ARI4B_HUMAN - dbPTM
ARI4B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARI4B_HUMAN
UniProt AC Q4LE39
Protein Name AT-rich interactive domain-containing protein 4B
Gene Name ARID4B
Organism Homo sapiens (Human).
Sequence Length 1312
Subcellular Localization Nucleus . Cytoplasm . Cytoplasmic in breast cancer cells.
Protein Description Acts as a transcriptional repressor. May function in the assembly and/or enzymatic activity of the Sin3A corepressor complex or in mediating interactions between the complex and other regulatory complexes..
Protein Sequence MKALDEPPYLTVGTDVSAKYRGAFCEAKIKTAKRLVKVKVTFRHDSSTVEVQDDHIKGPLKVGAIVEVKNLDGAYQEAVINKLTDASWYTVVFDDGDEKTLRRSSLCLKGERHFAESETLDQLPLTNPEHFGTPVIGKKTNRGRRSNHIPEEESSSSSSDEDEDDRKQIDELLGKVVCVDYISLDKKKALWFPALVVCPDCSDEIAVKKDNILVRSFKDGKFTSVPRKDVHEITSDTAPKPDAVLKQAFEQALEFHKSRTIPANWKTELKEDSSSSEAEEEEEEEDDEKEKEDNSSEEEEEIEPFPEERENFLQQLYKFMEDRGTPINKRPVLGYRNLNLFKLFRLVHKLGGFDNIESGAVWKQVYQDLGIPVLNSAAGYNVKCAYKKYLYGFEEYCRSANIEFQMALPEKVVNKQCKECENVKEIKVKEENETEIKEIKMEEERNIIPREEKPIEDEIERKENIKPSLGSKKNLLESIPTHSDQEKEVNIKKPEDNENLDDKDDDTTRVDESLNIKVEAEEEKAKSGDETNKEEDEDDEEAEEEEEEEEEEEDEDDDDNNEEEEFECYPPGMKVQVRYGRGKNQKMYEASIKDSDVEGGEVLYLVHYCGWNVRYDEWIKADKIVRPADKNVPKIKHRKKIKNKLDKEKDKDEKYSPKNCKLRRLSKPPFQTNPSPEMVSKLDLTDAKNSDTAHIKSIEITSILNGLQASESSAEDSEQEDERGAQDMDNNGKEESKIDHLTNNRNDLISKEEQNSSSLLEENKVHADLVISKPVSKSPERLRKDIEVLSEDTDYEEDEVTKKRKDVKKDTTDKSSKPQIKRGKRRYCNTEECLKTGSPGKKEEKAKNKESLCMENSSNSSSDEDEEETKAKMTPTKKYNGLEEKRKSLRTTGFYSGFSEVAEKRIKLLNNSDERLQNSRAKDRKDVWSSIQGQWPKKTLKELFSDSDTEAAASPPHPAPEEGVAEESLQTVAEEESCSPSVELEKPPPVNVDSKPIEEKTVEVNDRKAEFPSSGSNSVLNTPPTTPESPSSVTVTEGSRQQSSVTVSEPLAPNQEEVRSIKSETDSTIEVDSVAGELQDLQSEGNSSPAGFDASVSSSSSNQPEPEHPEKACTGQKRVKDAQGGGSSSKKQKRSHKATVVNNKKKGKGTNSSDSEELSAGESITKSQPVKSVSTGMKSHSTKSPARTQSPGKCGKNGDKDPDLKEPSNRLPKVYKWSFQMSDLENMTSAERITILQEKLQEIRKHYLSLKSEVASIDRRRKRLKKKERESAATSSSSSSPSSSSITAAVMLTLAEPSMSSASQNGMSVECR
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
9PhosphorylationKALDEPPYLTVGTDV
CCCCCCCEEECCCCC
26.2223663014
11PhosphorylationLDEPPYLTVGTDVSA
CCCCCEEECCCCCCH
15.8523663014
14PhosphorylationPPYLTVGTDVSAKYR
CCEEECCCCCCHHHC
28.9723663014
17PhosphorylationLTVGTDVSAKYRGAF
EECCCCCCHHHCCCC
23.1223663014
20PhosphorylationGTDVSAKYRGAFCEA
CCCCCHHHCCCCHHH
17.6222817900
28UbiquitinationRGAFCEAKIKTAKRL
CCCCHHHHHHHCCEE
23.57-
57UbiquitinationEVQDDHIKGPLKVGA
EEECCCCCCCCEEEE
51.5629967540
89PhosphorylationKLTDASWYTVVFDDG
HCCCCCCEEEEECCC
6.27-
90PhosphorylationLTDASWYTVVFDDGD
CCCCCCEEEEECCCC
12.16-
104PhosphorylationDEKTLRRSSLCLKGE
CCEEEEHHEEHHCCC
22.6430266825
105PhosphorylationEKTLRRSSLCLKGER
CEEEEHHEEHHCCCC
22.6930266825
109AcetylationRRSSLCLKGERHFAE
EHHEEHHCCCCCCCC
58.7026051181
117PhosphorylationGERHFAESETLDQLP
CCCCCCCCCCCCCCC
32.2423312004
119PhosphorylationRHFAESETLDQLPLT
CCCCCCCCCCCCCCC
44.9329255136
126PhosphorylationTLDQLPLTNPEHFGT
CCCCCCCCCHHHCCC
46.9529255136
133PhosphorylationTNPEHFGTPVIGKKT
CCHHHCCCCCCCCCC
17.2829255136
138AcetylationFGTPVIGKKTNRGRR
CCCCCCCCCCCCCCC
45.3525953088
154PhosphorylationNHIPEEESSSSSSDE
CCCCCCCCCCCCCCC
38.5125137130
155PhosphorylationHIPEEESSSSSSDED
CCCCCCCCCCCCCCC
37.2025137130
156PhosphorylationIPEEESSSSSSDEDE
CCCCCCCCCCCCCCH
43.4425137130
157PhosphorylationPEEESSSSSSDEDED
CCCCCCCCCCCCCHH
35.4925137130
158PhosphorylationEEESSSSSSDEDEDD
CCCCCCCCCCCCHHH
43.7025137130
159PhosphorylationEESSSSSSDEDEDDR
CCCCCCCCCCCHHHH
47.1425137130
223PhosphorylationSFKDGKFTSVPRKDV
EECCCCCCCCCCCHH
32.0924719451
257UbiquitinationEQALEFHKSRTIPAN
HHHHHHHHHCCCCCC
47.1332015554
258PhosphorylationQALEFHKSRTIPANW
HHHHHHHHCCCCCCC
26.5322210691
260PhosphorylationLEFHKSRTIPANWKT
HHHHHHCCCCCCCCH
38.1022210691
267PhosphorylationTIPANWKTELKEDSS
CCCCCCCHHCCCCCC
37.8627732954
273PhosphorylationKTELKEDSSSSEAEE
CHHCCCCCCCCCHHH
32.9628985074
274PhosphorylationTELKEDSSSSEAEEE
HHCCCCCCCCCHHHH
50.6425056879
275PhosphorylationELKEDSSSSEAEEEE
HCCCCCCCCCHHHHH
35.8325056879
276PhosphorylationLKEDSSSSEAEEEEE
CCCCCCCCCHHHHHH
42.6528985074
295PhosphorylationEKEKEDNSSEEEEEI
HHHHCCCCCHHHHHH
51.9928355574
296PhosphorylationKEKEDNSSEEEEEIE
HHHCCCCCHHHHHHC
56.1128355574
317PhosphorylationENFLQQLYKFMEDRG
HHHHHHHHHHHHHCC
9.6122115753
335PhosphorylationNKRPVLGYRNLNLFK
CCCCCCCCCCCCHHH
7.68-
388AcetylationNVKCAYKKYLYGFEE
CCCHHHHHHHHCHHH
28.0126051181
389PhosphorylationVKCAYKKYLYGFEEY
CCHHHHHHHHCHHHH
10.8728985074
424AcetylationCKECENVKEIKVKEE
HHCCCCCCCCEEEEC
66.3625953088
429SumoylationNVKEIKVKEENETEI
CCCCCEEEECCHHHH
55.07-
429AcetylationNVKEIKVKEENETEI
CCCCCEEEECCHHHH
55.0726051181
429SumoylationNVKEIKVKEENETEI
CCCCCEEEECCHHHH
55.0728112733
437AcetylationEENETEIKEIKMEEE
ECCHHHHEECCHHHH
47.3426051181
440SumoylationETEIKEIKMEEERNI
HHHHEECCHHHHHCC
41.15-
440SumoylationETEIKEIKMEEERNI
HHHHEECCHHHHHCC
41.1528112733
462SumoylationIEDEIERKENIKPSL
CHHHHHHHHCCCCCC
42.1828112733
466UbiquitinationIERKENIKPSLGSKK
HHHHHCCCCCCCCCC
39.8929967540
468PhosphorylationRKENIKPSLGSKKNL
HHHCCCCCCCCCCHH
40.1223312004
471PhosphorylationNIKPSLGSKKNLLES
CCCCCCCCCCHHHHH
45.8326074081
472AcetylationIKPSLGSKKNLLESI
CCCCCCCCCHHHHHC
43.8326051181
478PhosphorylationSKKNLLESIPTHSDQ
CCCHHHHHCCCCCHH
33.5628450419
481PhosphorylationNLLESIPTHSDQEKE
HHHHHCCCCCHHHCC
32.1330266825
483PhosphorylationLESIPTHSDQEKEVN
HHHCCCCCHHHCCCC
43.3930266825
507PhosphorylationLDDKDDDTTRVDESL
CCCCCCCCCCCCHHH
24.4020068231
508PhosphorylationDDKDDDTTRVDESLN
CCCCCCCCCCCHHHC
35.3720068231
513PhosphorylationDTTRVDESLNIKVEA
CCCCCCHHHCEEEEE
23.4221815630
516UbiquitinationRVDESLNIKVEAEEE
CCCHHHCEEEEEHHH
6.8424816145
517SumoylationVDESLNIKVEAEEEK
CCHHHCEEEEEHHHH
32.7128112733
589PhosphorylationGKNQKMYEASIKDSD
CCCCEEEEEECCCCC
32.2332142685
602UbiquitinationSDVEGGEVLYLVHYC
CCCCCCEEEEEEEEC
4.8829967540
630AcetylationKIVRPADKNVPKIKH
CCCCCCCCCCCCHHC
63.0525953088
647AcetylationKIKNKLDKEKDKDEK
HHHHHHHHCCCCCCC
76.687307331
649AcetylationKNKLDKEKDKDEKYS
HHHHHHCCCCCCCCC
75.677307343
654AcetylationKEKDKDEKYSPKNCK
HCCCCCCCCCCCCCC
62.257307355
655PhosphorylationEKDKDEKYSPKNCKL
CCCCCCCCCCCCCCC
28.3223312004
656PhosphorylationKDKDEKYSPKNCKLR
CCCCCCCCCCCCCCE
40.2330576142
665UbiquitinationKNCKLRRLSKPPFQT
CCCCCEECCCCCCCC
6.6229967540
666PhosphorylationNCKLRRLSKPPFQTN
CCCCEECCCCCCCCC
41.1123401153
672PhosphorylationLSKPPFQTNPSPEMV
CCCCCCCCCCCHHHH
49.8530266825
675PhosphorylationPPFQTNPSPEMVSKL
CCCCCCCCHHHHHCC
35.2522167270
680PhosphorylationNPSPEMVSKLDLTDA
CCCHHHHHCCCCCCC
26.6230266825
685PhosphorylationMVSKLDLTDAKNSDT
HHHCCCCCCCCCCCC
33.3123186163
688UbiquitinationKLDLTDAKNSDTAHI
CCCCCCCCCCCCCEE
60.8529967540
690PhosphorylationDLTDAKNSDTAHIKS
CCCCCCCCCCCEEEE
35.3120068231
697PhosphorylationSDTAHIKSIEITSIL
CCCCEEEEEEHHHHH
25.5030177828
701PhosphorylationHIKSIEITSILNGLQ
EEEEEEHHHHHHHHH
9.2730177828
702PhosphorylationIKSIEITSILNGLQA
EEEEEHHHHHHHHHC
30.6430177828
710PhosphorylationILNGLQASESSAEDS
HHHHHHCCCCCCCCC
25.6720873877
712PhosphorylationNGLQASESSAEDSEQ
HHHHCCCCCCCCCHH
32.1420873877
713PhosphorylationGLQASESSAEDSEQE
HHHCCCCCCCCCHHH
31.4620873877
717PhosphorylationSESSAEDSEQEDERG
CCCCCCCCHHHHHHC
32.4620873877
723UbiquitinationDSEQEDERGAQDMDN
CCHHHHHHCCCCCCC
59.0524816145
725UbiquitinationEQEDERGAQDMDNNG
HHHHHHCCCCCCCCC
14.3924816145
751SumoylationNRNDLISKEEQNSSS
CHHHHCCHHHHCCHH
59.2728112733
751UbiquitinationNRNDLISKEEQNSSS
CHHHHCCHHHHCCHH
59.2729967540
756PhosphorylationISKEEQNSSSLLEEN
CCHHHHCCHHHHHHC
22.4628555341
757PhosphorylationSKEEQNSSSLLEENK
CHHHHCCHHHHHHCC
32.3321815630
758PhosphorylationKEEQNSSSLLEENKV
HHHHCCHHHHHHCCC
36.4721815630
772PhosphorylationVHADLVISKPVSKSP
CCCEEEEECCCCCCH
24.3523927012
773UbiquitinationHADLVISKPVSKSPE
CCEEEEECCCCCCHH
38.0124816145
775UbiquitinationDLVISKPVSKSPERL
EEEEECCCCCCHHHH
15.0024816145
776PhosphorylationLVISKPVSKSPERLR
EEEECCCCCCHHHHH
35.6230278072
778PhosphorylationISKPVSKSPERLRKD
EECCCCCCHHHHHHH
25.2023927012
790PhosphorylationRKDIEVLSEDTDYEE
HHHHHHHCCCCCCCC
38.3029255136
793PhosphorylationIEVLSEDTDYEEDEV
HHHHCCCCCCCCHHH
36.1129255136
795PhosphorylationVLSEDTDYEEDEVTK
HHCCCCCCCCHHHHH
24.2625463755
801PhosphorylationDYEEDEVTKKRKDVK
CCCCHHHHHHHHHHC
28.8822167270
809UbiquitinationKKRKDVKKDTTDKSS
HHHHHHCCCCCCCCC
61.2224816145
811UbiquitinationRKDVKKDTTDKSSKP
HHHHCCCCCCCCCCH
45.8624816145
818UbiquitinationTTDKSSKPQIKRGKR
CCCCCCCHHHHCCCC
42.9729967540
827PhosphorylationIKRGKRRYCNTEECL
HHCCCCCCCCHHHHH
8.2923312004
830PhosphorylationGKRRYCNTEECLKTG
CCCCCCCHHHHHHHC
29.6023312004
836PhosphorylationNTEECLKTGSPGKKE
CHHHHHHHCCCCHHH
29.9121712546
837UbiquitinationTEECLKTGSPGKKEE
HHHHHHHCCCCHHHH
30.2024816145
838PhosphorylationEECLKTGSPGKKEEK
HHHHHHCCCCHHHHH
35.3930576142
851PhosphorylationEKAKNKESLCMENSS
HHHCCHHHCCCCCCC
28.6022468782
874PhosphorylationEETKAKMTPTKKYNG
HHHHHCCCCCCCCCC
27.4029396449
876PhosphorylationTKAKMTPTKKYNGLE
HHHCCCCCCCCCCHH
30.8829396449
878AcetylationAKMTPTKKYNGLEEK
HCCCCCCCCCCHHHH
46.5620167786
879PhosphorylationKMTPTKKYNGLEEKR
CCCCCCCCCCHHHHH
18.9326074081
888PhosphorylationGLEEKRKSLRTTGFY
CHHHHHHHHHHHCCC
27.41-
895PhosphorylationSLRTTGFYSGFSEVA
HHHHHCCCCCHHHHH
14.8329978859
896PhosphorylationLRTTGFYSGFSEVAE
HHHHCCCCCHHHHHH
30.9721815630
899PhosphorylationTGFYSGFSEVAEKRI
HCCCCCHHHHHHHHH
34.3925159151
904AcetylationGFSEVAEKRIKLLNN
CHHHHHHHHHHHHCC
50.0823954790
904UbiquitinationGFSEVAEKRIKLLNN
CHHHHHHHHHHHHCC
50.0829967540
912PhosphorylationRIKLLNNSDERLQNS
HHHHHCCCHHHHHHH
39.5125159151
919PhosphorylationSDERLQNSRAKDRKD
CHHHHHHHHHCCHHH
22.2124732914
930PhosphorylationDRKDVWSSIQGQWPK
CHHHHHHHHCCCCCH
11.8325159151
943PhosphorylationPKKTLKELFSDSDTE
CHHHHHHHCCCCCCC
4.8133259812
1013PhosphorylationDRKAEFPSSGSNSVL
CEECCCCCCCCCCCC
53.2928450419
1014PhosphorylationRKAEFPSSGSNSVLN
EECCCCCCCCCCCCC
46.6222115753
1016PhosphorylationAEFPSSGSNSVLNTP
CCCCCCCCCCCCCCC
28.0730108239
1018PhosphorylationFPSSGSNSVLNTPPT
CCCCCCCCCCCCCCC
29.6730108239
1022PhosphorylationGSNSVLNTPPTTPES
CCCCCCCCCCCCCCC
26.8730278072
1025PhosphorylationSVLNTPPTTPESPSS
CCCCCCCCCCCCCCC
57.0730278072
1026PhosphorylationVLNTPPTTPESPSSV
CCCCCCCCCCCCCCE
30.7230278072
1029PhosphorylationTPPTTPESPSSVTVT
CCCCCCCCCCCEEEC
31.1423401153
1031PhosphorylationPTTPESPSSVTVTEG
CCCCCCCCCEEECCC
46.8830278072
1032PhosphorylationTTPESPSSVTVTEGS
CCCCCCCCEEECCCC
25.7822115753
1034PhosphorylationPESPSSVTVTEGSRQ
CCCCCCEEECCCCEE
24.5330278072
1036PhosphorylationSPSSVTVTEGSRQQS
CCCCEEECCCCEEEE
25.8422115753
1039PhosphorylationSVTVTEGSRQQSSVT
CEEECCCCEEEEEEE
22.2330278072
1044UbiquitinationEGSRQQSSVTVSEPL
CCCEEEEEEEECCCC
19.9224816145
1046UbiquitinationSRQQSSVTVSEPLAP
CEEEEEEEECCCCCC
21.9124816145
1048PhosphorylationQQSSVTVSEPLAPNQ
EEEEEEECCCCCCCH
24.9128555341
1060PhosphorylationPNQEEVRSIKSETDS
CCHHHHHHCCCCCCC
39.2725159151
1067PhosphorylationSIKSETDSTIEVDSV
HCCCCCCCCEEEEEH
38.4118669648
1073PhosphorylationDSTIEVDSVAGELQD
CCCEEEEEHHHHHHH
21.0218669648
1094UbiquitinationSSPAGFDASVSSSSS
CCCCCCCCCCCCCCC
15.0124816145
1096UbiquitinationPAGFDASVSSSSSNQ
CCCCCCCCCCCCCCC
7.4424816145
1130UbiquitinationQGGGSSSKKQKRSHK
CCCCCCCHHHHHCCC
62.2624816145
1131AcetylationGGGSSSKKQKRSHKA
CCCCCCHHHHHCCCC
64.107373275
1132UbiquitinationGGSSSKKQKRSHKAT
CCCCCHHHHHCCCCE
50.5624816145
1150PhosphorylationNKKKGKGTNSSDSEE
CCCCCCCCCCCCHHH
35.1023927012
1152PhosphorylationKKGKGTNSSDSEELS
CCCCCCCCCCHHHHH
35.0523927012
1153PhosphorylationKGKGTNSSDSEELSA
CCCCCCCCCHHHHHC
47.4225159151
1155PhosphorylationKGTNSSDSEELSAGE
CCCCCCCHHHHHCCC
34.6130278072
1159PhosphorylationSSDSEELSAGESITK
CCCHHHHHCCCCCCC
37.1923927012
1159UbiquitinationSSDSEELSAGESITK
CCCHHHHHCCCCCCC
37.1929967540
1163PhosphorylationEELSAGESITKSQPV
HHHHCCCCCCCCCCC
34.3423403867
1165PhosphorylationLSAGESITKSQPVKS
HHCCCCCCCCCCCEE
33.6423403867
1174PhosphorylationSQPVKSVSTGMKSHS
CCCCEECCCCCCCCC
26.7427251275
1178AcetylationKSVSTGMKSHSTKSP
EECCCCCCCCCCCCC
46.497822309
1179PhosphorylationSVSTGMKSHSTKSPA
ECCCCCCCCCCCCCC
17.4923312004
1181PhosphorylationSTGMKSHSTKSPART
CCCCCCCCCCCCCCC
44.6223312004
1182PhosphorylationTGMKSHSTKSPARTQ
CCCCCCCCCCCCCCC
30.0730576142
1183AcetylationGMKSHSTKSPARTQS
CCCCCCCCCCCCCCC
58.417822321
1184PhosphorylationMKSHSTKSPARTQSP
CCCCCCCCCCCCCCC
24.7125849741
1188PhosphorylationSTKSPARTQSPGKCG
CCCCCCCCCCCCCCC
35.1930576142
1190PhosphorylationKSPARTQSPGKCGKN
CCCCCCCCCCCCCCC
34.7025849741
1200AcetylationKCGKNGDKDPDLKEP
CCCCCCCCCCCCCCC
72.9826051181
1245UbiquitinationEKLQEIRKHYLSLKS
HHHHHHHHHHHHHHH
42.1129967540
1249PhosphorylationEIRKHYLSLKSEVAS
HHHHHHHHHHHHHHH
26.9523532336
1252PhosphorylationKHYLSLKSEVASIDR
HHHHHHHHHHHHHHH
42.4718691976
1256PhosphorylationSLKSEVASIDRRRKR
HHHHHHHHHHHHHHH
30.1417192257

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 ARI4B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARI4B_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 ARI4B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HDAC1_HUMANHDAC1physical
12724404
HDAC2_HUMANHDAC2physical
12724404
SDS3_HUMANSUDS3physical
12724404
SIN3A_HUMANSIN3Aphysical
12724404
SP130_HUMANSAP130physical
12724404
CUL4B_HUMANCUL4Bphysical
25189618
DDB1_HUMANDDB1physical
25189618
SP130_HUMANSAP130physical
26344197
SAP30_HUMANSAP30physical
26344197
SIN3A_HUMANSIN3Aphysical
26344197

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 ARI4B_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-790; THR-793; SER-1014;THR-1022 AND THR-1026, 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-675; SER-790; THR-793;TYR-795; SER-1153 AND SER-1155, AND MASS 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-666; SER-675; SER-790;THR-793; SER-912; THR-1150; SER-1152; SER-1153; SER-1155 AND SER-1159,AND MASS SPECTROMETRY.
"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-1256, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-778, AND MASSSPECTROMETRY.
"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-710; SER-712; SER-713AND SER-717, AND MASS SPECTROMETRY.
"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 THR-1022 AND SER-1029, ANDMASS SPECTROMETRY.

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