dbPTM

NEDD1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NEDD1_HUMAN
UniProt AC	Q8NHV4
Protein Name	Protein NEDD1
Gene Name	NEDD1
Organism	Homo sapiens (Human).
Sequence Length	660
Subcellular Localization	Cytoplasm, cytoskeleton, microtubule organizing center, centrosome .
Protein Description	Required for mitosis progression. Promotes the nucleation of microtubules from the spindle..
Protein Sequence	MQENLRFASSGDDIKIWDASSMTLVDKFNPHTSPHGISSICWSSNNNFLVTASSSGDKIVVSSCKCKPVPLLELAEGQKQTCVNLNSTSMYLVSGGLNNTVNIWDLKSKRVHRSLKDHKDQVTCVTYNWNDCYIASGSLSGEIILHSVTTNLSSTPFGHGSNQSVRHLKYSLFKKSLLGSVSDNGIVTLWDVNSQSPYHNFDSVHKAPASGICFSPVNELLFVTIGLDKRIILYDTSSKKLVKTLVADTPLTAVDFMPDGATLAIGSSRGKIYQYDLRMLKSPVKTISAHKTSVQCIAFQYSTVLTKSSLNKGCSNKPTTVNKRSVNVNAASGGVQNSGIVREAPATSIATVLPQPMTSAMGKGTVAVQEKAGLPRSINTDTLSKETDSGKNQDFSSFDDTGKSSLGDMFSPIRDDAVVNKGSDESIGKGDGFDFLPQLNSVFPPRKNPVTSSTSVLHSSPLNVFMGSPGKEENENRDLTAESKKIYMGKQESKDSFKQLAKLVTSGAESGNLNTSPSSNQTRNSEKFEKPENEIEAQLICEPPINGSSTPNPKIASSVTAGVASSLSEKIADSIGNNRQNAPLTSIQIRFIQNMIQETLDDFREACHRDIVNLQVEMIKQFHMQLNEMHSLLERYSVNEGLVAEIERLREENKRLRAHF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4 (in isoform 3)	Phosphorylation	-	21.45	24300666
15	Ubiquitination	ASSGDDIKIWDASSM CCCCCCEEEEECCCC	44.75	-
16 (in isoform 3)	Phosphorylation	-	4.04	24300666
17 (in isoform 3)	Phosphorylation	-	7.07	24300666
65	Acetylation	KIVVSSCKCKPVPLL EEEEEECEEEEECEE	47.44	25953088
81	Phosphorylation	LAEGQKQTCVNLNST ECCCCCCEEEECCCC	26.00	22595525
88	Phosphorylation	TCVNLNSTSMYLVSG EEEECCCCCEEEEEC	19.21	22595525
89	Phosphorylation	CVNLNSTSMYLVSGG EEECCCCCEEEEECC	12.78	22595525
91	Phosphorylation	NLNSTSMYLVSGGLN ECCCCCEEEEECCCC	12.06	20068231
94	Phosphorylation	STSMYLVSGGLNNTV CCCEEEEECCCCCCE	25.25	20068231
100	Phosphorylation	VSGGLNNTVNIWDLK EECCCCCCEEEHHHC	17.54	20068231
108	Phosphorylation	VNIWDLKSKRVHRSL EEEHHHCCHHHHHHH	32.75	22595525
114	Phosphorylation	KSKRVHRSLKDHKDQ CCHHHHHHHCCCCCC	25.54	20068231
171	Phosphorylation	SVRHLKYSLFKKSLL HHHHHHHHHHHHHHH	26.24	24719451
176	Phosphorylation	KYSLFKKSLLGSVSD HHHHHHHHHHCCCCC	29.44	-
180	Phosphorylation	FKKSLLGSVSDNGIV HHHHHHCCCCCCCEE	20.58	-
182	Phosphorylation	KSLLGSVSDNGIVTL HHHHCCCCCCCEEEE	27.36	-
215	Phosphorylation	PASGICFSPVNELLF CCCCCCCCCHHHEEE	24.43	22595525
234	Phosphorylation	LDKRIILYDTSSKKL CCCEEEEEECCCHHH	13.53	20068231
236	Phosphorylation	KRIILYDTSSKKLVK CEEEEEECCCHHHHH	22.73	20068231
237	Phosphorylation	RIILYDTSSKKLVKT EEEEEECCCHHHHHH	36.94	20068231
238	Phosphorylation	IILYDTSSKKLVKTL EEEEECCCHHHHHHH	35.58	20068231
239	Acetylation	ILYDTSSKKLVKTLV EEEECCCHHHHHHHH	50.31	25953088
243	Ubiquitination	TSSKKLVKTLVADTP CCCHHHHHHHHCCCC	46.72	21906983
246	Ubiquitination	KKLVKTLVADTPLTA HHHHHHHHCCCCCEE	5.69	-
247	Ubiquitination	KLVKTLVADTPLTAV HHHHHHHCCCCCEEE	20.33	-
250	Ubiquitination	KTLVADTPLTAVDFM HHHHCCCCCEEEEEC	28.41	21906983
271	Malonylation	AIGSSRGKIYQYDLR EEECCCCEEEEEEHH	36.81	26320211
271	Ubiquitination	AIGSSRGKIYQYDLR EEECCCCEEEEEEHH	36.81	-
278	Ubiquitination	KIYQYDLRMLKSPVK EEEEEEHHHHCCCCE	26.03	-
281	Ubiquitination	QYDLRMLKSPVKTIS EEEHHHHCCCCEEHH	43.29	-
282	Phosphorylation	YDLRMLKSPVKTISA EEHHHHCCCCEEHHC	30.85	22595525
285	Ubiquitination	RMLKSPVKTISAHKT HHHCCCCEEHHCCCC	43.45	-
286	Phosphorylation	MLKSPVKTISAHKTS HHCCCCEEHHCCCCH	22.02	22595525
289	Phosphorylation	SPVKTISAHKTSVQC CCCEEHHCCCCHHHE	12.35	24719451
292	Phosphorylation	KTISAHKTSVQCIAF EEHHCCCCHHHEEEE	25.02	30576142
301	Phosphorylation	VQCIAFQYSTVLTKS HHEEEEEEEEEECHH	10.39	23532336
302	Phosphorylation	QCIAFQYSTVLTKSS HEEEEEEEEEECHHH	10.97	30576142
303	Phosphorylation	CIAFQYSTVLTKSSL EEEEEEEEEECHHHC	18.01	30576142
312	Ubiquitination	LTKSSLNKGCSNKPT ECHHHCCCCCCCCCC	67.59	-
317	Ubiquitination	LNKGCSNKPTTVNKR CCCCCCCCCCCCCCC	27.70	-
319	Phosphorylation	KGCSNKPTTVNKRSV CCCCCCCCCCCCCCC	45.01	23532336
325	Phosphorylation	PTTVNKRSVNVNAAS CCCCCCCCCCCCCCC	21.47	29978859
332	Phosphorylation	SVNVNAASGGVQNSG CCCCCCCCCCCCCCC	33.40	20860994
338	Phosphorylation	ASGGVQNSGIVREAP CCCCCCCCCCCEECC	16.89	20860994
348	O-linked_Glycosylation	VREAPATSIATVLPQ CEECCCCEEEEECCC	16.60	30379171
371	2-Hydroxyisobutyrylation	GTVAVQEKAGLPRSI CEEEEHHHCCCCCCC	30.57	-
371	Ubiquitination	GTVAVQEKAGLPRSI CEEEEHHHCCCCCCC	30.57	-
377	Phosphorylation	EKAGLPRSINTDTLS HHCCCCCCCCCCCCC	20.46	25159151
378	Ubiquitination	KAGLPRSINTDTLSK HCCCCCCCCCCCCCC	7.31	-
382	Phosphorylation	PRSINTDTLSKETDS CCCCCCCCCCCCCCC	30.78	19509060
384	Phosphorylation	SINTDTLSKETDSGK CCCCCCCCCCCCCCC	30.45	27251275
385	Ubiquitination	INTDTLSKETDSGKN CCCCCCCCCCCCCCC	68.68	-
387	Phosphorylation	TDTLSKETDSGKNQD CCCCCCCCCCCCCCC	38.92	22595525
389	Phosphorylation	TLSKETDSGKNQDFS CCCCCCCCCCCCCCC	60.12	22595525
391	Ubiquitination	SKETDSGKNQDFSSF CCCCCCCCCCCCCCC	56.22	21906983
396	Phosphorylation	SGKNQDFSSFDDTGK CCCCCCCCCCCCCCC	38.08	25159151
397	Phosphorylation	GKNQDFSSFDDTGKS CCCCCCCCCCCCCCC	32.46	25159151
398	Ubiquitination	KNQDFSSFDDTGKSS CCCCCCCCCCCCCCC	10.77	21906983
401	Phosphorylation	DFSSFDDTGKSSLGD CCCCCCCCCCCCCCC	48.64	25159151
404	Phosphorylation	SFDDTGKSSLGDMFS CCCCCCCCCCCCCCC	31.94	25159151
405	Phosphorylation	FDDTGKSSLGDMFSP CCCCCCCCCCCCCCC	39.60	25159151
411	Phosphorylation	SSLGDMFSPIRDDAV CCCCCCCCCCCCCCE	16.87	30266825
412	Phosphorylation	SLGDMFSPIRDDAVV CCCCCCCCCCCCCEE	17.86	27251275
418	Phosphorylation	SPIRDDAVVNKGSDE CCCCCCCEEECCCCC	6.66	24719451
423	Phosphorylation	DAVVNKGSDESIGKG CCEEECCCCCCCCCC	39.55	22199227
426	Phosphorylation	VNKGSDESIGKGDGF EECCCCCCCCCCCCC	41.45	22199227
429	Ubiquitination	GSDESIGKGDGFDFL CCCCCCCCCCCCCCH	52.76	-
451	Phosphorylation	PPRKNPVTSSTSVLH CCCCCCCCCCCEEEC	20.44	27174698
452	Phosphorylation	PRKNPVTSSTSVLHS CCCCCCCCCCEEECC	31.67	25159151
453	Phosphorylation	RKNPVTSSTSVLHSS CCCCCCCCCEEECCC	18.48	22496350
454	Phosphorylation	KNPVTSSTSVLHSSP CCCCCCCCEEECCCC	23.71	27174698
455	Phosphorylation	NPVTSSTSVLHSSPL CCCCCCCEEECCCCC	25.32	22199227
459	Phosphorylation	SSTSVLHSSPLNVFM CCCEEECCCCCEEEC	29.50	30576142
460	Phosphorylation	STSVLHSSPLNVFMG CCEEECCCCCEEECC	23.74	21815630
468	Phosphorylation	PLNVFMGSPGKEENE CCEEECCCCCCHHCC	20.77	25159151
480	Phosphorylation	ENENRDLTAESKKIY HCCCCCCCHHHHHHH	32.44	30576142
483	Phosphorylation	NRDLTAESKKIYMGK CCCCCHHHHHHHCCC	36.46	30576142
487	Phosphorylation	TAESKKIYMGKQESK CHHHHHHHCCCCCCH	14.54	-
493	O-linked_Glycosylation	IYMGKQESKDSFKQL HHCCCCCCHHHHHHH	38.99	30379171
493	Phosphorylation	IYMGKQESKDSFKQL HHCCCCCCHHHHHHH	38.99	22595525
494	Acetylation	YMGKQESKDSFKQLA HCCCCCCHHHHHHHH	57.55	7431099
496	Phosphorylation	GKQESKDSFKQLAKL CCCCCHHHHHHHHHH	37.77	22595525
500	Phosphorylation	SKDSFKQLAKLVTSG CHHHHHHHHHHHHHC	4.71	24719451
505	Phosphorylation	KQLAKLVTSGAESGN HHHHHHHHHCCCCCC	31.70	23927012
506	Phosphorylation	QLAKLVTSGAESGNL HHHHHHHHCCCCCCC	28.64	23927012
510	Phosphorylation	LVTSGAESGNLNTSP HHHHCCCCCCCCCCC	32.23	23927012
515	Phosphorylation	AESGNLNTSPSSNQT CCCCCCCCCCCCCCC	45.22	30266825
516	Phosphorylation	ESGNLNTSPSSNQTR CCCCCCCCCCCCCCC	23.01	19664994
518	Phosphorylation	GNLNTSPSSNQTRNS CCCCCCCCCCCCCCC	41.51	30266825
519	Phosphorylation	NLNTSPSSNQTRNSE CCCCCCCCCCCCCCH	36.02	29255136
522	Phosphorylation	TSPSSNQTRNSEKFE CCCCCCCCCCCHHCC	35.75	25159151
523	Phosphorylation	SPSSNQTRNSEKFEK CCCCCCCCCCHHCCC	34.61	24719451
525	Phosphorylation	SSNQTRNSEKFEKPE CCCCCCCCHHCCCCC	38.58	28387310
548	Phosphorylation	CEPPINGSSTPNPKI ECCCCCCCCCCCCHH	26.93	25850435
549	Phosphorylation	EPPINGSSTPNPKIA CCCCCCCCCCCCHHH	49.64	30576142
550	Phosphorylation	PPINGSSTPNPKIAS CCCCCCCCCCCHHHH	28.87	25159151
555	Phosphorylation	SSTPNPKIASSVTAG CCCCCCHHHHHHHHH	4.79	27251275
557	Phosphorylation	TPNPKIASSVTAGVA CCCCHHHHHHHHHHH	28.90	20860994
558	Phosphorylation	PNPKIASSVTAGVAS CCCHHHHHHHHHHHH	17.92	27174698
560	Phosphorylation	PKIASSVTAGVASSL CHHHHHHHHHHHHHH	21.46	27174698
565	Phosphorylation	SVTAGVASSLSEKIA HHHHHHHHHHHHHHH	29.43	25159151
566	Phosphorylation	VTAGVASSLSEKIAD HHHHHHHHHHHHHHH	26.61	27174698
568	Phosphorylation	AGVASSLSEKIADSI HHHHHHHHHHHHHHC	38.50	25159151
570	Ubiquitination	VASSLSEKIADSIGN HHHHHHHHHHHHCCC	39.56	21906983
573	Phosphorylation	SLSEKIADSIGNNRQ HHHHHHHHHCCCCCC	44.24	27251275
574	Phosphorylation	LSEKIADSIGNNRQN HHHHHHHHCCCCCCC	24.31	20860994
577	Ubiquitination	KIADSIGNNRQNAPL HHHHHCCCCCCCCCC	38.55	21906983
586	Phosphorylation	RQNAPLTSIQIRFIQ CCCCCCHHHHHHHHH	21.85	22595525
636	Phosphorylation	MHSLLERYSVNEGLV HHHHHHHHCCCHHHH	13.95	-
637	Phosphorylation	HSLLERYSVNEGLVA HHHHHHHCCCHHHHH	25.37	14702039

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
377	S	Phosphorylation	Kinase	NEK9	Q8TD19	PSP
382	T	Phosphorylation	Kinase	PLK1	P53350	Uniprot
397	S	Phosphorylation	Kinase	PLK1	P53350	Uniprot
405	S	Phosphorylation	Kinase	AURKA	O14965	GPS
411	S	Phosphorylation	Kinase	CDK1	P06493	PSP
426	S	Phosphorylation	Kinase	PLK1	P53350	Uniprot
460	S	Phosphorylation	Kinase	CDK1	P06493	PSP
550	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot
637	S	Phosphorylation	Kinase	PLK1	P53350	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
382	T	Phosphorylation	19509060
During mitosis, prior phosphorylation on Thr-550 by CDK1 promotes subsequent phosphorylation by PLK1 on Thr-382, Ser-397, Ser-426 and Ser-637.
397	S	Phosphorylation	19509060
During mitosis, prior phosphorylation on Thr-550 by CDK1 promotes subsequent phosphorylation by PLK1 on Thr-382, Ser-397, Ser-426 and Ser-637.
426	S	Phosphorylation	19509060
During mitosis, prior phosphorylation on Thr-550 by CDK1 promotes subsequent phosphorylation by PLK1 on Thr-382, Ser-397, Ser-426 and Ser-637.
550	T	Phosphorylation	19509060
During mitosis, prior phosphorylation on Thr-550 by CDK1 promotes subsequent phosphorylation by PLK1 on Thr-382, Ser-397, Ser-426 and Ser-637.
637	S	Phosphorylation	19509060
During mitosis, prior phosphorylation on Thr-550 by CDK1 promotes subsequent phosphorylation by PLK1 on Thr-382, Ser-397, Ser-426 and Ser-637.

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 NEDD1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HAUS6_HUMAN	HAUS6	physical	19369198
ACTB_HUMAN	ACTB	physical	23443559
CPNS1_HUMAN	CAPNS1	physical	23443559
CSKP_HUMAN	CASK	physical	23443559
TCPB_HUMAN	CCT2	physical	23443559
TCPG_HUMAN	CCT3	physical	23443559
TCPD_HUMAN	CCT4	physical	23443559
TCPE_HUMAN	CCT5	physical	23443559
TCPZ_HUMAN	CCT6A	physical	23443559
TCPH_HUMAN	CCT7	physical	23443559
TCPQ_HUMAN	CCT8	physical	23443559
CHCH1_HUMAN	CHCHD1	physical	23443559
CILP1_HUMAN	CILP	physical	23443559
CRTC2_HUMAN	CRTC2	physical	23443559
CRTC3_HUMAN	CRTC3	physical	23443559
TBB5_HUMAN	TUBB	physical	23443559
DCST1_HUMAN	DCST1	physical	23443559
RT18B_HUMAN	MRPS18B	physical	23443559
F117B_HUMAN	FAM117B	physical	23443559
MZT2B_HUMAN	MZT2B	physical	23443559
ROA1_HUMAN	HNRNPA1	physical	23443559
ROA2_HUMAN	HNRNPA2B1	physical	23443559
HNRPF_HUMAN	HNRNPF	physical	23443559
HNRPU_HUMAN	HNRNPU	physical	23443559
HS71L_HUMAN	HSPA1L	physical	23443559
GRP75_HUMAN	HSPA9	physical	23443559
IRS4_HUMAN	IRS4	physical	23443559
LY65B_HUMAN	LY6G5B	physical	23443559
LYSC_HUMAN	LYZ	physical	23443559
RM46_HUMAN	MRPL46	physical	23443559
RT26_HUMAN	MRPS26	physical	23443559
RL13_HUMAN	RPL13	physical	23443559
PFD2_HUMAN	PFDN2	physical	23443559
RAVR1_HUMAN	RAVER1	physical	23443559
RL3_HUMAN	RPL3	physical	23443559
RL38_HUMAN	RPL38	physical	23443559
RS19_HUMAN	RPS19	physical	23443559
RS2_HUMAN	RPS2	physical	23443559
RS3_HUMAN	RPS3	physical	23443559
RS3A_HUMAN	RPS3A	physical	23443559
RS4X_HUMAN	RPS4X	physical	23443559
RS9_HUMAN	RPS9	physical	23443559
SCO2_HUMAN	SCO2	physical	23443559
TCAL4_HUMAN	TCEAL4	physical	23443559
TCPA_HUMAN	TCP1	physical	23443559
TFAM_HUMAN	TFAM	physical	23443559
THOC4_HUMAN	ALYREF	physical	23443559
TMPSD_HUMAN	TMPRSS13	physical	23443559
TBA1C_HUMAN	TUBA1C	physical	23443559
TBG1_HUMAN	TUBG1	physical	23443559
GCP3_HUMAN	TUBGCP3	physical	23443559
GCP4_HUMAN	TUBGCP4	physical	23443559
GCP6_HUMAN	TUBGCP6	physical	23443559
ZWINT_HUMAN	ZWINT	physical	23443559
ARL1_HUMAN	ARL1	physical	26496610
TCPZ_HUMAN	CCT6A	physical	26496610
CRY1_HUMAN	CRY1	physical	26496610
ECHM_HUMAN	ECHS1	physical	26496610
HELLS_HUMAN	HELLS	physical	26496610
LG3BP_HUMAN	LGALS3BP	physical	26496610
M3K4_HUMAN	MAP3K4	physical	26496610
PCM1_HUMAN	PCM1	physical	26496610
PLCB3_HUMAN	PLCB3	physical	26496610
PPM1A_HUMAN	PPM1A	physical	26496610
RL27_HUMAN	RPL27	physical	26496610
TCPA_HUMAN	TCP1	physical	26496610
TCPG_HUMAN	CCT3	physical	26496610
TBG1_HUMAN	TUBG1	physical	26496610
YBOX3_HUMAN	YBX3	physical	26496610
TRADD_HUMAN	TRADD	physical	26496610
ATPK_HUMAN	ATP5J2	physical	26496610
TOM20_HUMAN	TOMM20	physical	26496610
GCP3_HUMAN	TUBGCP3	physical	26496610
TCPH_HUMAN	CCT7	physical	26496610
TCPD_HUMAN	CCT4	physical	26496610
TCPB_HUMAN	CCT2	physical	26496610
RPC6_HUMAN	POLR3F	physical	26496610
SYFM_HUMAN	FARS2	physical	26496610
TCPQ_HUMAN	CCT8	physical	26496610
GCP2_HUMAN	TUBGCP2	physical	26496610
AFG32_HUMAN	AFG3L2	physical	26496610
TCPE_HUMAN	CCT5	physical	26496610
CP131_HUMAN	CEP131	physical	26496610
WDFY3_HUMAN	WDFY3	physical	26496610
ZN292_HUMAN	ZNF292	physical	26496610
FBX28_HUMAN	FBXO28	physical	26496610
MTCL1_HUMAN	MTCL1	physical	26496610
GCP4_HUMAN	TUBGCP4	physical	26496610
NDK7_HUMAN	NME7	physical	26496610
TXD11_HUMAN	TXNDC11	physical	26496610
PPHLN_HUMAN	PPHLN1	physical	26496610
NUP54_HUMAN	NUP54	physical	26496610
URFB1_HUMAN	UHRF1BP1	physical	26496610
BOREA_HUMAN	CDCA8	physical	26496610
CEP72_HUMAN	CEP72	physical	26496610
HERP2_HUMAN	HERPUD2	physical	26496610
DERL1_HUMAN	DERL1	physical	26496610
CEP97_HUMAN	CEP97	physical	26496610
CJ088_HUMAN	C10orf88	physical	26496610
MAGT1_HUMAN	MAGT1	physical	26496610
ZN644_HUMAN	ZNF644	physical	26496610
ING5_HUMAN	ING5	physical	26496610
CCD77_HUMAN	CCDC77	physical	26496610
GCP6_HUMAN	TUBGCP6	physical	26496610
GCP5_HUMAN	TUBGCP5	physical	26496610
NRBP2_HUMAN	NRBP2	physical	26496610
MZT1_HUMAN	MZT1	physical	26496610
MZT2A_HUMAN	MZT2A	physical	26496610
CNDH2_HUMAN	NCAPH2	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 NEDD1_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-516, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Sequential phosphorylation of Nedd1 by Cdk1 and Plk1 is required fortargeting of the gammaTuRC to the centrosome."; Zhang X., Chen Q., Feng J., Hou J., Yang F., Liu J., Jiang Q.,Zhang C.; J. Cell Sci. 122:2240-2251(2009). Cited for: FUNCTION, PHOSPHORYLATION AT THR-550 BY CDK1, AND PHOSPHORYLATION ATTHR-382; SER-397; SER-426 AND SER-637 BY PLK1.	19509060 [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-516, AND MASSSPECTROMETRY.	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-516, 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 SER-397; SER-411 ANDSER-516, AND MASS SPECTROMETRY.	18691976 [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 SER-516 AND SER-574, ANDMASS SPECTROMETRY.	19007248 [Abstract]

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