dbPTM

H14_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H14_HUMAN
UniProt AC	P10412
Protein Name	Histone H1.4
Gene Name	HIST1H1E
Organism	Homo sapiens (Human).
Sequence Length	219
Subcellular Localization	Nucleus. Chromosome. Mainly localizes in heterochromatin. Dysplays a punctuate staining pattern in the nucleus.
Protein Description	Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity)..
Protein Sequence	MSETAPAAPAAPAPAEKTPVKKKARKSAGAAKRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEAKPKAKKAGAAKAKKPAGAAKKPKKATGAATPKKSAKKTPKKAKKPAAAAGAKKAKSPKKAKAAKPKKAPKSPAKAKAVKPKAAKPKTAKPKAAKPKKAAAKKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSETAPAAP ------CCCCCCCCC	43.59	20068231
2	Phosphorylation	------MSETAPAAP ------CCCCCCCCC	43.59	29255136
4	Phosphorylation	----MSETAPAAPAA ----CCCCCCCCCCC	30.54	29255136
17	Acetylation	AAPAPAEKTPVKKKA CCCCCCCCCCCCHHH	61.30	21466224
17	Ubiquitination	AAPAPAEKTPVKKKA CCCCCCCCCCCCHHH	61.30	19608861
18	Phosphorylation	APAPAEKTPVKKKAR CCCCCCCCCCCHHHH	25.48	29255136
21	Acetylation	PAEKTPVKKKARKSA CCCCCCCCHHHHHHH	50.16	21466224
21	Ubiquitination	PAEKTPVKKKARKSA CCCCCCCCHHHHHHH	50.16	21890473
22	Ubiquitination	AEKTPVKKKARKSAG CCCCCCCHHHHHHHH	52.48	-
26	"N6,N6-dimethyllysine"	PVKKKARKSAGAAKR CCCHHHHHHHHHHHH	49.90	-
26	Acetylation	PVKKKARKSAGAAKR CCCHHHHHHHHHHHH	49.90	15469825
26	Methylation	PVKKKARKSAGAAKR CCCHHHHHHHHHHHH	49.90	15469825
27	Phosphorylation	VKKKARKSAGAAKRK CCHHHHHHHHHHHHH	26.78	28176443
32	Acetylation	RKSAGAAKRKASGPP HHHHHHHHHHHCCCC	54.63	19854283
34	Acetylation	SAGAAKRKASGPPVS HHHHHHHHHCCCCHH	46.31	17043054
34	Malonylation	SAGAAKRKASGPPVS HHHHHHHHHCCCCHH	46.31	26320211
34	Methylation	SAGAAKRKASGPPVS HHHHHHHHHCCCCHH	46.31	-
34	Other	SAGAAKRKASGPPVS HHHHHHHHHCCCCHH	46.31	-
34	Succinylation	SAGAAKRKASGPPVS HHHHHHHHHCCCCHH	46.31	-
34	Succinylation	SAGAAKRKASGPPVS HHHHHHHHHCCCCHH	46.31	-
34	Ubiquitination	SAGAAKRKASGPPVS HHHHHHHHHCCCCHH	46.31	-
36	Phosphorylation	GAAKRKASGPPVSEL HHHHHHHCCCCHHHH	55.67	29255136
41	Phosphorylation	KASGPPVSELITKAV HHCCCCHHHHHHHHH	32.24	30266825
45	Phosphorylation	PPVSELITKAVAASK CCHHHHHHHHHHHHH	26.10	30266825
46	Acetylation	PVSELITKAVAASKE CHHHHHHHHHHHHHH	33.59	23954790
46	Hydroxylation	PVSELITKAVAASKE CHHHHHHHHHHHHHH	33.59	24681537
46	Malonylation	PVSELITKAVAASKE CHHHHHHHHHHHHHH	33.59	26320211
46	Ubiquitination	PVSELITKAVAASKE CHHHHHHHHHHHHHH	33.59	19608861
51	Phosphorylation	ITKAVAASKERSGVS HHHHHHHHHHCCCCC	25.88	26546556
52	Acetylation	TKAVAASKERSGVSL HHHHHHHHHCCCCCH	53.04	17043054
52	Hydroxylation	TKAVAASKERSGVSL HHHHHHHHHCCCCCH	53.04	24681537
52	Other	TKAVAASKERSGVSL HHHHHHHHHCCCCCH	53.04	-
52	Ubiquitination	TKAVAASKERSGVSL HHHHHHHHHCCCCCH	53.04	17043054
54	Citrullination	AVAASKERSGVSLAA HHHHHHHCCCCCHHH	42.31	-
54	Citrullination	AVAASKERSGVSLAA HHHHHHHCCCCCHHH	42.31	-
54	Methylation	AVAASKERSGVSLAA HHHHHHHCCCCCHHH	42.31	-
55	Phosphorylation	VAASKERSGVSLAAL HHHHHHCCCCCHHHH	44.64	30266825
58	Phosphorylation	SKERSGVSLAALKKA HHHCCCCCHHHHHHH	18.80	30266825
63	Acetylation	GVSLAALKKALAAAG CCCHHHHHHHHHHCC	31.13	25825284
63	Hydroxylation	GVSLAALKKALAAAG CCCHHHHHHHHHHCC	31.13	24681537
63	Malonylation	GVSLAALKKALAAAG CCCHHHHHHHHHHCC	31.13	26320211
63	Methylation	GVSLAALKKALAAAG CCCHHHHHHHHHHCC	31.13	-
63	Succinylation	GVSLAALKKALAAAG CCCHHHHHHHHHHCC	31.13	23954790
63	Ubiquitination	GVSLAALKKALAAAG CCCHHHHHHHHHHCC	31.13	19608861
64	Sumoylation	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	-
64	Acetylation	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	17043054
64	Hydroxylation	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	24681537
64	Malonylation	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	26320211
64	Methylation	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	17043054
64	Other	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	-
64	Sumoylation	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	17043054
64	Ubiquitination	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	17043054
71	Phosphorylation	KALAAAGYDVEKNNS HHHHHCCCCCHHCCC	16.46	28152594
75	Acetylation	AAGYDVEKNNSRIKL HCCCCCHHCCCCCCC	62.37	21466224
75	Malonylation	AAGYDVEKNNSRIKL HCCCCCHHCCCCCCC	62.37	26320211
75	Methylation	AAGYDVEKNNSRIKL HCCCCCHHCCCCCCC	62.37	17043054
75	Ubiquitination	AAGYDVEKNNSRIKL HCCCCCHHCCCCCCC	62.37	17043054
78	Phosphorylation	YDVEKNNSRIKLGLK CCCHHCCCCCCCCHH	44.79	23401153
85	Acetylation	SRIKLGLKSLVSKGT CCCCCCHHHHHHCCC	39.69	23236377
85	Malonylation	SRIKLGLKSLVSKGT CCCCCCHHHHHHCCC	39.69	26320211
85	Other	SRIKLGLKSLVSKGT CCCCCCHHHHHHCCC	39.69	-
85	Ubiquitination	SRIKLGLKSLVSKGT CCCCCCHHHHHHCCC	39.69	21890473
86	Phosphorylation	RIKLGLKSLVSKGTL CCCCCHHHHHHCCCE	38.76	20860994
89	Phosphorylation	LGLKSLVSKGTLVQT CCHHHHHHCCCEEEE	30.57	17877366
90	Acetylation	GLKSLVSKGTLVQTK CHHHHHHCCCEEEEC	48.73	23954790
90	Hydroxylation	GLKSLVSKGTLVQTK CHHHHHHCCCEEEEC	48.73	24681537
90	Malonylation	GLKSLVSKGTLVQTK CHHHHHHCCCEEEEC	48.73	26320211
90	Other	GLKSLVSKGTLVQTK CHHHHHHCCCEEEEC	48.73	-
90	Ubiquitination	GLKSLVSKGTLVQTK CHHHHHHCCCEEEEC	48.73	17043054
92	Phosphorylation	KSLVSKGTLVQTKGT HHHHHCCCEEEECCC	27.74	17877366
96	Phosphorylation	SKGTLVQTKGTGASG HCCCEEEECCCCCCC	24.78	28111955
97	Acetylation	KGTLVQTKGTGASGS CCCEEEECCCCCCCC	37.07	17043054
97	Hydroxylation	KGTLVQTKGTGASGS CCCEEEECCCCCCCC	37.07	24681537
97	Malonylation	KGTLVQTKGTGASGS CCCEEEECCCCCCCC	37.07	26320211
97	Methylation	KGTLVQTKGTGASGS CCCEEEECCCCCCCC	37.07	17043054
97	Succinylation	KGTLVQTKGTGASGS CCCEEEECCCCCCCC	37.07	-
97	Ubiquitination	KGTLVQTKGTGASGS CCCEEEECCCCCCCC	37.07	17043054
99	Phosphorylation	TLVQTKGTGASGSFK CEEEECCCCCCCCEE	31.00	26657352
102	Phosphorylation	QTKGTGASGSFKLNK EECCCCCCCCEECCC	35.99	25159151
104	Phosphorylation	KGTGASGSFKLNKKA CCCCCCCCEECCCCC	19.40	23401153
106	Acetylation	TGASGSFKLNKKAAS CCCCCCEECCCCCCC	53.50	19608861
106	Malonylation	TGASGSFKLNKKAAS CCCCCCEECCCCCCC	53.50	26320211
106	Methylation	TGASGSFKLNKKAAS CCCCCCEECCCCCCC	53.50	-
106	Other	TGASGSFKLNKKAAS CCCCCCEECCCCCCC	53.50	-
106	Ubiquitination	TGASGSFKLNKKAAS CCCCCCEECCCCCCC	53.50	-
109	Ubiquitination	SGSFKLNKKAASGEA CCCEECCCCCCCCCC	54.98	-
110	Ubiquitination	GSFKLNKKAASGEAK CCEECCCCCCCCCCC	48.38	21890473
113	Phosphorylation	KLNKKAASGEAKPKA ECCCCCCCCCCCHHH	41.86	26657352
117	Ubiquitination	KAASGEAKPKAKKAG CCCCCCCCHHHHHHC	42.63	21890473
119	Methylation	ASGEAKPKAKKAGAA CCCCCCHHHHHHCHH	72.61	-
119	Ubiquitination	ASGEAKPKAKKAGAA CCCCCCHHHHHHCHH	72.61	-
121	Methylation	GEAKPKAKKAGAAKA CCCCHHHHHHCHHHC	49.64	-
129	Acetylation	KAGAAKAKKPAGAAK HHCHHHCCCCCCCCC	59.59	163871
129	Methylation	KAGAAKAKKPAGAAK HHCHHHCCCCCCCCC	59.59	-
130	Acetylation	AGAAKAKKPAGAAKK HCHHHCCCCCCCCCC	44.98	163875
136	Acetylation	KKPAGAAKKPKKATG CCCCCCCCCCCCCCC	69.90	163879
136	Ubiquitination	KKPAGAAKKPKKATG CCCCCCCCCCCCCCC	69.90	-
137	Acetylation	KPAGAAKKPKKATGA CCCCCCCCCCCCCCC	58.29	163883
137	Ubiquitination	KPAGAAKKPKKATGA CCCCCCCCCCCCCCC	58.29	-
140	Lactylation	GAAKKPKKATGAATP CCCCCCCCCCCCCCC	60.76	31645732
140	Ubiquitination	GAAKKPKKATGAATP CCCCCCCCCCCCCCC	60.76	21890473
142	Phosphorylation	AKKPKKATGAATPKK CCCCCCCCCCCCCCC	35.91	28176443
146	Phosphorylation	KKATGAATPKKSAKK CCCCCCCCCCCCCCC	34.80	30266825
148	Acetylation	ATGAATPKKSAKKTP CCCCCCCCCCCCCCC	55.81	30585169
148	Methylation	ATGAATPKKSAKKTP CCCCCCCCCCCCCCC	55.81	-
148	Ubiquitination	ATGAATPKKSAKKTP CCCCCCCCCCCCCCC	55.81	21890473
150	ADP-ribosylation	GAATPKKSAKKTPKK CCCCCCCCCCCCCHH	51.99	27723750
150	Phosphorylation	GAATPKKSAKKTPKK CCCCCCCCCCCCCHH	51.99	24732914
154	Phosphorylation	PKKSAKKTPKKAKKP CCCCCCCCCHHHCCH	39.37	21601212
159	Methylation	KKTPKKAKKPAAAAG CCCCHHHCCHHHHHC	69.07	-
159	Ubiquitination	KKTPKKAKKPAAAAG CCCCHHHCCHHHHHC	69.07	-
160	Acetylation	KTPKKAKKPAAAAGA CCCHHHCCHHHHHCH	44.76	19861021
160	Ubiquitination	KTPKKAKKPAAAAGA CCCHHHCCHHHHHCH	44.76	21906983
168	Acetylation	PAAAAGAKKAKSPKK HHHHHCHHHCCCHHH	52.96	17043054
168	Ubiquitination	PAAAAGAKKAKSPKK HHHHHCHHHCCCHHH	52.96	17043054
169	Acetylation	AAAAGAKKAKSPKKA HHHHCHHHCCCHHHH	61.59	30585175
169	Methylation	AAAAGAKKAKSPKKA HHHHCHHHCCCHHHH	61.59	-
171	Methylation	AAGAKKAKSPKKAKA HHCHHHCCCHHHHHC	75.95	-
172	Phosphorylation	AGAKKAKSPKKAKAA HCHHHCCCHHHHHCC	46.97	16377619
177	Methylation	AKSPKKAKAAKPKKA CCCHHHHHCCCCCCC	58.73	-
186	Methylation	AKPKKAPKSPAKAKA CCCCCCCCCHHHHHC	74.14	-
187	Phosphorylation	KPKKAPKSPAKAKAV CCCCCCCCHHHHHCC	29.09	30266825
192	Methylation	PKSPAKAKAVKPKAA CCCHHHHHCCCCCCC	53.67	-
195	Ubiquitination	PAKAKAVKPKAAKPK HHHHHCCCCCCCCCC	45.73	-
197	Ubiquitination	KAKAVKPKAAKPKTA HHHCCCCCCCCCCCC	56.08	-

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
18	T	Phosphorylation	Kinase	CDK1	P06493	PSP
18	T	Phosphorylation	Kinase	CDK2	P24941	PSP
36	S	Phosphorylation	Kinase	PKACA	P17612	PSP
36	S	Phosphorylation	Kinase	PRKACA	P05132	GPS
146	T	Phosphorylation	Kinase	CDK2	P24941	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
26	K	Acetylation	15469825
Acetylated at Lys-26.
26	K	Acetylation	15469825
Deacetylated at Lys-26 by SIRT1.
54	R	Citrullination	-
Citrullination at Arg-54 (H1R54ci) by PADI4 takes place within the DNA-binding site of H1 and results in its displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance.

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 H14_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CBX5_HUMAN	CBX5	physical	16127177
MED8_HUMAN	MED8	physical	22939629
IL7RA_HUMAN	IL7R	physical	23151878
EXOS4_HUMAN	EXOSC4	physical	22863883
TOM1_HUMAN	TOM1	physical	22863883
VP26A_HUMAN	VPS26A	physical	22863883
YBOX2_HUMAN	YBX2	physical	28514442
LEO1_HUMAN	LEO1	physical	28514442
ZN346_HUMAN	ZNF346	physical	28514442
UBF1_HUMAN	UBTF	physical	28514442
CMS1_HUMAN	CMSS1	physical	28514442
RBM19_HUMAN	RBM19	physical	28514442
RS3_HUMAN	RPS3	physical	28514442
CTR9_HUMAN	CTR9	physical	28514442
Z354A_HUMAN	ZNF354A	physical	28514442
ZNF16_HUMAN	ZNF16	physical	28514442
LIN41_HUMAN	TRIM71	physical	28514442
GLE1_HUMAN	GLE1	physical	28514442
ZN184_HUMAN	ZNF184	physical	28514442
KRR1_HUMAN	KRR1	physical	28514442
DDX55_HUMAN	DDX55	physical	28514442
NOG2_HUMAN	GNL2	physical	28514442
I20L2_HUMAN	ISG20L2	physical	28514442
ZNF48_HUMAN	ZNF48	physical	28514442
NSD2_HUMAN	WHSC1	physical	28514442
RBMS1_HUMAN	RBMS1	physical	28514442
RS2_HUMAN	RPS2	physical	28514442
MOV10_HUMAN	MOV10	physical	28514442
RS17_HUMAN	RPS17	physical	28514442
TOE1_HUMAN	TOE1	physical	28514442
RS15_HUMAN	RPS15	physical	28514442
RBM34_HUMAN	RBM34	physical	28514442
SF3B2_HUMAN	SF3B2	physical	28514442
RS16_HUMAN	RPS16	physical	28514442
RRP12_HUMAN	RRP12	physical	28514442
GLYR1_HUMAN	GLYR1	physical	28514442
LARP1_HUMAN	LARP1	physical	28514442
RL37A_HUMAN	RPL37A	physical	28514442
RL26L_HUMAN	RPL26L1	physical	28514442
SPB1_HUMAN	FTSJ3	physical	28514442
PUM3_HUMAN	KIAA0020	physical	28514442
NOC3L_HUMAN	NOC3L	physical	28514442
STAU1_HUMAN	STAU1	physical	28514442
SYFM_HUMAN	FARS2	physical	28514442
SF3B1_HUMAN	SF3B1	physical	28514442
ZCHC9_HUMAN	ZCCHC9	physical	28514442
CTCF_HUMAN	CTCF	physical	28514442
RRP8_HUMAN	RRP8	physical	28514442
DDX18_HUMAN	DDX18	physical	28514442
DKC1_HUMAN	DKC1	physical	28514442
IF2B3_HUMAN	IGF2BP3	physical	28514442
RENT1_HUMAN	UPF1	physical	28514442
REXO4_HUMAN	REXO4	physical	28514442
TEX10_HUMAN	TEX10	physical	28514442
RS10_HUMAN	RPS10	physical	28514442
DDX10_HUMAN	DDX10	physical	28514442
BRX1_HUMAN	BRIX1	physical	28514442
CEBPZ_HUMAN	CEBPZ	physical	28514442
RS19_HUMAN	RPS19	physical	28514442
KRI1_HUMAN	KRI1	physical	28514442
DHX30_HUMAN	DHX30	physical	28514442
RBM28_HUMAN	RBM28	physical	28514442
STAU2_HUMAN	STAU2	physical	28514442
MAK16_HUMAN	MAK16	physical	28514442
NMNA1_HUMAN	NMNAT1	physical	28514442
PURA_HUMAN	PURA	physical	28514442
PK1IP_HUMAN	PAK1IP1	physical	28514442
NOP2_HUMAN	NOP2	physical	28514442
LA_HUMAN	SSB	physical	28514442
DDX31_HUMAN	DDX31	physical	28514442
NOP14_HUMAN	NOP14	physical	28514442
ELAV2_HUMAN	ELAVL2	physical	28514442
RS3A_HUMAN	RPS3A	physical	28514442
CD11B_HUMAN	CDK11B	physical	28514442
DDX27_HUMAN	DDX27	physical	28514442
RS20_HUMAN	RPS20	physical	28514442
UIF_HUMAN	FYTTD1	physical	28514442
ZN668_HUMAN	ZNF668	physical	28514442
SRSF1_HUMAN	SRSF1	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 H14_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-17 AND LYS-46, AND MASSSPECTROMETRY.	19608861 [Abstract]
"Human SirT1 interacts with histone H1 and promotes formation offacultative heterochromatin."; Vaquero A., Scher M., Lee D., Erdjument-Bromage H., Tempst P.,Reinberg D.; Mol. Cell 16:93-105(2004). Cited for: ACETYLATION AT LYS-26.	15469825 [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-2; THR-4 AND THR-18, ANDMASS SPECTROMETRY.	19413330 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18; SER-36; SER-41;THR-142; THR-146 AND SER-187, AND MASS SPECTROMETRY.	19007248 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18; SER-27 AND SER-36,AND MASS SPECTROMETRY.	17287340 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18 AND SER-187, AND MASSSPECTROMETRY.	17081983 [Abstract]
"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 THR-18, 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 THR-18, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18, AND MASSSPECTROMETRY.	17924679 [Abstract]

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