dbPTM

FKBP4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FKBP4_HUMAN
UniProt AC	Q02790
Protein Name	Peptidyl-prolyl cis-trans isomerase FKBP4
Gene Name	FKBP4
Organism	Homo sapiens (Human).
Sequence Length	459
Subcellular Localization	Cytoplasm, cytosol . Mitochondrion . Nucleus . Cytoplasm, cytoskeleton . Cell projection, axon . Shuttles from mitochondria to nucleus co-localizes in mitochondria with the glucocorticoid receptor (PubMed:21730050). Colocalized with MAPT/TAU in the
Protein Description	Immunophilin protein with PPIase and co-chaperone activities. Component of steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments. The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May have a protective role against oxidative stress in mitochondria..
Protein Sequence	MTAEEMKATESGAQSAPLPMEGVDISPKQDEGVLKVIKREGTGTEMPMIGDRVFVHYTGWLLDGTKFDSSLDRKDKFSFDLGKGEVIKAWDIAIATMKVGEVCHITCKPEYAYGSAGSPPKIPPNATLVFEVELFEFKGEDLTEEEDGGIIRRIQTRGEGYAKPNEGAIVEVALEGYYKDKLFDQRELRFEIGEGENLDLPYGLERAIQRMEKGEHSIVYLKPSYAFGSVGKEKFQIPPNAELKYELHLKSFEKAKESWEMNSEEKLEQSTIVKERGTVYFKEGKYKQALLQYKKIVSWLEYESSFSNEEAQKAQALRLASHLNLAMCHLKLQAFSAAIESCNKALELDSNNEKGLFRRGEAHLAVNDFELARADFQKVLQLYPNNKAAKTQLAVCQQRIRRQLAREKKLYANMFERLAEEENKAKAEASSGDHPTDTEMKEEQKSNTAGSQSQVETEA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MTAEEMKA -------CCHHHHHH	7.86	-
2	Acetylation	------MTAEEMKAT ------CCHHHHHHC	42.66	-
7	Ubiquitination	-MTAEEMKATESGAQ -CCHHHHHHCCCCCC	56.27	32015554
9	O-linked_Glycosylation	TAEEMKATESGAQSA CHHHHHHCCCCCCCC	25.76	OGP
9	Phosphorylation	TAEEMKATESGAQSA CHHHHHHCCCCCCCC	25.76	25850435
11	Phosphorylation	EEMKATESGAQSAPL HHHHHCCCCCCCCCC	34.77	25850435
15	Phosphorylation	ATESGAQSAPLPMEG HCCCCCCCCCCCCCC	31.18	25850435
20	Sulfoxidation	AQSAPLPMEGVDISP CCCCCCCCCCCCCCC	10.36	28465586
26	Phosphorylation	PMEGVDISPKQDEGV CCCCCCCCCCCCCCC	22.91	21815630
28	Acetylation	EGVDISPKQDEGVLK CCCCCCCCCCCCCEE	64.69	23236377
28	Neddylation	EGVDISPKQDEGVLK CCCCCCCCCCCCCEE	64.69	32015554
28	Ubiquitination	EGVDISPKQDEGVLK CCCCCCCCCCCCCEE	64.69	21906983
29	Ubiquitination	GVDISPKQDEGVLKV CCCCCCCCCCCCEEE	58.32	23000965
31	Ubiquitination	DISPKQDEGVLKVIK CCCCCCCCCCEEEEE	49.02	21890473
35	2-Hydroxyisobutyrylation	KQDEGVLKVIKREGT CCCCCCEEEEEECCC	39.24	-
35	Ubiquitination	KQDEGVLKVIKREGT CCCCCCEEEEEECCC	39.24	29967540
38	Ubiquitination	EGVLKVIKREGTGTE CCCEEEEEECCCCCC	47.59	21890473
43	Ubiquitination	VIKREGTGTEMPMIG EEEECCCCCCCCCCC	30.45	21890473
46	Sulfoxidation	REGTGTEMPMIGDRV ECCCCCCCCCCCCEE	2.47	21406390
52	Methylation	EMPMIGDRVFVHYTG CCCCCCCEEEEEEHH	20.68	-
63	Ubiquitination	HYTGWLLDGTKFDSS EEHHEEECCCCCCCC	61.62	21963094
66	Ubiquitination	GWLLDGTKFDSSLDR HEEECCCCCCCCCCC	53.34	32015554
69	Phosphorylation	LDGTKFDSSLDRKDK ECCCCCCCCCCCCCC	35.61	29449344
70	Phosphorylation	DGTKFDSSLDRKDKF CCCCCCCCCCCCCCC	35.81	29449344
74	Ubiquitination	FDSSLDRKDKFSFDL CCCCCCCCCCCEEEC	66.01	23000965
76	2-Hydroxyisobutyrylation	SSLDRKDKFSFDLGK CCCCCCCCCEEECCC	46.04	-
76	Acetylation	SSLDRKDKFSFDLGK CCCCCCCCCEEECCC	46.04	25953088
76	Ubiquitination	SSLDRKDKFSFDLGK CCCCCCCCCEEECCC	46.04	23000965
78	Phosphorylation	LDRKDKFSFDLGKGE CCCCCCCEEECCCCC	24.48	25849741
83	Succinylation	KFSFDLGKGEVIKAW CCEEECCCCCCEEEE	60.23	23954790
83	Ubiquitination	KFSFDLGKGEVIKAW CCEEECCCCCCEEEE	60.23	23000965
88	Ubiquitination	LGKGEVIKAWDIAIA CCCCCCEEEEEEEEE	48.91	23000965
106	O-linked_Glycosylation	VGEVCHITCKPEYAY CCCEEEEEECCCCCC	7.27	30379171
106	Phosphorylation	VGEVCHITCKPEYAY CCCEEEEEECCCCCC	7.27	28152594
108	Acetylation	EVCHITCKPEYAYGS CEEEEEECCCCCCCC	32.03	25953088
108	Ubiquitination	EVCHITCKPEYAYGS CEEEEEECCCCCCCC	32.03	21963094
111	Phosphorylation	HITCKPEYAYGSAGS EEEECCCCCCCCCCC	17.41	28152594
113	Phosphorylation	TCKPEYAYGSAGSPP EECCCCCCCCCCCCC	15.65	28152594
115	Phosphorylation	KPEYAYGSAGSPPKI CCCCCCCCCCCCCCC	19.44	25849741
118	Phosphorylation	YAYGSAGSPPKIPPN CCCCCCCCCCCCCCC	37.43	25159151
127	Phosphorylation	PKIPPNATLVFEVEL CCCCCCCEEEEEEEE	30.05	26074081
134	Ubiquitination	TLVFEVELFEFKGED EEEEEEEEEEEECCC	6.35	22817900
136	Ubiquitination	VFEVELFEFKGEDLT EEEEEEEEEECCCCC	60.10	21890473
143	Phosphorylation	EFKGEDLTEEEDGGI EEECCCCCCCCCCCE	54.39	21815630
161	Phosphorylation	IQTRGEGYAKPNEGA EEECCCCCCCCCCCC	13.72	28152594
177	Ubiquitination	VEVALEGYYKDKLFD EEEEEEEECCCCCCC	9.66	21890473
179	Ubiquitination	VALEGYYKDKLFDQR EEEEEECCCCCCCCC	39.64	33845483
181	Acetylation	LEGYYKDKLFDQREL EEEECCCCCCCCCEE	47.07	25953088
181	Ubiquitination	LEGYYKDKLFDQREL EEEECCCCCCCCCEE	47.07	21906983
199	Ubiquitination	IGEGENLDLPYGLER ECCCCCCCCCCHHHH	58.12	21890473
202	Nitration	GENLDLPYGLERAIQ CCCCCCCCHHHHHHH	41.46	-
205	Ubiquitination	LDLPYGLERAIQRME CCCCCHHHHHHHHHH	35.39	21890473
209	Ubiquitination	YGLERAIQRMEKGEH CHHHHHHHHHHCCCC	37.37	22817900
213	2-Hydroxyisobutyrylation	RAIQRMEKGEHSIVY HHHHHHHCCCCEEEE	61.32	-
213	Acetylation	RAIQRMEKGEHSIVY HHHHHHHCCCCEEEE	61.32	25953088
217	Phosphorylation	RMEKGEHSIVYLKPS HHHCCCCEEEEEECC	14.94	28152594
220	Phosphorylation	KGEHSIVYLKPSYAF CCCCEEEEEECCEEC	13.82	25159151
222	2-Hydroxyisobutyrylation	EHSIVYLKPSYAFGS CCEEEEEECCEECCC	17.77	-
222	Acetylation	EHSIVYLKPSYAFGS CCEEEEEECCEECCC	17.77	23954790
222	Succinylation	EHSIVYLKPSYAFGS CCEEEEEECCEECCC	17.77	23954790
222	Ubiquitination	EHSIVYLKPSYAFGS CCEEEEEECCEECCC	17.77	23000965
224	Phosphorylation	SIVYLKPSYAFGSVG EEEEEECCEECCCCC	27.75	23186163
225	Phosphorylation	IVYLKPSYAFGSVGK EEEEECCEECCCCCC	17.93	28152594
229	Phosphorylation	KPSYAFGSVGKEKFQ ECCEECCCCCCCCCC	22.65	28152594
229	Ubiquitination	KPSYAFGSVGKEKFQ ECCEECCCCCCCCCC	22.65	21890473
232	Acetylation	YAFGSVGKEKFQIPP EECCCCCCCCCCCCC	56.42	156809
234	2-Hydroxyisobutyrylation	FGSVGKEKFQIPPNA CCCCCCCCCCCCCCC	46.16	-
237	Ubiquitination	VGKEKFQIPPNAELK CCCCCCCCCCCCCEE	7.43	23000965
240	Ubiquitination	EKFQIPPNAELKYEL CCCCCCCCCCEEEEE	40.47	23000965
242	Ubiquitination	FQIPPNAELKYELHL CCCCCCCCEEEEEEH	53.05	23000965
244	Ubiquitination	IPPNAELKYELHLKS CCCCCCEEEEEEHHH	28.34	22817900
250	2-Hydroxyisobutyrylation	LKYELHLKSFEKAKE EEEEEEHHHHHHHHH	42.21	-
250	Acetylation	LKYELHLKSFEKAKE EEEEEEHHHHHHHHH	42.21	25953088
250	Ubiquitination	LKYELHLKSFEKAKE EEEEEEHHHHHHHHH	42.21	21906983
254	Ubiquitination	LHLKSFEKAKESWEM EEHHHHHHHHHHHCC	63.85	22817900
258	Phosphorylation	SFEKAKESWEMNSEE HHHHHHHHHCCCCHH	27.85	25849741
261	Sulfoxidation	KAKESWEMNSEEKLE HHHHHHCCCCHHHHH	5.63	30846556
263	Phosphorylation	KESWEMNSEEKLEQS HHHHCCCCHHHHHHH	45.91	21815630
268	Ubiquitination	MNSEEKLEQSTIVKE CCCHHHHHHHHEEEE	54.26	22053931
274	2-Hydroxyisobutyrylation	LEQSTIVKERGTVYF HHHHHEEEECCEEEE	37.53	-
274	Acetylation	LEQSTIVKERGTVYF HHHHHEEEECCEEEE	37.53	16916647
274	Succinylation	LEQSTIVKERGTVYF HHHHHEEEECCEEEE	37.53	23954790
274	Ubiquitination	LEQSTIVKERGTVYF HHHHHEEEECCEEEE	37.53	22817900
282	2-Hydroxyisobutyrylation	ERGTVYFKEGKYKQA ECCEEEEECCCHHHH	48.12	-
282	Acetylation	ERGTVYFKEGKYKQA ECCEEEEECCCHHHH	48.12	19608861
282	Malonylation	ERGTVYFKEGKYKQA ECCEEEEECCCHHHH	48.12	32601280
282	Ubiquitination	ERGTVYFKEGKYKQA ECCEEEEECCCHHHH	48.12	23000965
285	Ubiquitination	TVYFKEGKYKQALLQ EEEEECCCHHHHHHH	50.82	23000965
286	Phosphorylation	VYFKEGKYKQALLQY EEEECCCHHHHHHHH	21.13	22817900
287	2-Hydroxyisobutyrylation	YFKEGKYKQALLQYK EEECCCHHHHHHHHH	32.36	-
287	Acetylation	YFKEGKYKQALLQYK EEECCCHHHHHHHHH	32.36	26051181
287	Ubiquitination	YFKEGKYKQALLQYK EEECCCHHHHHHHHH	32.36	23000965
293	Phosphorylation	YKQALLQYKKIVSWL HHHHHHHHHHHHHHH	17.76	20068231
294	2-Hydroxyisobutyrylation	KQALLQYKKIVSWLE HHHHHHHHHHHHHHH	24.06	-
294	Acetylation	KQALLQYKKIVSWLE HHHHHHHHHHHHHHH	24.06	25953088
294	Succinylation	KQALLQYKKIVSWLE HHHHHHHHHHHHHHH	24.06	23954790
294	Ubiquitination	KQALLQYKKIVSWLE HHHHHHHHHHHHHHH	24.06	32015554
298	Phosphorylation	LQYKKIVSWLEYESS HHHHHHHHHHHHHCC	29.44	27251275
304	Phosphorylation	VSWLEYESSFSNEEA HHHHHHHCCCCCHHH	35.46	28348404
305	Phosphorylation	SWLEYESSFSNEEAQ HHHHHHCCCCCHHHH	22.28	27251275
309	Ubiquitination	YESSFSNEEAQKAQA HHCCCCCHHHHHHHH	54.21	21890473
313	Ubiquitination	FSNEEAQKAQALRLA CCCHHHHHHHHHHHH	49.90	21906983
328	Glutathionylation	SHLNLAMCHLKLQAF HHHHHHHHHHHHHHH	2.57	22555962
331	Acetylation	NLAMCHLKLQAFSAA HHHHHHHHHHHHHHH	18.19	26051181
333	Ubiquitination	AMCHLKLQAFSAAIE HHHHHHHHHHHHHHH	38.48	21890473
336	Phosphorylation	HLKLQAFSAAIESCN HHHHHHHHHHHHHHH	21.58	23312004
341	Phosphorylation	AFSAAIESCNKALEL HHHHHHHHHHHHHCC	19.51	21712546
342	Glutathionylation	FSAAIESCNKALELD HHHHHHHHHHHHCCC	3.82	22555962
342	S-palmitoylation	FSAAIESCNKALELD HHHHHHHHHHHHCCC	3.82	26865113
342	Ubiquitination	FSAAIESCNKALELD HHHHHHHHHHHHCCC	3.82	21890473
344	Acetylation	AAIESCNKALELDSN HHHHHHHHHHCCCCC	59.69	26051181
344	Ubiquitination	AAIESCNKALELDSN HHHHHHHHHHCCCCC	59.69	29967540
345	Ubiquitination	AIESCNKALELDSNN HHHHHHHHHCCCCCC	7.71	22505724
350	Phosphorylation	NKALELDSNNEKGLF HHHHCCCCCCCCCCE	54.93	21815630
354	2-Hydroxyisobutyrylation	ELDSNNEKGLFRRGE CCCCCCCCCCEECCE	64.14	-
354	Acetylation	ELDSNNEKGLFRRGE CCCCCCCCCCEECCE	64.14	23954790
354	Malonylation	ELDSNNEKGLFRRGE CCCCCCCCCCEECCE	64.14	26320211
354	Ubiquitination	ELDSNNEKGLFRRGE CCCCCCCCCCEECCE	64.14	23000965
359	Methylation	NEKGLFRRGEAHLAV CCCCCEECCEEEEEE	39.71	-
363	Ubiquitination	LFRRGEAHLAVNDFE CEECCEEEEEECHHH	15.26	22817900
364	Ubiquitination	FRRGEAHLAVNDFEL EECCEEEEEECHHHH	7.99	21890473
373	Methylation	VNDFELARADFQKVL ECHHHHHHHHHHHHH	47.52	-
378	Acetylation	LARADFQKVLQLYPN HHHHHHHHHHHHCCC	44.93	21466224
378	Ubiquitination	LARADFQKVLQLYPN HHHHHHHHHHHHCCC	44.93	23000965
379	Ubiquitination	ARADFQKVLQLYPNN HHHHHHHHHHHCCCC	2.61	22817900
381	Ubiquitination	ADFQKVLQLYPNNKA HHHHHHHHHCCCCHH	41.77	22817900
387	Acetylation	LQLYPNNKAAKTQLA HHHCCCCHHHHHHHH	57.26	25953088
387	Ubiquitination	LQLYPNNKAAKTQLA HHHCCCCHHHHHHHH	57.26	21906983
390	2-Hydroxyisobutyrylation	YPNNKAAKTQLAVCQ CCCCHHHHHHHHHHH	41.48	-
390	Acetylation	YPNNKAAKTQLAVCQ CCCCHHHHHHHHHHH	41.48	25953088
390	Malonylation	YPNNKAAKTQLAVCQ CCCCHHHHHHHHHHH	41.48	26320211
390	Ubiquitination	YPNNKAAKTQLAVCQ CCCCHHHHHHHHHHH	41.48	22505724
396	Glutathionylation	AKTQLAVCQQRIRRQ HHHHHHHHHHHHHHH	2.07	22555962
400	Ubiquitination	LAVCQQRIRRQLARE HHHHHHHHHHHHHHH	3.56	27667366
408	Ubiquitination	RRQLAREKKLYANMF HHHHHHHHHHHHHHH	42.39	22817900
409	Ubiquitination	RQLAREKKLYANMFE HHHHHHHHHHHHHHH	41.81	22817900
411	Phosphorylation	LAREKKLYANMFERL HHHHHHHHHHHHHHH	12.57	25159151
417	Methylation	LYANMFERLAEEENK HHHHHHHHHHHHHHH	28.12	-
424	Ubiquitination	RLAEEENKAKAEASS HHHHHHHHHHHHHHC	55.32	22817900
426	Ubiquitination	AEEENKAKAEASSGD HHHHHHHHHHHHCCC	48.66	21906983
430	Phosphorylation	NKAKAEASSGDHPTD HHHHHHHHCCCCCCH	26.76	30278072
431	Phosphorylation	KAKAEASSGDHPTDT HHHHHHHCCCCCCHH	56.11	30278072
436	Phosphorylation	ASSGDHPTDTEMKEE HHCCCCCCHHHHHHH	52.73	23401153
438	Phosphorylation	SGDHPTDTEMKEEQK CCCCCCHHHHHHHHH	40.22	21955146
440	Sulfoxidation	DHPTDTEMKEEQKSN CCCCHHHHHHHHHHC	7.80	30846556
441	Acetylation	HPTDTEMKEEQKSNT CCCHHHHHHHHHHCC	52.44	25953088
441	Sumoylation	HPTDTEMKEEQKSNT CCCHHHHHHHHHHCC	52.44	25114211
441	Ubiquitination	HPTDTEMKEEQKSNT CCCHHHHHHHHHHCC	52.44	33845483
445	Acetylation	TEMKEEQKSNTAGSQ HHHHHHHHHCCCCCH	49.29	26051181
445	Ubiquitination	TEMKEEQKSNTAGSQ HHHHHHHHHCCCCCH	49.29	33845483
446	Phosphorylation	EMKEEQKSNTAGSQS HHHHHHHHCCCCCHH	38.82	30278072
448	Phosphorylation	KEEQKSNTAGSQSQV HHHHHHCCCCCHHHC	39.21	30278072
451	Phosphorylation	QKSNTAGSQSQVETE HHHCCCCCHHHCCCC	24.97	17525332
453	Phosphorylation	SNTAGSQSQVETEA- HCCCCCHHHCCCCC-	37.58	25159151
457	Phosphorylation	GSQSQVETEA----- CCHHHCCCCC-----	38.05	23403867

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
143	T	Phosphorylation	Kinase	CK2	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of FKBP4_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 FKBP4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SAE1_HUMAN	SAE1	physical	17353931
LOXH1_HUMAN	LOXHD1	physical	17353931
IRF4_HUMAN	IRF4	physical	10714679
PAHX_HUMAN	PHYH	physical	10051602
GCR_HUMAN	NR3C1	physical	8341706
GLMN_HUMAN	GLMN	physical	11164950
HS90A_HUMAN	HSP90AA1	physical	21170051
STIP1_HUMAN	STIP1	physical	21170051
HSF1_HUMAN	HSF1	physical	11583998
HS90A_HUMAN	HSP90AA1	physical	22678819
GLMN_HUMAN	GLMN	physical	12604780
GLMN_HUMAN	GLMN	physical	10051602
SARDH_HUMAN	SARDH	physical	22939629
TAF9_HUMAN	TAF9	physical	22939629
GCR_RAT	Nr3c1	physical	23686112
GCR_CAVPO	Nr3c1	physical	23686112
S10A2_HUMAN	S100A2	physical	20188096
S10A6_HUMAN	S100A6	physical	20188096
S10A1_HUMAN	S100A1	physical	20188096
HS90A_HUMAN	HSP90AA1	physical	20188096
HS90B_HUMAN	HSP90AB1	physical	25036637
SGT1_HUMAN	SUGT1	physical	25036637
HS90A_HUMAN	HSP90AA1	physical	25036637
CYBP_HUMAN	CACYBP	physical	25036637
CDC37_HUMAN	CDC37	physical	25036637
AHSA1_HUMAN	AHSA1	physical	25036637
CHRD1_HUMAN	CHORDC1	physical	25036637
GLMN_HUMAN	GLMN	physical	25036637
TEBP_HUMAN	PTGES3	physical	25036637
UBP19_HUMAN	USP19	physical	25036637
LSM7_HUMAN	LSM7	physical	25036637
HS90A_HUMAN	HSP90AA1	physical	10642522
HSP74_HUMAN	HSPA4	physical	10642522
TAU_HUMAN	MAPT	physical	20133804
PLSI_HUMAN	PLS1	physical	26344197
AAKB1_HUMAN	PRKAB1	physical	26344197
GCR_HUMAN	NR3C1	physical	16131566
AHSA1_HUMAN	AHSA1	physical	22504172
HS90A_HUMAN	HSP90AA1	physical	22504172
HS90A_HUMAN	HSP90AA1	physical	28514442
HS90B_HUMAN	HSP90AB1	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 FKBP4_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-282, AND MASS SPECTROMETRY.	19608861 [Abstract]
"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-274, AND MASS SPECTROMETRY.	16916647 [Abstract]
Phosphorylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451 AND SER-453, ANDMASS SPECTROMETRY.	19413330 [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-453, AND MASSSPECTROMETRY.	18669648 [Abstract]
"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-451 AND SER-453, ANDMASS SPECTROMETRY.	17525332 [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-451, AND MASSSPECTROMETRY.	16964243 [Abstract]