dbPTM

HP1B3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HP1B3_HUMAN
UniProt AC	Q5SSJ5
Protein Name	Heterochromatin protein 1-binding protein 3
Gene Name	HP1BP3
Organism	Homo sapiens (Human).
Sequence Length	553
Subcellular Localization	Nucleus . Chromosome . localized in nuclei but not in nucleoli in interphase. Colocalized with chromosomes in mitosis, with a gradually increased during G1 progression and a maximum level during late G1 phase (G1/S).
Protein Description	Component of heterochromatin that maintains heterochromatin integrity during G1/S progression and regulates the duration of G1 phase to critically influence cell proliferative capacity. [PubMed: 24830416). Mediates chromatin condensation during hypoxia]
Protein Sequence	MATDTSQGELVHPKALPLIVGAQLIHADKLGEKVEDSTMPIRRTVNSTRETPPKSKLAEGEEEKPEPDISSEESVSTVEEQENETPPATSSEAEQPKGEPENEEKEENKSSEETKKDEKDQSKEKEKKVKKTIPSWATLSASQLARAQKQTPMASSPRPKMDAILTEAIKACFQKSGASVVAIRKYIIHKYPSLELERRGYLLKQALKRELNRGVIKQVKGKGASGSFVVVQKSRKTPQKSRNRKNRSSAVDPEPQVKLEDVLPLAFTRLCEPKEASYSLIRKYVSQYYPKLRVDIRPQLLKNALQRAVERGQLEQITGKGASGTFQLKKSGEKPLLGGSLMEYAILSAIAAMNEPKTCSTTALKKYVLENHPGTNSNYQMHLLKKTLQKCEKNGWMEQISGKGFSGTFQLCFPYYPSPGVLFPKKEPDDSRDEDEDEDESSEEDSEDEEPPPKRRLQKKTPAKSPGKAASVKQRGSKPAPKVSAAQRGKARPLPKKAPPKAKTPAKKTRPSSTVIKKPSGGSSKKPATSARKEVKLPGKGKSTMKKSFRVKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MATDTSQGE ------CCCCCCCCC	17.74	20068231
3	Phosphorylation	-----MATDTSQGEL -----CCCCCCCCCC	38.21	22167270
5	Phosphorylation	---MATDTSQGELVH ---CCCCCCCCCCCC	20.70	29255136
6	Phosphorylation	--MATDTSQGELVHP --CCCCCCCCCCCCC	38.71	23401153
9 (in isoform 2)	Phosphorylation	-	39.73	29116813
13 (in isoform 2)	Phosphorylation	-	19.01	29116813
14	Ubiquitination	QGELVHPKALPLIVG CCCCCCCCHHHHEEE	47.91	21890473
14 (in isoform 1)	Ubiquitination	-	47.91	21890473
14 (in isoform 5)	Ubiquitination	-	47.91	21890473
29	2-Hydroxyisobutyrylation	AQLIHADKLGEKVED EEEEEHHHHCCCCCC	60.21	-
29	Acetylation	AQLIHADKLGEKVED EEEEEHHHHCCCCCC	60.21	23749302
29	Ubiquitination	AQLIHADKLGEKVED EEEEEHHHHCCCCCC	60.21	33845483
33	Ubiquitination	HADKLGEKVEDSTMP EHHHHCCCCCCCCCC	49.48	33845483
37	Phosphorylation	LGEKVEDSTMPIRRT HCCCCCCCCCCCCCC	17.07	26074081
38	Phosphorylation	GEKVEDSTMPIRRTV CCCCCCCCCCCCCCC	39.01	26074081
39	Sulfoxidation	EKVEDSTMPIRRTVN CCCCCCCCCCCCCCC	2.77	21406390
44	Phosphorylation	STMPIRRTVNSTRET CCCCCCCCCCCCCCC	17.75	26055452
47	Phosphorylation	PIRRTVNSTRETPPK CCCCCCCCCCCCCCH	25.22	23401153
48	Phosphorylation	IRRTVNSTRETPPKS CCCCCCCCCCCCCHH	27.59	23401153
51	Phosphorylation	TVNSTRETPPKSKLA CCCCCCCCCCHHHCC	41.42	25159151
55	Phosphorylation	TRETPPKSKLAEGEE CCCCCCHHHCCCCCC	38.38	23403867
64	Sumoylation	LAEGEEEKPEPDISS CCCCCCCCCCCCCCC	58.94	28112733
70	Phosphorylation	EKPEPDISSEESVST CCCCCCCCCCHHCCC	38.79	30278072
71	Phosphorylation	KPEPDISSEESVSTV CCCCCCCCCHHCCCH	45.80	30278072
74	Phosphorylation	PDISSEESVSTVEEQ CCCCCCHHCCCHHHH	19.81	30278072
76	Phosphorylation	ISSEESVSTVEEQEN CCCCHHCCCHHHHCC	35.69	30278072
77	Phosphorylation	SSEESVSTVEEQENE CCCHHCCCHHHHCCC	29.76	30278072
85	Phosphorylation	VEEQENETPPATSSE HHHHCCCCCCCCCCC	46.27	30278072
89	Phosphorylation	ENETPPATSSEAEQP CCCCCCCCCCCCCCC	38.26	30576142
89	Ubiquitination	ENETPPATSSEAEQP CCCCCCCCCCCCCCC	38.26	22817900
90	Phosphorylation	NETPPATSSEAEQPK CCCCCCCCCCCCCCC	28.43	25850435
90	Ubiquitination	NETPPATSSEAEQPK CCCCCCCCCCCCCCC	28.43	22817900
91	Phosphorylation	ETPPATSSEAEQPKG CCCCCCCCCCCCCCC	36.15	30576142
92	Ubiquitination	TPPATSSEAEQPKGE CCCCCCCCCCCCCCC	56.86	22817900
93	Ubiquitination	PPATSSEAEQPKGEP CCCCCCCCCCCCCCC	23.75	21890473
93 (in isoform 2)	Ubiquitination	-	23.75	21890473
97	Sumoylation	SSEAEQPKGEPENEE CCCCCCCCCCCCCHH	75.50	28112733
110	Phosphorylation	EEKEENKSSEETKKD HHHHHCCCHHHHHHH	55.34	26657352
111	Phosphorylation	EKEENKSSEETKKDE HHHHCCCHHHHHHHH	40.85	29255136
111	Ubiquitination	EKEENKSSEETKKDE HHHHCCCHHHHHHHH	40.85	24816145
114	Phosphorylation	ENKSSEETKKDEKDQ HCCCHHHHHHHHHHH	39.07	23927012
121 (in isoform 5)	Phosphorylation	-	68.42	28634120
127	Ubiquitination	DQSKEKEKKVKKTIP HHHHHHHHHHHHHHC	74.14	22817900
128	Ubiquitination	QSKEKEKKVKKTIPS HHHHHHHHHHHHHCH	61.45	22817900
130	Ubiquitination	KEKEKKVKKTIPSWA HHHHHHHHHHHCHHH	53.75	22817900
131	Ubiquitination	EKEKKVKKTIPSWAT HHHHHHHHHHCHHHH	55.46	21890473
131 (in isoform 1)	Ubiquitination	-	55.46	21890473
132	Phosphorylation	KEKKVKKTIPSWATL HHHHHHHHHCHHHHC	32.19	19060867
132	Ubiquitination	KEKKVKKTIPSWATL HHHHHHHHHCHHHHC	32.19	32015554
135	Phosphorylation	KVKKTIPSWATLSAS HHHHHHCHHHHCCHH	26.03	22199227
138	Phosphorylation	KTIPSWATLSASQLA HHHCHHHHCCHHHHH	18.26	26657352
139 (in isoform 3)	Ubiquitination	-	2.88	21890473
140	Phosphorylation	IPSWATLSASQLARA HCHHHHCCHHHHHHH	22.86	25159151
142	Phosphorylation	SWATLSASQLARAQK HHHHCCHHHHHHHHH	23.50	17525332
146	Methylation	LSASQLARAQKQTPM CCHHHHHHHHHHCCC	46.25	115386917
149	Ubiquitination	SQLARAQKQTPMASS HHHHHHHHHCCCCCC	55.97	24816145
151	Phosphorylation	LARAQKQTPMASSPR HHHHHHHCCCCCCCC	23.28	23927012
155	Phosphorylation	QKQTPMASSPRPKMD HHHCCCCCCCCHHHH	34.32	30266825
156	Phosphorylation	KQTPMASSPRPKMDA HHCCCCCCCCHHHHH	18.52	29255136
160	Acetylation	MASSPRPKMDAILTE CCCCCCHHHHHHHHH	51.17	25953088
160	Ubiquitination	MASSPRPKMDAILTE CCCCCCHHHHHHHHH	51.17	29967540
166	Phosphorylation	PKMDAILTEAIKACF HHHHHHHHHHHHHHH	19.77	26074081
170	Ubiquitination	AILTEAIKACFQKSG HHHHHHHHHHHHHCC	46.26	32015554
175	Acetylation	AIKACFQKSGASVVA HHHHHHHHCCCEEEE	30.52	26051181
175	Ubiquitination	AIKACFQKSGASVVA HHHHHHHHCCCEEEE	30.52	29967540
176	Phosphorylation	IKACFQKSGASVVAI HHHHHHHCCCEEEEE	28.89	19691289
184	Ubiquitination	GASVVAIRKYIIHKY CCEEEEEEHHHHHHC	18.91	33845483
190	Acetylation	IRKYIIHKYPSLELE EEHHHHHHCCCHHHH	48.74	25825284
190	Malonylation	IRKYIIHKYPSLELE EEHHHHHHCCCHHHH	48.74	26320211
190	Ubiquitination	IRKYIIHKYPSLELE EEHHHHHHCCCHHHH	48.74	19608861
193	Phosphorylation	YIIHKYPSLELERRG HHHHHCCCHHHHHHH	31.24	25599653
204	Acetylation	ERRGYLLKQALKREL HHHHHHHHHHHHHHH	30.81	27178108
204	Ubiquitination	ERRGYLLKQALKREL HHHHHHHHHHHHHHH	30.81	29967540
220	Ubiquitination	RGVIKQVKGKGASGS HCCCHHHCCCCCCCC	53.03	24816145
222	Ubiquitination	VIKQVKGKGASGSFV CCHHHCCCCCCCCEE	45.65	33845483
225	Phosphorylation	QVKGKGASGSFVVVQ HHCCCCCCCCEEEEE	43.57	20860994
233	Ubiquitination	GSFVVVQKSRKTPQK CCEEEEECCCCCCCC	40.39	29967540
236	Ubiquitination	VVVQKSRKTPQKSRN EEEECCCCCCCCCCC	72.19	24816145
240	Acetylation	KSRKTPQKSRNRKNR CCCCCCCCCCCCCCC	53.22	12432513
245	Acetylation	PQKSRNRKNRSSAVD CCCCCCCCCCCCCCC	61.33	12432527
245	Ubiquitination	PQKSRNRKNRSSAVD CCCCCCCCCCCCCCC	61.33	33845483
248	Phosphorylation	SRNRKNRSSAVDPEP CCCCCCCCCCCCCCC	31.85	23401153
249	Phosphorylation	RNRKNRSSAVDPEPQ CCCCCCCCCCCCCCC	29.13	29255136
253	Ubiquitination	NRSSAVDPEPQVKLE CCCCCCCCCCCCCHH	48.87	21890473
253 (in isoform 2)	Ubiquitination	-	48.87	21890473
258	Sumoylation	VDPEPQVKLEDVLPL CCCCCCCCHHHHHHH	40.69	28112733
258	Ubiquitination	VDPEPQVKLEDVLPL CCCCCCCCHHHHHHH	40.69	24816145
274	2-Hydroxyisobutyrylation	FTRLCEPKEASYSLI HHHHCCCHHHHHHHH	43.55	-
274	Acetylation	FTRLCEPKEASYSLI HHHHCCCHHHHHHHH	43.55	26051181
274	Ubiquitination	FTRLCEPKEASYSLI HHHHCCCHHHHHHHH	43.55	24816145
277	Phosphorylation	LCEPKEASYSLIRKY HCCCHHHHHHHHHHH	19.15	28152594
278	Phosphorylation	CEPKEASYSLIRKYV CCCHHHHHHHHHHHH	17.97	28152594
279	Phosphorylation	EPKEASYSLIRKYVS CCHHHHHHHHHHHHH	18.15	28152594
282	Ubiquitination	EASYSLIRKYVSQYY HHHHHHHHHHHHHHC	29.55	23000965
283	2-Hydroxyisobutyrylation	ASYSLIRKYVSQYYP HHHHHHHHHHHHHCH	42.90	-
283	Acetylation	ASYSLIRKYVSQYYP HHHHHHHHHHHHHCH	42.90	26051181
283	Ubiquitination	ASYSLIRKYVSQYYP HHHHHHHHHHHHHCH	42.90	33845483
284	Phosphorylation	SYSLIRKYVSQYYPK HHHHHHHHHHHHCHH	8.76	28152594
286	Phosphorylation	SLIRKYVSQYYPKLR HHHHHHHHHHCHHHC	14.91	28152594
288	Phosphorylation	IRKYVSQYYPKLRVD HHHHHHHHCHHHCCC	17.77	28152594
289	Phosphorylation	RKYVSQYYPKLRVDI HHHHHHHCHHHCCCC	6.05	28152594
291	Acetylation	YVSQYYPKLRVDIRP HHHHHCHHHCCCCHH	32.57	26051181
291	Malonylation	YVSQYYPKLRVDIRP HHHHHCHHHCCCCHH	32.57	32601280
291	Ubiquitination	YVSQYYPKLRVDIRP HHHHHCHHHCCCCHH	32.57	22817900
291 (in isoform 1)	Ubiquitination	-	32.57	21890473
302	Acetylation	DIRPQLLKNALQRAV CCHHHHHHHHHHHHH	49.09	25953088
302	Ubiquitination	DIRPQLLKNALQRAV CCHHHHHHHHHHHHH	49.09	29967540
320	Ubiquitination	QLEQITGKGASGTFQ CCEECCCCCCCCCEE	42.53	23000965
323	Phosphorylation	QITGKGASGTFQLKK ECCCCCCCCCEEECC	47.21	28674419
327	Ubiquitination	KGASGTFQLKKSGEK CCCCCCEEECCCCCC	52.81	23000965
328	Ubiquitination	GASGTFQLKKSGEKP CCCCCEEECCCCCCC	7.06	23000965
329	Ubiquitination	ASGTFQLKKSGEKPL CCCCEEECCCCCCCC	33.82	29967540
358	Phosphorylation	AAMNEPKTCSTTALK HHHCCCCCCCHHHHH	23.54	24043423
360	Phosphorylation	MNEPKTCSTTALKKY HCCCCCCCHHHHHHH	33.74	24043423
361	Phosphorylation	NEPKTCSTTALKKYV CCCCCCCHHHHHHHH	20.45	24043423
362	Phosphorylation	EPKTCSTTALKKYVL CCCCCCHHHHHHHHH	17.44	24043423
365	2-Hydroxyisobutyrylation	TCSTTALKKYVLENH CCCHHHHHHHHHHCC	39.33	-
365	Acetylation	TCSTTALKKYVLENH CCCHHHHHHHHHHCC	39.33	25953088
365	Ubiquitination	TCSTTALKKYVLENH CCCHHHHHHHHHHCC	39.33	23000965
366	Ubiquitination	CSTTALKKYVLENHP CCHHHHHHHHHHCCC	41.25	23000965
367	Phosphorylation	STTALKKYVLENHPG CHHHHHHHHHHCCCC	14.53	26356563
375	Phosphorylation	VLENHPGTNSNYQMH HHHCCCCCCCHHHHH	39.67	28152594
377	Phosphorylation	ENHPGTNSNYQMHLL HCCCCCCCHHHHHHH	36.43	28152594
379	Phosphorylation	HPGTNSNYQMHLLKK CCCCCCHHHHHHHHH	13.66	27155012
385	Acetylation	NYQMHLLKKTLQKCE HHHHHHHHHHHHHHH	50.50	26051181
385	Ubiquitination	NYQMHLLKKTLQKCE HHHHHHHHHHHHHHH	50.50	29967540
393	Acetylation	KTLQKCEKNGWMEQI HHHHHHHHCCHHHHH	70.95	26051181
393	Ubiquitination	KTLQKCEKNGWMEQI HHHHHHHHCCHHHHH	70.95	29967540
403	Ubiquitination	WMEQISGKGFSGTFQ HHHHHCCCCCCEEEE	50.41	-
408	Phosphorylation	SGKGFSGTFQLCFPY CCCCCCEEEEEECCC	13.65	33259812
418	Phosphorylation	LCFPYYPSPGVLFPK EECCCCCCCCCCCCC	20.40	-
426	Ubiquitination	PGVLFPKKEPDDSRD CCCCCCCCCCCCCCC	74.78	24816145
430	Ubiquitination	FPKKEPDDSRDEDED CCCCCCCCCCCCCCC	57.18	33845483
431	Phosphorylation	PKKEPDDSRDEDEDE CCCCCCCCCCCCCCC	49.35	30175587
441	Phosphorylation	EDEDEDESSEEDSED CCCCCCCCCCCCCCC	56.20	28355574
442	Phosphorylation	DEDEDESSEEDSEDE CCCCCCCCCCCCCCC	42.85	28355574
444	Ubiquitination	DEDESSEEDSEDEEP CCCCCCCCCCCCCCC	69.64	24816145
446	Phosphorylation	DESSEEDSEDEEPPP CCCCCCCCCCCCCCC	50.67	28355574
461	Phosphorylation	KRRLQKKTPAKSPGK CCCCCCCCCCCCCCC	35.20	30576142
464	Ubiquitination	LQKKTPAKSPGKAAS CCCCCCCCCCCCCHH	59.39	24816145
465	Phosphorylation	QKKTPAKSPGKAASV CCCCCCCCCCCCHHH	40.78	25849741
468	Ubiquitination	TPAKSPGKAASVKQR CCCCCCCCCHHHHHC	44.13	33845483
480	Ubiquitination	KQRGSKPAPKVSAAQ HHCCCCCCCCCCHHH	21.93	24816145
482	Ubiquitination	RGSKPAPKVSAAQRG CCCCCCCCCCHHHCC	51.43	24816145
508	Ubiquitination	KAKTPAKKTRPSSTV CCCCCCCCCCCCCEE	52.45	24816145
509	Phosphorylation	AKTPAKKTRPSSTVI CCCCCCCCCCCCEEE	47.29	29396449
512	Phosphorylation	PAKKTRPSSTVIKKP CCCCCCCCCEEEECC	35.04	28985074
513	Phosphorylation	AKKTRPSSTVIKKPS CCCCCCCCEEEECCC	29.40	29970186
514	Phosphorylation	KKTRPSSTVIKKPSG CCCCCCCEEEECCCC	30.50	29396449
518	Ubiquitination	PSSTVIKKPSGGSSK CCCEEEECCCCCCCC	33.04	24816145
520	Phosphorylation	STVIKKPSGGSSKKP CEEEECCCCCCCCCC	65.74	24732914
523	Phosphorylation	IKKPSGGSSKKPATS EECCCCCCCCCCCCC	42.37	24732914
524	Phosphorylation	KKPSGGSSKKPATSA ECCCCCCCCCCCCCC	48.23	24732914
529	Phosphorylation	GSSKKPATSARKEVK CCCCCCCCCCCCCCC	31.29	22817900
530	Phosphorylation	SSKKPATSARKEVKL CCCCCCCCCCCCCCC	28.34	22817900
533	Acetylation	KPATSARKEVKLPGK CCCCCCCCCCCCCCC	67.58	26051181
536	Acetylation	TSARKEVKLPGKGKS CCCCCCCCCCCCCCC	50.48	25953088
544	Phosphorylation	LPGKGKSTMKKSFRV CCCCCCCCCCHHHCC	36.17	-
546	Ubiquitination	GKGKSTMKKSFRVKK CCCCCCCCHHHCCCC	45.41	24816145
548	Phosphorylation	GKSTMKKSFRVKK-- CCCCCCHHHCCCC--	16.87	20068230

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 HP1B3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of HP1B3_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 HP1B3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
LMNB1_HUMAN	LMNB1	physical	22939629
PCDA2_HUMAN	PCDHA2	physical	22939629
NOP16_HUMAN	NOP16	physical	22939629
LAP2A_HUMAN	TMPO	physical	22939629
LAP2B_HUMAN	TMPO	physical	22939629
LAMP2_HUMAN	LAMP2	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
SON_HUMAN	SON	physical	22939629
ZN326_HUMAN	ZNF326	physical	22939629
K2C3_HUMAN	KRT3	physical	22939629
RL1D1_HUMAN	RSL1D1	physical	22939629
RRP7A_HUMAN	RRP7A	physical	22939629
UT14A_HUMAN	UTP14A	physical	22939629
SURF4_HUMAN	SURF4	physical	22939629
RL5_HUMAN	RPL5	physical	22939629
NFIA_HUMAN	NFIA	physical	22939629
NXF1_HUMAN	NXF1	physical	22939629
SPB1_HUMAN	FTSJ3	physical	22939629
TPBG_HUMAN	TPBG	physical	22939629
TRA2A_HUMAN	TRA2A	physical	22939629
MIC60_HUMAN	IMMT	physical	22939629
NOP2_HUMAN	NOP2	physical	22939629
RS14_HUMAN	RPS14	physical	22939629
SRSF7_HUMAN	SRSF7	physical	22939629
VTNC_HUMAN	VTN	physical	22939629
ZCH18_HUMAN	ZC3H18	physical	22939629
RBM14_HUMAN	RBM14	physical	22939629
LN28A_HUMAN	LIN28A	physical	24778252
TRBP2_HUMAN	TARBP2	physical	24778252
IPO7_HUMAN	IPO7	physical	28514442
DDI2_HUMAN	DDI2	physical	28514442
NUSAP_HUMAN	NUSAP1	physical	28514442
RL30_HUMAN	RPL30	physical	28514442
IPO8_HUMAN	IPO8	physical	28514442
IMB1_HUMAN	KPNB1	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 HP1B3_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]
"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-190, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-248 AND SER-249, ANDMASS SPECTROMETRY.	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-142, AND MASSSPECTROMETRY.	17525332 [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 SER-441; SER-442 ANDSER-446, AND MASS SPECTROMETRY.	17287340 [Abstract]
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction."; Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.; Mol. Cell. Proteomics 6:1952-1967(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-132 AND SER-142, ANDMASS SPECTROMETRY.	17693683 [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 SER-6 AND SER-156, AND MASSSPECTROMETRY.	17081983 [Abstract]