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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Acetylation | ------MAAGTAAAL ------CCHHHHHHH | 18.01 | 20068231 | |
5 | Phosphorylation | ---MAAGTAAALAFL ---CCHHHHHHHHHH | 14.38 | 20873877 | |
13 | Phosphorylation | AAALAFLSQESRTRA HHHHHHHCHHHCCCC | 26.00 | 21955146 | |
16 | Phosphorylation | LAFLSQESRTRAGGV HHHHCHHHCCCCCCC | 31.17 | 21955146 | |
18 | Phosphorylation | FLSQESRTRAGGVGG HHCHHHCCCCCCCCC | 33.86 | 21406692 | |
19 | Methylation | LSQESRTRAGGVGGL HCHHHCCCCCCCCCC | 30.08 | 115485511 | |
27 | Methylation | AGGVGGLRVPAPVTM CCCCCCCCCCCCEEE | 35.33 | 24129315 | |
41 | Glutathionylation | MDSFFFGCELSGHTR ECEEEECEEECCCEE | 3.93 | 22555962 | |
53 | Sumoylation | HTRSFTFKVEEEDDA CEEEEEEEEECCCCH | 45.75 | - | |
102 | Acetylation | AVPVANLKLSCQPML EEEEECCEEECEECC | 37.86 | 26051181 | |
102 | Ubiquitination | AVPVANLKLSCQPML EEEEECCEEECEECC | 37.86 | 29967540 | |
105 | Glutathionylation | VANLKLSCQPMLSLD EECCEEECEECCCCC | 8.36 | 22555962 | |
125 | Sumoylation | PPVTFRLKSGSGPVR CCEEEEECCCCCCEE | 48.81 | - | |
125 | Ubiquitination | PPVTFRLKSGSGPVR CCEEEEECCCCCCEE | 48.81 | 29967540 | |
125 | Sumoylation | PPVTFRLKSGSGPVR CCEEEEECCCCCCEE | 48.81 | - | |
126 | Phosphorylation | PVTFRLKSGSGPVRI CEEEEECCCCCCEEE | 42.66 | 21406692 | |
128 | Phosphorylation | TFRLKSGSGPVRITG EEEECCCCCCEEEEE | 47.19 | 23403867 | |
134 | Phosphorylation | GSGPVRITGRHQIVT CCCCEEEEEEEEEEE | 20.00 | 23403867 | |
141 | Phosphorylation | TGRHQIVTMSNDVSE EEEEEEEEEECCCCH | 19.26 | 25137130 | |
143 | Phosphorylation | RHQIVTMSNDVSEEE EEEEEEEECCCCHHH | 22.10 | 26552605 | |
147 | Phosphorylation | VTMSNDVSEEESEEE EEEECCCCHHHHHHH | 42.00 | 17081983 | |
151 | Phosphorylation | NDVSEEESEEEEEDS CCCCHHHHHHHCCCC | 54.29 | 17081983 | |
158 | Phosphorylation | SEEEEEDSDEEEVEL HHHHCCCCCHHHHHH | 50.64 | 17081983 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NPM3_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
CE126_HUMAN | KIAA1377 | physical | 16169070 | |
NPM_HUMAN | NPM1 | physical | 22362753 | |
NPM_HUMAN | NPM1 | physical | 22939629 | |
NUCL_HUMAN | NCL | physical | 22863883 | |
NPM2_HUMAN | NPM2 | physical | 25416956 | |
ARGL1_HUMAN | ARGLU1 | physical | 26344197 | |
ATPB_HUMAN | ATP5B | physical | 26344197 | |
EF1G_HUMAN | EEF1G | physical | 26344197 | |
NUCL_HUMAN | NCL | physical | 26344197 | |
NPM_HUMAN | NPM1 | physical | 26344197 | |
TPD53_HUMAN | TPD52L1 | physical | 26344197 | |
1433E_HUMAN | YWHAE | physical | 26344197 |
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. |
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Acetylation | |
Reference | PubMed |
"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 | |
Reference | PubMed |
"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. |