NPM_HUMAN - dbPTM
NPM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NPM_HUMAN
UniProt AC P06748
Protein Name Nucleophosmin
Gene Name NPM1
Organism Homo sapiens (Human).
Sequence Length 294
Subcellular Localization Nucleus, nucleolus . Nucleus, nucleoplasm . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Generally nucleolar, but is translocated to the nucleoplasm in case of serum starvation or treatment with anticancer drugs. Has been found
Protein Description Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication: phosphorylation by PLK2 is able to trigger centriole replication. Negatively regulates the activation of EIF2AK2/PKR and suppresses apoptosis through inhibition of EIF2AK2/PKR autophosphorylation. Antagonizes the inhibitory effect of ATF5 on cell proliferation and relieves ATF5-induced G2/M blockade. [PubMed: 22528486 In complex with MYC enhances the transcription of MYC target genes]
Protein Sequence MEDSMDMDMSPLRPQNYLFGCELKADKDYHFKVDNDENEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEITPPVVLRLKCGSGPVHISGQHLVAVEEDAESEDEEEEDVKLLSISGKRSAPGGGSKVPQKKVKLAADEDDDDDDEEDDDEDDDDDDFDDEEAEEKAPVKKSIRDTPAKNAQKSNQNGKDSKPSSTPRSKGQESFKKQEKTPKTPKGPSSVEDIKAKMQASIEKGGSLPKVEAKFINYVKNCFRMTDQEAIQDLWQWRKSL
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
1Acetylation-------MEDSMDMD
-------CCCCCCCC
13.4120068231
4Phosphorylation----MEDSMDMDMSP
----CCCCCCCCCCC
11.9029255136
10PhosphorylationDSMDMDMSPLRPQNY
CCCCCCCCCCCCCCE
19.2729255136
17PhosphorylationSPLRPQNYLFGCELK
CCCCCCCEEEEEEEE
9.7322617229
24AcetylationYLFGCELKADKDYHF
EEEEEEEECCCCCEE
32.0423954790
24UbiquitinationYLFGCELKADKDYHF
EEEEEEEECCCCCEE
32.04-
27SumoylationGCELKADKDYHFKVD
EEEEECCCCCEEEEC
66.11-
272-HydroxyisobutyrylationGCELKADKDYHFKVD
EEEEECCCCCEEEEC
66.11-
27AcetylationGCELKADKDYHFKVD
EEEEECCCCCEEEEC
66.1123954790
27SuccinylationGCELKADKDYHFKVD
EEEEECCCCCEEEEC
66.1123954790
27SumoylationGCELKADKDYHFKVD
EEEEECCCCCEEEEC
66.1125218447
27UbiquitinationGCELKADKDYHFKVD
EEEEECCCCCEEEEC
66.1119608861
27 (in isoform 2)Ubiquitination-66.11-
29PhosphorylationELKADKDYHFKVDND
EEECCCCCEEEECCC
18.2020090780
32UbiquitinationADKDYHFKVDNDENE
CCCCCEEEECCCCCC
35.0521890473
32SumoylationADKDYHFKVDNDENE
CCCCCEEEECCCCCC
35.05-
322-HydroxyisobutyrylationADKDYHFKVDNDENE
CCCCCEEEECCCCCC
35.05-
32AcetylationADKDYHFKVDNDENE
CCCCCEEEECCCCCC
35.0519608861
32MalonylationADKDYHFKVDNDENE
CCCCCEEEECCCCCC
35.0526320211
32SumoylationADKDYHFKVDNDENE
CCCCCEEEECCCCCC
35.0519608861
32UbiquitinationADKDYHFKVDNDENE
CCCCCEEEECCCCCC
35.0521890473
32 (in isoform 1)Ubiquitination-35.0521890473
32 (in isoform 2)Ubiquitination-35.0521890473
32UbiquitinationADKDYHFKVDNDENE
CCCCCEEEECCCCCC
35.0521890473
43PhosphorylationDENEHQLSLRTVSLG
CCCCEEEEEEEEECC
14.8323401153
45MethylationNEHQLSLRTVSLGAG
CCEEEEEEEEECCCC
29.70115485503
46PhosphorylationEHQLSLRTVSLGAGA
CEEEEEEEEECCCCC
21.5321712546
48PhosphorylationQLSLRTVSLGAGAKD
EEEEEEEECCCCCCC
22.0725159151
542-HydroxyisobutyrylationVSLGAGAKDELHIVE
EECCCCCCCEEEEEE
51.31-
54AcetylationVSLGAGAKDELHIVE
EECCCCCCCEEEEEE
51.3123954790
54SumoylationVSLGAGAKDELHIVE
EECCCCCCCEEEEEE
51.31-
54UbiquitinationVSLGAGAKDELHIVE
EECCCCCCCEEEEEE
51.3121906983
54 (in isoform 1)Ubiquitination-51.3121890473
54 (in isoform 2)Ubiquitination-51.3121890473
65SulfoxidationHIVEAEAMNYEGSPI
EEEEEECCCCCCCCE
4.0630846556
67NitrationVEAEAMNYEGSPIKV
EEEECCCCCCCCEEE
14.47-
67PhosphorylationVEAEAMNYEGSPIKV
EEEECCCCCCCCEEE
14.4722167270
67 (in isoform 2)Phosphorylation-14.4718669648
70PhosphorylationEAMNYEGSPIKVTLA
ECCCCCCCCEEEEEE
16.1229255136
70 (in isoform 2)Phosphorylation-16.1218669648
732-HydroxyisobutyrylationNYEGSPIKVTLATLK
CCCCCCEEEEEEEEE
32.33-
73AcetylationNYEGSPIKVTLATLK
CCCCCCEEEEEEEEE
32.3326051181
73SumoylationNYEGSPIKVTLATLK
CCCCCCEEEEEEEEE
32.33-
73UbiquitinationNYEGSPIKVTLATLK
CCCCCCEEEEEEEEE
32.33-
75O-linked_GlycosylationEGSPIKVTLATLKMS
CCCCEEEEEEEEEEE
12.9823301498
75PhosphorylationEGSPIKVTLATLKMS
CCCCEEEEEEEEEEE
12.9822167270
75 (in isoform 2)Phosphorylation-12.9818669648
78PhosphorylationPIKVTLATLKMSVQP
CEEEEEEEEEEEECC
29.9822167270
78 (in isoform 2)Phosphorylation-29.9818669648
80UbiquitinationKVTLATLKMSVQPTV
EEEEEEEEEEECCEE
25.44-
80 (in isoform 2)Ubiquitination-25.44-
81SulfoxidationVTLATLKMSVQPTVS
EEEEEEEEEECCEEE
5.5128183972
82PhosphorylationTLATLKMSVQPTVSL
EEEEEEEEECCEEEE
18.9329255136
86PhosphorylationLKMSVQPTVSLGGFE
EEEEECCEEEECCEE
12.9729255136
88O-linked_GlycosylationMSVQPTVSLGGFEIT
EEECCEEEECCEEEC
24.6323301498
88PhosphorylationMSVQPTVSLGGFEIT
EEECCEEEECCEEEC
24.6329255136
88 (in isoform 2)Phosphorylation-24.6318220336
95PhosphorylationSLGGFEITPPVVLRL
EECCEEECCCEEEEE
17.8425159151
95 (in isoform 2)Phosphorylation-17.8418669648
101MethylationITPPVVLRLKCGSGP
ECCCEEEEEEECCCC
22.08116265613
106O-linked_GlycosylationVLRLKCGSGPVHISG
EEEEEECCCCEEECC
49.7723301498
106PhosphorylationVLRLKCGSGPVHISG
EEEEEECCCCEEECC
49.7723927012
112O-linked_GlycosylationGSGPVHISGQHLVAV
CCCCEEECCEEEEEE
19.9523301498
112PhosphorylationGSGPVHISGQHLVAV
CCCCEEECCEEEEEE
19.9523927012
125O-linked_GlycosylationAVEEDAESEDEEEED
EEECCCCCCCCHHHH
52.6623301498
125PhosphorylationAVEEDAESEDEEEED
EEECCCCCCCCHHHH
52.6629255136
125 (in isoform 2)Phosphorylation-52.6618669648
134SumoylationDEEEEDVKLLSISGK
CCHHHHEEEEEEECC
56.91-
135PhosphorylationEEEEDVKLLSISGKR
CHHHHEEEEEEECCC
4.57-
137PhosphorylationEEDVKLLSISGKRSA
HHHEEEEEEECCCCC
25.7423927012
137 (in isoform 2)Phosphorylation-25.7418669648
138PhosphorylationEDVKLLSISGKRSAP
HHEEEEEEECCCCCC
6.76-
139PhosphorylationDVKLLSISGKRSAPG
HEEEEEEECCCCCCC
34.5822167270
139 (in isoform 2)Phosphorylation-34.5818669648
141UbiquitinationKLLSISGKRSAPGGG
EEEEEECCCCCCCCC
36.0721890473
141SumoylationKLLSISGKRSAPGGG
EEEEEECCCCCCCCC
36.07-
1412-HydroxyisobutyrylationKLLSISGKRSAPGGG
EEEEEECCCCCCCCC
36.07-
141AcetylationKLLSISGKRSAPGGG
EEEEEECCCCCCCCC
36.0723954790
141MalonylationKLLSISGKRSAPGGG
EEEEEECCCCCCCCC
36.0726320211
141MethylationKLLSISGKRSAPGGG
EEEEEECCCCCCCCC
36.0768493
141SumoylationKLLSISGKRSAPGGG
EEEEEECCCCCCCCC
36.0728112733
141UbiquitinationKLLSISGKRSAPGGG
EEEEEECCCCCCCCC
36.0721890473
141 (in isoform 1)Ubiquitination-36.0721890473
141 (in isoform 2)Ubiquitination-36.0721890473
141UbiquitinationKLLSISGKRSAPGGG
EEEEEECCCCCCCCC
36.0721890473
143PhosphorylationLSISGKRSAPGGGSK
EEEECCCCCCCCCCC
42.1522617229
149PhosphorylationRSAPGGGSKVPQKKV
CCCCCCCCCCCHHHE
33.4826657352
150SumoylationSAPGGGSKVPQKKVK
CCCCCCCCCCHHHEE
62.30-
1502-HydroxyisobutyrylationSAPGGGSKVPQKKVK
CCCCCCCCCCHHHEE
62.30-
150AcetylationSAPGGGSKVPQKKVK
CCCCCCCCCCHHHEE
62.3016916647
150SumoylationSAPGGGSKVPQKKVK
CCCCCCCCCCHHHEE
62.3028112733
150UbiquitinationSAPGGGSKVPQKKVK
CCCCCCCCCCHHHEE
62.3019608861
152PhosphorylationPGGGSKVPQKKVKLA
CCCCCCCCHHHEEEC
43.97-
154AcetylationGGSKVPQKKVKLAAD
CCCCCCHHHEEECCC
54.1616916647
155AcetylationGSKVPQKKVKLAADE
CCCCCHHHEEECCCC
39.087303085
155UbiquitinationGSKVPQKKVKLAADE
CCCCCHHHEEECCCC
39.0821906983
155 (in isoform 1)Ubiquitination-39.0821890473
155 (in isoform 2)Ubiquitination-39.0821890473
156PhosphorylationSKVPQKKVKLAADED
CCCCHHHEEECCCCC
8.71-
157AcetylationKVPQKKVKLAADEDD
CCCHHHEEECCCCCC
41.0926051181
157UbiquitinationKVPQKKVKLAADEDD
CCCHHHEEECCCCCC
41.0921906983
157 (in isoform 1)Ubiquitination-41.0921890473
157 (in isoform 2)Ubiquitination-41.0921890473
164PhosphorylationKLAADEDDDDDDEED
EECCCCCCCCCCCCC
60.22-
189AcetylationDDEEAEEKAPVKKSI
CHHHHHHHCCCCHHH
49.8826051181
189UbiquitinationDDEEAEEKAPVKKSI
CHHHHHHHCCCCHHH
49.881890473
189 (in isoform 1)Ubiquitination-49.8821890473
189 (in isoform 2)Ubiquitination-49.8821890473
191PhosphorylationEEAEEKAPVKKSIRD
HHHHHHCCCCHHHCC
49.91-
193AcetylationAEEKAPVKKSIRDTP
HHHHCCCCHHHCCCH
39.4826051181
193UbiquitinationAEEKAPVKKSIRDTP
HHHHCCCCHHHCCCH
39.4821906983
193 (in isoform 1)Ubiquitination-39.4821890473
193 (in isoform 2)Ubiquitination-39.4821890473
195PhosphorylationEKAPVKKSIRDTPAK
HHCCCCHHHCCCHHH
19.6930266825
197MethylationAPVKKSIRDTPAKNA
CCCCHHHCCCHHHHH
49.17115485495
198 (in isoform 2)Phosphorylation-56.2020068231
199PhosphorylationVKKSIRDTPAKNAQK
CCHHHCCCHHHHHHH
18.4623927012
202SumoylationSIRDTPAKNAQKSNQ
HHCCCHHHHHHHHCC
54.76-
202AcetylationSIRDTPAKNAQKSNQ
HHCCCHHHHHHHHCC
54.7619666589
202SumoylationSIRDTPAKNAQKSNQ
HHCCCHHHHHHHHCC
54.76-
202UbiquitinationSIRDTPAKNAQKSNQ
HHCCCHHHHHHHHCC
54.7621906983
202 (in isoform 1)Ubiquitination-54.7621890473
207ADP-ribosylationPAKNAQKSNQNGKDS
HHHHHHHHCCCCCCC
31.4128190768
207PhosphorylationPAKNAQKSNQNGKDS
HHHHHHHHCCCCCCC
31.4126074081
208 (in isoform 2)Phosphorylation-46.5025159151
212AcetylationQKSNQNGKDSKPSST
HHHCCCCCCCCCCCC
67.3916916647
212SuccinylationQKSNQNGKDSKPSST
HHHCCCCCCCCCCCC
67.3923954790
214PhosphorylationSNQNGKDSKPSSTPR
HCCCCCCCCCCCCCC
50.3721601212
215SumoylationNQNGKDSKPSSTPRS
CCCCCCCCCCCCCCH
60.08-
215AcetylationNQNGKDSKPSSTPRS
CCCCCCCCCCCCCCH
60.0823954790
215SumoylationNQNGKDSKPSSTPRS
CCCCCCCCCCCCCCH
60.0828112733
217PhosphorylationNGKDSKPSSTPRSKG
CCCCCCCCCCCCHHH
51.0525159151
218PhosphorylationGKDSKPSSTPRSKGQ
CCCCCCCCCCCHHHH
51.4630278072
219PhosphorylationKDSKPSSTPRSKGQE
CCCCCCCCCCHHHHH
27.3630278072
219 (in isoform 2)Ubiquitination-27.3621890473
221 (in isoform 2)Ubiquitination-51.6021890473
222PhosphorylationKPSSTPRSKGQESFK
CCCCCCCHHHHHHHH
42.2030576142
223SumoylationPSSTPRSKGQESFKK
CCCCCCHHHHHHHHC
66.93-
2232-HydroxyisobutyrylationPSSTPRSKGQESFKK
CCCCCCHHHHHHHHC
66.93-
223AcetylationPSSTPRSKGQESFKK
CCCCCCHHHHHHHHC
66.9323749302
223SumoylationPSSTPRSKGQESFKK
CCCCCCHHHHHHHHC
66.93-
223UbiquitinationPSSTPRSKGQESFKK
CCCCCCHHHHHHHHC
66.93-
227PhosphorylationPRSKGQESFKKQEKT
CCHHHHHHHHCCCCC
34.1823401153
228 (in isoform 2)Ubiquitination-12.9421890473
229SumoylationSKGQESFKKQEKTPK
HHHHHHHHCCCCCCC
63.93-
2292-HydroxyisobutyrylationSKGQESFKKQEKTPK
HHHHHHHHCCCCCCC
63.93-
229AcetylationSKGQESFKKQEKTPK
HHHHHHHHCCCCCCC
63.9316107701
229SuccinylationSKGQESFKKQEKTPK
HHHHHHHHCCCCCCC
63.9323954790
229SumoylationSKGQESFKKQEKTPK
HHHHHHHHCCCCCCC
63.9316107701
229UbiquitinationSKGQESFKKQEKTPK
HHHHHHHHCCCCCCC
63.93-
230SumoylationKGQESFKKQEKTPKT
HHHHHHHCCCCCCCC
62.77-
230AcetylationKGQESFKKQEKTPKT
HHHHHHHCCCCCCCC
62.7716107701
230SumoylationKGQESFKKQEKTPKT
HHHHHHHCCCCCCCC
62.7725114211
234PhosphorylationSFKKQEKTPKTPKGP
HHHCCCCCCCCCCCC
29.3020201521
237PhosphorylationKQEKTPKTPKGPSSV
CCCCCCCCCCCCCCH
31.2820201521
238 (in isoform 2)Ubiquitination-45.8121890473
239SumoylationEKTPKTPKGPSSVED
CCCCCCCCCCCCHHH
84.45-
2392-HydroxyisobutyrylationEKTPKTPKGPSSVED
CCCCCCCCCCCCHHH
84.45-
239AcetylationEKTPKTPKGPSSVED
CCCCCCCCCCCCHHH
84.4526051181
239MalonylationEKTPKTPKGPSSVED
CCCCCCCCCCCCHHH
84.4526320211
239SuccinylationEKTPKTPKGPSSVED
CCCCCCCCCCCCHHH
84.4523954790
239SumoylationEKTPKTPKGPSSVED
CCCCCCCCCCCCHHH
84.45-
239UbiquitinationEKTPKTPKGPSSVED
CCCCCCCCCCCCHHH
84.45-
242PhosphorylationPKTPKGPSSVEDIKA
CCCCCCCCCHHHHHH
56.5429255136
243PhosphorylationKTPKGPSSVEDIKAK
CCCCCCCCHHHHHHH
32.4329255136
243 (in isoform 3)Phosphorylation-32.4325849741
244 (in isoform 2)Ubiquitination-10.0721890473
248SumoylationPSSVEDIKAKMQASI
CCCHHHHHHHHHHHH
55.03-
248AcetylationPSSVEDIKAKMQASI
CCCHHHHHHHHHHHH
55.0323749302
248MalonylationPSSVEDIKAKMQASI
CCCHHHHHHHHHHHH
55.0330639696
248MethylationPSSVEDIKAKMQASI
CCCHHHHHHHHHHHH
55.0372662745
248SumoylationPSSVEDIKAKMQASI
CCCHHHHHHHHHHHH
55.0328112733
248UbiquitinationPSSVEDIKAKMQASI
CCCHHHHHHHHHHHH
55.0321906983
248 (in isoform 1)Ubiquitination-55.0321890473
250SumoylationSVEDIKAKMQASIEK
CHHHHHHHHHHHHHC
26.92-
2502-HydroxyisobutyrylationSVEDIKAKMQASIEK
CHHHHHHHHHHHHHC
26.92-
250AcetylationSVEDIKAKMQASIEK
CHHHHHHHHHHHHHC
26.9216107701
250SumoylationSVEDIKAKMQASIEK
CHHHHHHHHHHHHHC
26.9228112733
250UbiquitinationSVEDIKAKMQASIEK
CHHHHHHHHHHHHHC
26.9221906983
250 (in isoform 1)Ubiquitination-26.9221890473
254PhosphorylationIKAKMQASIEKGGSL
HHHHHHHHHHCCCCC
17.8729255136
254 (in isoform 3)Phosphorylation-17.8726055452
257AcetylationKMQASIEKGGSLPKV
HHHHHHHCCCCCCHH
67.8919608861
257MalonylationKMQASIEKGGSLPKV
HHHHHHHCCCCCCHH
67.8926320211
257SumoylationKMQASIEKGGSLPKV
HHHHHHHCCCCCCHH
67.8919608861
257UbiquitinationKMQASIEKGGSLPKV
HHHHHHHCCCCCCHH
67.8921906983
257 (in isoform 1)Ubiquitination-67.8921890473
257 (in isoform 3)Acetylation-67.8919608861
260PhosphorylationASIEKGGSLPKVEAK
HHHHCCCCCCHHHHH
50.6023927012
263SumoylationEKGGSLPKVEAKFIN
HCCCCCCHHHHHHHH
58.98-
263AcetylationEKGGSLPKVEAKFIN
HCCCCCCHHHHHHHH
58.9826051181
263SumoylationEKGGSLPKVEAKFIN
HCCCCCCHHHHHHHH
58.9815897463
263UbiquitinationEKGGSLPKVEAKFIN
HCCCCCCHHHHHHHH
58.98-
267UbiquitinationSLPKVEAKFINYVKN
CCCHHHHHHHHHHHH
33.0221890473
267SumoylationSLPKVEAKFINYVKN
CCCHHHHHHHHHHHH
33.02-
267AcetylationSLPKVEAKFINYVKN
CCCHHHHHHHHHHHH
33.0219608861
267MalonylationSLPKVEAKFINYVKN
CCCHHHHHHHHHHHH
33.0230639696
267SuccinylationSLPKVEAKFINYVKN
CCCHHHHHHHHHHHH
33.0223954790
267SumoylationSLPKVEAKFINYVKN
CCCHHHHHHHHHHHH
33.0219608861
267UbiquitinationSLPKVEAKFINYVKN
CCCHHHHHHHHHHHH
33.0221890473
267 (in isoform 1)Ubiquitination-33.0221890473
273UbiquitinationAKFINYVKNCFRMTD
HHHHHHHHHHHHCCC
37.3221890473
2732-HydroxyisobutyrylationAKFINYVKNCFRMTD
HHHHHHHHHHHHCCC
37.32-
273AcetylationAKFINYVKNCFRMTD
HHHHHHHHHHHHCCC
37.3219608861
273MalonylationAKFINYVKNCFRMTD
HHHHHHHHHHHHCCC
37.3226320211
273MethylationAKFINYVKNCFRMTD
HHHHHHHHHHHHCCC
37.3268521
273SuccinylationAKFINYVKNCFRMTD
HHHHHHHHHHHHCCC
37.3223954790
273SumoylationAKFINYVKNCFRMTD
HHHHHHHHHHHHCCC
37.3228112733
273UbiquitinationAKFINYVKNCFRMTD
HHHHHHHHHHHHCCC
37.3221890473
273 (in isoform 1)Ubiquitination-37.3221890473
278SulfoxidationYVKNCFRMTDQEAIQ
HHHHHHHCCCHHHHH
2.1330846556
279PhosphorylationVKNCFRMTDQEAIQD
HHHHHHCCCHHHHHH
30.2125159151
292AcetylationQDLWQWRKSL-----
HHHHHHHHHC-----
53.8216107701
292SumoylationQDLWQWRKSL-----
HHHHHHHHHC-----
53.8216107701
293PhosphorylationDLWQWRKSL------
HHHHHHHHC------
30.6429496963
338Phosphorylation---------------------------------------------------
---------------------------------------------------
-
342Phosphorylation-------------------------------------------------------
-------------------------------------------------------
-
343Phosphorylation--------------------------------------------------------
--------------------------------------------------------
-
419Phosphorylation------------------------------------------------------------------------------------------------------------------------------------
------------------------------------------------------------------------------------------------------------------------------------
-
497Phosphorylation------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
-
567Phosphorylation----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
-
644Phosphorylation---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
-
664Phosphorylation-----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
-----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
-

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
4SPhosphorylationKinasePLK3Q9H4B4
PSP
4SPhosphorylationKinasePLK2Q9NYY3
Uniprot
4SPhosphorylationKinasePLK1P53350
Uniprot
48SPhosphorylationKinaseAKT1P31749
PSP
70SPhosphorylationKinaseNEK2P51955
PSP
70SPhosphorylationKinaseCDK1P06493
PSP
70SPhosphorylationKinaseCDK2P24941
PSP
88SPhosphorylationKinaseNEK2P51955
PSP
125SPhosphorylationKinaseATRQ13535
PSP
125SPhosphorylationKinaseAURAO14965
PSP
125SPhosphorylationKinaseAURBQ96GD4
PSP
125SPhosphorylationKinaseCDK2P24941
Uniprot
125SPhosphorylationKinaseCK2A1P68400
PSP
137SPhosphorylationKinaseCDC7O00311
PSP
199TPhosphorylationKinaseCDK2P24941
Uniprot
199TPhosphorylationKinaseMAP3K8P41279
GPS
199TPhosphorylationKinaseCDK6Q00534
Uniprot
199TPhosphorylationKinaseCDK1P06493
Uniprot
199TPhosphorylationKinaseCDC7O00311
PSP
219TPhosphorylationKinaseCDK1P06493
Uniprot
227SPhosphorylationKinasePKC-FAMILY-GPS
227SPhosphorylationKinasePKC_GROUP-PhosphoELM
234TPhosphorylationKinaseCDK2P24941
PSP
234TPhosphorylationKinaseCDK1P06493
Uniprot
237TPhosphorylationKinaseCDK1P06493
Uniprot
-KUbiquitinationE3 ubiquitin ligaseSTUB1Q9UNE7
PMID:15126367
-KUbiquitinationE3 ubiquitin ligaseBRCA1P38398
PMID:15184379
-KUbiquitinationE3 ubiquitin ligaseRNF144BQ7Z419
PMID:20864535

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
4SPhosphorylation

15388344
4SPhosphorylation

15388344
4SPhosphorylation

15388344
70SPhosphorylation

15388344
125SPhosphorylation

15388344
199TPhosphorylation

15388344
199TPhosphorylation

15388344
199TPhosphorylation

15388344
199TPhosphorylation

15388344
199TPhosphorylation

15388344
219TPhosphorylation

15388344
234TPhosphorylation

15388344
237TPhosphorylation

15388344

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 NPM_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
H31T_HUMANHIST3H3physical
11602260
AKT1_HUMANAKT1physical
18931307
GRB2_HUMANGRB2physical
14968112
CENPF_HUMANCENPFphysical
14968112
CSKI1_HUMANCASKIN1physical
14968112
CC14A_HUMANCDC14Aphysical
14968112
P85A_HUMANPIK3R1physical
14968112
NUP98_HUMANNUP98physical
14968112
PPID_HUMANPPIDphysical
14968112
GRB7_HUMANGRB7physical
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CND3_HUMANNCAPGphysical
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NUMA1_HUMANNUMA1physical
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PADI4_HUMANPADI4physical
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BRCA1_HUMANBRCA1physical
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BARD1_HUMANBARD1physical
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TYY1_HUMANYY1physical
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H2A2C_HUMANHIST2H2ACphysical
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H2B2E_HUMANHIST2H2BEphysical
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FANCA_HUMANFANCAphysical
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FANCC_HUMANFANCCphysical
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AP2A_HUMANTFAP2Aphysical
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HDAC1_HUMANHDAC1physical
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HDAC2_HUMANHDAC2physical
17318229
NUCL_HUMANNCLphysical
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ACACA_HUMANACACAphysical
20431927
HNRPM_HUMANHNRNPMphysical
20431927
HNRPU_HUMANHNRNPUphysical
20431927
DDX21_HUMANDDX21physical
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H12_HUMANHIST1H1Cphysical
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SIR1_HUMANSIRT1physical
20431927
YBOX1_HUMANYBX1physical
20431927
PYC_HUMANPCphysical
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YBOX3_HUMANYBX3physical
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H1X_HUMANH1FXphysical
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H11_HUMANHIST1H1Aphysical
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P53_MOUSETrp53physical
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CDN2A_MOUSECdkn2aphysical
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ARF_MOUSECdkn2aphysical
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ZN668_HUMANZNF668physical
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UBP36_HUMANUSP36physical
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CTCF_HUMANCTCFphysical
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CDN1A_HUMANCDKN1Aphysical
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SENP3_HUMANSENP3physical
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CDN2A_HUMANCDKN2Aphysical
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ARF_HUMANCDKN2Aphysical
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RB_HUMANRB1physical
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PARP1_HUMANPARP1physical
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H31_HUMANHIST1H3Aphysical
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CENPA_HUMANCENPAphysical
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H31_HUMANHIST1H3Aphysical
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NPM_HUMANNPM1physical
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UBC_HUMANUBCphysical
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PA2G4_HUMANPA2G4physical
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MDM2_HUMANMDM2physical
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PLCG1_HUMANPLCG1physical
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GRB2_HUMANGRB2physical
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P53_HUMANTP53physical
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G3P_HUMANGAPDHphysical
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SIAH1_HUMANSIAH1physical
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RL14_HUMANRPL14physical
22939629
RS6_HUMANRPS6physical
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RL24_HUMANRPL24physical
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RL6_HUMANRPL6physical
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RS4X_HUMANRPS4Xphysical
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PRP6_HUMANPRPF6physical
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RL10L_HUMANRPL10Lphysical
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NUP50_HUMANNUP50physical
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CPSF1_HUMANCPSF1physical
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CPSF2_HUMANCPSF2physical
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CPSF4_HUMANCPSF4physical
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CPSF3_HUMANCPSF3physical
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HS90B_HUMANHSP90AB1physical
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PAR6B_HUMANPARD6Bphysical
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CDC37_HUMANCDC37physical
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CLH1_HUMANCLTCphysical
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TERA_HUMANVCPphysical
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NPM_HUMANNPM1physical
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EF1A1_HUMANEEF1A1physical
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TAB1_HUMANTAB1physical
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STK38_HUMANSTK38physical
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COPB_HUMANCOPB1physical
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DDX3X_HUMANDDX3Xphysical
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RINI_HUMANRNH1physical
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OSBL1_HUMANOSBPL1Aphysical
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EIF3H_HUMANEIF3Hphysical
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ENOA_HUMANENO1physical
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HSPB1_HUMANHSPB1physical
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COF1_HUMANCFL1physical
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FLNC_HUMANFLNCphysical
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PP1G_HUMANPPP1CCphysical
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RLA1_HUMANRPLP1physical
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CE152_HUMANCEP152physical
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SMD1_HUMANSNRPD1physical
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ATPA_HUMANATP5A1physical
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RHG05_HUMANARHGAP5physical
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KAP0_HUMANPRKAR1Aphysical
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GID8_HUMANGID8physical
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1433Z_HUMANYWHAZphysical
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DICER_HUMANDICER1physical
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GRWD1_HUMANGRWD1physical
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CALU_HUMANCALUphysical
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ABCF2_HUMANABCF2physical
26496610
G3BP1_HUMANG3BP1physical
26496610
NPM3_HUMANNPM3physical
26496610
RACK1_HUMANGNB2L1physical
26496610
NEP1_HUMANEMG1physical
26496610
MBB1A_HUMANMYBBP1Aphysical
26496610
NOP56_HUMANNOP56physical
26496610
IF2B3_HUMANIGF2BP3physical
26496610
PSIP1_HUMANPSIP1physical
26496610
SP16H_HUMANSUPT16Hphysical
26496610
RL35_HUMANRPL35physical
26496610
RRP5_HUMANPDCD11physical
26496610
LAR4B_HUMANLARP4Bphysical
26496610
RRP12_HUMANRRP12physical
26496610
LARP1_HUMANLARP1physical
26496610
RL13A_HUMANRPL13Aphysical
26496610
NOG1_HUMANGTPBP4physical
26496610
RL36_HUMANRPL36physical
26496610
C1TM_HUMANMTHFD1Lphysical
26496610
ELYS_HUMANAHCTF1physical
26496610
FA98A_HUMANFAM98Aphysical
26496610
PAIRB_HUMANSERBP1physical
26496610
RL1D1_HUMANRSL1D1physical
26496610
GNL3_HUMANGNL3physical
26496610
SND1_HUMANSND1physical
26496610
NOB1_HUMANNOB1physical
26496610
NOG2_HUMANGNL2physical
26496610
HP1B3_HUMANHP1BP3physical
26496610
RS27L_HUMANRPS27Lphysical
26496610
DDX47_HUMANDDX47physical
26496610
EIF3L_HUMANEIF3Lphysical
26496610
RTCB_HUMANRTCBphysical
26496610
TR112_HUMANTRMT112physical
26496610
DHX29_HUMANDHX29physical
26496610
TEX10_HUMANTEX10physical
26496610
NSUN2_HUMANNSUN2physical
26496610
PAPD1_HUMANMTPAPphysical
26496610
NAT10_HUMANNAT10physical
26496610
TSR1_HUMANTSR1physical
26496610
NKRF_HUMANNKRFphysical
26496610
MEPCE_HUMANMEPCEphysical
26496610
BCCIP_HUMANBCCIPphysical
26496610
PNO1_HUMANPNO1physical
26496610
RT22_HUMANMRPS22physical
26496610
DDX24_HUMANDDX24physical
26496610
WDR18_HUMANWDR18physical
26496610
SFR19_HUMANSCAF1physical
26496610
NOL6_HUMANNOL6physical
26496610
DDX50_HUMANDDX50physical
26496610
CCD86_HUMANCCDC86physical
26496610
MUS81_HUMANMUS81physical
26496610
DOT1L_HUMANDOT1Lphysical
26496610
ZN622_HUMANZNF622physical
26496610
DHX57_HUMANDHX57physical
26496610
H2AV_HUMANH2AFVphysical
26496610
LARP4_HUMANLARP4physical
26496610
BUD23_HUMANWBSCR22physical
26496610
DNJB4_HUMANDNAJB4physical
20145123
NPM_HUMANNPM1physical
20145123
TF65_HUMANRELAphysical
19074833
SP1_HUMANSP1physical
19074833
AP2A_HUMANTFAP2Aphysical
19074833
CD24_HUMANCD24physical
25600590
CDN2A_HUMANCDKN2Aphysical
25600590
ARF_HUMANCDKN2Aphysical
25600590
NEPRO_HUMANC3orf17physical
28514442
RPP25_HUMANRPP25physical
28514442
RP25L_HUMANRPP25Lphysical
28514442
RL36L_HUMANRPL36ALphysical
28514442
RPP40_HUMANRPP40physical
28514442
NMNA1_HUMANNMNAT1physical
28514442
RRP8_HUMANRRP8physical
28514442
ZN800_HUMANZNF800physical
28514442
RPP38_HUMANRPP38physical
28514442
DDX31_HUMANDDX31physical
28514442
NPM3_HUMANNPM3physical
28514442
NVL_HUMANNVLphysical
28514442
RL3_HUMANRPL3physical
28514442
RL26L_HUMANRPL26L1physical
28514442
REXO4_HUMANREXO4physical
28514442
RPF1_HUMANRPF1physical
28514442
PUM3_HUMANKIAA0020physical
28514442
PAPD5_HUMANPAPD5physical
28514442
SPB1_HUMANFTSJ3physical
28514442
SPT2_HUMANSPTY2D1physical
28514442
RL7L_HUMANRPL7L1physical
28514442
BRX1_HUMANBRIX1physical
28514442
DDX56_HUMANDDX56physical
28514442
POP7_HUMANPOP7physical
28514442
GLYR1_HUMANGLYR1physical
28514442
NOC3L_HUMANNOC3Lphysical
28514442
SENP5_HUMANSENP5physical
28514442
NPA1P_HUMANURB1physical
28514442
HJURP_HUMANHJURPphysical
28514442
NOP2_HUMANNOP2physical
28514442
NOP53_HUMANGLTSCR2physical
28514442
NOG1_HUMANGTPBP4physical
28514442
DDX24_HUMANDDX24physical
28514442
MBB1A_HUMANMYBBP1Aphysical
28514442
RPF2_HUMANRPF2physical
28514442
RL4_HUMANRPL4physical
28514442
DDX21_HUMANDDX21physical
28514442
TEX10_HUMANTEX10physical
28514442
DDX27_HUMANDDX27physical
28514442
RBM34_HUMANRBM34physical
28514442
NOG2_HUMANGNL2physical
28514442
NOC2L_HUMANNOC2Lphysical
28514442
POP1_HUMANPOP1physical
28514442
RBM28_HUMANRBM28physical
28514442
RL23A_HUMANRPL23Aphysical
28514442
SURF6_HUMANSURF6physical
28514442
ZFP62_HUMANZFP62physical
28514442
DDX51_HUMANDDX51physical
28514442
RL7A_HUMANRPL7Aphysical
28514442
CC137_HUMANCCDC137physical
28514442
MAK16_HUMANMAK16physical
28514442
NUCL_HUMANNCLphysical
28514442
CENPC_HUMANCENPCphysical
28514442
E2AK2_HUMANEIF2AK2physical
12882984
P53_HUMANTP53physical
15964625
CDN1A_HUMANCDKN1Aphysical
15964625
CDN2A_HUMANCDKN2Aphysical
16679321
ARF_HUMANCDKN2Aphysical
16679321
FBXW7_HUMANFBXW7physical
28920929
CENPW_HUMANCENPWphysical
28920929
TAT_HV1H2tatphysical
28920929

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 NPM_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-4; SER-10; THR-95; SER-125; SER-139 ANDSER-254, AND MASS SPECTROMETRY.
"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-32; LYS-150; LYS-257;LYS-267 AND LYS-273, AND MASS SPECTROMETRY.
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-150; LYS-154 AND LYS-212,AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Polo-like kinase 2-dependent phosphorylation of NPM/B23 on serine 4triggers centriole duplication.";
Krause A., Hoffmann I.;
PLoS ONE 5:E9849-E9849(2010).
Cited for: FUNCTION, PHOSPHORYLATION AT SER-4 BY PLK2, AND MUTAGENESIS OF SER-4;THR-95; SER-125 AND THR-199.
"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-70 AND SER-125, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-125, ANDMASS 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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-4; SER-10; THR-95; SER-125; SER-139 ANDSER-254, 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-125, AND MASSSPECTROMETRY.
"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-70; THR-75; THR-95;SER-125; SER-139; THR-234; THR-237; SER-243; SER-254; SER-260 ANDTHR-279, 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-70; SER-125 AND SER-254,AND MASS SPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND MASSSPECTROMETRY.
"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-70; SER-88; SER-125 ANDTHR-279, AND MASS SPECTROMETRY.
"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-10; SER-70; SER-125;SER-243; SER-254 AND SER-260, AND MASS 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-70; SER-125; SER-137;THR-199; THR-234; THR-237 AND SER-260, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; THR-75; THR-95;SER-137; THR-199; SER-254 AND SER-260, AND MASS SPECTROMETRY.
"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-70; SER-125 AND SER-254,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 SER-4; SER-10; SER-70;THR-95; THR-199 AND SER-254, AND MASS SPECTROMETRY.
"B23/nucleophosmin serine 4 phosphorylation mediates mitotic functionsof polo-like kinase 1.";
Zhang H., Shi X., Paddon H., Hampong M., Dai W., Pelech S.;
J. Biol. Chem. 279:35726-35734(2004).
Cited for: PHOSPHORYLATION AT SER-4 BY PLK1.
"Nucleophosmin phosphorylation by v-cyclin-CDK6 controls KSHVlatency.";
Sarek G., Jaerviluoma A., Moore H.M., Tojkander S., Vartia S.,Biberfeld P., Laiho M., Ojala P.M.;
PLoS Pathog. 6:E1000818-E1000818(2010).
Cited for: PHOSPHORYLATION AT THR-199 BY CDK6.
"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 THR-199, AND MASSSPECTROMETRY.
Sumoylation
ReferencePubMed
"Sumoylation induced by the Arf tumor suppressor: a p53-independentfunction.";
Tago K., Chiocca S., Sherr C.J.;
Proc. Natl. Acad. Sci. U.S.A. 102:7689-7694(2005).
Cited for: SUMOYLATION AT LYS-230 AND LYS-263.

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