dbPTM

DLGP5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DLGP5_HUMAN
UniProt AC	Q15398
Protein Name	Disks large-associated protein 5
Gene Name	DLGAP5
Organism	Homo sapiens (Human).
Sequence Length	846
Subcellular Localization	Nucleus. Cytoplasm. Cytoplasm, cytoskeleton, spindle. Localizes to the spindle in mitotic cells. Colocalizes with CDH1 at sites of cell-cell contact in intestinal epithelial cells.
Protein Description	Potential cell cycle regulator that may play a role in carcinogenesis of cancer cells. Mitotic phosphoprotein regulated by the ubiquitin-proteasome pathway. Key regulator of adherens junction integrity and differentiation that may be involved in CDH1-mediated adhesion and signaling in epithelial cells..
Protein Sequence	MSSSHFASRHRKDISTEMIRTKIAHRKSLSQKENRHKEYERNRHFGLKDVNIPTLEGRILVELDETSQGLVPEKTNVKPRAMKTILGDQRKQMLQKYKEEKQLQKLKEQREKAKRGIFKVGRYRPDMPCFLLSNQNAVKAEPKKAIPSSVRITRSKAKDQMEQTKIDNESDVRAIRPGPRQTSEKKVSDKEKKVVQPVMPTSLRMTRSATQAAKQVPRTVSSTTARKPVTRAANENEPEGKVPSKGRPAKNVETKPDKGISCKVDSEENTLNSQTNATSGMNPDGVLSKMENLPEINTAKIKGKNSFAPKDFMFQPLDGLKTYQVTPMTPRSANAFLTPSYTWTPLKTEVDESQATKEILAQKCKTYSTKTIQQDSNKLPCPLGPLTVWHEEHVLNKNEATTKNLNGLPIKEVPSLERNEGRIAQPHHGVPYFRNILQSETEKLTSHCFEWDRKLELDIPDDAKDLIRTAVGQTRLLMKERFKQFEGLVDDCEYKRGIKETTCTDLDGFWDMVSFQIEDVIHKFNNLIKLEESGWQVNNNMNHNMNKNVFRKKVVSGIASKPKQDDAGRIAARNRLAAIKNAMRERIRQEECAETAVSVIPKEVDKIVFDAGFFRVESPVKLFSGLSVSSEGPSQRLGTPKSVNKAVSQSRNEMGIPQQTTSPENAGPQNTKSEHVKKTLFLSIPESRSSIEDAQCPGLPDLIEENHVVNKTDLKVDCLSSERMSLPLLAGGVADDINTNKKEGISDVVEGMELNSSITSQDVLMSSPEKNTASQNSILEEGETKISQSELFDNKSLTTECHLLDSPGLNCSNPFTQLERRHQEHARHISFGGNLITFSPLQPGEF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSSSHFASR ------CCCHHHHHH	40.31	25627689
3	Phosphorylation	-----MSSSHFASRH -----CCCHHHHHHC	26.91	25627689
8	Phosphorylation	MSSSHFASRHRKDIS CCCHHHHHHCCCCCC	27.89	-
15	Phosphorylation	SRHRKDISTEMIRTK HHCCCCCCHHHHHHH	28.57	21815630
16	Phosphorylation	RHRKDISTEMIRTKI HCCCCCCHHHHHHHH	29.88	30001349
28	Phosphorylation	TKIAHRKSLSQKENR HHHHHHHCCHHHHHH	32.96	-
30	Phosphorylation	IAHRKSLSQKENRHK HHHHHCCHHHHHHHH	46.42	-
32	Ubiquitination	HRKSLSQKENRHKEY HHHCCHHHHHHHHHH	54.29	24816145
54	Phosphorylation	LKDVNIPTLEGRILV CCCCCCCCCCCEEEE	33.37	29214152
66	Phosphorylation	ILVELDETSQGLVPE EEEEECCCCCCCCCC	26.47	29978859
67	Phosphorylation	LVELDETSQGLVPEK EEEECCCCCCCCCCC	21.87	30576142
83	Ubiquitination	NVKPRAMKTILGDQR CCCHHHHHHHHHHHH	31.28	33845483
83	Acetylation	NVKPRAMKTILGDQR CCCHHHHHHHHHHHH	31.28	25953088
84	Phosphorylation	VKPRAMKTILGDQRK CCHHHHHHHHHHHHH	14.35	-
133	Phosphorylation	DMPCFLLSNQNAVKA CCCEEEECCCCCCCC	38.22	28555341
148	O-linked_Glycosylation	EPKKAIPSSVRITRS CCCCCCCCCCEECHH	35.04	30379171
148	Phosphorylation	EPKKAIPSSVRITRS CCCCCCCCCCEECHH	35.04	26434776
149	Phosphorylation	PKKAIPSSVRITRSK CCCCCCCCCEECHHH	15.29	26434776
158	Methylation	RITRSKAKDQMEQTK EECHHHHHHHHHHHC	52.83	-
164	O-linked_Glycosylation	AKDQMEQTKIDNESD HHHHHHHHCCCCHHH	19.36	30379171
165	Ubiquitination	KDQMEQTKIDNESDV HHHHHHHCCCCHHHH	47.99	33845483
182	Phosphorylation	IRPGPRQTSEKKVSD CCCCCCCCCCCCCCH	39.88	29083192
183	Phosphorylation	RPGPRQTSEKKVSDK CCCCCCCCCCCCCHH	38.80	29083192
188	Phosphorylation	QTSEKKVSDKEKKVV CCCCCCCCHHHHHCC	52.42	29083192
192	Acetylation	KKVSDKEKKVVQPVM CCCCHHHHHCCCCCC	57.52	7826035
193	Sumoylation	KVSDKEKKVVQPVMP CCCHHHHHCCCCCCC	49.05	-
199	Sulfoxidation	KKVVQPVMPTSLRMT HHCCCCCCCCCHHHC	3.69	21406390
201	Phosphorylation	VVQPVMPTSLRMTRS CCCCCCCCCHHHCHH	23.46	22199227
202	Phosphorylation	VQPVMPTSLRMTRSA CCCCCCCCHHHCHHH	14.22	28348404
204	Methylation	PVMPTSLRMTRSATQ CCCCCCHHHCHHHHH	24.97	-
208	Phosphorylation	TSLRMTRSATQAAKQ CCHHHCHHHHHHHHH	26.88	20068231
210	Phosphorylation	LRMTRSATQAAKQVP HHHCHHHHHHHHHCC	21.71	20068231
214	Ubiquitination	RSATQAAKQVPRTVS HHHHHHHHHCCCCCC	55.64	24816145
214	Acetylation	RSATQAAKQVPRTVS HHHHHHHHHCCCCCC	55.64	25953088
219	Phosphorylation	AAKQVPRTVSSTTAR HHHHCCCCCCCCCCC	20.76	14729942
221	Phosphorylation	KQVPRTVSSTTARKP HHCCCCCCCCCCCCC	22.73	20068231
222	Phosphorylation	QVPRTVSSTTARKPV HCCCCCCCCCCCCCC	25.99	20068231
223	Phosphorylation	VPRTVSSTTARKPVT CCCCCCCCCCCCCCC	19.57	20068231
224	Phosphorylation	PRTVSSTTARKPVTR CCCCCCCCCCCCCCC	26.81	14729942
230	Phosphorylation	TTARKPVTRAANENE CCCCCCCCCCCCCCC	24.10	20068231
241	Ubiquitination	NENEPEGKVPSKGRP CCCCCCCCCCCCCCC	49.68	24816145
270	Phosphorylation	KVDSEENTLNSQTNA ECCCCCCCCCCCCCC	30.51	29759185
273	Phosphorylation	SEENTLNSQTNATSG CCCCCCCCCCCCCCC	41.30	29759185
275	Phosphorylation	ENTLNSQTNATSGMN CCCCCCCCCCCCCCC	27.00	29759185
279	Phosphorylation	NSQTNATSGMNPDGV CCCCCCCCCCCCHHH	33.37	28555341
290	Sulfoxidation	PDGVLSKMENLPEIN CHHHHHHHHCCCCCC	3.57	21406390
298	Phosphorylation	ENLPEINTAKIKGKN HCCCCCCCCCCCCCC	34.68	28555341
306	Phosphorylation	AKIKGKNSFAPKDFM CCCCCCCCCCCCCCE	26.69	29496963
310	Ubiquitination	GKNSFAPKDFMFQPL CCCCCCCCCCEEECC	61.23	29967540
313	Sulfoxidation	SFAPKDFMFQPLDGL CCCCCCCEEECCCCC	4.35	21406390
322	Phosphorylation	QPLDGLKTYQVTPMT ECCCCCCEEEECCCC	24.99	29396449
326	Phosphorylation	GLKTYQVTPMTPRSA CCCEEEECCCCCCCC	7.57	25159151
329	Phosphorylation	TYQVTPMTPRSANAF EEEECCCCCCCCCCC	19.43	25159151
332	Phosphorylation	VTPMTPRSANAFLTP ECCCCCCCCCCCCCC	27.38	21712546
338	Phosphorylation	RSANAFLTPSYTWTP CCCCCCCCCCCCCCC	12.07	26055452
340	Phosphorylation	ANAFLTPSYTWTPLK CCCCCCCCCCCCCCC	29.93	28450419
341	Phosphorylation	NAFLTPSYTWTPLKT CCCCCCCCCCCCCCC	13.90	28450419
342	Phosphorylation	AFLTPSYTWTPLKTE CCCCCCCCCCCCCCC	27.48	22617229
344	Phosphorylation	LTPSYTWTPLKTEVD CCCCCCCCCCCCCCC	15.79	25159151
347	Sumoylation	SYTWTPLKTEVDESQ CCCCCCCCCCCCHHH	43.79	-
347	Ubiquitination	SYTWTPLKTEVDESQ CCCCCCCCCCCCHHH	43.79	29967540
347	Sumoylation	SYTWTPLKTEVDESQ CCCCCCCCCCCCHHH	43.79	28112733
348	Phosphorylation	YTWTPLKTEVDESQA CCCCCCCCCCCHHHH	49.26	28450419
353	Phosphorylation	LKTEVDESQATKEIL CCCCCCHHHHHHHHH	22.20	28450419
356	Phosphorylation	EVDESQATKEILAQK CCCHHHHHHHHHHHH	22.90	28450419
357	Ubiquitination	VDESQATKEILAQKC CCHHHHHHHHHHHHC	45.86	29967540
363	Ubiquitination	TKEILAQKCKTYSTK HHHHHHHHCCCCCCC	31.90	29967540
366	Phosphorylation	ILAQKCKTYSTKTIQ HHHHHCCCCCCCCHH	31.98	25003641
367	Phosphorylation	LAQKCKTYSTKTIQQ HHHHCCCCCCCCHHC	10.39	25003641
368	Phosphorylation	AQKCKTYSTKTIQQD HHHCCCCCCCCHHCC	28.76	-
370	Ubiquitination	KCKTYSTKTIQQDSN HCCCCCCCCHHCCCC	37.38	29967540
370	Acetylation	KCKTYSTKTIQQDSN HCCCCCCCCHHCCCC	37.38	25953088
376	Phosphorylation	TKTIQQDSNKLPCPL CCCHHCCCCCCCCCC	31.37	-
397	Ubiquitination	HEEHVLNKNEATTKN CHHHHCCCCCCCCCC	52.59	29967540
401	Phosphorylation	VLNKNEATTKNLNGL HCCCCCCCCCCCCCC	31.93	15145941
402	Phosphorylation	LNKNEATTKNLNGLP CCCCCCCCCCCCCCC	25.61	15145941
403	Ubiquitination	NKNEATTKNLNGLPI CCCCCCCCCCCCCCH	55.90	29967540
411	Ubiquitination	NLNGLPIKEVPSLER CCCCCCHHCCCCCCC	51.20	29967540
415	Phosphorylation	LPIKEVPSLERNEGR CCHHCCCCCCCCCCC	48.30	25159151
439	Phosphorylation	YFRNILQSETEKLTS HHHHHHHHHHHHHHH	42.94	21406692
441	Phosphorylation	RNILQSETEKLTSHC HHHHHHHHHHHHHHH	43.60	20068231
443	Ubiquitination	ILQSETEKLTSHCFE HHHHHHHHHHHHHHH	65.57	29967540
454	Ubiquitination	HCFEWDRKLELDIPD HHHHHHHCCCCCCCC	43.79	29967540
464	Ubiquitination	LDIPDDAKDLIRTAV CCCCCCHHHHHHHHH	61.12	29967540
469	Phosphorylation	DAKDLIRTAVGQTRL CHHHHHHHHHHHHHH	20.78	-
483	Ubiquitination	LLMKERFKQFEGLVD HHHHHHHHHHCCCHH	61.37	29967540
495	Ubiquitination	LVDDCEYKRGIKETT CHHHCCHHCCCCCCE	23.12	29967540
529	Ubiquitination	HKFNNLIKLEESGWQ HHHHCCEEHHHHCCC	53.68	29967540
547	Ubiquitination	NMNHNMNKNVFRKKV CCCCCCCHHHHHHHH	43.66	29967540
553	Ubiquitination	NKNVFRKKVVSGIAS CHHHHHHHHHHCCCC	43.54	29967540
556	Phosphorylation	VFRKKVVSGIASKPK HHHHHHHHCCCCCCC	27.72	25262027
560	Phosphorylation	KVVSGIASKPKQDDA HHHHCCCCCCCCCHH	47.79	20860994
561	Ubiquitination	VVSGIASKPKQDDAG HHHCCCCCCCCCHHH	47.41	24816145
563	Ubiquitination	SGIASKPKQDDAGRI HCCCCCCCCCHHHHH	70.83	29967540
580	Ubiquitination	RNRLAAIKNAMRERI HHHHHHHHHHHHHHH	33.65	24816145
580	Acetylation	RNRLAAIKNAMRERI HHHHHHHHHHHHHHH	33.65	25953088
618	Phosphorylation	AGFFRVESPVKLFSG CCCEEECCCEEEEEC	31.94	23401153
624	Phosphorylation	ESPVKLFSGLSVSSE CCCEEEEECCEECCC	49.62	21712546
627	Phosphorylation	VKLFSGLSVSSEGPS EEEEECCEECCCCHH	24.39	25159151
629	Phosphorylation	LFSGLSVSSEGPSQR EEECCEECCCCHHHC	21.21	25159151
630	Phosphorylation	FSGLSVSSEGPSQRL EECCEECCCCHHHCC	44.40	25159151
634	Phosphorylation	SVSSEGPSQRLGTPK EECCCCHHHCCCCCH	38.50	25159151
639	Phosphorylation	GPSQRLGTPKSVNKA CHHHCCCCCHHHHHH	31.94	22167270
642	Phosphorylation	QRLGTPKSVNKAVSQ HCCCCCHHHHHHHHH	31.93	22167270
645	Ubiquitination	GTPKSVNKAVSQSRN CCCHHHHHHHHHHHH	48.27	24816145
648	Phosphorylation	KSVNKAVSQSRNEMG HHHHHHHHHHHHCCC	27.57	26074081
650	Phosphorylation	VNKAVSQSRNEMGIP HHHHHHHHHHCCCCC	29.57	26074081
654	Sulfoxidation	VSQSRNEMGIPQQTT HHHHHHCCCCCCCCC	7.23	21406390
660	Phosphorylation	EMGIPQQTTSPENAG CCCCCCCCCCCCCCC	24.80	23401153
661	Phosphorylation	MGIPQQTTSPENAGP CCCCCCCCCCCCCCC	37.64	30278072
662	Phosphorylation	GIPQQTTSPENAGPQ CCCCCCCCCCCCCCC	33.34	25159151
671	Phosphorylation	ENAGPQNTKSEHVKK CCCCCCCCCCHHHHH	30.60	30278072
673	Phosphorylation	AGPQNTKSEHVKKTL CCCCCCCCHHHHHHH	30.78	26074081
679	Phosphorylation	KSEHVKKTLFLSIPE CCHHHHHHHEEECCC	19.61	23090842
683	Phosphorylation	VKKTLFLSIPESRSS HHHHHEEECCCCHHC	28.85	23090842
687	Phosphorylation	LFLSIPESRSSIEDA HEEECCCCHHCHHHH	31.91	18669648
689	Phosphorylation	LSIPESRSSIEDAQC EECCCCHHCHHHHCC	44.97	30266825
690	Phosphorylation	SIPESRSSIEDAQCP ECCCCHHCHHHHCCC	28.96	30266825
711	Ubiquitination	EENHVVNKTDLKVDC HHCCCCCCCCCEEEC	31.63	29967540
715	Ubiquitination	VVNKTDLKVDCLSSE CCCCCCCEEECCCCC	38.55	29967540
720	Phosphorylation	DLKVDCLSSERMSLP CCEEECCCCCCCCHH	36.16	30576142
721	Phosphorylation	LKVDCLSSERMSLPL CEEECCCCCCCCHHH	19.10	30576142
725	Phosphorylation	CLSSERMSLPLLAGG CCCCCCCCHHHHCCC	32.81	30266825
746	Phosphorylation	TNKKEGISDVVEGME CCHHCCCCHHHHHCC	34.90	27080861
756	Phosphorylation	VEGMELNSSITSQDV HHHCCCCCCCCCHHH	35.42	26074081
757	Phosphorylation	EGMELNSSITSQDVL HHCCCCCCCCCHHHH	28.89	15987997
759	Phosphorylation	MELNSSITSQDVLMS CCCCCCCCCHHHHHC	23.45	26074081
760	Phosphorylation	ELNSSITSQDVLMSS CCCCCCCCHHHHHCC	23.78	30278072
766	Phosphorylation	TSQDVLMSSPEKNTA CCHHHHHCCCCCCCC	38.28	22199227
767	Phosphorylation	SQDVLMSSPEKNTAS CHHHHHCCCCCCCCC	24.10	30576142
772	Phosphorylation	MSSPEKNTASQNSIL HCCCCCCCCCCHHHH	38.46	23663014
774	Phosphorylation	SPEKNTASQNSILEE CCCCCCCCCHHHHHC	28.05	17525332
777	Phosphorylation	KNTASQNSILEEGET CCCCCCHHHHHCCCC	22.40	19664994
784	Phosphorylation	SILEEGETKISQSEL HHHHCCCCCCCHHHH	44.53	21712546
785	Ubiquitination	ILEEGETKISQSELF HHHCCCCCCCHHHHC	35.74	32015554
787	Phosphorylation	EEGETKISQSELFDN HCCCCCCCHHHHCCC	29.25	25159151
789	Phosphorylation	GETKISQSELFDNKS CCCCCCHHHHCCCCC	29.49	25159151
796	Phosphorylation	SELFDNKSLTTECHL HHHCCCCCCCCEEEE	36.88	25159151
798	Phosphorylation	LFDNKSLTTECHLLD HCCCCCCCCEEEECC	27.86	23898821
799	Phosphorylation	FDNKSLTTECHLLDS CCCCCCCCEEEECCC	41.74	21082442
806	Phosphorylation	TECHLLDSPGLNCSN CEEEECCCCCCCCCC	22.34	23401153
809 (in isoform 3)	Phosphorylation	-	7.11	28796482
811 (in isoform 3)	Phosphorylation	-	5.10	28796482
812	Phosphorylation	DSPGLNCSNPFTQLE CCCCCCCCCHHHHHH	46.60	25159151
816	Phosphorylation	LNCSNPFTQLERRHQ CCCCCHHHHHHHHHH	33.24	24732914
822 (in isoform 3)	Phosphorylation	-	43.53	19691289
823 (in isoform 3)	Phosphorylation	-	42.21	19691289
826 (in isoform 3)	Phosphorylation	-	12.18	19691289
827 (in isoform 3)	Phosphorylation	-	29.58	19691289
828 (in isoform 3)	Phosphorylation	-	22.34	19691289
830	Phosphorylation	QEHARHISFGGNLIT HHHHHCEEECCEEEE	16.24	25159151
830 (in isoform 3)	Phosphorylation	-	16.24	19691289
836 (in isoform 3)	Phosphorylation	-	4.19	25247763
837	Phosphorylation	SFGGNLITFSPLQPG EECCEEEEECCCCCC	22.64	28450419
839	Phosphorylation	GGNLITFSPLQPGEF CCEEEEECCCCCCCC	18.95	25159151

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
67	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
329	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot
401	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot
402	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot
618	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
627	S	Phosphorylation	Kinase	AURA	O14965	PSP
639	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot
642	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
725	S	Phosphorylation	Kinase	AURA	O14965	PSP
757	S	Phosphorylation	Kinase	AURA	O14965	PSP
759	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot
830	S	Phosphorylation	Kinase	AURA	O14965	PSP
839	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	FBXO7	Q9Y3I1	PMID:15145941

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DLGP5_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 DLGP5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CDK1_HUMAN	CDK1	physical	15145941
A4_HUMAN	APP	physical	21832049
AURKA_HUMAN	AURKA	physical	22939629
MTUS2_HUMAN	MTUS2	physical	25416956
IMB1_HUMAN	KPNB1	physical	26496610
RSRC1_HUMAN	RSRC1	physical	26496610

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 DLGP5_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-332; SER-662 ANDSER-830, AND MASS 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 THR-326; THR-329; THR-338;THR-344; SER-618; THR-639; SER-642; SER-662; SER-725; SER-777;THR-784; THR-799; SER-806 AND SER-812, AND MASS SPECTROMETRY.	18669648 [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-806; SER-812; SER-830AND SER-839, AND MASS SPECTROMETRY.	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 SER-618; SER-662; SER-774;SER-777; SER-787 AND SER-789, AND MASS SPECTROMETRY.	19007248 [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-774 AND SER-777, ANDMASS SPECTROMETRY.	17525332 [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-662; SER-689 ANDSER-777, AND MASS SPECTROMETRY.	16565220 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-639; SER-642; SER-662AND SER-777, AND MASS SPECTROMETRY.	16964243 [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-839, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Phosphorylation and stabilization of HURP by Aurora-A: implication ofHURP as a transforming target of Aurora-A."; Yu C.T., Hsu J.M., Lee Y.C., Tsou A.P., Chou C.K., Huang C.Y.; Mol. Cell. Biol. 25:5789-5800(2005). Cited for: PHOSPHORYLATION AT SER-627; SER-725; SER-757 AND SER-830.	15987997 [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-662, AND MASSSPECTROMETRY.	15302935 [Abstract]
"Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-phosphorylated hepatoma up-regulated protein (HURP) proteolysis by aproline-rich region."; Hsu J.-M., Lee Y.-C.G., Yu C.-T.R., Huang C.-Y.F.; J. Biol. Chem. 279:32592-32602(2004). Cited for: FUNCTION, INTERACTION WITH CDK1; FBXO7 AND SCF COMPLEX,UBIQUITINATION, AND PHOSPHORYLATION AT SER-67; THR-329; THR-401;THR-402; SER-618; THR-639; SER-642; THR-759 AND SER-839.	15145941 [Abstract]