PSIP1_HUMAN - dbPTM
PSIP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PSIP1_HUMAN
UniProt AC O75475
Protein Name PC4 and SFRS1-interacting protein
Gene Name PSIP1
Organism Homo sapiens (Human).
Sequence Length 530
Subcellular Localization Nucleus . Remains chromatin-associated throughout the cell cycle.
Protein Description Transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. Involved in particular in lens epithelial cell gene regulation and stress responses. May play an important role in lens epithelial to fiber cell terminal differentiation. May play a protective role during stress-induced apoptosis. Isoform 2 is a more general and stronger transcriptional coactivator. Isoform 2 may also act as an adapter to coordinate pre-mRNA splicing. Cellular cofactor for lentiviral integration..
Protein Sequence MTRDFKPGDLIFAKMKGYPHWPARVDEVPDGAVKPPTNKLPIFFFGTHETAFLGPKDIFPYSENKEKYGKPNKRKGFNEGLWEIDNNPKVKFSSQQAATKQSNASSDVEVEEKETSVSKEDTDHEEKASNEDVTKAVDITTPKAARRGRKRKAEKQVETEEAGVVTTATASVNLKVSPKRGRPAATEVKIPKPRGRPKMVKQPCPSESDIITEEDKSKKKGQEEKQPKKQPKKDEEGQKEEDKPRKEPDKKEGKKEVESKRKNLAKTGVTSTSDSEEEGDDQEGEKKRKGGRNFQTAHRRNMLKGQHEKEAADRKRKQEEQMETEQQNKDEGKKPEVKKVEKKRETSMDSRLQRIHAEIKNSLKIDNLDVNRCIEALDELASLQVTMQQAQKHTEMITTLKKIRRFKVSQVIMEKSTMLYNKFKNMFLVGEGDSVITQVLNKSLAEQRQHEEANKTKDQGKKGPNKKLEKEQTGSKTLNGGSDAQDGNQPQHNGESNEDSKDNHEASTKKKPSSEERETEISLKDSTLDN
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
6Acetylation--MTRDFKPGDLIFA
--CCCCCCCCCEEEE
52.9925953088
6Ubiquitination--MTRDFKPGDLIFA
--CCCCCCCCCEEEE
52.9923000965
6 (in isoform 1)Ubiquitination-52.9921890473
6 (in isoform 2)Ubiquitination-52.9921890473
14AcetylationPGDLIFAKMKGYPHW
CCCEEEEECCCCCCC
30.3226051181
14UbiquitinationPGDLIFAKMKGYPHW
CCCEEEEECCCCCCC
30.32-
16MalonylationDLIFAKMKGYPHWPA
CEEEEECCCCCCCCC
55.3626320211
16UbiquitinationDLIFAKMKGYPHWPA
CEEEEECCCCCCCCC
55.3632015554
18PhosphorylationIFAKMKGYPHWPARV
EEEECCCCCCCCCCC
6.0925159151
34AcetylationEVPDGAVKPPTNKLP
CCCCCCCCCCCCCCC
44.7525953088
34UbiquitinationEVPDGAVKPPTNKLP
CCCCCCCCCCCCCCC
44.7527667366
34 (in isoform 1)Ubiquitination-44.7521890473
34 (in isoform 2)Ubiquitination-44.7521890473
37O-linked_GlycosylationDGAVKPPTNKLPIFF
CCCCCCCCCCCCEEE
54.2123301498
392-HydroxyisobutyrylationAVKPPTNKLPIFFFG
CCCCCCCCCCEEEEE
59.11-
39UbiquitinationAVKPPTNKLPIFFFG
CCCCCCCCCCEEEEE
59.1122817900
61PhosphorylationGPKDIFPYSENKEKY
CHHHCCCCCCCHHHH
20.1930576142
62PhosphorylationPKDIFPYSENKEKYG
HHHCCCCCCCHHHHC
34.6225159151
65AcetylationIFPYSENKEKYGKPN
CCCCCCCHHHHCCCC
52.0826051181
65UbiquitinationIFPYSENKEKYGKPN
CCCCCCCHHHHCCCC
52.0832015554
70UbiquitinationENKEKYGKPNKRKGF
CCHHHHCCCCCCCCC
42.1822817900
73UbiquitinationEKYGKPNKRKGFNEG
HHHCCCCCCCCCCCC
65.1022817900
75SumoylationYGKPNKRKGFNEGLW
HCCCCCCCCCCCCCE
70.26-
75SumoylationYGKPNKRKGFNEGLW
HCCCCCCCCCCCCCE
70.2628112733
75UbiquitinationYGKPNKRKGFNEGLW
HCCCCCCCCCCCCCE
70.2621890473
75 (in isoform 1)Ubiquitination-70.2621890473
75 (in isoform 2)Ubiquitination-70.2621890473
89AcetylationWEIDNNPKVKFSSQQ
EECCCCCCCCCCCHH
61.2526051181
89UbiquitinationWEIDNNPKVKFSSQQ
EECCCCCCCCCCCHH
61.2521890473
89 (in isoform 1)Ubiquitination-61.2521890473
89 (in isoform 2)Ubiquitination-61.2521890473
91AcetylationIDNNPKVKFSSQQAA
CCCCCCCCCCCHHHH
45.7325953088
91UbiquitinationIDNNPKVKFSSQQAA
CCCCCCCCCCCHHHH
45.73-
93PhosphorylationNNPKVKFSSQQAATK
CCCCCCCCCHHHHHC
22.8623663014
94PhosphorylationNPKVKFSSQQAATKQ
CCCCCCCCHHHHHCC
29.4628450419
99PhosphorylationFSSQQAATKQSNASS
CCCHHHHHCCCCCCC
32.4123663014
100AcetylationSSQQAATKQSNASSD
CCHHHHHCCCCCCCC
47.1826051181
100UbiquitinationSSQQAATKQSNASSD
CCHHHHHCCCCCCCC
47.1822817900
100 (in isoform 1)Ubiquitination-47.1821890473
100 (in isoform 2)Ubiquitination-47.1821890473
102PhosphorylationQQAATKQSNASSDVE
HHHHHCCCCCCCCCE
35.6023927012
105PhosphorylationATKQSNASSDVEVEE
HHCCCCCCCCCEEEE
31.1829255136
106PhosphorylationTKQSNASSDVEVEEK
HCCCCCCCCCEEEEH
43.1729255136
113UbiquitinationSDVEVEEKETSVSKE
CCCEEEEHHCCCCHH
53.4333845483
115PhosphorylationVEVEEKETSVSKEDT
CEEEEHHCCCCHHHC
45.5623401153
116PhosphorylationEVEEKETSVSKEDTD
EEEEHHCCCCHHHCC
26.0329255136
118PhosphorylationEEKETSVSKEDTDHE
EEHHCCCCHHHCCHH
30.0529255136
119AcetylationEKETSVSKEDTDHEE
EHHCCCCHHHCCHHH
58.4126051181
119UbiquitinationEKETSVSKEDTDHEE
EHHCCCCHHHCCHHH
58.4133845483
122PhosphorylationTSVSKEDTDHEEKAS
CCCCHHHCCHHHHHC
40.1129255136
127UbiquitinationEDTDHEEKASNEDVT
HHCCHHHHHCCCCCH
54.8833845483
129PhosphorylationTDHEEKASNEDVTKA
CCHHHHHCCCCCHHH
52.3929255136
134PhosphorylationKASNEDVTKAVDITT
HHCCCCCHHHHHCCC
26.1322167270
135AcetylationASNEDVTKAVDITTP
HCCCCCHHHHHCCCH
46.3826051181
135UbiquitinationASNEDVTKAVDITTP
HCCCCCHHHHHCCCH
46.3822817900
135 (in isoform 1)Ubiquitination-46.3821890473
135 (in isoform 2)Ubiquitination-46.3821890473
140PhosphorylationVTKAVDITTPKAARR
CHHHHHCCCHHHHHH
32.3623401153
141PhosphorylationTKAVDITTPKAARRG
HHHHHCCCHHHHHHH
24.1129255136
143UbiquitinationAVDITTPKAARRGRK
HHHCCCHHHHHHHCH
53.2233845483
159PhosphorylationKAEKQVETEEAGVVT
HHHHHHCHHCCCEEE
40.0228176443
166PhosphorylationTEEAGVVTTATASVN
HHCCCEEEEEEEEEE
14.3328176443
167PhosphorylationEEAGVVTTATASVNL
HCCCEEEEEEEEEEE
15.4828176443
169PhosphorylationAGVVTTATASVNLKV
CCEEEEEEEEEEEEE
19.8528176443
171PhosphorylationVVTTATASVNLKVSP
EEEEEEEEEEEEECC
13.7430266825
177PhosphorylationASVNLKVSPKRGRPA
EEEEEEECCCCCCCC
24.1022167270
180UbiquitinationNLKVSPKRGRPAATE
EEEECCCCCCCCCCE
50.1433845483
186PhosphorylationKRGRPAATEVKIPKP
CCCCCCCCEEECCCC
43.3426074081
189UbiquitinationRPAATEVKIPKPRGR
CCCCCEEECCCCCCC
47.2433845483
192UbiquitinationATEVKIPKPRGRPKM
CCEEECCCCCCCCCC
51.3133845483
201AcetylationRGRPKMVKQPCPSES
CCCCCCCCCCCCCHH
45.0525953088
201MalonylationRGRPKMVKQPCPSES
CCCCCCCCCCCCCHH
45.0526320211
201MethylationRGRPKMVKQPCPSES
CCCCCCCCCCCCCHH
45.05115972479
201UbiquitinationRGRPKMVKQPCPSES
CCCCCCCCCCCCCHH
45.0533845483
204S-palmitoylationPKMVKQPCPSESDII
CCCCCCCCCCHHHCC
5.5421044946
206O-linked_GlycosylationMVKQPCPSESDIITE
CCCCCCCCHHHCCCH
57.3523301498
206PhosphorylationMVKQPCPSESDIITE
CCCCCCCCHHHCCCH
57.3523401153
207UbiquitinationVKQPCPSESDIITEE
CCCCCCCHHHCCCHH
37.2633845483
208PhosphorylationKQPCPSESDIITEED
CCCCCCHHHCCCHHH
38.1530266825
212PhosphorylationPSESDIITEEDKSKK
CCHHHCCCHHHHHHC
33.3925159151
216AcetylationDIITEEDKSKKKGQE
HCCCHHHHHHCCCCH
68.4123749302
216UbiquitinationDIITEEDKSKKKGQE
HCCCHHHHHHCCCCH
68.4133845483
217PhosphorylationIITEEDKSKKKGQEE
CCCHHHHHHCCCCHH
63.1329083192
220AcetylationEEDKSKKKGQEEKQP
HHHHHHCCCCHHCCC
70.3512435649
225AcetylationKKKGQEEKQPKKQPK
HCCCCHHCCCCCCCC
71.7612435659
228AcetylationGQEEKQPKKQPKKDE
CCHHCCCCCCCCCCC
62.6412435669
229AcetylationQEEKQPKKQPKKDEE
CHHCCCCCCCCCCCC
77.7619810387
232AcetylationKQPKKQPKKDEEGQK
CCCCCCCCCCCCCCC
71.0620167786
242UbiquitinationEEGQKEEDKPRKEPD
CCCCCCCCCCCCCCC
68.3124816145
250SumoylationKPRKEPDKKEGKKEV
CCCCCCCHHHHHHHH
64.54-
250SumoylationKPRKEPDKKEGKKEV
CCCCCCCHHHHHHHH
64.54-
251SumoylationPRKEPDKKEGKKEVE
CCCCCCHHHHHHHHH
78.18-
251UbiquitinationPRKEPDKKEGKKEVE
CCCCCCHHHHHHHHH
78.1824816145
254SumoylationEPDKKEGKKEVESKR
CCCHHHHHHHHHHHH
47.02-
254SumoylationEPDKKEGKKEVESKR
CCCHHHHHHHHHHHH
47.02-
255SumoylationPDKKEGKKEVESKRK
CCHHHHHHHHHHHHH
77.25-
258PhosphorylationKEGKKEVESKRKNLA
HHHHHHHHHHHHHHH
52.1932142685
259PhosphorylationEGKKEVESKRKNLAK
HHHHHHHHHHHHHHH
42.8328258704
263PhosphorylationEVESKRKNLAKTGVT
HHHHHHHHHHHHCCC
49.6232645325
264PhosphorylationVESKRKNLAKTGVTS
HHHHHHHHHHHCCCC
6.0832142685
266PhosphorylationSKRKNLAKTGVTSTS
HHHHHHHHHCCCCCC
49.3232142685
267PhosphorylationKRKNLAKTGVTSTSD
HHHHHHHHCCCCCCC
31.1423927012
270PhosphorylationNLAKTGVTSTSDSEE
HHHHHCCCCCCCCCC
27.8626846344
271PhosphorylationLAKTGVTSTSDSEEE
HHHHCCCCCCCCCCC
24.4126846344
272PhosphorylationAKTGVTSTSDSEEEG
HHHCCCCCCCCCCCC
27.4729255136
273PhosphorylationKTGVTSTSDSEEEGD
HHCCCCCCCCCCCCC
38.6229255136
275PhosphorylationGVTSTSDSEEEGDDQ
CCCCCCCCCCCCCCC
46.8329255136
295UbiquitinationRKGGRNFQTAHRRNM
CCCCCCHHHHHHHHH
41.1324816145
304UbiquitinationAHRRNMLKGQHEKEA
HHHHHHHHHHHHHHH
45.8424816145
324PhosphorylationKQEEQMETEQQNKDE
HHHHHHHHHHHHHHC
33.48-
333AcetylationQQNKDEGKKPEVKKV
HHHHHCCCCHHHHHH
64.2126051181
346PhosphorylationKVEKKRETSMDSRLQ
HHHHHHHHCHHHHHH
33.1326074081
347PhosphorylationVEKKRETSMDSRLQR
HHHHHHHCHHHHHHH
18.8130576142
350PhosphorylationKRETSMDSRLQRIHA
HHHHCHHHHHHHHHH
26.6726074081
360AcetylationQRIHAEIKNSLKIDN
HHHHHHHHHCCCCCC
31.8026822725
360UbiquitinationQRIHAEIKNSLKIDN
HHHHHHHHHCCCCCC
31.8023000965
364SumoylationAEIKNSLKIDNLDVN
HHHHHCCCCCCCCHH
48.08-
364AcetylationAEIKNSLKIDNLDVN
HHHHHCCCCCCCCHH
48.0826051181
364SumoylationAEIKNSLKIDNLDVN
HHHHHCCCCCCCCHH
48.08-
364UbiquitinationAEIKNSLKIDNLDVN
HHHHHCCCCCCCCHH
48.0823000965
364 (in isoform 1)Ubiquitination-48.0821890473
373GlutathionylationDNLDVNRCIEALDEL
CCCCHHHHHHHHHHH
2.5122555962
392AcetylationVTMQQAQKHTEMITT
HHHHHHHHHHHHHHH
56.3521466224
394PhosphorylationMQQAQKHTEMITTLK
HHHHHHHHHHHHHHH
33.9920068231
398PhosphorylationQKHTEMITTLKKIRR
HHHHHHHHHHHHHHC
25.4320068231
399PhosphorylationKHTEMITTLKKIRRF
HHHHHHHHHHHHHCC
26.1720068231
401AcetylationTEMITTLKKIRRFKV
HHHHHHHHHHHCCCH
44.0221466224
401UbiquitinationTEMITTLKKIRRFKV
HHHHHHHHHHHCCCH
44.0232015554
402UbiquitinationEMITTLKKIRRFKVS
HHHHHHHHHHCCCHH
44.5522817900
4072-HydroxyisobutyrylationLKKIRRFKVSQVIME
HHHHHCCCHHHHHHH
38.88-
407MalonylationLKKIRRFKVSQVIME
HHHHHCCCHHHHHHH
38.8826320211
407UbiquitinationLKKIRRFKVSQVIME
HHHHHCCCHHHHHHH
38.8822817900
407 (in isoform 1)Ubiquitination-38.8821890473
409PhosphorylationKIRRFKVSQVIMEKS
HHHCCCHHHHHHHHH
21.2223401153
415UbiquitinationVSQVIMEKSTMLYNK
HHHHHHHHHHHHHHH
33.5723000965
415 (in isoform 1)Ubiquitination-33.5721890473
416PhosphorylationSQVIMEKSTMLYNKF
HHHHHHHHHHHHHHH
13.0223401153
417PhosphorylationQVIMEKSTMLYNKFK
HHHHHHHHHHHHHHC
23.4323401153
420PhosphorylationMEKSTMLYNKFKNMF
HHHHHHHHHHHCCEE
12.8923401153
422AcetylationKSTMLYNKFKNMFLV
HHHHHHHHHCCEEEE
44.1325953088
422UbiquitinationKSTMLYNKFKNMFLV
HHHHHHHHHCCEEEE
44.1322817900
422 (in isoform 1)Ubiquitination-44.1321890473
424UbiquitinationTMLYNKFKNMFLVGE
HHHHHHHCCEEEECC
49.4621890473
424 (in isoform 1)Ubiquitination-49.4621890473
426SulfoxidationLYNKFKNMFLVGEGD
HHHHHCCEEEECCCC
2.5728183972
434PhosphorylationFLVGEGDSVITQVLN
EEECCCCHHHHHHHC
26.6926055452
437PhosphorylationGEGDSVITQVLNKSL
CCCCHHHHHHHCHHH
15.5217525332
442NeddylationVITQVLNKSLAEQRQ
HHHHHHCHHHHHHHH
42.5632015554
442UbiquitinationVITQVLNKSLAEQRQ
HHHHHHCHHHHHHHH
42.5623000965
443PhosphorylationITQVLNKSLAEQRQH
HHHHHCHHHHHHHHH
31.5725159151
461AcetylationNKTKDQGKKGPNKKL
HHHHHCCCCCCCCCC
49.267663193
462AcetylationKTKDQGKKGPNKKLE
HHHHCCCCCCCCCCC
83.12133527
466AcetylationQGKKGPNKKLEKEQT
CCCCCCCCCCCHHHC
62.977963435
476AcetylationEKEQTGSKTLNGGSD
CHHHCCCCCCCCCCC
59.3826051181
477PhosphorylationKEQTGSKTLNGGSDA
HHHCCCCCCCCCCCC
27.4425002506
482PhosphorylationSKTLNGGSDAQDGNQ
CCCCCCCCCCCCCCC
31.0428450419
496PhosphorylationQPQHNGESNEDSKDN
CCCCCCCCCCCCCCC
47.0928450419
500PhosphorylationNGESNEDSKDNHEAS
CCCCCCCCCCCCHHH
35.4125159151
507PhosphorylationSKDNHEASTKKKPSS
CCCCCHHHCCCCCCH
37.4623186163
508PhosphorylationKDNHEASTKKKPSSE
CCCCHHHCCCCCCHH
54.6620068231
513PhosphorylationASTKKKPSSEERETE
HHCCCCCCHHHHHHC
60.3025159151
514PhosphorylationSTKKKPSSEERETEI
HCCCCCCHHHHHHCE
52.5923401153
517CitrullinationKKPSSEERETEISLK
CCCCHHHHHHCEECC
52.68-
517CitrullinationKKPSSEERETEISLK
CCCCHHHHHHCEECC
52.68-
519PhosphorylationPSSEERETEISLKDS
CCHHHHHHCEECCCC
44.8530266825
522PhosphorylationEERETEISLKDSTLD
HHHHHCEECCCCCCC
24.1230266825
524AcetylationRETEISLKDSTLDN-
HHHCEECCCCCCCC-
42.7326051181
524UbiquitinationRETEISLKDSTLDN-
HHHCEECCCCCCCC-
42.7322817900
524 (in isoform 1)Ubiquitination-42.7321890473
526PhosphorylationTEISLKDSTLDN---
HCEECCCCCCCC---
29.3125159151
527PhosphorylationEISLKDSTLDN----
CEECCCCCCCC----
48.5425159151

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
206SPhosphorylationKinaseCDC7O00311
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PSIP1_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 PSIP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRSF1_HUMANSRSF1physical
9885563
POL_HV1H2gag-polphysical
16260736
POL_HV1H2gag-polphysical
15895093
POL_HV1H2gag-polphysical
21454548
RS24_HUMANRPS24physical
22939629
RL6_HUMANRPL6physical
22939629
SON_HUMANSONphysical
22939629
SPB1_HUMANFTSJ3physical
22939629
TRA2B_HUMANTRA2Bphysical
22939629
SAP18_HUMANSAP18physical
22939629
RRS1_HUMANRRS1physical
22939629
TPBG_HUMANTPBGphysical
22939629
ZCH18_HUMANZC3H18physical
22939629
RS11_HUMANRPS11physical
22939629
TR150_HUMANTHRAP3physical
22939629
U2AF1_HUMANU2AF1physical
22939629
SP16H_HUMANSUPT16Hphysical
22939629
HMGA1_HUMANHMGA1physical
18850631
HMGA2_HUMANHMGA2physical
18850631
SUMO1_HUMANSUMO1physical
22748127

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 PSIP1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-106; THR-141; THR-167;SER-177; SER-273; SER-275 AND SER-522, AND MASS SPECTROMETRY.
"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-105; SER-106; THR-141;THR-270; THR-272; SER-273 AND SER-275, AND MASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273 AND SER-275, ANDMASS SPECTROMETRY.
"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-106; THR-141; SER-271;THR-272; SER-273; SER-275; SER-434; SER-443; SER-522 AND THR-527, ANDMASS SPECTROMETRY.
"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-106; THR-122; SER-129;SER-273 AND SER-275, AND MASS SPECTROMETRY.
"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 THR-122; SER-273 ANDSER-275, AND MASS SPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275, AND MASSSPECTROMETRY.
"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-106, AND MASSSPECTROMETRY.
"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 THR-437, AND MASSSPECTROMETRY.
"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-141, AND MASSSPECTROMETRY.

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