dbPTM

NOP58_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NOP58_HUMAN
UniProt AC	Q9Y2X3
Protein Name	Nucleolar protein 58
Gene Name	NOP58
Organism	Homo sapiens (Human).
Sequence Length	529
Subcellular Localization	Nucleus, nucleolus. Nucleus, nucleoplasm .
Protein Description	Required for 60S ribosomal subunit biogenesis (By similarity). Core component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles. Required for the biogenesis of box C/D snoRNAs such as U3, U8 and U14 snoRNAs..
Protein Sequence	MLVLFETSVGYAIFKVLNEKKLQEVDSLWKEFETPEKANKIVKLKHFEKFQDTAEALAAFTALMEGKINKQLKKVLKKIVKEAHEPLAVADAKLGGVIKEKLNLSCIHSPVVNELMRGIRSQMDGLIPGVEPREMAAMCLGLAHSLSRYRLKFSADKVDTMIVQAISLLDDLDKELNNYIMRCREWYGWHFPELGKIISDNLTYCKCLQKVGDRKNYASAKLSELLPEEVEAEVKAAAEISMGTEVSEEDICNILHLCTQVIEISEYRTQLYEYLQNRMMAIAPNVTVMVGELVGARLIAHAGSLLNLAKHAASTVQILGAEKALFRALKSRRDTPKYGLIYHASLVGQTSPKHKGKISRMLAAKTVLAIRYDAFGEDSSSAMGVENRAKLEARLRTLEDRGIRKISGTGKALAKTEKYEHKSEVKTYDPSGDSTLPTCSKKRKIEQVDKEDEITEKKAKKAKIKVKVEEEEEEKVAEEEETSVKKKKKRGKKKHIKEEPLSEEEPCTSTAIASPEKKKKKKKKRENED

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Phosphorylation	LFETSVGYAIFKVLN EEECHHHHHHHHHHC	8.38	-
21	Ubiquitination	FKVLNEKKLQEVDSL HHHHCHHHHHHHHHH	49.58	29967540
27	Phosphorylation	KKLQEVDSLWKEFET HHHHHHHHHHHHCCC	41.11	23186163
30	Acetylation	QEVDSLWKEFETPEK HHHHHHHHHCCCHHH	58.79	25953088
30	Ubiquitination	QEVDSLWKEFETPEK HHHHHHHHHCCCHHH	58.79	29967540
34	Phosphorylation	SLWKEFETPEKANKI HHHHHCCCHHHHHHH	41.91	27794612
37	2-Hydroxyisobutyrylation	KEFETPEKANKIVKL HHCCCHHHHHHHEEC	59.47	-
37	Acetylation	KEFETPEKANKIVKL HHCCCHHHHHHHEEC	59.47	25953088
37	Ubiquitination	KEFETPEKANKIVKL HHCCCHHHHHHHEEC	59.47	29967540
49	Acetylation	VKLKHFEKFQDTAEA EECCCHHHHHHHHHH	47.59	19829213
49	Ubiquitination	VKLKHFEKFQDTAEA EECCCHHHHHHHHHH	47.59	29967540
64	Sulfoxidation	LAAFTALMEGKINKQ HHHHHHHHHCCHHHH	6.22	21406390
67	Acetylation	FTALMEGKINKQLKK HHHHHHCCHHHHHHH	29.78	27452117
67	Ubiquitination	FTALMEGKINKQLKK HHHHHHCCHHHHHHH	29.78	23503661
70	Ubiquitination	LMEGKINKQLKKVLK HHHCCHHHHHHHHHH	61.55	23503661
73	Ubiquitination	GKINKQLKKVLKKIV CCHHHHHHHHHHHHH	38.04	23503661
77	Ubiquitination	KQLKKVLKKIVKEAH HHHHHHHHHHHHHHC	43.36	22817900
78	Ubiquitination	QLKKVLKKIVKEAHE HHHHHHHHHHHHHCC	48.87	22817900
81	Acetylation	KVLKKIVKEAHEPLA HHHHHHHHHHCCCHH	53.29	26051181
81	Malonylation	KVLKKIVKEAHEPLA HHHHHHHHHHCCCHH	53.29	26320211
81	Ubiquitination	KVLKKIVKEAHEPLA HHHHHHHHHHCCCHH	53.29	21906983
93	2-Hydroxyisobutyrylation	PLAVADAKLGGVIKE CHHHCCCCCCCHHHH	48.49	-
93	Acetylation	PLAVADAKLGGVIKE CHHHCCCCCCCHHHH	48.49	25953088
93	Malonylation	PLAVADAKLGGVIKE CHHHCCCCCCCHHHH	48.49	26320211
93	Ubiquitination	PLAVADAKLGGVIKE CHHHCCCCCCCHHHH	48.49	22817900
99	Acetylation	AKLGGVIKEKLNLSC CCCCCHHHHHCCCHH	46.52	26051181
99	Ubiquitination	AKLGGVIKEKLNLSC CCCCCHHHHHCCCHH	46.52	27667366
101	2-Hydroxyisobutyrylation	LGGVIKEKLNLSCIH CCCHHHHHCCCHHCC	37.36	-
101	Acetylation	LGGVIKEKLNLSCIH CCCHHHHHCCCHHCC	37.36	25953088
101	Ubiquitination	LGGVIKEKLNLSCIH CCCHHHHHCCCHHCC	37.36	23503661
105	Phosphorylation	IKEKLNLSCIHSPVV HHHHCCCHHCCHHHH	15.22	21712546
109	Phosphorylation	LNLSCIHSPVVNELM CCCHHCCHHHHHHHH	10.24	25159151
121	Phosphorylation	ELMRGIRSQMDGLIP HHHHHHHHHHCCCCC	28.12	21712546
123	Sulfoxidation	MRGIRSQMDGLIPGV HHHHHHHHCCCCCCC	4.68	28183972
139	Glutathionylation	PREMAAMCLGLAHSL HHHHHHHHHHHHHHH	2.03	22555962
145	Phosphorylation	MCLGLAHSLSRYRLK HHHHHHHHHHHHCCC	23.56	20860994
147	Phosphorylation	LGLAHSLSRYRLKFS HHHHHHHHHHCCCCC	30.22	20860994
152	Acetylation	SLSRYRLKFSADKVD HHHHHCCCCCHHHHH	28.42	19810459
152	Ubiquitination	SLSRYRLKFSADKVD HHHHHCCCCCHHHHH	28.42	33845483
157	Sumoylation	RLKFSADKVDTMIVQ CCCCCHHHHHHHHHH	41.55	28112733
179	Phosphorylation	LDKELNNYIMRCREW HCHHHHHHHHHHHHH	8.60	-
205	S-palmitoylation	ISDNLTYCKCLQKVG HHCCCHHHHHHHHHC	1.80	26865113
206	Acetylation	SDNLTYCKCLQKVGD HCCCHHHHHHHHHCC	27.80	26051181
206	Ubiquitination	SDNLTYCKCLQKVGD HCCCHHHHHHHHHCC	27.80	23000965
210	Acetylation	TYCKCLQKVGDRKNY HHHHHHHHHCCCCCH	34.93	25953088
210	Ubiquitination	TYCKCLQKVGDRKNY HHHHHHHHHCCCCCH	34.93	23000965
215	Acetylation	LQKVGDRKNYASAKL HHHHCCCCCHHHHHH	60.08	25953088
215	Ubiquitination	LQKVGDRKNYASAKL HHHHCCCCCHHHHHH	60.08	23503661
221	Acetylation	RKNYASAKLSELLPE CCCHHHHHHHHHCHH	50.48	25953088
221	Ubiquitination	RKNYASAKLSELLPE CCCHHHHHHHHHCHH	50.48	21906983
269	Phosphorylation	IEISEYRTQLYEYLQ HHHHHHHHHHHHHHH	23.25	28152594
272	Phosphorylation	SEYRTQLYEYLQNRM HHHHHHHHHHHHHHH	7.85	27273156
274	Phosphorylation	YRTQLYEYLQNRMMA HHHHHHHHHHHHHHH	10.46	28152594
278	Methylation	LYEYLQNRMMAIAPN HHHHHHHHHHHHCCC	11.86	115485417
304	Phosphorylation	RLIAHAGSLLNLAKH HHHHHHHHHHHHHHH	30.39	28355574
310	Acetylation	GSLLNLAKHAASTVQ HHHHHHHHHHHHHHH	36.62	26051181
310	Ubiquitination	GSLLNLAKHAASTVQ HHHHHHHHHHHHHHH	36.62	21963094
323	2-Hydroxyisobutyrylation	VQILGAEKALFRALK HHHHCHHHHHHHHHH	50.27	-
323	Acetylation	VQILGAEKALFRALK HHHHCHHHHHHHHHH	50.27	27452117
323	Ubiquitination	VQILGAEKALFRALK HHHHCHHHHHHHHHH	50.27	23000965
337	Acetylation	KSRRDTPKYGLIYHA HCCCCCCCCEEEEEH	54.78	26051181
337	Ubiquitination	KSRRDTPKYGLIYHA HCCCCCCCCEEEEEH	54.78	21906983
338	Phosphorylation	SRRDTPKYGLIYHAS CCCCCCCCEEEEEHH	20.54	23403867
342	Phosphorylation	TPKYGLIYHASLVGQ CCCCEEEEEHHHCCC	9.07	21712546
345	Phosphorylation	YGLIYHASLVGQTSP CEEEEEHHHCCCCCC	15.41	21712546
350	Phosphorylation	HASLVGQTSPKHKGK EHHHCCCCCCCCCCH	40.86	22167270
351	Phosphorylation	ASLVGQTSPKHKGKI HHHCCCCCCCCCCHH	24.86	22167270
353	Acetylation	LVGQTSPKHKGKISR HCCCCCCCCCCHHHH	58.68	26051181
353	Sumoylation	LVGQTSPKHKGKISR HCCCCCCCCCCHHHH	58.68	28112733
357	Acetylation	TSPKHKGKISRMLAA CCCCCCCHHHHHHHH	42.16	7299123
365	2-Hydroxyisobutyrylation	ISRMLAAKTVLAIRY HHHHHHHHHHHHHEE	33.29	-
365	Acetylation	ISRMLAAKTVLAIRY HHHHHHHHHHHHHEE	33.29	25953088
365	Ubiquitination	ISRMLAAKTVLAIRY HHHHHHHHHHHHHEE	33.29	33845483
366	Phosphorylation	SRMLAAKTVLAIRYD HHHHHHHHHHHHEEC	18.94	28851738
372	Phosphorylation	KTVLAIRYDAFGEDS HHHHHHEECCCCCCC	12.90	28851738
379	Phosphorylation	YDAFGEDSSSAMGVE ECCCCCCCCCCCCCC	23.14	25159151
380	Phosphorylation	DAFGEDSSSAMGVEN CCCCCCCCCCCCCCC	34.14	19690332
381	Phosphorylation	AFGEDSSSAMGVENR CCCCCCCCCCCCCCH	26.65	27251275
383	Sulfoxidation	GEDSSSAMGVENRAK CCCCCCCCCCCCHHH	7.16	21406390
397	O-linked_Glycosylation	KLEARLRTLEDRGIR HHHHHHHHHHHHCCE	38.81	23301498
397	Phosphorylation	KLEARLRTLEDRGIR HHHHHHHHHHHHCCE	38.81	23312004
401	Methylation	RLRTLEDRGIRKISG HHHHHHHHCCEECCC	32.82	115485409
407	Phosphorylation	DRGIRKISGTGKALA HHCCEECCCCCHHHH	33.08	23882029
409	Phosphorylation	GIRKISGTGKALAKT CCEECCCCCHHHHCH	28.81	23882029
411	2-Hydroxyisobutyrylation	RKISGTGKALAKTEK EECCCCCHHHHCHHC	39.81	-
411	Acetylation	RKISGTGKALAKTEK EECCCCCHHHHCHHC	39.81	25953088
411	Sumoylation	RKISGTGKALAKTEK EECCCCCHHHHCHHC	39.81	28112733
411	Ubiquitination	RKISGTGKALAKTEK EECCCCCHHHHCHHC	39.81	33845483
415	Sumoylation	GTGKALAKTEKYEHK CCCHHHHCHHCCCCC	59.05	-
415	Sumoylation	GTGKALAKTEKYEHK CCCHHHHCHHCCCCC	59.05	25218447
419	Phosphorylation	ALAKTEKYEHKSEVK HHHCHHCCCCCCCCC	19.62	-
422	Sumoylation	KTEKYEHKSEVKTYD CHHCCCCCCCCCEEC	36.05	28112733
422	Ubiquitination	KTEKYEHKSEVKTYD CHHCCCCCCCCCEEC	36.05	22817900
426	Acetylation	YEHKSEVKTYDPSGD CCCCCCCCEECCCCC	37.00	26051181
426	Sumoylation	YEHKSEVKTYDPSGD CCCCCCCCEECCCCC	37.00	28112733
426	Ubiquitination	YEHKSEVKTYDPSGD CCCCCCCCEECCCCC	37.00	21963094
427	Phosphorylation	EHKSEVKTYDPSGDS CCCCCCCEECCCCCC	38.03	28152594
428	Phosphorylation	HKSEVKTYDPSGDST CCCCCCEECCCCCCC	21.82	28152594
431	Phosphorylation	EVKTYDPSGDSTLPT CCCEECCCCCCCCCC	52.95	25262027
434	Phosphorylation	TYDPSGDSTLPTCSK EECCCCCCCCCCCCC	35.06	25627689
435	Phosphorylation	YDPSGDSTLPTCSKK ECCCCCCCCCCCCCC	41.31	25262027
438	Phosphorylation	SGDSTLPTCSKKRKI CCCCCCCCCCCCCCH	32.31	25262027
439	S-nitrosylation	GDSTLPTCSKKRKIE CCCCCCCCCCCCCHH	5.47	2212679
440	Phosphorylation	DSTLPTCSKKRKIEQ CCCCCCCCCCCCHHH	43.63	21815630
441	2-Hydroxyisobutyrylation	STLPTCSKKRKIEQV CCCCCCCCCCCHHHC	59.76	-
441	Acetylation	STLPTCSKKRKIEQV CCCCCCCCCCCHHHC	59.76	25953088
441	Malonylation	STLPTCSKKRKIEQV CCCCCCCCCCCHHHC	59.76	26320211
441	Sumoylation	STLPTCSKKRKIEQV CCCCCCCCCCCHHHC	59.76	28112733
441	Ubiquitination	STLPTCSKKRKIEQV CCCCCCCCCCCHHHC	59.76	32015554
442	Ubiquitination	TLPTCSKKRKIEQVD CCCCCCCCCCHHHCC	42.50	-
444	Sumoylation	PTCSKKRKIEQVDKE CCCCCCCCHHHCCCC	60.52	-
444	Acetylation	PTCSKKRKIEQVDKE CCCCCCCCHHHCCCC	60.52	26051181
444	Sumoylation	PTCSKKRKIEQVDKE CCCCCCCCHHHCCCC	60.52	28112733
450	Acetylation	RKIEQVDKEDEITEK CCHHHCCCCCHHCHH	69.11	25953088
457	Acetylation	KEDEITEKKAKKAKI CCCHHCHHHHHHCCC	49.75	25953088
460	Acetylation	EITEKKAKKAKIKVK HHCHHHHHHCCCEEE	63.24	19608861
463	Acetylation	EKKAKKAKIKVKVEE HHHHHHCCCEEEECH	52.52	19608861
463	Sumoylation	EKKAKKAKIKVKVEE HHHHHHCCCEEEECH	52.52	19608861
465	Sumoylation	KAKKAKIKVKVEEEE HHHHCCCEEEECHHH	34.98	28112733
467	Sumoylation	KKAKIKVKVEEEEEE HHCCCEEEECHHHHH	38.64	-
467	Acetylation	KKAKIKVKVEEEEEE HHCCCEEEECHHHHH	38.64	26051181
467	Sumoylation	KKAKIKVKVEEEEEE HHCCCEEEECHHHHH	38.64	25114211
475	Acetylation	VEEEEEEKVAEEEET ECHHHHHHHHHHHHH	50.45	26051181
482	Phosphorylation	KVAEEEETSVKKKKK HHHHHHHHHHHHHHH	41.94	29255136
483	Phosphorylation	VAEEEETSVKKKKKR HHHHHHHHHHHHHHH	34.91	29255136
485	Acetylation	EEEETSVKKKKKRGK HHHHHHHHHHHHHCC	59.65	26051181
485	Sumoylation	EEEETSVKKKKKRGK HHHHHHHHHHHHHCC	59.65	28112733
485	Ubiquitination	EEEETSVKKKKKRGK HHHHHHHHHHHHHCC	59.65	33845483
497	Sumoylation	RGKKKHIKEEPLSEE HCCCCCCCCCCCCCC	56.60	-
497	Sumoylation	RGKKKHIKEEPLSEE HCCCCCCCCCCCCCC	56.60	28112733
502	Phosphorylation	HIKEEPLSEEEPCTS CCCCCCCCCCCCCCC	54.39	19664994
507	Carbamidation	PLSEEEPCTSTAIAS CCCCCCCCCCHHCCC	5.48	17322306
508	Phosphorylation	LSEEEPCTSTAIASP CCCCCCCCCHHCCCH	39.57	29255136
509	Phosphorylation	SEEEPCTSTAIASPE CCCCCCCCHHCCCHH	23.66	29255136
510	Phosphorylation	EEEPCTSTAIASPEK CCCCCCCHHCCCHHH	12.16	29255136
514	Phosphorylation	CTSTAIASPEKKKKK CCCHHCCCHHHHHHH	27.72	29255136

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 NOP58_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NOP58_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 NOP58_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RL4_HUMAN	RPL4	physical	22939629
RS13_HUMAN	RPS13	physical	22939629
RS7_HUMAN	RPS7	physical	22939629
RL6_HUMAN	RPL6	physical	22939629
RL5_HUMAN	RPL5	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RS15A_HUMAN	RPS15A	physical	22939629
RL7_HUMAN	RPL7	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RL19_HUMAN	RPL19	physical	22939629
RS11_HUMAN	RPS11	physical	22939629
RL18A_HUMAN	RPL18A	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
U2AF1_HUMAN	U2AF1	physical	22939629
RL37A_HUMAN	RPL37A	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RL11_HUMAN	RPL11	physical	22939629
RL1D1_HUMAN	RSL1D1	physical	22939629
RS14_HUMAN	RPS14	physical	22939629
RL30_HUMAN	RPL30	physical	22939629
SPB1_HUMAN	FTSJ3	physical	22939629
UT14A_HUMAN	UTP14A	physical	22939629
RRS1_HUMAN	RRS1	physical	22939629
PRPF3_HUMAN	PRPF3	physical	22939629
SNUT1_HUMAN	SART1	physical	22939629
DCA13_HUMAN	DCAF13	physical	26344197
DDX24_HUMAN	DDX24	physical	26344197
DDX27_HUMAN	DDX27	physical	26344197
DDX47_HUMAN	DDX47	physical	26344197
DDX56_HUMAN	DDX56	physical	26344197
ESF1_HUMAN	ESF1	physical	26344197
GLYR1_HUMAN	GLYR1	physical	26344197
GNL1_HUMAN	GNL1	physical	26344197
NOG1_HUMAN	GTPBP4	physical	26344197
PUM3_HUMAN	KIAA0020	physical	26344197
IMA5_HUMAN	KPNA1	physical	26344197
IMA7_HUMAN	KPNA6	physical	26344197
KRR1_HUMAN	KRR1	physical	26344197
MPP10_HUMAN	MPHOSPH10	physical	26344197
NAT10_HUMAN	NAT10	physical	26344197
MK67I_HUMAN	NIFK	physical	26344197
NOC3L_HUMAN	NOC3L	physical	26344197
NOL6_HUMAN	NOL6	physical	26344197
NOLC1_HUMAN	NOLC1	physical	26344197
NOP2_HUMAN	NOP2	physical	26344197
RPA49_HUMAN	POLR1E	physical	26344197
RPC6_HUMAN	POLR3F	physical	26344197
RL18A_HUMAN	RPL18A	physical	26344197
RS7_HUMAN	RPS7	physical	26344197
RRP12_HUMAN	RRP12	physical	26344197
TBL3_HUMAN	TBL3	physical	26344197
UTP15_HUMAN	UTP15	physical	26344197
WDR36_HUMAN	WDR36	physical	26344197
NUFP1_HUMAN	NUFIP1	physical	25404746
ZNHI3_HUMAN	ZNHIT3	physical	25404746
RUVB1_HUMAN	RUVBL1	physical	25404746

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 NOP58_HUMAN

Related Literatures of Post-Translational Modification

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-502 AND SER-514, ANDMASS SPECTROMETRY.	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-351; SER-502 ANDSER-514, AND MASS SPECTROMETRY.	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 SER-502 AND SER-514, ANDMASS SPECTROMETRY.	18691976 [Abstract]
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, AND MASSSPECTROMETRY.	19367720 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND MASSSPECTROMETRY.	18220336 [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-482; SER-483; SER-502AND SER-514, AND MASS SPECTROMETRY.	19007248 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, AND MASSSPECTROMETRY.	16565220 [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-502 AND SER-514, ANDMASS SPECTROMETRY.	17081983 [Abstract]
Sumoylation
Reference	PubMed
"A proteomic screen for nucleolar SUMO targets shows SUMOylationmodulates the function of Nop5/Nop58."; Westman B.J., Verheggen C., Hutten S., Lam Y.W., Bertrand E.,Lamond A.I.; Mol. Cell 39:618-631(2010). Cited for: SUMOYLATION AT LYS-467 AND LYS-497.	20797632 [Abstract]