dbPTM

ATN1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ATN1_HUMAN
UniProt AC	P54259
Protein Name	Atrophin-1
Gene Name	ATN1
Organism	Homo sapiens (Human).
Sequence Length	1190
Subcellular Localization	Nucleus. Cytoplasm, perinuclear region. Cell junction. Shuttles between nucleus and cytoplasm. Colocalizes with FAT1 in the perinuclear area, at cell-cell junctions and leading edges of cells (By similarity). Colocalizes with MTG8 in discrete nuclear
Protein Description	Transcriptional corepressor. Recruits NR2E1 to repress transcription. Promotes vascular smooth cell (VSMC) migration and orientation (By similarity). Corepressor of MTG8 transcriptional repression. Has some intrinsic repression activity which is independent of the number of poly-Gln (polyQ) repeats..
Protein Sequence	MKTRQNKDSMSMRSGRKKEAPGPREELRSRGRASPGGVSTSSSDGKAEKSRQTAKKARVEEASTPKVNKQGRSEEISESESEETNAPKKTKTEQELPRPQSPSDLDSLDGRSLNDDGSSDPRDIDQDNRSTSPSIYSPGSVENDSDSSSGLSQGPARPYHPPPLFPPSPQPPDSTPRQPEASFEPHPSVTPTGYHAPMEPPTSRMFQAPPGAPPPHPQLYPGGTGGVLSGPPMGPKGGGAASSVGGPNGGKQHPPPTTPISVSSSGASGAPPTKPPTTPVGGGNLPSAPPPANFPHVTPNLPPPPALRPLNNASASPPGLGAQPLPGHLPSPHAMGQGMGGLPPGPEKGPTLAPSPHSLPPASSSAPAPPMRFPYSSSSSSSAAASSSSSSSSSSASPFPASQALPSYPHSFPPPTSLSVSNQPPKYTQPSLPSQAVWSQGPPPPPPYGRLLANSNAHPGPFPPSTGAQSTAHPPVSTHHHHHQQQQQQQQQQQQQQQQQQQHHGNSGPPPPGAFPHPLEGGSSHHAHPYAMSPSLGSLRPYPPGPAHLPPPHSQVSYSQAGPNGPPVSSSSNSSSSTSQGSYPCSHPSPSQGPQGAPYPFPPVPTVTTSSATLSTVIATVASSPAGYKTASPPGPPPYGKRAPSPGAYKTATPPGYKPGSPPSFRTGTPPGYRGTSPPAGPGTFKPGSPTVGPGPLPPAGPSGLPSLPPPPAAPASGPPLSATQIKQEPAEEYETPESPVPPARSPSPPPKVVDVPSHASQSARFNKHLDRGFNSCARSDLYFVPLEGSKLAKKRADLVEKVRREAEQRAREEKEREREREREKEREREKERELERSVKLAQEGRAPVECPSLGPVPHRPPFEPGSAVATVPPYLGPDTPALRTLSEYARPHVMSPGNRNHPFYVPLGAVDPGLLGYNVPALYSSDPAAREREREARERDLRDRLKPGFEVKPSELEPLHGVPGPGLDPFPRHGGLALQPGPPGLHPFPFHPSLGPLERERLALAAGPALRPDMSYAERLAAERQHAERVAALGNDPLARLQMLNVTPHHHQHSHIHSHLHLHQQDAIHAASASVHPLIDPLASGSHLTRIPYPAGTLPNPLLPHPLHENEVLRHQLFAAPYRDLPASLSAPMSAAHQLQAMHAQSAELQRLALEQQQWLHAHHPLHSVPLPAQEDYYSHLKKESDKPL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MKTRQNKDS ------CCCCCCHHH	64.81	12432405
7	Acetylation	-MKTRQNKDSMSMRS -CCCCCCHHHCCCCC	42.73	12432417
9	Phosphorylation	KTRQNKDSMSMRSGR CCCCCHHHCCCCCCC	17.86	-
11	Phosphorylation	RQNKDSMSMRSGRKK CCCHHHCCCCCCCCC	18.26	-
29	Phosphorylation	GPREELRSRGRASPG CCHHHHHHCCCCCCC	52.27	25627689
34	Phosphorylation	LRSRGRASPGGVSTS HHHCCCCCCCCCCCC	23.79	29255136
39	Phosphorylation	RASPGGVSTSSSDGK CCCCCCCCCCCCCCC	26.33	23927012
40	Phosphorylation	ASPGGVSTSSSDGKA CCCCCCCCCCCCCCH	30.16	25159151
41	Phosphorylation	SPGGVSTSSSDGKAE CCCCCCCCCCCCCHH	21.97	23927012
42	Phosphorylation	PGGVSTSSSDGKAEK CCCCCCCCCCCCHHH	32.32	25159151
43	Phosphorylation	GGVSTSSSDGKAEKS CCCCCCCCCCCHHHH	50.58	23927012
46	Acetylation	STSSSDGKAEKSRQT CCCCCCCCHHHHHHH	59.36	25953088
63	Phosphorylation	KARVEEASTPKVNKQ HHHHHHHCCCCCCCC	48.82	20068231
64	Phosphorylation	ARVEEASTPKVNKQG HHHHHHCCCCCCCCC	33.89	21815630
73	Phosphorylation	KVNKQGRSEEISESE CCCCCCCCHHCCHHH	46.54	22167270
77	Phosphorylation	QGRSEEISESESEET CCCCHHCCHHHCCCC	38.05	29255136
79	Phosphorylation	RSEEISESESEETNA CCHHCCHHHCCCCCC	39.36	29255136
81	Phosphorylation	EEISESESEETNAPK HHCCHHHCCCCCCCC	50.43	29255136
84	Phosphorylation	SESESEETNAPKKTK CHHHCCCCCCCCCCC	32.40	22167270
92	Phosphorylation	NAPKKTKTEQELPRP CCCCCCCCHHHCCCC	48.40	30576142
101	Phosphorylation	QELPRPQSPSDLDSL HHCCCCCCCHHHHCC	29.11	29255136
103	Phosphorylation	LPRPQSPSDLDSLDG CCCCCCCHHHHCCCC	56.93	30266825
107	Phosphorylation	QSPSDLDSLDGRSLN CCCHHHHCCCCCCCC	35.34	23927012
112	Phosphorylation	LDSLDGRSLNDDGSS HHCCCCCCCCCCCCC	36.73	29255136
118	Phosphorylation	RSLNDDGSSDPRDID CCCCCCCCCCHHHCC	38.26	23663014
119	Phosphorylation	SLNDDGSSDPRDIDQ CCCCCCCCCHHHCCC	58.10	29255136
130	Phosphorylation	DIDQDNRSTSPSIYS HCCCCCCCCCCCCCC	39.22	27732954
131	Phosphorylation	IDQDNRSTSPSIYSP CCCCCCCCCCCCCCC	41.23	26657352
132	Phosphorylation	DQDNRSTSPSIYSPG CCCCCCCCCCCCCCC	20.21	26657352
134	Phosphorylation	DNRSTSPSIYSPGSV CCCCCCCCCCCCCCC	33.65	27732954
136	Phosphorylation	RSTSPSIYSPGSVEN CCCCCCCCCCCCCCC	17.10	27732954
137	Phosphorylation	STSPSIYSPGSVEND CCCCCCCCCCCCCCC	22.55	27732954
159	Phosphorylation	SQGPARPYHPPPLFP CCCCCCCCCCCCCCC	22.77	23312004
168	Phosphorylation	PPPLFPPSPQPPDST CCCCCCCCCCCCCCC	36.08	30266825
174	Phosphorylation	PSPQPPDSTPRQPEA CCCCCCCCCCCCCCC	46.19	23663014
175	Phosphorylation	SPQPPDSTPRQPEAS CCCCCCCCCCCCCCC	29.85	23663014
188	Phosphorylation	ASFEPHPSVTPTGYH CCCCCCCCCCCCCCC	35.27	27251275
190	Phosphorylation	FEPHPSVTPTGYHAP CCCCCCCCCCCCCCC	21.33	27251275
192	Phosphorylation	PHPSVTPTGYHAPME CCCCCCCCCCCCCCC	40.79	27251275
261	Phosphorylation	PPPTTPISVSSSGAS CCCCCCCEECCCCCC	19.70	23879269
263	Phosphorylation	PTTPISVSSSGASGA CCCCCEECCCCCCCC	16.40	23879269
273	Phosphorylation	GASGAPPTKPPTTPV CCCCCCCCCCCCCCC	55.94	23879269
351	Phosphorylation	PGPEKGPTLAPSPHS CCCCCCCCCCCCCCC	44.19	27080861
355	Phosphorylation	KGPTLAPSPHSLPPA CCCCCCCCCCCCCCC	29.63	28985074
358	Phosphorylation	TLAPSPHSLPPASSS CCCCCCCCCCCCCCC	46.05	25159151
363	Phosphorylation	PHSLPPASSSAPAPP CCCCCCCCCCCCCCC	30.51	27080861
364	O-linked_Glycosylation	HSLPPASSSAPAPPM CCCCCCCCCCCCCCC	32.40	30059200
364	Phosphorylation	HSLPPASSSAPAPPM CCCCCCCCCCCCCCC	32.40	27080861
365	Phosphorylation	SLPPASSSAPAPPMR CCCCCCCCCCCCCCC	35.46	27080861
388	Phosphorylation	SSAAASSSSSSSSSS CCCCCCCCCCCCCCC	31.57	-
389	Phosphorylation	SAAASSSSSSSSSSA CCCCCCCCCCCCCCC	35.87	-
390	Phosphorylation	AAASSSSSSSSSSAS CCCCCCCCCCCCCCC	35.87	-
391	Phosphorylation	AASSSSSSSSSSASP CCCCCCCCCCCCCCC	35.87	-
427	Phosphorylation	VSNQPPKYTQPSLPS CCCCCCCCCCCCCCC	19.17	24043423
428	Phosphorylation	SNQPPKYTQPSLPSQ CCCCCCCCCCCCCCH	39.88	24043423
431	Phosphorylation	PPKYTQPSLPSQAVW CCCCCCCCCCCHHHH	42.99	24043423
434	Phosphorylation	YTQPSLPSQAVWSQG CCCCCCCCHHHHCCC	35.74	24043423
439	Phosphorylation	LPSQAVWSQGPPPPP CCCHHHHCCCCCCCC	20.75	24043423
448	Phosphorylation	GPPPPPPYGRLLANS CCCCCCCCHHHCCCC	22.20	24043423
538	Phosphorylation	AMSPSLGSLRPYPPG CCCCCCCCCCCCCCC	26.88	24719451
627	Phosphorylation	TVASSPAGYKTASPP HHHCCCCCCCCCCCC	28.05	15302935
630	Phosphorylation	SSPAGYKTASPPGPP CCCCCCCCCCCCCCC	24.71	30266825
632	Phosphorylation	PAGYKTASPPGPPPY CCCCCCCCCCCCCCC	36.54	30266825
639	Phosphorylation	SPPGPPPYGKRAPSP CCCCCCCCCCCCCCC	40.84	23403867
640	Phosphorylation	PPGPPPYGKRAPSPG CCCCCCCCCCCCCCC	20.81	15302935
641	Acetylation	PGPPPYGKRAPSPGA CCCCCCCCCCCCCCC	39.27	19608861
645	Phosphorylation	PYGKRAPSPGAYKTA CCCCCCCCCCCCCCC	34.67	30266825
646	Phosphorylation	YGKRAPSPGAYKTAT CCCCCCCCCCCCCCC	30.30	18669648
648	Phosphorylation	KRAPSPGAYKTATPP CCCCCCCCCCCCCCC	13.16	18669648
649	Phosphorylation	RAPSPGAYKTATPPG CCCCCCCCCCCCCCC	18.13	23403867
651	Phosphorylation	PSPGAYKTATPPGYK CCCCCCCCCCCCCCC	24.08	23927012
653	Phosphorylation	PGAYKTATPPGYKPG CCCCCCCCCCCCCCC	34.94	23927012
656	Phosphorylation	YKTATPPGYKPGSPP CCCCCCCCCCCCCCC	44.28	18669648
657	Phosphorylation	KTATPPGYKPGSPPS CCCCCCCCCCCCCCC	21.56	23927012
661	Phosphorylation	PPGYKPGSPPSFRTG CCCCCCCCCCCCCCC	42.01	23401153
664	Phosphorylation	YKPGSPPSFRTGTPP CCCCCCCCCCCCCCC	30.64	23927012
667	Phosphorylation	GSPPSFRTGTPPGYR CCCCCCCCCCCCCCC	43.31	23403867
669	Phosphorylation	PPSFRTGTPPGYRGT CCCCCCCCCCCCCCC	26.20	25159151
673	Phosphorylation	RTGTPPGYRGTSPPA CCCCCCCCCCCCCCC	16.19	28985074
676	Phosphorylation	TPPGYRGTSPPAGPG CCCCCCCCCCCCCCC	29.12	28290473
677	Phosphorylation	PPGYRGTSPPAGPGT CCCCCCCCCCCCCCC	31.54	25159151
684	Phosphorylation	SPPAGPGTFKPGSPT CCCCCCCCCCCCCCC	31.45	20873877
689	Phosphorylation	PGTFKPGSPTVGPGP CCCCCCCCCCCCCCC	26.40	20873877
691	Phosphorylation	TFKPGSPTVGPGPLP CCCCCCCCCCCCCCC	39.53	20068231
703	Phosphorylation	PLPPAGPSGLPSLPP CCCCCCCCCCCCCCC	52.63	29496963
707	Phosphorylation	AGPSGLPSLPPPPAA CCCCCCCCCCCCCCC	59.56	29496963
717	Phosphorylation	PPPAAPASGPPLSAT CCCCCCCCCCCCCCC	51.26	20068231
722	Phosphorylation	PASGPPLSATQIKQE CCCCCCCCCCCCCCC	34.74	20068231
724	Phosphorylation	SGPPLSATQIKQEPA CCCCCCCCCCCCCCH	27.70	20068231
729	Phosphorylation	SATQIKQEPAEEYET CCCCCCCCCHHHCCC	41.28	18669648
734	Phosphorylation	KQEPAEEYETPESPV CCCCHHHCCCCCCCC	19.33	23927012
736	Phosphorylation	EPAEEYETPESPVPP CCHHHCCCCCCCCCC	31.30	23927012
739	Phosphorylation	EEYETPESPVPPARS HHCCCCCCCCCCCCC	32.19	30278072
741	Phosphorylation	YETPESPVPPARSPS CCCCCCCCCCCCCCC	14.28	18669648
743	Phosphorylation	TPESPVPPARSPSPP CCCCCCCCCCCCCCC	40.31	18669648
746	Phosphorylation	SPVPPARSPSPPPKV CCCCCCCCCCCCCCE	31.66	30278072
748	Phosphorylation	VPPARSPSPPPKVVD CCCCCCCCCCCCEEC	51.81	30278072
758	Phosphorylation	PKVVDVPSHASQSAR CCEECCCCCHHHHHH	31.37	23927012
761	Phosphorylation	VDVPSHASQSARFNK ECCCCCHHHHHHHHH	21.17	23186163
763	Phosphorylation	VPSHASQSARFNKHL CCCCHHHHHHHHHHH	20.93	23186163
780	Phosphorylation	GFNSCARSDLYFVPL CCHHCCCCCEEEEEC	17.28	20068231
783	Phosphorylation	SCARSDLYFVPLEGS HCCCCCEEEEECCCH	13.92	20068231
790	Phosphorylation	YFVPLEGSKLAKKRA EEEECCCHHHHHHHH	18.34	20068231
791	Acetylation	FVPLEGSKLAKKRAD EEECCCHHHHHHHHH	64.42	26051181
887	Phosphorylation	TPALRTLSEYARPHV CHHHHHHHHHCCCCC	28.13	27080861
889	Phosphorylation	ALRTLSEYARPHVMS HHHHHHHHCCCCCCC	12.44	29214152
896	Phosphorylation	YARPHVMSPGNRNHP HCCCCCCCCCCCCCC	28.68	23401153
905	Phosphorylation	GNRNHPFYVPLGAVD CCCCCCCEEECCCCC	12.95	17360941
942	Ubiquitination	REARERDLRDRLKPG HHHHHHHHHHHCCCC	8.43	21890473
947	Ubiquitination	RDLRDRLKPGFEVKP HHHHHHCCCCCCCCH	43.94	2189047
1002	Methylation	LGPLERERLALAAGP CCHHHHHHHHHHCCC	31.33	-
1115	Asymmetric dimethylarginine	LHENEVLRHQLFAAP CCHHHHHHHHHHCCC	22.23	-
1115	Methylation	LHENEVLRHQLFAAP CCHHHHHHHHHHCCC	22.23	-
1183	Sumoylation	EDYYSHLKKESDKPL HHHHHHHHHHCCCCC	49.42	28112733

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
734	S	Phosphorylation	Kinase	MK08	P45983	PhosphoELM
734	S	Phosphorylation	Kinase	MK10	P53779	PhosphoELM
739	S	Phosphorylation	Kinase	JNK1	P45983	PSP
739	S	Phosphorylation	Kinase	MAPK10	P53779	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
739	S	Phosphorylation		12812981
Phosphorylated in vitro by MAPK8/JNK1 on Ser-739.

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 ATN1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KAT7_HUMAN	KAT7	physical	16169070
TLE1_HUMAN	TLE1	physical	16169070
VIME_HUMAN	VIM	physical	16169070
RERE_HUMAN	RERE	physical	10814707
BAIP2_HUMAN	BAIAP2	physical	10332026
CTND2_HUMAN	CTNND2	physical	10332026
DVL1_HUMAN	DVL1	physical	10332026
MAGI2_HUMAN	MAGI2	physical	9647693
ITCH_HUMAN	ITCH	physical	9647693
WWP2_HUMAN	WWP2	physical	9647693
WWP1_HUMAN	WWP1	physical	9647693
MAGI1_HUMAN	MAGI1	physical	9647693
ACT1_DROME	Act5C	physical	16481466
7UP1_DROME	svp	physical	16481466
7UP2_DROME	svp	physical	16481466
NR2E1_HUMAN	NR2E1	physical	16481466
MTG8_HUMAN	RUNX1T1	physical	10973986
BAIP2_HUMAN	BAIAP2	physical	16713569
MTG8_HUMAN	RUNX1T1	physical	16713569
EWS_HUMAN	EWSR1	physical	16713569
GCC1_HUMAN	GCC1	physical	16713569
KR412_HUMAN	KRTAP4-12	physical	16713569
LENG8_HUMAN	LENG8	physical	16713569
MDFI_HUMAN	MDFI	physical	16713569
EFC4B_HUMAN	CRACR2A	physical	16713569
NCK2_HUMAN	NCK2	physical	16713569
RHXF2_HUMAN	RHOXF2	physical	16713569
PLS1_HUMAN	PLSCR1	physical	16713569
PSME3_HUMAN	PSME3	physical	16713569
RBPMS_HUMAN	RBPMS	physical	16713569
TRIP6_HUMAN	TRIP6	physical	16713569
WDR5_HUMAN	WDR5	physical	16713569
WWP2_HUMAN	WWP2	physical	16713569
AGRIN_HUMAN	AGRN	physical	16713569
ATN1_HUMAN	ATN1	physical	16713569
BAG6_HUMAN	BAG6	physical	16713569
CACB1_HUMAN	CACNB1	physical	16713569
MTG8R_HUMAN	CBFA2T2	physical	16713569
CENPJ_HUMAN	CENPJ	physical	16713569
CHRD_HUMAN	CHRD	physical	16713569
CRIP2_HUMAN	CRIP2	physical	16713569
DVL2_HUMAN	DVL2	physical	16713569
FBLN3_HUMAN	EFEMP1	physical	16713569
FBLN4_HUMAN	EFEMP2	physical	16713569
MEGF6_HUMAN	MEGF6	physical	16713569
MEGF8_HUMAN	MEGF8	physical	16713569
FBLN1_HUMAN	FBLN1	physical	16713569
G3P_HUMAN	GAPDH	physical	16713569
GRN_HUMAN	GRN	physical	16713569
PGBM_HUMAN	HSPG2	physical	16713569
JAG2_HUMAN	JAG2	physical	16713569
SSPO_HUMAN	SSPO	physical	16713569
LTBP1_HUMAN	LTBP1	physical	16713569
LTBP4_HUMAN	LTBP4	physical	16713569
MBP_HUMAN	MBP	physical	16713569
MEG11_HUMAN	MEGF11	physical	16713569
NELL1_HUMAN	NELL1	physical	16713569
NELL2_HUMAN	NELL2	physical	16713569
GGYF1_HUMAN	GIGYF1	physical	16713569
PFKAL_HUMAN	PFKL	physical	16713569
ZN363_HUMAN	RCHY1	physical	16713569
SLIT1_HUMAN	SLIT1	physical	16713569
STXB4_HUMAN	STXBP4	physical	16713569
SYVN1_HUMAN	SYVN1	physical	16713569
TEP1_HUMAN	TEP1	physical	16713569
PKCB1_HUMAN	ZMYND8	physical	16713569
RBM10_HUMAN	RBM10	physical	16713569
ALG13_HUMAN	ALG13	physical	16713569
FBLN5_HUMAN	FBLN5	physical	16713569
LRP2_HUMAN	LRP2	physical	16713569
PCSK5_HUMAN	PCSK5	physical	16713569
PSA3_HUMAN	PSMA3	physical	16713569
WWP1_HUMAN	WWP1	physical	16713569
AES_HUMAN	AES	physical	16713569
ARF3_HUMAN	ARF3	physical	16713569
PRC2A_HUMAN	PRRC2A	physical	16713569
NOC2L_HUMAN	NOC2L	physical	16713569
DMPK_HUMAN	DMPK	physical	16713569
ECM1_HUMAN	ECM1	physical	16713569
FBLN2_HUMAN	FBLN2	physical	16713569
MA7D1_HUMAN	MAP7D1	physical	16713569
PRC2B_HUMAN	PRRC2B	physical	16713569
ZSWM8_HUMAN	ZSWIM8	physical	16713569
K1H1_HUMAN	KRT31	physical	16713569
KAT6A_HUMAN	KAT6A	physical	16713569
KAT6B_HUMAN	KAT6B	physical	16713569
RFOX2_HUMAN	RBFOX2	physical	16713569
RERE_HUMAN	RERE	physical	16713569
RNF31_HUMAN	RNF31	physical	16713569
SIAH1_HUMAN	SIAH1	physical	16713569
SIAH2_HUMAN	SIAH2	physical	16713569
SPAG5_HUMAN	SPAG5	physical	16713569
ARIP4_HUMAN	RAD54L2	physical	16713569
UBP54_HUMAN	USP54	physical	16713569
SIAH1_HUMAN	SIAH1	physical	21988832

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
125370	Dentatorubral-pallidoluysian atrophy (DRPLA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ATN1_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-641, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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 SER-101, 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 SER-77; SER-79; SER-101;SER-103; SER-107; THR-651; THR-653; SER-661; TYR-734; SER-746 ANDSER-748, AND MASS SPECTROMETRY.	18669648 [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-77; SER-79; SER-101;SER-103; SER-107; SER-739; SER-746 AND SER-748, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-77; SER-101;SER-107; SER-112; SER-119; SER-632; SER-645; THR-653; SER-661;THR-669; SER-746 AND SER-748, AND MASS SPECTROMETRY.	15302935 [Abstract]
"Dentatorubral-pallidoluysian atrophy protein is phosphorylated by c-Jun NH2-terminal kinase."; Okamura-Oho Y., Miyashita T., Nagao K., Shima S., Ogata Y., Katada T.,Nishina H., Yamada M.; Hum. Mol. Genet. 12:1535-1542(2003). Cited for: PHOSPHORYLATION AT SER-739.	12812981 [Abstract]

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