UniProt ID | P2R3B_HUMAN | |
---|---|---|
UniProt AC | Q9Y5P8 | |
Protein Name | Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta | |
Gene Name | PPP2R3B | |
Organism | Homo sapiens (Human). | |
Sequence Length | 575 | |
Subcellular Localization | Nucleus . | |
Protein Description | The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.. | |
Protein Sequence | MPPGKVLQPVLKMKVDELFLYWLSEASTQRMLQDCLRRIKAPGRDQPTPGDGEQPGAWPTAPLAAPRPSGLEPPGTPGPGPALPLGAASSPRNAPHVRGTRRSAGTRVVQTRKEEPLPPATSQSIPTFYFPRGRPQDSVNVDAVISKIESTFARFPHERATMDDMGLVAKACGCPLYWKGPLFYGAGGERTGSVSVHKFVAMWRKILQNCHDDAAKFVHLLMSPGCNYLVQEDFVPFLQDVVNTHPGLSFLKEASEFHSRYITTVIQRIFYAVNRSWSGRITCAELRRSSFLQNVALLEEEADINQLTEFFSYEHFYVIYCKFWELDTDHDLLIDADDLARHNDHALSTKMIDRIFSGAVTRGRKVQKEGKISYADFVWFLISEEDKKTPTSIEYWFRCMDLDGDGALSMFELEYFYEEQCRRLDSMAIEALPFQDCLCQMLDLVKPRTEGKITLQDLKRCKLANVFFDTFFNIEKYLDHEQKEQISLLRDGDSGGPELSDWEKYAAEEYDILVAEETAGEPWEDGFEAELSPVEQKLSALRSPLAQRPFFEAPSPLGAVDLYEYACGDEDLEPL | |
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 |
---|---|---|---|---|---|
12 | Ubiquitination | KVLQPVLKMKVDELF CCCHHHHHCCHHHHH | 36.59 | - | |
89 | Phosphorylation | ALPLGAASSPRNAPH CCCCCCCCCCCCCCC | 40.10 | 18691976 | |
90 | Phosphorylation | LPLGAASSPRNAPHV CCCCCCCCCCCCCCC | 24.13 | 17192257 | |
113 | Ubiquitination | TRVVQTRKEEPLPPA CEEEECCCCCCCCCC | 70.58 | - | |
147 | Ubiquitination | NVDAVISKIESTFAR CHHHHHHHHHHHHHC | 39.09 | - | |
170 | Ubiquitination | DDMGLVAKACGCPLY CHHHHHHHHHCCCEE | 36.41 | - | |
179 | Ubiquitination | CGCPLYWKGPLFYGA HCCCEEEECCEEECC | 36.77 | - | |
184 | Phosphorylation | YWKGPLFYGAGGERT EEECCEEECCCCCCC | 17.47 | 22817900 | |
249 | Phosphorylation | VNTHPGLSFLKEASE HHHCCCHHHHHHHHH | 34.15 | 24719451 | |
348 | Phosphorylation | RHNDHALSTKMIDRI HCCCCHHHHHHHHHH | 27.11 | 24719451 | |
349 | Phosphorylation | HNDHALSTKMIDRIF CCCCHHHHHHHHHHH | 26.02 | 24719451 | |
350 | Ubiquitination | NDHALSTKMIDRIFS CCCHHHHHHHHHHHH | 30.40 | - | |
357 | Phosphorylation | KMIDRIFSGAVTRGR HHHHHHHHCCCCCCC | 24.38 | 24719451 | |
452 | Ubiquitination | VKPRTEGKITLQDLK CCCCCCCCCCHHHHH | 26.70 | 29967540 | |
459 | Ubiquitination | KITLQDLKRCKLANV CCCHHHHHHCCCCCC | 65.13 | 29967540 | |
483 | Ubiquitination | KYLDHEQKEQISLLR HHCCHHHHHHHEEEC | 48.91 | 29967540 | |
510 | Phosphorylation | EKYAAEEYDILVAEE HHHHHHHCCEEEEEE | 10.37 | 28102081 | |
518 | Phosphorylation | DILVAEETAGEPWED CEEEEEECCCCCCCC | 31.31 | 28102081 | |
532 | Phosphorylation | DGFEAELSPVEQKLS CCCCCCCCHHHHHHH | 20.57 | 28102081 | |
543 | Phosphorylation | QKLSALRSPLAQRPF HHHHHHHCHHHCCCC | 25.72 | 28122231 |
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 P2R3B_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of P2R3B_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 P2R3B_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
TM14B_HUMAN | TMEM14B | physical | 21516116 |
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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Phosphorylation | |
Reference | PubMed |
"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-90, AND MASSSPECTROMETRY. | |
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-184, AND MASSSPECTROMETRY. |