dbPTM

NUDC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NUDC_HUMAN
UniProt AC	Q9Y266
Protein Name	Nuclear migration protein nudC
Gene Name	NUDC
Organism	Homo sapiens (Human).
Sequence Length	331
Subcellular Localization	Cytoplasm, cytoskeleton. Nucleus. In a filamentous pattern adjacent to the nucleus of migrating cerebellar granule cells. Colocalizes with tubulin and dynein and with the microtubule organizing center. Distributed throughout the cytoplasm of non-migr
Protein Description	Plays a role in neurogenesis and neuronal migration (By similarity). Necessary for correct formation of mitotic spindles and chromosome separation during mitosis. Necessary for cytokinesis and cell proliferation..
Protein Sequence	MGGEQEEERFDGMLLAMAQQHEGGVQELVNTFFSFLRRKTDFFIGGEEGMAEKLITQTFSHHNQLAQKTRREKRARQEAERREKAERAARLAKEAKSETSGPQIKELTDEEAERLQLEIDQKKDAENHEAQLKNGSLDSPGKQDTEEDEEEDEKDKGKLKPNLGNGADLPNYRWTQTLSELDLAVPFCVNFRLKGKDMVVDIQRRHLRVGLKGQPAIIDGELYNEVKVEESSWLIEDGKVVTVHLEKINKMEWWSRLVSSDPEINTKKINPENSKLSDLDSETRSMVEKMMYDQRQKSMGLPTSDEQKKQEILKKFMDQHPEMDFSKAKFN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
19	Ubiquitination	GMLLAMAQQHEGGVQ HHHHHHHHHCCCHHH	31.88	21890473
24	Ubiquitination	MAQQHEGGVQELVNT HHHHCCCHHHHHHHH	18.23	22817900
39	2-Hydroxyisobutyrylation	FFSFLRRKTDFFIGG HHHHHHHCCCEECCC	46.11	-
39	Acetylation	FFSFLRRKTDFFIGG HHHHHHHCCCEECCC	46.11	62135805
39	Ubiquitination	FFSFLRRKTDFFIGG HHHHHHHCCCEECCC	46.11	-
40	Phosphorylation	FSFLRRKTDFFIGGE HHHHHHCCCEECCCC	35.91	-
47	Ubiquitination	TDFFIGGEEGMAEKL CCEECCCCCCHHHHH	46.28	24816145
50	Sulfoxidation	FIGGEEGMAEKLITQ ECCCCCCHHHHHHHH	5.01	21406390
53	Ubiquitination	GEEGMAEKLITQTFS CCCCHHHHHHHHHHH	35.33	29967540
56	Ubiquitination	GMAEKLITQTFSHHN CHHHHHHHHHHHHHH	31.80	22817900
58	Phosphorylation	AEKLITQTFSHHNQL HHHHHHHHHHHHHHH	20.60	28857561
60	Phosphorylation	KLITQTFSHHNQLAQ HHHHHHHHHHHHHHH	27.50	28857561
68	2-Hydroxyisobutyrylation	HHNQLAQKTRREKRA HHHHHHHHHHHHHHH	38.09	-
68	Acetylation	HHNQLAQKTRREKRA HHHHHHHHHHHHHHH	38.09	25953088
68	Ubiquitination	HHNQLAQKTRREKRA HHHHHHHHHHHHHHH	38.09	21906983
72	Ubiquitination	LAQKTRREKRARQEA HHHHHHHHHHHHHHH	43.53	21890473
73	Ubiquitination	AQKTRREKRARQEAE HHHHHHHHHHHHHHH	49.93	22817900
74	Ubiquitination	QKTRREKRARQEAER HHHHHHHHHHHHHHH	30.19	22817900
76	Ubiquitination	TRREKRARQEAERRE HHHHHHHHHHHHHHH	38.62	21890473
77	Ubiquitination	RREKRARQEAERREK HHHHHHHHHHHHHHH	53.95	22817900
81	Ubiquitination	RARQEAERREKAERA HHHHHHHHHHHHHHH	60.14	22817900
93	Acetylation	ERAARLAKEAKSETS HHHHHHHHHHHHCCC	63.90	11921613
96	Sumoylation	ARLAKEAKSETSGPQ HHHHHHHHHCCCCCC	50.33	-
96	Sumoylation	ARLAKEAKSETSGPQ HHHHHHHHHCCCCCC	50.33	-
96	Ubiquitination	ARLAKEAKSETSGPQ HHHHHHHHHCCCCCC	50.33	33845483
97	Phosphorylation	RLAKEAKSETSGPQI HHHHHHHHCCCCCCH	53.83	28985074
99	Phosphorylation	AKEAKSETSGPQIKE HHHHHHCCCCCCHHH	46.18	25262027
100	Phosphorylation	KEAKSETSGPQIKEL HHHHHCCCCCCHHHC	44.41	25627689
100	Ubiquitination	KEAKSETSGPQIKEL HHHHHCCCCCCHHHC	44.41	24816145
104	Ubiquitination	SETSGPQIKELTDEE HCCCCCCHHHCCHHH	4.16	24816145
105	Acetylation	ETSGPQIKELTDEEA CCCCCCHHHCCHHHH	41.23	23236377
105	Ubiquitination	ETSGPQIKELTDEEA CCCCCCHHHCCHHHH	41.23	21906983
108	Phosphorylation	GPQIKELTDEEAERL CCCHHHCCHHHHHHH	42.32	29255136
109	Ubiquitination	PQIKELTDEEAERLQ CCHHHCCHHHHHHHH	65.45	22817900
113	Ubiquitination	ELTDEEAERLQLEID HCCHHHHHHHHHHHH	58.15	22817900
122	2-Hydroxyisobutyrylation	LQLEIDQKKDAENHE HHHHHHHHHHHHHHH	49.20	-
122	Acetylation	LQLEIDQKKDAENHE HHHHHHHHHHHHHHH	49.20	25953088
122	Ubiquitination	LQLEIDQKKDAENHE HHHHHHHHHHHHHHH	49.20	21906983
123	Ubiquitination	QLEIDQKKDAENHEA HHHHHHHHHHHHHHH	57.44	22817900
125	Ubiquitination	EIDQKKDAENHEAQL HHHHHHHHHHHHHHH	28.50	21890473
126	Ubiquitination	IDQKKDAENHEAQLK HHHHHHHHHHHHHHH	70.07	22817900
127	Ubiquitination	DQKKDAENHEAQLKN HHHHHHHHHHHHHHC	39.77	22817900
129	Ubiquitination	KKDAENHEAQLKNGS HHHHHHHHHHHHCCC	50.09	21890473
130	Ubiquitination	KDAENHEAQLKNGSL HHHHHHHHHHHCCCC	16.68	22817900
131	Ubiquitination	DAENHEAQLKNGSLD HHHHHHHHHHCCCCC	50.41	22817900
133	Ubiquitination	ENHEAQLKNGSLDSP HHHHHHHHCCCCCCC	47.37	32015554
134	Ubiquitination	NHEAQLKNGSLDSPG HHHHHHHCCCCCCCC	54.61	22817900
136	Phosphorylation	EAQLKNGSLDSPGKQ HHHHHCCCCCCCCCC	38.10	23927012
139	Phosphorylation	LKNGSLDSPGKQDTE HHCCCCCCCCCCCCC	40.62	29255136
145	Phosphorylation	DSPGKQDTEEDEEED CCCCCCCCCCCHHHH	38.49	29255136
145	Ubiquitination	DSPGKQDTEEDEEED CCCCCCCCCCCHHHH	38.49	22817900
147	Ubiquitination	PGKQDTEEDEEEDEK CCCCCCCCCHHHHHH	73.20	21890473
153	Ubiquitination	EEDEEEDEKDKGKLK CCCHHHHHHHCCCCC	67.45	24816145
157	Ubiquitination	EEDEKDKGKLKPNLG HHHHHHCCCCCCCCC	51.14	24816145
160	Ubiquitination	EKDKGKLKPNLGNGA HHHCCCCCCCCCCCC	35.03	-
162	Ubiquitination	DKGKLKPNLGNGADL HCCCCCCCCCCCCCC	60.02	22817900
163	Ubiquitination	KGKLKPNLGNGADLP CCCCCCCCCCCCCCC	8.38	22817900
166	Ubiquitination	LKPNLGNGADLPNYR CCCCCCCCCCCCCCC	20.76	22817900
172	Phosphorylation	NGADLPNYRWTQTLS CCCCCCCCCCCCCHH	12.94	26074081
179	Phosphorylation	YRWTQTLSELDLAVP CCCCCCHHHHCCCCC	39.23	28348404
179	Ubiquitination	YRWTQTLSELDLAVP CCCCCCHHHHCCCCC	39.23	22817900
180	Ubiquitination	RWTQTLSELDLAVPF CCCCCHHHHCCCCCE	49.79	22817900
183	Ubiquitination	QTLSELDLAVPFCVN CCHHHHCCCCCEEEE	8.94	22817900
184	Ubiquitination	TLSELDLAVPFCVNF CHHHHCCCCCEEEEE	13.45	22817900
194	Acetylation	FCVNFRLKGKDMVVD EEEEEEECCCCEEEE	60.71	23749302
194	Ubiquitination	FCVNFRLKGKDMVVD EEEEEEECCCCEEEE	60.71	22817900
196	2-Hydroxyisobutyrylation	VNFRLKGKDMVVDIQ EEEEECCCCEEEEHH	40.85	-
196	Acetylation	VNFRLKGKDMVVDIQ EEEEECCCCEEEEHH	40.85	23749302
196	Ubiquitination	VNFRLKGKDMVVDIQ EEEEECCCCEEEEHH	40.85	21906983
198	Sulfoxidation	FRLKGKDMVVDIQRR EEECCCCEEEEHHHH	3.45	21406390
198	Ubiquitination	FRLKGKDMVVDIQRR EEECCCCEEEEHHHH	3.45	22817900
200	Ubiquitination	LKGKDMVVDIQRRHL ECCCCEEEEHHHHHH	4.27	21890473
202	Ubiquitination	GKDMVVDIQRRHLRV CCCEEEEHHHHHHHC	2.01	22817900
204	Ubiquitination	DMVVDIQRRHLRVGL CEEEEHHHHHHHCCC	28.46	21890473
212	Ubiquitination	RHLRVGLKGQPAIID HHHHCCCCCCCEEEC	49.96	21906983
216	Ubiquitination	VGLKGQPAIIDGELY CCCCCCCEEECCEEE	11.95	22817900
218	Ubiquitination	LKGQPAIIDGELYNE CCCCCEEECCEEECE	6.38	22817900
219	Ubiquitination	KGQPAIIDGELYNEV CCCCEEECCEEECEE	38.10	22817900
220	Ubiquitination	GQPAIIDGELYNEVK CCCEEECCEEECEEE	19.19	22817900
223	Phosphorylation	AIIDGELYNEVKVEE EEECCEEECEEEEEE	12.65	20068231
226	Ubiquitination	DGELYNEVKVEESSW CCEEECEEEEEECEE	8.19	21890473
231	Phosphorylation	NEVKVEESSWLIEDG CEEEEEECEEEEECC	17.20	24905233
232	Phosphorylation	EVKVEESSWLIEDGK EEEEEECEEEEECCE	29.22	24905233
239	Acetylation	SWLIEDGKVVTVHLE EEEEECCEEEEEEEE	45.94	19608861
239	Ubiquitination	SWLIEDGKVVTVHLE EEEEECCEEEEEEEE	45.94	32015554
240	Ubiquitination	WLIEDGKVVTVHLEK EEEECCEEEEEEEEH	5.51	24816145
247	2-Hydroxyisobutyrylation	VVTVHLEKINKMEWW EEEEEEEHHCCHHHH	58.92	-
248	Ubiquitination	VTVHLEKINKMEWWS EEEEEEHHCCHHHHH	4.35	27667366
250	Acetylation	VHLEKINKMEWWSRL EEEEHHCCHHHHHHH	41.49	25953088
250	Ubiquitination	VHLEKINKMEWWSRL EEEEHHCCHHHHHHH	41.49	-
251	Ubiquitination	HLEKINKMEWWSRLV EEEHHCCHHHHHHHH	4.50	22817900
253	Ubiquitination	EKINKMEWWSRLVSS EHHCCHHHHHHHHCC	8.54	21890473
255	Phosphorylation	INKMEWWSRLVSSDP HCCHHHHHHHHCCCC	19.46	27273156
255	Ubiquitination	INKMEWWSRLVSSDP HCCHHHHHHHHCCCC	19.46	22817900
257	Ubiquitination	KMEWWSRLVSSDPEI CHHHHHHHHCCCCCC	3.50	21890473
259	Phosphorylation	EWWSRLVSSDPEINT HHHHHHHCCCCCCCC	33.35	27273156
259	Ubiquitination	EWWSRLVSSDPEINT HHHHHHHCCCCCCCC	33.35	22817900
260	Phosphorylation	WWSRLVSSDPEINTK HHHHHHCCCCCCCCC	50.10	23401153
260	Ubiquitination	WWSRLVSSDPEINTK HHHHHHCCCCCCCCC	50.10	22817900
265	Ubiquitination	VSSDPEINTKKINPE HCCCCCCCCCCCCCC	44.15	22817900
266	Phosphorylation	SSDPEINTKKINPEN CCCCCCCCCCCCCCC	39.10	23186163
266	Ubiquitination	SSDPEINTKKINPEN CCCCCCCCCCCCCCC	39.10	21890473
267	2-Hydroxyisobutyrylation	SDPEINTKKINPENS CCCCCCCCCCCCCCC	47.36	-
267	Acetylation	SDPEINTKKINPENS CCCCCCCCCCCCCCC	47.36	25953088
267	Ubiquitination	SDPEINTKKINPENS CCCCCCCCCCCCCCC	47.36	21906983
268	Acetylation	DPEINTKKINPENSK CCCCCCCCCCCCCCC	45.75	25953088
268	Ubiquitination	DPEINTKKINPENSK CCCCCCCCCCCCCCC	45.75	22817900
269	Ubiquitination	PEINTKKINPENSKL CCCCCCCCCCCCCCC	12.70	22817900
271	Ubiquitination	INTKKINPENSKLSD CCCCCCCCCCCCCCC	45.69	22817900
272	Ubiquitination	NTKKINPENSKLSDL CCCCCCCCCCCCCCC	70.42	22817900
273	Ubiquitination	TKKINPENSKLSDLD CCCCCCCCCCCCCCC	45.78	22817900
274	Phosphorylation	KKINPENSKLSDLDS CCCCCCCCCCCCCCH	33.06	29255136
275	Acetylation	KINPENSKLSDLDSE CCCCCCCCCCCCCHH	64.69	23236377
275	Ubiquitination	KINPENSKLSDLDSE CCCCCCCCCCCCCHH	64.69	23000965
276	Ubiquitination	INPENSKLSDLDSET CCCCCCCCCCCCHHH	4.90	22817900
277	Phosphorylation	NPENSKLSDLDSETR CCCCCCCCCCCHHHH	39.60	29255136
278	Ubiquitination	PENSKLSDLDSETRS CCCCCCCCCCHHHHH	66.00	22505724
279	Ubiquitination	ENSKLSDLDSETRSM CCCCCCCCCHHHHHH	7.58	21890473
281	Phosphorylation	SKLSDLDSETRSMVE CCCCCCCHHHHHHHH	48.44	29255136
283	Phosphorylation	LSDLDSETRSMVEKM CCCCCHHHHHHHHHH	31.81	29255136
283	Ubiquitination	LSDLDSETRSMVEKM CCCCCHHHHHHHHHH	31.81	21890473
285	Phosphorylation	DLDSETRSMVEKMMY CCCHHHHHHHHHHHH	34.30	25159151
289	2-Hydroxyisobutyrylation	ETRSMVEKMMYDQRQ HHHHHHHHHHHHHHH	19.98	-
289	Ubiquitination	ETRSMVEKMMYDQRQ HHHHHHHHHHHHHHH	19.98	24816145
292	Phosphorylation	SMVEKMMYDQRQKSM HHHHHHHHHHHHHHC	12.86	-
293	Ubiquitination	MVEKMMYDQRQKSMG HHHHHHHHHHHHHCC	21.20	24816145
297	Ubiquitination	MMYDQRQKSMGLPTS HHHHHHHHHCCCCCC	44.60	27667366
298	Phosphorylation	MYDQRQKSMGLPTSD HHHHHHHHCCCCCCH	15.11	25159151
299	Sulfoxidation	YDQRQKSMGLPTSDE HHHHHHHCCCCCCHH	9.12	21406390
301	Ubiquitination	QRQKSMGLPTSDEQK HHHHHCCCCCCHHHH	2.91	27667366
303	Phosphorylation	QKSMGLPTSDEQKKQ HHHCCCCCCHHHHHH	54.58	24114839
304	Phosphorylation	KSMGLPTSDEQKKQE HHCCCCCCHHHHHHH	36.89	25159151
305	Ubiquitination	SMGLPTSDEQKKQEI HCCCCCCHHHHHHHH	65.90	27667366
308	2-Hydroxyisobutyrylation	LPTSDEQKKQEILKK CCCCHHHHHHHHHHH	55.14	-
308	Ubiquitination	LPTSDEQKKQEILKK CCCCHHHHHHHHHHH	55.14	21906983
309	Ubiquitination	PTSDEQKKQEILKKF CCCHHHHHHHHHHHH	53.51	22817900
312	Ubiquitination	DEQKKQEILKKFMDQ HHHHHHHHHHHHHHH	6.73	22817900
313	Ubiquitination	EQKKQEILKKFMDQH HHHHHHHHHHHHHHC	4.93	22817900
314	Ubiquitination	QKKQEILKKFMDQHP HHHHHHHHHHHHHCC	50.02	22817900
315	Acetylation	KKQEILKKFMDQHPE HHHHHHHHHHHHCCC	42.34	25953088
315	Ubiquitination	KKQEILKKFMDQHPE HHHHHHHHHHHHCCC	42.34	21906983
316	Ubiquitination	KQEILKKFMDQHPEM HHHHHHHHHHHCCCC	6.62	22817900
317	Sulfoxidation	QEILKKFMDQHPEMD HHHHHHHHHHCCCCC	7.14	21406390
317	Ubiquitination	QEILKKFMDQHPEMD HHHHHHHHHHCCCCC	7.14	22817900
318	Ubiquitination	EILKKFMDQHPEMDF HHHHHHHHHCCCCCH	46.93	22817900
319	Ubiquitination	ILKKFMDQHPEMDFS HHHHHHHHCCCCCHH	42.10	21890473
322	Ubiquitination	KFMDQHPEMDFSKAK HHHHHCCCCCHHHHC	49.62	22817900
323	Sulfoxidation	FMDQHPEMDFSKAKF HHHHCCCCCHHHHCC	8.10	30846556
323	Ubiquitination	FMDQHPEMDFSKAKF HHHHCCCCCHHHHCC	8.10	21890473
324	Ubiquitination	MDQHPEMDFSKAKFN HHHCCCCCHHHHCCC	42.90	22817900
325	Ubiquitination	DQHPEMDFSKAKFN- HHCCCCCHHHHCCC-	8.56	22817900
326	Phosphorylation	QHPEMDFSKAKFN-- HCCCCCHHHHCCC--	27.69	19060867
327	2-Hydroxyisobutyrylation	HPEMDFSKAKFN--- CCCCCHHHHCCC---	56.44	-
327	Acetylation	HPEMDFSKAKFN--- CCCCCHHHHCCC---	56.44	25953088
327	Methylation	HPEMDFSKAKFN--- CCCCCHHHHCCC---	56.44	42360665
327	Ubiquitination	HPEMDFSKAKFN--- CCCCCHHHHCCC---	56.44	21906983
328	Ubiquitination	PEMDFSKAKFN---- CCCCHHHHCCC----	22.07	22817900
329	Methylation	EMDFSKAKFN----- CCCHHHHCCC-----	49.53	115974295
329	Ubiquitination	EMDFSKAKFN----- CCCHHHHCCC-----	49.53	22817900
331	Ubiquitination	DFSKAKFN------- CHHHHCCC-------	50.72	22505724
332	Ubiquitination	FSKAKFN-------- HHHHCCC--------		21890473
335	Ubiquitination	AKFN----------- HCCC-----------		22505724
336	Ubiquitination	KFN------------ CCC------------		21890473
346	Ubiquitination	---------------------- ----------------------		24816145
350	Ubiquitination	-------------------------- --------------------------		24816145
354	Ubiquitination	------------------------------ ------------------------------		27667366
358	Ubiquitination	---------------------------------- ----------------------------------		27667366
365	Ubiquitination	----------------------------------------- -----------------------------------------		22817900
366	Ubiquitination	------------------------------------------ ------------------------------------------		22817900
369	Ubiquitination	--------------------------------------------- ---------------------------------------------		22817900
370	Ubiquitination	---------------------------------------------- ----------------------------------------------		22817900
371	Ubiquitination	----------------------------------------------- -----------------------------------------------		22817900
372	Ubiquitination	------------------------------------------------ ------------------------------------------------		21890473
375	Ubiquitination	--------------------------------------------------- ---------------------------------------------------		22817900
376	Ubiquitination	---------------------------------------------------- ----------------------------------------------------		21890473
384	Ubiquitination	------------------------------------------------------------ ------------------------------------------------------------		22505724
388	Ubiquitination	---------------------------------------------------------------- ----------------------------------------------------------------		22505724

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
40	T	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
274	S	Phosphorylation	Kinase	PLK1	P53350	Uniprot
326	S	Phosphorylation	Kinase	PLK1	P53350	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
274	S	Phosphorylation	12852857
Phosphorylation on Ser-274 and Ser-326 is necessary for correct formation of mitotic spindles and chromosome separation during mitosis.
326	S	Phosphorylation	12852857
Phosphorylation on Ser-274 and Ser-326 is necessary for correct formation of mitotic spindles and chromosome separation during mitosis.

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 NUDC_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PLK1_HUMAN	PLK1	physical	12852857
LIS1_HUMAN	PAFAH1B1	physical	9601647
LIS1_HUMAN	PAFAH1B1	physical	20675372
HS90A_HUMAN	HSP90AA1	physical	20675372
TRM1_HUMAN	TRMT1	physical	22939629
PPME1_HUMAN	PPME1	physical	22939629
ERF1_HUMAN	ETF1	physical	22863883
H33_HUMAN	H3F3A	physical	22863883
SYK_HUMAN	KARS	physical	22863883
PAPOA_HUMAN	PAPOLA	physical	22863883
TLN1_HUMAN	TLN1	physical	22863883
DNJA2_HUMAN	DNAJA2	physical	25036637
DNJB1_HUMAN	DNAJB1	physical	25036637
MAEL_HUMAN	MAEL	physical	25036637
DNJA1_HUMAN	DNAJA1	physical	25036637
RS17_HUMAN	RPS17	physical	25036637
ADAM9_HUMAN	ADAM9	physical	26344197
ICAL_HUMAN	CAST	physical	26344197
CCDC6_HUMAN	CCDC6	physical	26344197
G3P_HUMAN	GAPDH	physical	26344197
SODC_HUMAN	SOD1	physical	26344197
EMAL4_HUMAN	EML4	physical	25789526
WDR35_HUMAN	WDR35	physical	27173435
IF172_HUMAN	IFT172	physical	27173435

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 NUDC_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-239, 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-260 AND SER-281, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"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-139 AND THR-145, ANDMASS SPECTROMETRY.	19413330 [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-139 AND THR-145, ANDMASS SPECTROMETRY.	18669648 [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-139; THR-145 ANDSER-285, 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 SER-139 AND THR-145, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"A role for Plk1 phosphorylation of NudC in cytokinesis."; Zhou T., Aumais J.P., Liu X., Yu-Lee L.-Y., Erikson R.L.; Dev. Cell 5:127-138(2003). Cited for: FUNCTION, INTERACTION WITH PLK1, IDENTIFICATION IN A COMPLEX WITHDYNACTIN AND DYNEIN, MUTAGENESIS OF SER-274 AND SER-326, ANDPHOSPHORYLATION AT SER-274 AND SER-326.	12852857 [Abstract]

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