NPM_RAT - dbPTM
NPM_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NPM_RAT
UniProt AC P13084
Protein Name Nucleophosmin
Gene Name Npm1
Organism Rattus norvegicus (Rat).
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 MEDSMDMDMSPLRPQNYLFGCELKADKDYHFKVDNDENEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEITPPVVLRLKCGSGPVHISGQHLVAVEEDAESEDEDEEDVKLLGMSGKRSAPGGGNKVPQKKVKLDEDDDEDDEDDEDDEDDDDDDFDEEETEEKVPVKKSVRDTPAKNAQKSNQNGKDLKPSTPRSKGQESFKKQEKTPKTPKGPSSVEDIKAKMQASIEKGGSLPKVEAKFINYVKNCFRMTDQEAIQDLWQWRKSL
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		11.9027097102
10PhosphorylationDSMDMDMSPLRPQNY
CCCCCCCCCCCCCCE		19.2727097102
17PhosphorylationSPLRPQNYLFGCELK
CCCCCCCEEEEEEEE		9.7325575281
27SuccinylationGCELKADKDYHFKVD
EEEEECCCCCEEEEC		66.1126843850
27AcetylationGCELKADKDYHFKVD
EEEEECCCCCEEEEC		66.1122902405
32AcetylationADKDYHFKVDNDENE
CCCCCEEEECCCCCC		35.0525786129
43PhosphorylationDENEHQLSLRTVSLG
CCCCEEEEEEEEECC		14.83-
54AcetylationVSLGAGAKDELHIVE
EECCCCCCCEEEEEE		51.3122902405
67PhosphorylationVEAEAMNYEGSPIKV
EEEEHHCCCCCCEEE		14.4723589303
70PhosphorylationEAMNYEGSPIKVTLA
EHHCCCCCCEEEEEE		16.1223712012
75PhosphorylationEGSPIKVTLATLKMS
CCCCEEEEEEEEEEE		12.9822668510
78PhosphorylationPIKVTLATLKMSVQP
CEEEEEEEEEEEECC		29.9821630457
95PhosphorylationSLGGFEITPPVVLRL
EECCEEECCCEEEEE		17.84-
106PhosphorylationVLRLKCGSGPVHISG
EEEEEECCCCEEECC		49.7716641100
112PhosphorylationGSGPVHISGQHLVAV
CCCCEEECCEEEEEE		19.9528551015
125PhosphorylationAVEEDAESEDEDEED
EEECCCCCCCCCHHH		52.6623712012
139PhosphorylationDVKLLGMSGKRSAPG
HHHHEEECCCCCCCC		39.0921630457
141AcetylationKLLGMSGKRSAPGGG
HHEEECCCCCCCCCC		35.5568493
143PhosphorylationLGMSGKRSAPGGGNK
EEECCCCCCCCCCCC		42.1523984901
150AcetylationSAPGGGNKVPQKKVK
CCCCCCCCCCCCCCC		59.5725786129
154AcetylationGGNKVPQKKVKLDED
CCCCCCCCCCCCCCC		54.1625786129
185PhosphorylationDDFDEEETEEKVPVK
CCCCHHHHHHCCCCC		53.3728689409
198PhosphorylationVKKSVRDTPAKNAQK
CCCHHCCCHHHHHHH		18.0028432305
206ADP-ribosylationPAKNAQKSNQNGKDL
HHHHHHHHCCCCCCC		31.41-
211AcetylationQKSNQNGKDLKPSTP
HHHCCCCCCCCCCCC		68.3922902405
214SuccinylationNQNGKDLKPSTPRSK
CCCCCCCCCCCCCCH		47.2426843850
214AcetylationNQNGKDLKPSTPRSK
CCCCCCCCCCCCCCH		47.2422902405
216PhosphorylationNGKDLKPSTPRSKGQ
CCCCCCCCCCCCHHH		49.8326437020
217PhosphorylationGKDLKPSTPRSKGQE
CCCCCCCCCCCHHHH		31.1125532521
220PhosphorylationLKPSTPRSKGQESFK
CCCCCCCCHHHHHHH		42.2028432305
221AcetylationKPSTPRSKGQESFKK
CCCCCCCHHHHHHHC		66.9322902405
225PhosphorylationPRSKGQESFKKQEKT
CCCHHHHHHHCCCCC		34.1828432305
227AcetylationSKGQESFKKQEKTPK
CHHHHHHHCCCCCCC		63.9322902405
228AcetylationKGQESFKKQEKTPKT
HHHHHHHCCCCCCCC		62.77-
232PhosphorylationSFKKQEKTPKTPKGP
HHHCCCCCCCCCCCC		29.30-
235PhosphorylationKQEKTPKTPKGPSSV
CCCCCCCCCCCCCCH		31.2822817900
237AcetylationEKTPKTPKGPSSVED
CCCCCCCCCCCCHHH		84.4522902405
240PhosphorylationPKTPKGPSSVEDIKA
CCCCCCCCCHHHHHH		56.5428432305
241PhosphorylationKTPKGPSSVEDIKAK
CCCCCCCCHHHHHHH		32.4321738781
246AcetylationPSSVEDIKAKMQASI
CCCHHHHHHHHHHHH		55.03-
248AcetylationSVEDIKAKMQASIEK
CHHHHHHHHHHHHHC		26.9222902405
252PhosphorylationIKAKMQASIEKGGSL
HHHHHHHHHHCCCCC		17.8721630457
255 (in isoform 2)Acetylation-67.89-
255AcetylationKMQASIEKGGSLPKV
HHHHHHHCCCCCCHH		67.8922902405
258PhosphorylationASIEKGGSLPKVEAK
HHHHCCCCCCHHHHH		50.6016641100
261AcetylationEKGGSLPKVEAKFIN
HCCCCCCHHHHHHHH		58.9826302492
265AcetylationSLPKVEAKFINYVKN
CCCHHHHHHHHHHHH		33.0225786129
265SuccinylationSLPKVEAKFINYVKN
CCCHHHHHHHHHHHH		33.02-
271AcetylationAKFINYVKNCFRMTD
HHHHHHHHHHHHCCC		37.3225786129
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
4SPhosphorylationKinasePLK1Q62673
Uniprot
4SPhosphorylationKinasePLK2Q9R012
Uniprot
70SPhosphorylationKinaseCDK1P06493
PSP
125SPhosphorylationKinaseCDK2Q63699
Uniprot
198TPhosphorylationKinaseCDK1P39951
Uniprot
198TPhosphorylationKinaseCDK2Q63699
Uniprot
217TPhosphorylationKinaseCDK1P39951
Uniprot
232TPhosphorylationKinaseCDK1P39951
Uniprot
235TPhosphorylationKinaseCDK1P06493
PSP
235TPhosphorylationKinaseCDK1P39951
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_RAT !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of NPM_RAT !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NPM_RAT

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:regulation of aquaporin-2 phosphorylation at two sites.";
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-125, ANDMASS SPECTROMETRY.

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