NPM3_HUMAN - dbPTM
NPM3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NPM3_HUMAN
UniProt AC O75607
Protein Name Nucleoplasmin-3
Gene Name NPM3
Organism Homo sapiens (Human).
Sequence Length 178
Subcellular Localization Nucleus .
Protein Description May act as a chaperone..
Protein Sequence MAAGTAAALAFLSQESRTRAGGVGGLRVPAPVTMDSFFFGCELSGHTRSFTFKVEEEDDAEHVLALTMLCLTEGAKDECNVVEVVARNHDHQEIAVPVANLKLSCQPMLSLDDFQLQPPVTFRLKSGSGPVRITGRHQIVTMSNDVSEEESEEEEEDSDEEEVELCPILPAKKQGGRP
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
2Acetylation------MAAGTAAAL
------CCHHHHHHH
18.0120068231
5Phosphorylation---MAAGTAAALAFL
---CCHHHHHHHHHH
14.3820873877
13PhosphorylationAAALAFLSQESRTRA
HHHHHHHCHHHCCCC
26.0021955146
16PhosphorylationLAFLSQESRTRAGGV
HHHHCHHHCCCCCCC
31.1721955146
18PhosphorylationFLSQESRTRAGGVGG
HHCHHHCCCCCCCCC
33.8621406692
19MethylationLSQESRTRAGGVGGL
HCHHHCCCCCCCCCC
30.08115485511
27MethylationAGGVGGLRVPAPVTM
CCCCCCCCCCCCEEE
35.3324129315
41GlutathionylationMDSFFFGCELSGHTR
ECEEEECEEECCCEE
3.9322555962
53SumoylationHTRSFTFKVEEEDDA
CEEEEEEEEECCCCH
45.75-
102AcetylationAVPVANLKLSCQPML
EEEEECCEEECEECC
37.8626051181
102UbiquitinationAVPVANLKLSCQPML
EEEEECCEEECEECC
37.8629967540
105GlutathionylationVANLKLSCQPMLSLD
EECCEEECEECCCCC
8.3622555962
125SumoylationPPVTFRLKSGSGPVR
CCEEEEECCCCCCEE
48.81-
125UbiquitinationPPVTFRLKSGSGPVR
CCEEEEECCCCCCEE
48.8129967540
125SumoylationPPVTFRLKSGSGPVR
CCEEEEECCCCCCEE
48.81-
126PhosphorylationPVTFRLKSGSGPVRI
CEEEEECCCCCCEEE
42.6621406692
128PhosphorylationTFRLKSGSGPVRITG
EEEECCCCCCEEEEE
47.1923403867
134PhosphorylationGSGPVRITGRHQIVT
CCCCEEEEEEEEEEE
20.0023403867
141PhosphorylationTGRHQIVTMSNDVSE
EEEEEEEEEECCCCH
19.2625137130
143PhosphorylationRHQIVTMSNDVSEEE
EEEEEEEECCCCHHH
22.1026552605
147PhosphorylationVTMSNDVSEEESEEE
EEEECCCCHHHHHHH
42.0017081983
151PhosphorylationNDVSEEESEEEEEDS
CCCCHHHHHHHCCCC
54.2917081983
158PhosphorylationSEEEEEDSDEEEVEL
HHHHCCCCCHHHHHH
50.6417081983

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 NPM3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NPM3_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 NPM3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CE126_HUMANKIAA1377physical
16169070
NPM_HUMANNPM1physical
22362753
NPM_HUMANNPM1physical
22939629
NUCL_HUMANNCLphysical
22863883
NPM2_HUMANNPM2physical
25416956
ARGL1_HUMANARGLU1physical
26344197
ATPB_HUMANATP5Bphysical
26344197
EF1G_HUMANEEF1Gphysical
26344197
NUCL_HUMANNCLphysical
26344197
NPM_HUMANNPM1physical
26344197
TPD53_HUMANTPD52L1physical
26344197
1433E_HUMANYWHAEphysical
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 NPM3_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 ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-147; SER-151 ANDSER-158, 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-147; SER-151 ANDSER-158, AND MASS SPECTROMETRY.

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