFINTSKGQKCEF CCEEEECCCCCCCCC	30.24	31373491
232	Phosphorylation	SPYFINTSKGQKCEF CCEEEECCCCCCCCC	30.24	25159151
233	2-Hydroxyisobutyrylation	PYFINTSKGQKCEFQ CEEEECCCCCCCCCC	64.42	-
233	Acetylation	PYFINTSKGQKCEFQ CEEEECCCCCCCCCC	64.42	25953088
233	Malonylation	PYFINTSKGQKCEFQ CEEEECCCCCCCCCC	64.42	26320211
233	Ubiquitination	PYFINTSKGQKCEFQ CEEEECCCCCCCCCC	64.42	21890473
236	2-Hydroxyisobutyrylation	INTSKGQKCEFQDAY EECCCCCCCCCCEEE	44.38	-
236	Acetylation	INTSKGQKCEFQDAY EECCCCCCCCCCEEE	44.38	23954790
236	Malonylation	INTSKGQKCEFQDAY EECCCCCCCCCCEEE	44.38	32601280
236	Succinylation	INTSKGQKCEFQDAY EECCCCCCCCCCEEE	44.38	-
236	Succinylation	INTSKGQKCEFQDAY EECCCCCCCCCCEEE	44.38	27452117
236	Ubiquitination	INTSKGQKCEFQDAY EECCCCCCCCCCEEE	44.38	-
237	S-nitrosocysteine	NTSKGQKCEFQDAYV ECCCCCCCCCCEEEE	4.94	-
237	Glutathionylation	NTSKGQKCEFQDAYV ECCCCCCCCCCEEEE	4.94	22555962
237	S-nitrosylation	NTSKGQKCEFQDAYV ECCCCCCCCCCEEEE	4.94	18335467
237	S-palmitoylation	NTSKGQKCEFQDAYV ECCCCCCCCCCEEEE	4.94	29575903
243	Nitration	KCEFQDAYVLLSEKK CCCCCEEEEEEEHHH	10.42	-
243	Phosphorylation	KCEFQDAYVLLSEKK CCCCCEEEEEEEHHH	10.42	28152594
247	Phosphorylation	QDAYVLLSEKKISSI CEEEEEEEHHHHHHH	43.11	28152594
249	2-Hydroxyisobutyrylation	AYVLLSEKKISSIQS EEEEEEHHHHHHHHH	52.62	-
249	Acetylation	AYVLLSEKKISSIQS EEEEEEHHHHHHHHH	52.62	23954790
249	Succinylation	AYVLLSEKKISSIQS EEEEEEHHHHHHHHH	52.62	23954790
249	Ubiquitination	AYVLLSEKKISSIQS EEEEEEHHHHHHHHH	52.62	19608861
250	2-Hydroxyisobutyrylation	YVLLSEKKISSIQSI EEEEEHHHHHHHHHH	43.71	-
250	Acetylation	YVLLSEKKISSIQSI EEEEEHHHHHHHHHH	43.71	-
250	Malonylation	YVLLSEKKISSIQSI EEEEEHHHHHHHHHH	43.71	26320211
250	Succinylation	YVLLSEKKISSIQSI EEEEEHHHHHHHHHH	43.71	-
250	Succinylation	YVLLSEKKISSIQSI EEEEEHHHHHHHHHH	43.71	-
250	Ubiquitination	YVLLSEKKISSIQSI EEEEEHHHHHHHHHH	43.71	21890473
252	Phosphorylation	LLSEKKISSIQSIVP EEEHHHHHHHHHHHH	30.21	30266825
253	Phosphorylation	LSEKKISSIQSIVPA EEHHHHHHHHHHHHH	28.28	30266825
256	Phosphorylation	KKISSIQSIVPALEI HHHHHHHHHHHHHHH	24.71	30266825
269	2-Hydroxyisobutyrylation	EIANAHRKPLVIIAE HHHHCCCCCEEEEEE	32.60	-
269	Acetylation	EIANAHRKPLVIIAE HHHHCCCCCEEEEEE	32.60	19608861
269	Malonylation	EIANAHRKPLVIIAE HHHHCCCCCEEEEEE	32.60	26320211
269	Succinylation	EIANAHRKPLVIIAE HHHHCCCCCEEEEEE	32.60	27452117
292	2-Hydroxyisobutyrylation	TLVLNRLKVGLQVVA HHHHHHHCCCEEEEE	30.90	-
292	Acetylation	TLVLNRLKVGLQVVA HHHHHHHCCCEEEEE	30.90	26051181
292	Malonylation	TLVLNRLKVGLQVVA HHHHHHHCCCEEEEE	30.90	32601280
292	Methylation	TLVLNRLKVGLQVVA HHHHHHHCCCEEEEE	30.90	-
292	Ubiquitination	TLVLNRLKVGLQVVA HHHHHHHCCCEEEEE	30.90	21906983
301	2-Hydroxyisobutyrylation	GLQVVAVKAPGFGDN CEEEEEEECCCCCCC	38.84	-
301	Acetylation	GLQVVAVKAPGFGDN CEEEEEEECCCCCCC	38.84	25038526
301	Malonylation	GLQVVAVKAPGFGDN CEEEEEEECCCCCCC	38.84	26320211
301	Succinylation	GLQVVAVKAPGFGDN CEEEEEEECCCCCCC	38.84	-
301	Succinylation	GLQVVAVKAPGFGDN CEEEEEEECCCCCCC	38.84	23954790
301	Ubiquitination	GLQVVAVKAPGFGDN CEEEEEEECCCCCCC	38.84	-
314	Acetylation	DNRKNQLKDMAIATG CCHHHHHHHHHHHHC	35.38	-
330	Sulfoxidation	AVFGEEGLTLNLEDV CCCCCCCCEEECHHC	5.79	21406390
344	Acetylation	VQPHDLGKVGEVIVT CCHHHCCCCCEEEEE	55.13	25038526
352	2-Hydroxyisobutyrylation	VGEVIVTKDDAMLLK CCEEEEECCHHEHHC	42.59	-
352	Acetylation	VGEVIVTKDDAMLLK CCEEEEECCHHEHHC	42.59	19608861
352	Malonylation	VGEVIVTKDDAMLLK CCEEEEECCHHEHHC	42.59	26320211
352	Succinylation	VGEVIVTKDDAMLLK CCEEEEECCHHEHHC	42.59	-
352	Succinylation	VGEVIVTKDDAMLLK CCEEEEECCHHEHHC	42.59	-
352	Ubiquitination	VGEVIVTKDDAMLLK CCEEEEECCHHEHHC	42.59	21890473
359	2-Hydroxyisobutyrylation	KDDAMLLKGKGDKAQ CCHHEHHCCCCCHHH	55.40	-
359	Acetylation	KDDAMLLKGKGDKAQ CCHHEHHCCCCCHHH	55.40	19608861
359	Malonylation	KDDAMLLKGKGDKAQ CCHHEHHCCCCCHHH	55.40	26320211
359	Ubiquitination	KDDAMLLKGKGDKAQ CCHHEHHCCCCCHHH	55.40	21890473
364	Acetylation	LLKGKGDKAQIEKRI HHCCCCCHHHHHHHH	51.35	23749302
364	Succinylation	LLKGKGDKAQIEKRI HHCCCCCHHHHHHHH	51.35	23954790
369	Acetylation	GDKAQIEKRIQEIIE CCHHHHHHHHHHHHH	57.33	2402961
369	Ubiquitination	GDKAQIEKRIQEIIE CCHHHHHHHHHHHHH	57.33	-
381	Phosphorylation	IIEQLDVTTSEYEKE HHHHHCCCCHHHHHH	25.03	28152594
382	Phosphorylation	IEQLDVTTSEYEKEK HHHHCCCCHHHHHHH	21.29	28152594
383	Phosphorylation	EQLDVTTSEYEKEKL HHHCCCCHHHHHHHH	28.90	28152594
385	Phosphorylation	LDVTTSEYEKEKLNE HCCCCHHHHHHHHHH	31.88	25884760
387	2-Hydroxyisobutyrylation	VTTSEYEKEKLNERL CCCHHHHHHHHHHHH	60.28	-
387	Acetylation	VTTSEYEKEKLNERL CCCHHHHHHHHHHHH	60.28	25953088
389	Acetylation	TSEYEKEKLNERLAK CHHHHHHHHHHHHHH	68.62	23749302
389	Malonylation	TSEYEKEKLNERLAK CHHHHHHHHHHHHHH	68.62	26320211
396	2-Hydroxyisobutyrylation	KLNERLAKLSDGVAV HHHHHHHHHCCCEEE	53.79	-
396	Acetylation	KLNERLAKLSDGVAV HHHHHHHHHCCCEEE	53.79	19608861
396	Malonylation	KLNERLAKLSDGVAV HHHHHHHHHCCCEEE	53.79	32601280
396	Succinylation	KLNERLAKLSDGVAV HHHHHHHHHCCCEEE	53.79	-
396	Succinylation	KLNERLAKLSDGVAV HHHHHHHHHCCCEEE	53.79	27452117
396	Ubiquitination	KLNERLAKLSDGVAV HHHHHHHHHCCCEEE	53.79	19608861
398	Phosphorylation	NERLAKLSDGVAVLK HHHHHHHCCCEEEEE	31.45	21712546
405	2-Hydroxyisobutyrylation	SDGVAVLKVGGTSDV CCCEEEEEECCCCCE	32.03	-
409	Phosphorylation	AVLKVGGTSDVEVNE EEEEECCCCCEECCC	18.80	29255136
410	Phosphorylation	VLKVGGTSDVEVNEK EEEECCCCCEECCCH	42.82	29255136
417	2-Hydroxyisobutyrylation	SDVEVNEKKDRVTDA CCEECCCHHHHHHHH	55.56	-
417	Acetylation	SDVEVNEKKDRVTDA CCEECCCHHHHHHHH	55.56	23749302
417	Ubiquitination	SDVEVNEKKDRVTDA CCEECCCHHHHHHHH	55.56	21906983
418	Acetylation	DVEVNEKKDRVTDAL CEECCCHHHHHHHHH	44.59	25953088
418	Ubiquitination	DVEVNEKKDRVTDAL CEECCCHHHHHHHHH	44.59	-
422	Phosphorylation	NEKKDRVTDALNATR CCHHHHHHHHHHHHH	19.22	21712546
428	Phosphorylation	VTDALNATRAAVEEG HHHHHHHHHHHHHHC	21.55	21712546
442	S-nitrosocysteine	GIVLGGGCALLRCIP CCEEEHHHHHHHCHH	2.46	-
442	Glutathionylation	GIVLGGGCALLRCIP CCEEEHHHHHHHCHH	2.46	22555962
442	S-nitrosylation	GIVLGGGCALLRCIP CCEEEHHHHHHHCHH	2.46	18335467
442	S-palmitoylation	GIVLGGGCALLRCIP CCEEEHHHHHHHCHH	2.46	29575903
447	S-glutathionyl cysteine	GGCALLRCIPALDSL HHHHHHHCHHHHHCC	4.39	-
447	Glutathionylation	GGCALLRCIPALDSL HHHHHHHCHHHHHCC	4.39	22833525
447	S-nitrosylation	GGCALLRCIPALDSL HHHHHHHCHHHHHCC	4.39	22178444
451	Sulfoxidation	LLRCIPALDSLTPAN HHHCHHHHHCCCCCC	3.74	21406390
453	Phosphorylation	RCIPALDSLTPANED HCHHHHHCCCCCCCC	34.69	28857561
455	Phosphorylation	IPALDSLTPANEDQK HHHHHCCCCCCCCCH	25.06	30266825
462	Acetylation	TPANEDQKIGIEIIK CCCCCCCHHHHHHHH	56.04	25953088
469	2-Hydroxyisobutyrylation	KIGIEIIKRTLKIPA HHHHHHHHHHHCCCH	45.02	-
469	Acetylation	KIGIEIIKRTLKIPA HHHHHHHHHHHCCCH	45.02	19608861
469	Succinylation	KIGIEIIKRTLKIPA HHHHHHHHHHHCCCH	45.02	27452117
469	Sulfoxidation	KIGIEIIKRTLKIPA HHHHHHHHHHHCCCH	45.02	28465586
469	Ubiquitination	KIGIEIIKRTLKIPA HHHHHHHHHHHCCCH	45.02	21890473
471	Phosphorylation	GIEIIKRTLKIPAMT HHHHHHHHHCCCHHH	27.66	20068231
473	2-Hydroxyisobutyrylation	EIIKRTLKIPAMTIA HHHHHHHCCCHHHHH	46.13	-
473	Acetylation	EIIKRTLKIPAMTIA HHHHHHHCCCHHHHH	46.13	23749302
473	Malonylation	EIIKRTLKIPAMTIA HHHHHHHCCCHHHHH	46.13	26320211
473	Succinylation	EIIKRTLKIPAMTIA HHHHHHHCCCHHHHH	46.13	27452117
473	Ubiquitination	EIIKRTLKIPAMTIA HHHHHHHCCCHHHHH	46.13	19608861
478	Phosphorylation	TLKIPAMTIAKNAGV HHCCCHHHHHHHCCC	21.64	23312004
480	Sulfoxidation	KIPAMTIAKNAGVEG CCCHHHHHHHCCCCC	7.00	28183972
481	2-Hydroxyisobutyrylation	IPAMTIAKNAGVEGS CCHHHHHHHCCCCCH	43.40	-
481	Acetylation	IPAMTIAKNAGVEGS CCHHHHHHHCCCCCH	43.40	-
481	Succinylation	IPAMTIAKNAGVEGS CCHHHHHHHCCCCCH	43.40	-
481	Succinylation	IPAMTIAKNAGVEGS CCHHHHHHHCCCCCH	43.40	21890473
481	Ubiquitination	IPAMTIAKNAGVEGS CCHHHHHHHCCCCCH	43.40	21890473
488	Phosphorylation	KNAGVEGSLIVEKIM HHCCCCCHHHHHHHH	11.04	29255136
497	Phosphorylation	IVEKIMQSSSEVGYD HHHHHHHCCCCCCCH	20.60	20860994
498	Phosphorylation	VEKIMQSSSEVGYDA HHHHHHCCCCCCCHH	17.39	21406692
499	Phosphorylation	EKIMQSSSEVGYDAM HHHHHCCCCCCCHHH	41.36	21406692
503	Nitration	QSSSEVGYDAMAGDF HCCCCCCCHHHCHHH	13.00	-
503	Phosphorylation	QSSSEVGYDAMAGDF HCCCCCCCHHHCHHH	13.00	21406692
516	Acetylation	DFVNMVEKGIIDPTK HHHHHHHCCCCCHHH	43.96	23236377
516	Methylation	DFVNMVEKGIIDPTK HHHHHHHCCCCCHHH	43.96	23644510
516	Ubiquitination	DFVNMVEKGIIDPTK HHHHHHHCCCCCHHH	43.96	-
522	Phosphorylation	EKGIIDPTKVVRTAL HCCCCCHHHHHHHHH	32.49	28857561
523	2-Hydroxyisobutyrylation	KGIIDPTKVVRTALL CCCCCHHHHHHHHHH	44.09	-
523	Acetylation	KGIIDPTKVVRTALL CCCCCHHHHHHHHHH	44.09	19608861
523	Ubiquitination	KGIIDPTKVVRTALL CCCCCHHHHHHHHHH	44.09	19608861
527	Phosphorylation	DPTKVVRTALLDAAG CHHHHHHHHHHHHHH	15.28	18452278
537	Phosphorylation	LDAAGVASLLTTAEV HHHHHHHHHHHCCEE	22.85	28464451
540	Phosphorylation	AGVASLLTTAEVVVT HHHHHHHHCCEEEEE	29.29	20873877
541	Phosphorylation	GVASLLTTAEVVVTE HHHHHHHCCEEEEEE	22.31	30622161
547	Phosphorylation	TTAEVVVTEIPKEEK HCCEEEEEECCHHHC	19.31	28258704
551	Acetylation	VVVTEIPKEEKDPGM EEEEECCHHHCCCCC	81.70	25825284
551	Sumoylation	VVVTEIPKEEKDPGM EEEEECCHHHCCCCC	81.70	28112733

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
Oops, there are no upstream regulatory protein records of CH60_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CH60_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 CH60_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
H2B2E_HUMAN	HIST2H2BE	physical	9724719
BAK_HUMAN	BAK1	physical	12070120
BAX_HUMAN	BAX	physical	12070120
CASP3_HUMAN	CASP3	physical	10205158
CH10_HUMAN	HSPE1	physical	10205158
ALDH2_HUMAN	ALDH2	physical	12387818
CH10_HUMAN	HSPE1	physical	12387818
ALK_HUMAN	ALK	physical	14968112
CHIP_HUMAN	STUB1	physical	17317785
A4_HUMAN	APP	physical	17317785
ISG15_HUMAN	ISG15	physical	16009940
A4_HUMAN	APP	physical	21832049
GRP78_HUMAN	HSPA5	physical	22939629
GRP75_HUMAN	HSPA9	physical	22939629
HSP7C_HUMAN	HSPA8	physical	22939629
ROA2_HUMAN	HNRNPA2B1	physical	22939629
ITB1_HUMAN	ITGB1	physical	22939629
PUF60_HUMAN	PUF60	physical	22939629
DDX17_HUMAN	DDX17	physical	22939629
G3P_HUMAN	GAPDH	physical	22939629
EF1B_HUMAN	EEF1B2	physical	22939629
HS90B_HUMAN	HSP90AB1	physical	22939629
HEXI1_HUMAN	HEXIM1	physical	22939629
EF2_HUMAN	EEF2	physical	22939629
SEPT9_HUMAN	SEPT9	physical	22939629
CX056_HUMAN	CXorf56	physical	22939629
MCCB_HUMAN	MCCC2	physical	22939629
SCRB2_HUMAN	SCARB2	physical	22939629
S30BP_HUMAN	SAP30BP	physical	22939629
UBR4_HUMAN	UBR4	physical	22939629
FRIL_HUMAN	FTL	physical	22939629
CND1_HUMAN	NCAPD2	physical	22939629
PTN2_HUMAN	PTPN2	physical	22939629
GT251_HUMAN	COLGALT1	physical	22939629
RAB5B_HUMAN	RAB5B	physical	22939629
GID8_HUMAN	GID8	physical	22939629
STRN4_HUMAN	STRN4	physical	22939629
LAMB1_HUMAN	LAMB1	physical	22939629
IPYR_HUMAN	PPA1	physical	22939629
PLOD3_HUMAN	PLOD3	physical	22939629
SARNP_HUMAN	SARNP	physical	22939629
VATA_HUMAN	ATP6V1A	physical	22863883
PDIA3_HUMAN	PDIA3	physical	22863883
KRA59_HUMAN	KRTAP5-9	physical	25416956
K1H1_HUMAN	KRT31	physical	25416956
RGS20_HUMAN	RGS20	physical	25416956
TMCC2_HUMAN	TMCC2	physical	25416956
CEP70_HUMAN	CEP70	physical	25416956
LZTS2_HUMAN	LZTS2	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
SAMD3_HUMAN	SAMD3	physical	25416956
KR108_HUMAN	KRTAP10-8	physical	25416956
KR103_HUMAN	KRTAP10-3	physical	25416956
NT2NL_HUMAN	NOTCH2NL	physical	25416956
CCAR2_HUMAN	CCAR2	physical	26344197
GLOD4_HUMAN	GLOD4	physical	26344197
GMPPB_HUMAN	GMPPB	physical	26344197
HSP74_HUMAN	HSPA4	physical	26344197
CH10_HUMAN	HSPE1	physical	26344197
PACN3_HUMAN	PACSIN3	physical	26344197
S2533_HUMAN	SLC25A33	physical	26344197
TNG2_HUMAN	TANGO2	physical	26344197
TBB4B_HUMAN	TUBB4B	physical	26344197
LZTS2_HUMAN	LZTS2	physical	21516116
ACSF3_HUMAN	ACSF3	physical	28514442
MTU1_HUMAN	TRMU	physical	28514442
ACS2L_HUMAN	ACSS1	physical	28514442
HEMH_HUMAN	FECH	physical	28514442
MRM2_HUMAN	FTSJ2	physical	28514442
D39U1_HUMAN	SDR39U1	physical	28514442
S2539_HUMAN	SLC25A39	physical	28514442
NUD19_HUMAN	NUDT19	physical	28514442
MTG1_HUMAN	MTG1	physical	28514442
TRM2_HUMAN	TRMT2B	physical	28514442
PUSL1_HUMAN	PUSL1	physical	28514442
SYMM_HUMAN	MARS2	physical	28514442
NSUN4_HUMAN	NSUN4	physical	28514442
ACSF2_HUMAN	ACSF2	physical	28514442
SYNM_HUMAN	NARS2	physical	28514442
NPS3A_HUMAN	NIPSNAP3A	physical	28514442
FAH2B_HUMAN	FAHD2B	physical	28514442
TMM70_HUMAN	TMEM70	physical	28514442
TRM1L_HUMAN	TRMT1L	physical	28514442
EFGM_HUMAN	GFM1	physical	28514442
TRUA_HUMAN	PUS1	physical	28514442
CAF17_HUMAN	IBA57	physical	28514442
SYDM_HUMAN	DARS2	physical	28514442
CATH_HUMAN	CTSH	physical	28514442
HDHD5_HUMAN	CECR5	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
605280	Spastic paraplegia 13, autosomal dominant (SPG13)
612233	Leukodystrophy, hypomyelinating, 4 (HLD4)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CH60_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-31; LYS-82; LYS-125;LYS-130; LYS-202; LYS-218; LYS-269; LYS-352; LYS-359; LYS-396;LYS-469; LYS-473 AND LYS-523, AND MASS SPECTROMETRY.	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-133.	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-133.	21908771 [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-70, 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 SER-70, AND MASSSPECTROMETRY.	18669648 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-227, AND MASSSPECTROMETRY.	15592455 [Abstract]