dbPTM

CH60_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CH60_MOUSE
UniProt AC	P63038
Protein Name	60 kDa heat shock protein, mitochondrial
Gene Name	Hspd1
Organism	Mus musculus (Mouse).
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. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein..
Protein Sequence	MLRLPTVLRQMRPVSRALAPHLTRAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKDIGNIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSVQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEGLNLNLEDVQAHDLGKVGEVIVTKDDAMLLKGKGDKAHIEKRIQEITEQLDITTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALNATRAAVEEGIVLGGGCALLRCIPALDSLKPANEDQKIGIEIIKRALKIPAMTIAKNAGVEGSLIVEKILQSSSEVGYDAMLGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEAVVTEIPKEEKDPGMGAMGGMGGGMGGGMF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
15	Phosphorylation	LRQMRPVSRALAPHL HHHHCHHHHHHHHHH	17.96	-
31	Acetylation	RAYAKDVKFGADARA HHHHCCCCCCHHHHH	48.49	23864654
31	Succinylation	RAYAKDVKFGADARA HHHHCCCCCCHHHHH	48.49	-
31	Succinylation	RAYAKDVKFGADARA HHHHCCCCCCHHHHH	48.49	23806337
31	Ubiquitination	RAYAKDVKFGADARA HHHHCCCCCCHHHHH	48.49	27667366
58	Succinylation	VAVTMGPKGRTVIIE EEHHCCCCCCEEEEE	56.12	26388266
58	Ubiquitination	VAVTMGPKGRTVIIE EEHHCCCCCCEEEEE	56.12	-
61	Phosphorylation	TMGPKGRTVIIEQSW HCCCCCCEEEEEECC	25.40	25619855
67	Phosphorylation	RTVIIEQSWGSPKVT CEEEEEECCCCCCCC	22.18	25619855
70	Phosphorylation	IIEQSWGSPKVTKDG EEEECCCCCCCCCCC	18.45	25521595
72	Acetylation	EQSWGSPKVTKDGVT EECCCCCCCCCCCEE	65.32	23806337
72	Glutarylation	EQSWGSPKVTKDGVT EECCCCCCCCCCCEE	65.32	24703693
72	Ubiquitination	EQSWGSPKVTKDGVT EECCCCCCCCCCCEE	65.32	-
74	Phosphorylation	SWGSPKVTKDGVTVA CCCCCCCCCCCEEEE	29.55	22817900
75	Acetylation	WGSPKVTKDGVTVAK CCCCCCCCCCEEEEE	56.31	23576753
75	Malonylation	WGSPKVTKDGVTVAK CCCCCCCCCCEEEEE	56.31	26320211
75	Ubiquitination	WGSPKVTKDGVTVAK CCCCCCCCCCEEEEE	56.31	27667366
79	Phosphorylation	KVTKDGVTVAKSIDL CCCCCCEEEEEECCC	21.92	22817900
82	Acetylation	KDGVTVAKSIDLKDK CCCEEEEEECCCHHH	43.54	23806337
82	Malonylation	KDGVTVAKSIDLKDK CCCEEEEEECCCHHH	43.54	26320211
82	Succinylation	KDGVTVAKSIDLKDK CCCEEEEEECCCHHH	43.54	-
82	Succinylation	KDGVTVAKSIDLKDK CCCEEEEEECCCHHH	43.54	23806337
82	Ubiquitination	KDGVTVAKSIDLKDK CCCEEEEEECCCHHH	43.54	-
87	Acetylation	VAKSIDLKDKYKNIG EEEECCCHHHHHHHH	48.72	23576753
87	Ubiquitination	VAKSIDLKDKYKNIG EEEECCCHHHHHHHH	48.72	27667366
89	Acetylation	KSIDLKDKYKNIGAK EECCCHHHHHHHHHH	57.44	21728379
90	Phosphorylation	SIDLKDKYKNIGAKL ECCCHHHHHHHHHHH	21.28	-
91	Acetylation	IDLKDKYKNIGAKLV CCCHHHHHHHHHHHH	48.07	23576753
91	Malonylation	IDLKDKYKNIGAKLV CCCHHHHHHHHHHHH	48.07	26320211
91	Succinylation	IDLKDKYKNIGAKLV CCCHHHHHHHHHHHH	48.07	24315375
96	Acetylation	KYKNIGAKLVQDVAN HHHHHHHHHHHHHHH	43.93	23864654
96	Succinylation	KYKNIGAKLVQDVAN HHHHHHHHHHHHHHH	43.93	24315375
96	Ubiquitination	KYKNIGAKLVQDVAN HHHHHHHHHHHHHHH	43.93	-
113	Phosphorylation	NEEAGDGTTTATVLA CCCCCCCHHHHHHHH	26.22	26525534
117	Phosphorylation	GDGTTTATVLARSIA CCCHHHHHHHHHHHH	17.60	25338131
125	Acetylation	VLARSIAKEGFEKIS HHHHHHHHHHHHHHH	57.61	23576753
125	Succinylation	VLARSIAKEGFEKIS HHHHHHHHHHHHHHH	57.61	-
125	Succinylation	VLARSIAKEGFEKIS HHHHHHHHHHHHHHH	57.61	23806337
125	Ubiquitination	VLARSIAKEGFEKIS HHHHHHHHHHHHHHH	57.61	27667366
130	Acetylation	IAKEGFEKISKGANP HHHHHHHHHHCCCCC	50.44	23576753
130	Succinylation	IAKEGFEKISKGANP HHHHHHHHHHCCCCC	50.44	23806337
130	Ubiquitination	IAKEGFEKISKGANP HHHHHHHHHHCCCCC	50.44	27667366
133	N6-malonyllysine	EGFEKISKGANPVEI HHHHHHHCCCCCHHH	66.57	-
133	Acetylation	EGFEKISKGANPVEI HHHHHHHCCCCCHHH	66.57	23576753
133	Malonylation	EGFEKISKGANPVEI HHHHHHHCCCCCHHH	66.57	26320211
133	Succinylation	EGFEKISKGANPVEI HHHHHHHCCCCCHHH	66.57	23806337
133	Ubiquitination	EGFEKISKGANPVEI HHHHHHHCCCCCHHH	66.57	27667366
156	Acetylation	DAVIAELKKQSKPVT HHHHHHHHHCCCCCC	40.03	23576753
156	Succinylation	DAVIAELKKQSKPVT HHHHHHHHHCCCCCC	40.03	24315375
159	Phosphorylation	IAELKKQSKPVTTPE HHHHHHCCCCCCCHH	48.05	25619855
160	Acetylation	AELKKQSKPVTTPEE HHHHHCCCCCCCHHH	40.80	23864654
163	Phosphorylation	KKQSKPVTTPEEIAQ HHCCCCCCCHHHHHH	45.20	25619855
164	Phosphorylation	KQSKPVTTPEEIAQV HCCCCCCCHHHHHHH	29.01	25521595
180	Acetylation	TISANGDKDIGNIIS HCCCCCCCHHHHHHH	53.28	23954790
180	Succinylation	TISANGDKDIGNIIS HCCCCCCCHHHHHHH	53.28	23954790
187	Phosphorylation	KDIGNIISDAMKKVG CHHHHHHHHHHHHHC	18.60	-
191	Acetylation	NIISDAMKKVGRKGV HHHHHHHHHHCCCCE	46.13	23576753
191	Glutarylation	NIISDAMKKVGRKGV HHHHHHHHHHCCCCE	46.13	24703693
191	Succinylation	NIISDAMKKVGRKGV HHHHHHHHHHCCCCE	46.13	-
191	Succinylation	NIISDAMKKVGRKGV HHHHHHHHHHCCCCE	46.13	23806337
191	Ubiquitination	NIISDAMKKVGRKGV HHHHHHHHHHCCCCE	46.13	-
192	Acetylation	IISDAMKKVGRKGVI HHHHHHHHHCCCCEE	36.52	155893
196	Malonylation	AMKKVGRKGVITVKD HHHHHCCCCEEEEEC	52.15	26320211
200	Phosphorylation	VGRKGVITVKDGKTL HCCCCEEEEECCCCC	21.06	-
202	Acetylation	RKGVITVKDGKTLND CCCEEEEECCCCCCC	52.71	23576753
202	Glutarylation	RKGVITVKDGKTLND CCCEEEEECCCCCCC	52.71	24703693
202	Malonylation	RKGVITVKDGKTLND CCCEEEEECCCCCCC	52.71	26320211
202	Succinylation	RKGVITVKDGKTLND CCCEEEEECCCCCCC	52.71	-
202	Succinylation	RKGVITVKDGKTLND CCCEEEEECCCCCCC	52.71	23806337
205	Acetylation	VITVKDGKTLNDELE EEEEECCCCCCCHHH	61.03	23576753
205	Succinylation	VITVKDGKTLNDELE EEEEECCCCCCCHHH	61.03	-
205	Succinylation	VITVKDGKTLNDELE EEEEECCCCCCCHHH	61.03	23806337
206	Phosphorylation	ITVKDGKTLNDELEI EEEECCCCCCCHHHH	36.00	-
217	Sulfoxidation	ELEIIEGMKFDRGYI HHHHEECCCCCCCCC	2.25	21406390
218	Acetylation	LEIIEGMKFDRGYIS HHHEECCCCCCCCCC	55.78	23576753
218	Succinylation	LEIIEGMKFDRGYIS HHHEECCCCCCCCCC	55.78	-
218	Succinylation	LEIIEGMKFDRGYIS HHHEECCCCCCCCCC	55.78	23806337
218	Ubiquitination	LEIIEGMKFDRGYIS HHHEECCCCCCCCCC	55.78	-
223	Phosphorylation	GMKFDRGYISPYFIN CCCCCCCCCCCEEEE	10.10	23737553
225	Phosphorylation	KFDRGYISPYFINTS CCCCCCCCCEEEECC	12.69	23737553
227	Phosphorylation	DRGYISPYFINTSKG CCCCCCCEEEECCCC	15.42	23737553
231	Phosphorylation	ISPYFINTSKGQKCE CCCEEEECCCCCCCC	27.31	23737553
232	Phosphorylation	SPYFINTSKGQKCEF CCEEEECCCCCCCCC	30.24	25521595
233	Acetylation	PYFINTSKGQKCEFQ CEEEECCCCCCCCCC	64.42	23864654
233	Malonylation	PYFINTSKGQKCEFQ CEEEECCCCCCCCCC	64.42	26320211
233	Succinylation	PYFINTSKGQKCEFQ CEEEECCCCCCCCCC	64.42	-
233	Ubiquitination	PYFINTSKGQKCEFQ CEEEECCCCCCCCCC	64.42	27667366
236	Acetylation	INTSKGQKCEFQDAY EECCCCCCCCCCEEE	44.38	23576753
236	Succinylation	INTSKGQKCEFQDAY EECCCCCCCCCCEEE	44.38	-
236	Succinylation	INTSKGQKCEFQDAY EECCCCCCCCCCEEE	44.38	23806337
236	Ubiquitination	INTSKGQKCEFQDAY EECCCCCCCCCCEEE	44.38	-
237	S-nitrosocysteine	NTSKGQKCEFQDAYV ECCCCCCCCCCEEEE	4.94	-
237	Glutathionylation	NTSKGQKCEFQDAYV ECCCCCCCCCCEEEE	4.94	24333276
237	S-nitrosylation	NTSKGQKCEFQDAYV ECCCCCCCCCCEEEE	4.94	24895380
237	S-palmitoylation	NTSKGQKCEFQDAYV ECCCCCCCCCCEEEE	4.94	26165157
243	Phosphorylation	KCEFQDAYVLLSEKK CCCCCEEEEEEECCH	10.42	-
249	Acetylation	AYVLLSEKKISSVQS EEEEEECCHHCCHHH	52.62	23576753
249	Malonylation	AYVLLSEKKISSVQS EEEEEECCHHCCHHH	52.62	26320211
249	Succinylation	AYVLLSEKKISSVQS EEEEEECCHHCCHHH	52.62	24315375
250	Acetylation	YVLLSEKKISSVQSI EEEEECCHHCCHHHH	43.71	23576753
250	Glutarylation	YVLLSEKKISSVQSI EEEEECCHHCCHHHH	43.71	24703693
250	Malonylation	YVLLSEKKISSVQSI EEEEECCHHCCHHHH	43.71	26320211
250	Succinylation	YVLLSEKKISSVQSI EEEEECCHHCCHHHH	43.71	-
250	Succinylation	YVLLSEKKISSVQSI EEEEECCHHCCHHHH	43.71	23806337
252	Phosphorylation	LLSEKKISSVQSIVP EEECCHHCCHHHHHH	33.08	23140645
253	Phosphorylation	LSEKKISSVQSIVPA EECCHHCCHHHHHHH	27.87	23140645
256	Phosphorylation	KKISSVQSIVPALEI CHHCCHHHHHHHHHH	24.33	23140645
269	Acetylation	EIANAHRKPLVIIAE HHHHHCCCCEEEEEE	32.60	23576753
292	Acetylation	TLVLNRLKVGLQVVA HHHHHHHCCCEEEEE	30.90	23576753
292	Succinylation	TLVLNRLKVGLQVVA HHHHHHHCCCEEEEE	30.90	23806337
301	Acetylation	GLQVVAVKAPGFGDN CEEEEEEECCCCCCC	38.84	23806337
301	Glutarylation	GLQVVAVKAPGFGDN CEEEEEEECCCCCCC	38.84	24703693
301	Succinylation	GLQVVAVKAPGFGDN CEEEEEEECCCCCCC	38.84	-
301	Succinylation	GLQVVAVKAPGFGDN CEEEEEEECCCCCCC	38.84	23806337
301	Ubiquitination	GLQVVAVKAPGFGDN CEEEEEEECCCCCCC	38.84	-
314	Acetylation	DNRKNQLKDMAIATG CCHHHHHHHHHHHHC	35.38	23576753
314	Succinylation	DNRKNQLKDMAIATG CCHHHHHHHHHHHHC	35.38	23954790
352	Acetylation	VGEVIVTKDDAMLLK CCEEEEECCCCEECC	42.59	23576753
352	Glutarylation	VGEVIVTKDDAMLLK CCEEEEECCCCEECC	42.59	24703693
352	Succinylation	VGEVIVTKDDAMLLK CCEEEEECCCCEECC	42.59	-
352	Succinylation	VGEVIVTKDDAMLLK CCEEEEECCCCEECC	42.59	23806337
352	Ubiquitination	VGEVIVTKDDAMLLK CCEEEEECCCCEECC	42.59	-
359	Acetylation	KDDAMLLKGKGDKAH CCCCEECCCCCCHHH	55.40	23576753
359	Glutarylation	KDDAMLLKGKGDKAH CCCCEECCCCCCHHH	55.40	24703693
359	Succinylation	KDDAMLLKGKGDKAH CCCCEECCCCCCHHH	55.40	23806337
359	Ubiquitination	KDDAMLLKGKGDKAH CCCCEECCCCCCHHH	55.40	27667366
361	Acetylation	DAMLLKGKGDKAHIE CCEECCCCCCHHHHH	63.45	23201123
364	Acetylation	LLKGKGDKAHIEKRI ECCCCCCHHHHHHHH	51.00	23864654
369	Acetylation	GDKAHIEKRIQEITE CCHHHHHHHHHHHHH	54.95	23864654
375	Phosphorylation	EKRIQEITEQLDITT HHHHHHHHHHHCCCC	19.54	22817900
381	Phosphorylation	ITEQLDITTSEYEKE HHHHHCCCCHHHHHH	24.76	22817900
382	Phosphorylation	TEQLDITTSEYEKEK HHHHCCCCHHHHHHH	21.64	22817900
383	Phosphorylation	EQLDITTSEYEKEKL HHHCCCCHHHHHHHH	29.54	22817900
387	Acetylation	ITTSEYEKEKLNERL CCCHHHHHHHHHHHH	60.28	23864654
387	Succinylation	ITTSEYEKEKLNERL CCCHHHHHHHHHHHH	60.28	24315375
389	Acetylation	TSEYEKEKLNERLAK CHHHHHHHHHHHHHH	68.62	23576753
389	Malonylation	TSEYEKEKLNERLAK CHHHHHHHHHHHHHH	68.62	26320211
389	Succinylation	TSEYEKEKLNERLAK CHHHHHHHHHHHHHH	68.62	24315375
396	Acetylation	KLNERLAKLSDGVAV HHHHHHHHHCCCEEE	53.79	24062335
396	Succinylation	KLNERLAKLSDGVAV HHHHHHHHHCCCEEE	53.79	-
396	Succinylation	KLNERLAKLSDGVAV HHHHHHHHHCCCEEE	53.79	23806337
396	Ubiquitination	KLNERLAKLSDGVAV HHHHHHHHHCCCEEE	53.79	27667366
398	Phosphorylation	NERLAKLSDGVAVLK HHHHHHHCCCEEEEE	31.45	26525534
405	Succinylation	SDGVAVLKVGGTSDV CCCEEEEEECCCCCE	32.03	23954790
409	Phosphorylation	AVLKVGGTSDVEVNE EEEEECCCCCEECCC	18.80	26643407
410	Phosphorylation	VLKVGGTSDVEVNEK EEEECCCCCEECCCH	42.82	25521595
417	Acetylation	SDVEVNEKKDRVTDA CCEECCCHHHHHHHH	55.56	23864654
417	Ubiquitination	SDVEVNEKKDRVTDA CCEECCCHHHHHHHH	55.56	22790023
418	Acetylation	DVEVNEKKDRVTDAL CEECCCHHHHHHHHH	44.59	21728379
442	S-nitrosocysteine	GIVLGGGCALLRCIP CCEEEHHHHHHHHHH	2.46	-
442	Glutathionylation	GIVLGGGCALLRCIP CCEEEHHHHHHHHHH	2.46	24333276
442	S-nitrosylation	GIVLGGGCALLRCIP CCEEEHHHHHHHHHH	2.46	24895380
442	S-palmitoylation	GIVLGGGCALLRCIP CCEEEHHHHHHHHHH	2.46	28526873
447	S-nitrosocysteine	GGCALLRCIPALDSL HHHHHHHHHHHHHCC	4.39	-
447	S-nitrosylation	GGCALLRCIPALDSL HHHHHHHHHHHHHCC	4.39	21278135
447	S-palmitoylation	GGCALLRCIPALDSL HHHHHHHHHHHHHCC	4.39	26165157
455	Acetylation	IPALDSLKPANEDQK HHHHHCCCCCCCCCC	46.14	23576753
455	Succinylation	IPALDSLKPANEDQK HHHHHCCCCCCCCCC	46.14	-
455	Succinylation	IPALDSLKPANEDQK HHHHHCCCCCCCCCC	46.14	23806337
462	Acetylation	KPANEDQKIGIEIIK CCCCCCCCHHHHHHH	56.04	23864654
462	Succinylation	KPANEDQKIGIEIIK CCCCCCCCHHHHHHH	56.04	23806337
469	Acetylation	KIGIEIIKRALKIPA CHHHHHHHHHHCCCH	36.96	23576753
469	Malonylation	KIGIEIIKRALKIPA CHHHHHHHHHHCCCH	36.96	26320211
469	Succinylation	KIGIEIIKRALKIPA CHHHHHHHHHHCCCH	36.96	23806337
473	Acetylation	EIIKRALKIPAMTIA HHHHHHHCCCHHHHH	45.73	23806337
473	Succinylation	EIIKRALKIPAMTIA HHHHHHHCCCHHHHH	45.73	23806337
473	Ubiquitination	EIIKRALKIPAMTIA HHHHHHHCCCHHHHH	45.73	27667366
481	Acetylation	IPAMTIAKNAGVEGS CCHHHHHHHCCCCCC	43.40	23576753
481	Succinylation	IPAMTIAKNAGVEGS CCHHHHHHHCCCCCC	43.40	-
481	Succinylation	IPAMTIAKNAGVEGS CCHHHHHHHCCCCCC	43.40	23806337
481	Ubiquitination	IPAMTIAKNAGVEGS CCHHHHHHHCCCCCC	43.40	-
488	Phosphorylation	KNAGVEGSLIVEKIL HHCCCCCCHHHHHHH	11.04	25521595
493	Acetylation	EGSLIVEKILQSSSE CCCHHHHHHHHCCCC	37.51	7611619
497	Phosphorylation	IVEKILQSSSEVGYD HHHHHHHCCCCCCHH	32.17	29899451
516	Acetylation	DFVNMVEKGIIDPTK HHHHHHHCCCCCHHH	43.96	22733758
516	Succinylation	DFVNMVEKGIIDPTK HHHHHHHCCCCCHHH	43.96	23954790
523	Acetylation	KGIIDPTKVVRTALL CCCCCHHHHHHHHHH	44.09	22826441
527	Phosphorylation	DPTKVVRTALLDAAG CHHHHHHHHHHHHHH	15.28	25777480
537	Phosphorylation	LDAAGVASLLTTAEA HHHHHHHHHHHHHHH	22.85	25777480
540	Phosphorylation	AGVASLLTTAEAVVT HHHHHHHHHHHHHHC	29.29	25777480
541	Phosphorylation	GVASLLTTAEAVVTE HHHHHHHHHHHHHCC	23.59	25777480
547	Phosphorylation	TTAEAVVTEIPKEEK HHHHHHHCCCCHHHC	22.92	25777480
551	Acetylation	AVVTEIPKEEKDPGM HHHCCCCHHHCCCCC	81.70	23954790
554	Acetylation	TEIPKEEKDPGMGAM CCCCHHHCCCCCCCC	71.02	23954790

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_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CH60_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
TOM40_MOUSE	Tomm40	physical	12931191
GRP75_MOUSE	Hspa9	physical	12931191

Drug and Disease Associations

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

Regulatory Network of CH60_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-223, AND MASSSPECTROMETRY.	17203969 [Abstract]