dbPTM

DNJC7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DNJC7_HUMAN
UniProt AC	Q99615
Protein Name	DnaJ homolog subfamily C member 7
Gene Name	DNAJC7
Organism	Homo sapiens (Human).
Sequence Length	494
Subcellular Localization	Cytoplasm . Nucleus . Cytoplasm, cytoskeleton . Colocalizes with NR1I3 to microtubules.
Protein Description	Acts as co-chaperone regulating the molecular chaperones HSP70 and HSP90 in folding of steroid receptors, such as the glucocorticoid receptor and the progesterone receptor. Proposed to act as a recycling chaperone by facilitating the return of chaperone substrates to early stages of chaperoning if further folding is required. In vitro, induces ATP-independent dissociation of HSP90 but not of HSP70 from the chaperone-substrate complexes. Recruits NR1I3 to the cytoplasm (By similarity)..
Protein Sequence	MAAAAECDVVMAATEPELLDDQEAKREAETFKEQGNAYYAKKDYNEAYNYYTKAIDMCPKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAQQEFKNANAVMEYEKIAETDFEKRDFRKVVFCMDRALEFAPACHRFKILKAECLAMLGRYPEAQSVASDILRMDSTNADALYVRGLCLYYEDCIEKAVQFFVQALRMAPDHEKACIACRNAKALKAKKEDGNKAFKEGNYKLAYELYTEALGIDPNNIKTNAKLYCNRGTVNSKLRKLDDAIEDCTNAVKLDDTYIKAYLRRAQCYMDTEQYEEAVRDYEKVYQTEKTKEHKQLLKNAQLELKKSKRKDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEVQKEEEKKFKEVGEAFTILSDPKKKTRYDSGQDLDEEGMNMGDFDPNNIFKAFFGGPGGFSFEASGPGNFFFQFG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAAAECDV ------CCCHHCCCE	13.05	22814378
25	Ubiquitination	LLDDQEAKREAETFK HCCHHHHHHHHHHHH	50.44	24816145
32	Acetylation	KREAETFKEQGNAYY HHHHHHHHHHHCCEE	57.45	25953088
32	Malonylation	KREAETFKEQGNAYY HHHHHHHHHHHCCEE	57.45	26320211
38	Phosphorylation	FKEQGNAYYAKKDYN HHHHHCCEEECCCHH	14.14	25839225
39	Phosphorylation	KEQGNAYYAKKDYNE HHHHCCEEECCCHHH	14.99	28102081
41	2-Hydroxyisobutyrylation	QGNAYYAKKDYNEAY HHCCEEECCCHHHHH	30.01	-
41	Ubiquitination	QGNAYYAKKDYNEAY HHCCEEECCCHHHHH	30.01	21906983
42	Ubiquitination	GNAYYAKKDYNEAYN HCCEEECCCHHHHHH	58.22	22817900
48	Phosphorylation	KKDYNEAYNYYTKAI CCCHHHHHHHHHHHH	9.49	-
50	Phosphorylation	DYNEAYNYYTKAIDM CHHHHHHHHHHHHHH	10.39	19658100
51	Phosphorylation	YNEAYNYYTKAIDMC HHHHHHHHHHHHHHC	9.72	-
53	Acetylation	EAYNYYTKAIDMCPK HHHHHHHHHHHHCCC	27.50	26051181
53	Ubiquitination	EAYNYYTKAIDMCPK HHHHHHHHHHHHCCC	27.50	32015554
60	Acetylation	KAIDMCPKNASYYGN HHHHHCCCCCHHCHH	61.28	26051181
60	Ubiquitination	KAIDMCPKNASYYGN HHHHHCCCCCHHCHH	61.28	23000965
71	Phosphorylation	YYGNRAATLMMLGRF HCHHHHHHHHHHHHH	17.75	20068231
72	Ubiquitination	YGNRAATLMMLGRFR CHHHHHHHHHHHHHH	1.30	27667366
81	Ubiquitination	MLGRFREALGDAQQS HHHHHHHHHHCHHHH	16.76	21963094
94	Phosphorylation	QSVRLDDSFVRGHLR HHHCCCCHHHHHHCC	25.88	21815630
97	Methylation	RLDDSFVRGHLREGK CCCCHHHHHHCCCCC	25.46	-
99	Ubiquitination	DDSFVRGHLREGKCH CCHHHHHHCCCCCEE	15.91	27667366
104	Ubiquitination	RGHLREGKCHLSLGN HHHCCCCCEECCHHH	17.46	22817900
123	Ubiquitination	CRSFQRALELDHKNA HHHHHHHHHHCCCCH	7.96	22817900
126	Ubiquitination	FQRALELDHKNAQAQ HHHHHHHCCCCHHHH	41.14	21890473
126	Ubiquitination	FQRALELDHKNAQAQ HHHHHHHCCCCHHHH	41.14	21890473
128	2-Hydroxyisobutyrylation	RALELDHKNAQAQQE HHHHHCCCCHHHHHH	54.36	-
128	Acetylation	RALELDHKNAQAQQE HHHHHCCCCHHHHHH	54.36	23749302
128	Ubiquitination	RALELDHKNAQAQQE HHHHHCCCCHHHHHH	54.36	21906983
137	Acetylation	AQAQQEFKNANAVME HHHHHHHHHHHHHHH	55.16	25953088
137	Ubiquitination	AQAQQEFKNANAVME HHHHHHHHHHHHHHH	55.16	21906983
145	Phosphorylation	NANAVMEYEKIAETD HHHHHHHHHHHHCCC	12.39	27642862
151	Phosphorylation	EYEKIAETDFEKRDF HHHHHHCCCCCCCCH	36.65	-
155	2-Hydroxyisobutyrylation	IAETDFEKRDFRKVV HHCCCCCCCCHHHHH	58.21	-
155	Acetylation	IAETDFEKRDFRKVV HHCCCCCCCCHHHHH	58.21	23749302
155	Methylation	IAETDFEKRDFRKVV HHCCCCCCCCHHHHH	58.21	-
155	Ubiquitination	IAETDFEKRDFRKVV HHCCCCCCCCHHHHH	58.21	21906983
160	Ubiquitination	FEKRDFRKVVFCMDR CCCCCHHHHHHCHHH	42.62	22817900
175	S-nitrosocysteine	ALEFAPACHRFKILK HHHHHHHHHHHHHHH	2.00	-
175	Glutathionylation	ALEFAPACHRFKILK HHHHHHHHHHHHHHH	2.00	22555962
175	S-nitrosylation	ALEFAPACHRFKILK HHHHHHHHHHHHHHH	2.00	19483679
179	Ubiquitination	APACHRFKILKAECL HHHHHHHHHHHHHHH	47.27	22817900
182	Acetylation	CHRFKILKAECLAML HHHHHHHHHHHHHHH	45.68	25953088
182	Ubiquitination	CHRFKILKAECLAML HHHHHHHHHHHHHHH	45.68	21906983
185	Glutathionylation	FKILKAECLAMLGRY HHHHHHHHHHHHCCC	3.33	22555962
188	Sulfoxidation	LKAECLAMLGRYPEA HHHHHHHHHCCCHHH	2.35	21406390
189	Ubiquitination	KAECLAMLGRYPEAQ HHHHHHHHCCCHHHH	2.69	24816145
192	Phosphorylation	CLAMLGRYPEAQSVA HHHHHCCCHHHHHHH	12.02	22798277
197	Phosphorylation	GRYPEAQSVASDILR CCCHHHHHHHHHHHC	27.05	22798277
200	Phosphorylation	PEAQSVASDILRMDS HHHHHHHHHHHCCCC	24.03	22798277
207	Phosphorylation	SDILRMDSTNADALY HHHHCCCCCCCCHHH	17.76	21815630
212	Ubiquitination	MDSTNADALYVRGLC CCCCCCCHHHHHHHH	9.81	22817900
217	Ubiquitination	ADALYVRGLCLYYED CCHHHHHHHHHHHHH	15.65	21963094
221	Phosphorylation	YVRGLCLYYEDCIEK HHHHHHHHHHHHHHH	12.10	29496907
222	Phosphorylation	VRGLCLYYEDCIEKA HHHHHHHHHHHHHHH	7.73	29496907
235	Ubiquitination	KAVQFFVQALRMAPD HHHHHHHHHHHCCCC	29.53	29967540
238	Methylation	QFFVQALRMAPDHEK HHHHHHHHCCCCHHH	23.41	-
239	Sulfoxidation	FFVQALRMAPDHEKA HHHHHHHCCCCHHHH	7.07	30846556
239	Ubiquitination	FFVQALRMAPDHEKA HHHHHHHCCCCHHHH	7.07	29967540
245	2-Hydroxyisobutyrylation	RMAPDHEKACIACRN HCCCCHHHHHHHHCC	45.17	-
245	Acetylation	RMAPDHEKACIACRN HCCCCHHHHHHHHCC	45.17	25953088
245	Ubiquitination	RMAPDHEKACIACRN HCCCCHHHHHHHHCC	45.17	24816145
250	Ubiquitination	HEKACIACRNAKALK HHHHHHHHCCHHHHH	1.42	29967540
253	Ubiquitination	ACIACRNAKALKAKK HHHHHCCHHHHHCCH	4.52	29967540
259	Acetylation	NAKALKAKKEDGNKA CHHHHHCCHHHCCHH	55.92	7628139
266	Ubiquitination	KKEDGNKAFKEGNYK CHHHCCHHHHHCCHH	25.41	32015554
268	Acetylation	EDGNKAFKEGNYKLA HHCCHHHHHCCHHHH	70.35	25953088
268	Ubiquitination	EDGNKAFKEGNYKLA HHCCHHHHHCCHHHH	70.35	22817900
272	Phosphorylation	KAFKEGNYKLAYELY HHHHHCCHHHHHHHH	20.45	29496907
273	Ubiquitination	AFKEGNYKLAYELYT HHHHCCHHHHHHHHH	30.55	21890473
273	Acetylation	AFKEGNYKLAYELYT HHHHCCHHHHHHHHH	30.55	7709805
273	Ubiquitination	AFKEGNYKLAYELYT HHHHCCHHHHHHHHH	30.55	23000965
276	Phosphorylation	EGNYKLAYELYTEAL HCCHHHHHHHHHHHH	19.53	29496907
279	Phosphorylation	YKLAYELYTEALGID HHHHHHHHHHHHCCC	7.21	29496907
291	Ubiquitination	GIDPNNIKTNAKLYC CCCCCCCCCCCEEEE	37.54	29967540
295	Acetylation	NNIKTNAKLYCNRGT CCCCCCCEEEECCCH	41.90	25953088
295	Ubiquitination	NNIKTNAKLYCNRGT CCCCCCCEEEECCCH	41.90	29967540
303	Ubiquitination	LYCNRGTVNSKLRKL EEECCCHHHHHHHHH	9.42	33845483
306	Acetylation	NRGTVNSKLRKLDDA CCCHHHHHHHHHHHH	47.29	23749302
306	Malonylation	NRGTVNSKLRKLDDA CCCHHHHHHHHHHHH	47.29	26320211
306	Ubiquitination	NRGTVNSKLRKLDDA CCCHHHHHHHHHHHH	47.29	29967540
308	Ubiquitination	GTVNSKLRKLDDAIE CHHHHHHHHHHHHHH	41.02	22817900
309	Acetylation	TVNSKLRKLDDAIED HHHHHHHHHHHHHHH	67.70	26051181
309	Ubiquitination	TVNSKLRKLDDAIED HHHHHHHHHHHHHHH	67.70	29967540
312	Ubiquitination	SKLRKLDDAIEDCTN HHHHHHHHHHHHCCC	60.94	21890473
312	Ubiquitination	SKLRKLDDAIEDCTN HHHHHHHHHHHHCCC	60.94	33845483
317	Glutathionylation	LDDAIEDCTNAVKLD HHHHHHHCCCCCCCC	1.73	22555962
319	Ubiquitination	DAIEDCTNAVKLDDT HHHHHCCCCCCCCHH	49.41	32015554
322	Acetylation	EDCTNAVKLDDTYIK HHCCCCCCCCHHHHH	43.73	26051181
322	Ubiquitination	EDCTNAVKLDDTYIK HHCCCCCCCCHHHHH	43.73	23000965
324	Ubiquitination	CTNAVKLDDTYIKAY CCCCCCCCHHHHHHH	40.25	23000965
326	Phosphorylation	NAVKLDDTYIKAYLR CCCCCCHHHHHHHHH	27.15	21815630
327	Phosphorylation	AVKLDDTYIKAYLRR CCCCCHHHHHHHHHH	13.86	28102081
328	Ubiquitination	VKLDDTYIKAYLRRA CCCCHHHHHHHHHHH	1.92	21890473
328	Ubiquitination	VKLDDTYIKAYLRRA CCCCHHHHHHHHHHH	1.92	23000965
329	Acetylation	KLDDTYIKAYLRRAQ CCCHHHHHHHHHHHC	22.14	23236377
329	Ubiquitination	KLDDTYIKAYLRRAQ CCCHHHHHHHHHHHC	22.14	23000965
334	Ubiquitination	YIKAYLRRAQCYMDT HHHHHHHHHCCCCCH	26.81	23000965
337	Glutathionylation	AYLRRAQCYMDTEQY HHHHHHCCCCCHHHH	2.72	22555962
342	Ubiquitination	AQCYMDTEQYEEAVR HCCCCCHHHHHHHHH	47.07	33845483
344	Phosphorylation	CYMDTEQYEEAVRDY CCCCHHHHHHHHHHH	14.98	27642862
351	Phosphorylation	YEEAVRDYEKVYQTE HHHHHHHHHHHHHHH	13.69	27642862
355	Phosphorylation	VRDYEKVYQTEKTKE HHHHHHHHHHHCCHH	22.30	25839225
359	2-Hydroxyisobutyrylation	EKVYQTEKTKEHKQL HHHHHHHCCHHHHHH	69.18	-
359	Acetylation	EKVYQTEKTKEHKQL HHHHHHHCCHHHHHH	69.18	23749302
359	Ubiquitination	EKVYQTEKTKEHKQL HHHHHHHCCHHHHHH	69.18	33845483
364	Ubiquitination	TEKTKEHKQLLKNAQ HHCCHHHHHHHHHHC	43.67	22817900
366	Ubiquitination	KTKEHKQLLKNAQLE CCHHHHHHHHHHCHH	9.79	33845483
368	Acetylation	KEHKQLLKNAQLELK HHHHHHHHHHCHHHH	59.85	25953088
368	Ubiquitination	KEHKQLLKNAQLELK HHHHHHHHHHCHHHH	59.85	22817900
373	Ubiquitination	LLKNAQLELKKSKRK HHHHHCHHHHHHHCC	46.60	33845483
375	2-Hydroxyisobutyrylation	KNAQLELKKSKRKDY HHHCHHHHHHHCCCH	45.70	-
375	Acetylation	KNAQLELKKSKRKDY HHHCHHHHHHHCCCH	45.70	23749302
375	Ubiquitination	KNAQLELKKSKRKDY HHHCHHHHHHHCCCH	45.70	32015554
376	Ubiquitination	NAQLELKKSKRKDYY HHCHHHHHHHCCCHH	74.05	-
377	Phosphorylation	AQLELKKSKRKDYYK HCHHHHHHHCCCHHH	35.78	24719451
378	Ubiquitination	QLELKKSKRKDYYKI CHHHHHHHCCCHHHH	72.80	23000965
380	Ubiquitination	ELKKSKRKDYYKILG HHHHHHCCCHHHHHC	54.54	23000965
382	Phosphorylation	KKSKRKDYYKILGVD HHHHCCCHHHHHCCC	15.08	29496907
383	Phosphorylation	KSKRKDYYKILGVDK HHHCCCHHHHHCCCC	11.16	24719451
384	2-Hydroxyisobutyrylation	SKRKDYYKILGVDKN HHCCCHHHHHCCCCC	25.81	-
384	Ubiquitination	SKRKDYYKILGVDKN HHCCCHHHHHCCCCC	25.81	23000965
386	Ubiquitination	RKDYYKILGVDKNAS CCCHHHHHCCCCCCC	4.84	33845483
387	Ubiquitination	KDYYKILGVDKNASE CCHHHHHCCCCCCCH	29.11	22817900
388	Ubiquitination	DYYKILGVDKNASED CHHHHHCCCCCCCHH	9.44	22817900
390	Acetylation	YKILGVDKNASEDEI HHHHCCCCCCCHHHH	52.59	25953088
390	Ubiquitination	YKILGVDKNASEDEI HHHHCCCCCCCHHHH	52.59	23000965
393	Phosphorylation	LGVDKNASEDEIKKA HCCCCCCCHHHHHHH	55.78	28102081
398	Ubiquitination	NASEDEIKKAYRKRA CCCHHHHHHHHHHHH	29.33	33845483
399	Ubiquitination	ASEDEIKKAYRKRAL CCHHHHHHHHHHHHH	57.20	-
401	Phosphorylation	EDEIKKAYRKRALMH HHHHHHHHHHHHHHH	26.08	29496907
407	Sulfoxidation	AYRKRALMHHPDRHS HHHHHHHHHCCCCCC	2.38	30846556
412	Methylation	ALMHHPDRHSGASAE HHHHCCCCCCCCCHH	30.26	-
414	Phosphorylation	MHHPDRHSGASAEVQ HHCCCCCCCCCHHHH	36.63	28555341
417	Phosphorylation	PDRHSGASAEVQKEE CCCCCCCCHHHHHHH	28.61	29449344
422	Ubiquitination	GASAEVQKEEEKKFK CCCHHHHHHHHHHHH	72.73	33845483
429	Ubiquitination	KEEEKKFKEVGEAFT HHHHHHHHHHHHHHH	61.44	33845483
442	2-Hydroxyisobutyrylation	FTILSDPKKKTRYDS HHHCCCCCCCCCCCC	72.41	-
442	Ubiquitination	FTILSDPKKKTRYDS HHHCCCCCCCCCCCC	72.41	22817900
443	Ubiquitination	TILSDPKKKTRYDSG HHCCCCCCCCCCCCC	65.84	22817900
444	Ubiquitination	ILSDPKKKTRYDSGQ HCCCCCCCCCCCCCC	44.34	22817900
447	Phosphorylation	DPKKKTRYDSGQDLD CCCCCCCCCCCCCCC	21.49	26434776
449	Phosphorylation	KKKTRYDSGQDLDEE CCCCCCCCCCCCCCC	29.44	25159151

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 DNJC7_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DNJC7_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 DNJC7_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RAD9A_HUMAN	RAD9A	physical	11573955
HUS1_HUMAN	HUS1	physical	11573955
RAD1_HUMAN	RAD1	physical	11573955
HS90A_HUMAN	HSP90AA1	physical	12853476
HS71A_BOVIN	HSPA1A	physical	12853476
TPM1_HUMAN	TPM1	physical	22863883
HS71L_HUMAN	HSPA1L	physical	25036637
HSP74_HUMAN	HSPA4	physical	26344197
PYR1_HUMAN	CAD	physical	26496610
CLCA_HUMAN	CLTA	physical	26496610
CLH1_HUMAN	CLTC	physical	26496610
CPSM_HUMAN	CPS1	physical	26496610
IF2G_HUMAN	EIF2S3	physical	26496610
FAS_HUMAN	FASN	physical	26496610
PUR2_HUMAN	GART	physical	26496610
GNAS3_HUMAN	GNAS	physical	26496610
GNAS2_HUMAN	GNAS	physical	26496610
ALEX_HUMAN	GNAS	physical	26496610
GNAS1_HUMAN	GNAS	physical	26496610
HSP72_HUMAN	HSPA2	physical	26496610
HSP7C_HUMAN	HSPA8	physical	26496610
HS90B_HUMAN	HSP90AB1	physical	26496610
DNJB1_HUMAN	DNAJB1	physical	26496610
PUR4_HUMAN	PFAS	physical	26496610
RPB2_HUMAN	POLR2B	physical	26496610
PRKDC_HUMAN	PRKDC	physical	26496610
RNF5_HUMAN	RNF5	physical	26496610
SVIL_HUMAN	SVIL	physical	26496610
TCPG_HUMAN	CCT3	physical	26496610
OFD1_HUMAN	OFD1	physical	26496610
BAG2_HUMAN	BAG2	physical	26496610
EPN4_HUMAN	CLINT1	physical	26496610
K0100_HUMAN	KIAA0100	physical	26496610
CHIP_HUMAN	STUB1	physical	26496610
STIP1_HUMAN	STIP1	physical	26496610
DNJB4_HUMAN	DNAJB4	physical	26496610
SYNPO_HUMAN	SYNPO	physical	26496610
TRI32_HUMAN	TRIM32	physical	26496610
VP13A_HUMAN	VPS13A	physical	26496610
SCC4_HUMAN	MAU2	physical	26496610
HERC4_HUMAN	HERC4	physical	26496610
VP13C_HUMAN	VPS13C	physical	26496610
IF122_HUMAN	IFT122	physical	26496610
TDRD9_HUMAN	TDRD9	physical	26496610
MISP_HUMAN	MISP	physical	26496610
VP13B_HUMAN	VPS13B	physical	26496610
LAMA1_HUMAN	LAMA1	physical	26496610
EMAL5_HUMAN	EML5	physical	28514442
VP13B_HUMAN	VPS13B	physical	28514442
BBS10_HUMAN	BBS10	physical	28514442
K0100_HUMAN	KIAA0100	physical	28514442
NPHP1_HUMAN	NPHP1	physical	28514442
FANCB_HUMAN	FANCB	physical	28514442
URGCP_HUMAN	URGCP	physical	28514442
WDR41_HUMAN	WDR41	physical	28514442
GREB1_HUMAN	GREB1	physical	28514442
CE034_HUMAN	C5orf34	physical	28514442
WDR19_HUMAN	WDR19	physical	28514442
VP13C_HUMAN	VPS13C	physical	28514442
VP13A_HUMAN	VPS13A	physical	28514442
MTO1_HUMAN	MTO1	physical	28514442
CTC1_HUMAN	CTC1	physical	28514442
PLD2_HUMAN	PLD2	physical	28514442
NEUL4_HUMAN	NEURL4	physical	28514442
MOCOS_HUMAN	MOCOS	physical	28514442
IF172_HUMAN	IFT172	physical	28514442
PWP2_HUMAN	PWP2	physical	28514442
SMG8_HUMAN	SMG8	physical	28514442
DPOE1_HUMAN	POLE	physical	28514442
WDR35_HUMAN	WDR35	physical	28514442
WDR62_HUMAN	WDR62	physical	28514442
DNA2_HUMAN	DNA2	physical	28514442
ESPL1_HUMAN	ESPL1	physical	28514442
NPHP4_HUMAN	NPHP4	physical	28514442
IF140_HUMAN	IFT140	physical	28514442
FUND2_HUMAN	FUNDC2	physical	28514442
LRWD1_HUMAN	LRWD1	physical	28514442
MED16_HUMAN	MED16	physical	28514442
DPOE2_HUMAN	POLE2	physical	28514442
KI20B_HUMAN	KIF20B	physical	28514442
UBP19_HUMAN	USP19	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 DNJC7_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"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-50, AND MASSSPECTROMETRY.	15592455 [Abstract]