NPM_MOUSE - dbPTM
NPM_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NPM_MOUSE
UniProt AC Q61937
Protein Name Nucleophosmin
Gene Name Npm1
Organism Mus musculus (Mouse).
Sequence Length 292
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. Colocalizes w
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. In complex with MYC enhances the transcription of MYC target genes..
Protein Sequence MEDSMDMDMSPLRPQNYLFGCELKADKDYHFKVDNDENEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEITPPVVLRLKCGSGPVHISGQHLVAVEEDAESEDEDEEDVKLLGMSGKRSAPGGGNKVPQKKVKLDEDDEDDDEDDEDDEDDDDDDFDEEETEEKVPVKKSVRDTPAKNAQKSNQNGKDLKPSTPRSKGQESFKKQEKTPKTPKGPSSVEDIKAKMQASIEKGGSLPKVEAKFINYVKNCFRMTDQEAIQDLWQWRKSL
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		13.41-
4Phosphorylation----MEDSMDMDMSP
----CCCCCCCCCCC		11.9026824392
10PhosphorylationDSMDMDMSPLRPQNY
CCCCCCCCCCCCCCE		19.2723527152
17PhosphorylationSPLRPQNYLFGCELK
CCCCCCCEEEEEEEE		9.7321149613
27AcetylationGCELKADKDYHFKVD
EEEEECCCCCEEEEC		66.1166695887
27UbiquitinationGCELKADKDYHFKVD
EEEEECCCCCEEEEC		66.11-
29PhosphorylationELKADKDYHFKVDND
EEECCCCCEEEECCC		18.2025367039
32AcetylationADKDYHFKVDNDENE
CCCCCEEEECCCCCC		35.0568491
32UbiquitinationADKDYHFKVDNDENE
CCCCCEEEECCCCCC		35.05-
43PhosphorylationDENEHQLSLRTVSLG
CCCCEEEEEEEEECC		14.8324899341
46PhosphorylationEHQLSLRTVSLGAGA
CEEEEEEEEECCCCC		21.5325619855
48PhosphorylationQLSLRTVSLGAGAKD
EEEEEEEECCCCCCC		22.0725619855
54UbiquitinationVSLGAGAKDELHIVE
EECCCCCCCEEEEEE		51.31-
67PhosphorylationVEAEAMNYEGSPIKV
EEEEHHCCCCCCEEE		14.4725521595
70PhosphorylationEAMNYEGSPIKVTLA
EHHCCCCCCEEEEEE		16.1224925903
75PhosphorylationEGSPIKVTLATLKMS
CCCCEEEEEEEEEEE		12.9826160508
78PhosphorylationPIKVTLATLKMSVQP
CEEEEEEEEEEEECC		29.9819060867
82PhosphorylationTLATLKMSVQPTVSL
EEEEEEEEECCEEEE		18.9326643407
86PhosphorylationLKMSVQPTVSLGGFE
EEEEECCEEEECCEE		12.9723984901
88PhosphorylationMSVQPTVSLGGFEIT
EEECCEEEECCEEEC		24.6326745281
95PhosphorylationSLGGFEITPPVVLRL
EECCEEECCCEEEEE		17.8426745281
106PhosphorylationVLRLKCGSGPVHISG
EEEEEECCCCEEECC		49.7725521595
112PhosphorylationGSGPVHISGQHLVAV
CCCCEEECCEEEEEE		19.9524925903
125PhosphorylationAVEEDAESEDEDEED
EEECCCCCCCCCHHH		52.6624925903
139PhosphorylationDVKLLGMSGKRSAPG
HHHHEEECCCCCCCC		39.0926824392
141AcetylationKLLGMSGKRSAPGGG
HHEEECCCCCCCCCC		35.5568495
141UbiquitinationKLLGMSGKRSAPGGG
HHEEECCCCCCCCCC		35.55-
143PhosphorylationLGMSGKRSAPGGGNK
EEECCCCCCCCCCCC		42.1525266776
150AcetylationSAPGGGNKVPQKKVK
CCCCCCCCCCCCCCC		59.5768499
154AcetylationGGNKVPQKKVKLDED
CCCCCCCCCCCCCCC		54.1668503
154UbiquitinationGGNKVPQKKVKLDED
CCCCCCCCCCCCCCC		54.16-
155AcetylationGNKVPQKKVKLDEDD
CCCCCCCCCCCCCCC		39.087303091
185PhosphorylationDDFDEEETEEKVPVK
CCCCHHHHHHCCCCC		53.3725619855
194PhosphorylationEKVPVKKSVRDTPAK
HCCCCCCHHCCCHHH		19.3725266776
198PhosphorylationVKKSVRDTPAKNAQK
CCCHHCCCHHHHHHH		18.0026824392
206ADP-ribosylationPAKNAQKSNQNGKDL
HHHHHHHHCCCCCCC		31.41-
211AcetylationQKSNQNGKDLKPSTP
HHHCCCCCCCCCCCC		68.39109345
214AcetylationNQNGKDLKPSTPRSK
CCCCCCCCCCCCCCH		47.24-
214MalonylationNQNGKDLKPSTPRSK
CCCCCCCCCCCCCCH		47.2426320211
216PhosphorylationNGKDLKPSTPRSKGQ
CCCCCCCCCCCCHHH		49.8327566939
217PhosphorylationGKDLKPSTPRSKGQE
CCCCCCCCCCCHHHH		31.1126824392
220PhosphorylationLKPSTPRSKGQESFK
CCCCCCCCHHHHHHH		42.2026745281
221AcetylationKPSTPRSKGQESFKK
CCCCCCCHHHHHHHC		66.9315620105
225PhosphorylationPRSKGQESFKKQEKT
CCCHHHHHHHCCCCC		34.1826824392
227AcetylationSKGQESFKKQEKTPK
CHHHHHHHCCCCCCC		63.9368507
228AcetylationKGQESFKKQEKTPKT
HHHHHHHCCCCCCCC		62.7712563253
231AcetylationESFKKQEKTPKTPKG
HHHHCCCCCCCCCCC		68.58-
232PhosphorylationSFKKQEKTPKTPKGP
HHHCCCCCCCCCCCC		29.3026239621
235PhosphorylationKQEKTPKTPKGPSSV
CCCCCCCCCCCCCCH		31.2826239621
237MalonylationEKTPKTPKGPSSVED
CCCCCCCCCCCCHHH		84.4526320211
237UbiquitinationEKTPKTPKGPSSVED
CCCCCCCCCCCCHHH		84.45-
240PhosphorylationPKTPKGPSSVEDIKA
CCCCCCCCCHHHHHH		56.5423684622
241PhosphorylationKTPKGPSSVEDIKAK
CCCCCCCCHHHHHHH		32.4327087446
246UbiquitinationPSSVEDIKAKMQASI
CCCHHHHHHHHHHHH		55.03-
248UbiquitinationSVEDIKAKMQASIEK
CHHHHHHHHHHHHHC		26.92-
248AcetylationSVEDIKAKMQASIEK
CHHHHHHHHHHHHHC		26.92-
248MalonylationSVEDIKAKMQASIEK
CHHHHHHHHHHHHHC		26.9226320211
249OxidationVEDIKAKMQASIEKG
HHHHHHHHHHHHHCC		4.8717203969
252PhosphorylationIKAKMQASIEKGGSL
HHHHHHHHHHCCCCC		17.8722942356
255UbiquitinationKMQASIEKGGSLPKV
HHHHHHHCCCCCCHH		67.89-
255AcetylationKMQASIEKGGSLPKV
HHHHHHHCCCCCCHH		67.8923806337
255MalonylationKMQASIEKGGSLPKV
HHHHHHHCCCCCCHH		67.8926320211
258PhosphorylationASIEKGGSLPKVEAK
HHHHCCCCCCHHHHH		50.6026824392
261UbiquitinationEKGGSLPKVEAKFIN
HCCCCCCHHHHHHHH		58.98-
265AcetylationSLPKVEAKFINYVKN
CCCHHHHHHHHHHHH		33.0223806337
265SuccinylationSLPKVEAKFINYVKN
CCCHHHHHHHHHHHH		33.0223806337
265UbiquitinationSLPKVEAKFINYVKN
CCCHHHHHHHHHHHH		33.02-
265MalonylationSLPKVEAKFINYVKN
CCCHHHHHHHHHHHH		33.0226320211
271UbiquitinationAKFINYVKNCFRMTD
HHHHHHHHHHHHCCC		37.32-
271AcetylationAKFINYVKNCFRMTD
HHHHHHHHHHHHCCC		37.3223806337
273GlutathionylationFINYVKNCFRMTDQE
HHHHHHHHHHCCCHH		1.5724333276
277PhosphorylationVKNCFRMTDQEAIQD
HHHHHHCCCHHHHHH		30.21-
290AcetylationQDLWQWRKSL-----
HHHHHHHHHC-----		53.82-
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
4SPhosphorylationKinasePLK1Q07832
Uniprot
4SPhosphorylationKinasePLK2P53351
Uniprot
48SPhosphorylationKinasePKACAP17612
PSP
88SPhosphorylationKinasePKACAP17612
PSP
95TPhosphorylationKinasePKACAP17612
PSP
125SPhosphorylationKinaseCSNK2A1P68400
GPS
125SPhosphorylationKinasePKACAP17612
PSP
198TPhosphorylationKinaseCDK1P11440
Uniprot
198TPhosphorylationKinaseCDK2P24941
PSP
198TPhosphorylationKinaseCDK2P97377
Uniprot
217TPhosphorylationKinaseCDK1P11440
Uniprot
232TPhosphorylationKinaseCDK1P11440
Uniprot
235TPhosphorylationKinaseCDK1P11440
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
4SPhosphorylation

-
4SPhosphorylation

-
4SPhosphorylation

-
70SPhosphorylation

-
125SPhosphorylation

-
198TPhosphorylation

-
198TPhosphorylation

-
198TPhosphorylation

-
198TPhosphorylation

-
217TPhosphorylation

-
232TPhosphorylation

-
235TPhosphorylation

-
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FBXW7_MOUSEFbxw7physical
18625840
SRSF2_MOUSESrsf2physical
16376875
RL7_MOUSERpl7physical
18809582
RS3_MOUSERps3physical
18809582
RL4_MOUSERpl4physical
18809582
RL5_MOUSERpl5physical
18809582
RL13A_MOUSERpl13aphysical
18809582
RL22_MOUSERpl22physical
18809582
RL27_MOUSERpl27physical
18809582
RS3A_MOUSERps3a1physical
18809582
RS5_MOUSERps5physical
18809582
RS6_MOUSERps6physical
18809582
RS7_MOUSERps7physical
18809582
NUCL_MOUSENclphysical
18809582
CPSF6_MOUSECpsf6physical
18809582
ROA1_MOUSEHnrnpa1physical
18809582
HNRH2_MOUSEHnrnph2physical
18809582
EF2_MOUSEEef2physical
18809582
DDX1_MOUSEDdx1physical
18809582
DHX9_MOUSEDhx9physical
18809582
EBPL_MOUSEEbplphysical
18809582
NUP50_MOUSENup50physical
18809582
NUP62_MOUSENup62physical
18809582
BRCA1_MOUSEBrca1physical
18809582
RL5_MOUSERpl5physical
16648475
ROCK2_MOUSERock2physical
17015463
VIME_MOUSEVimphysical
17015463
CDN2A_MOUSECdkn2aphysical
15485902
ARF_MOUSECdkn2aphysical
15485902
E2AK2_MOUSEEif2ak2physical
12882984
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NPM_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND MASSSPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-125, AND MASSSPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, AND MASSSPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND MASSSPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, AND MASSSPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND MASSSPECTROMETRY.
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line.";
Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
Mol. Cell. Proteomics 3:279-286(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252 AND SER-258, ANDMASS SPECTROMETRY.

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