| UniProt ID | PI51B_HUMAN | |
|---|---|---|
| UniProt AC | O14986 | |
| Protein Name | Phosphatidylinositol 4-phosphate 5-kinase type-1 beta | |
| Gene Name | PIP5K1B | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 540 | |
| Subcellular Localization | Endomembrane system. Associated with membranes.. | |
| Protein Description | Participates in the biosynthesis of phosphatidylinositol 4,5-bisphosphate. Mediates RAC1-dependent reorganization of actin filaments. Contributes to the activation of PLD2. Together with PIP5K1A is required after stimulation of G-protein coupled receptors for stable platelet adhesion (By similarity).. | |
| Protein Sequence | MSSAAENGEAAPGKQNEEKTYKKTASSAIKGAIQLGIGYTVGNLTSKPERDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYLYSICSEPLIELSNPGASGSLFFVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGGINIRIVVMNNVLPRSMRMHFTYDLKGSTYKRRASRKEREKSNPTFKDLDFLQDMHEGLYFDTETYNALMKTLQRDCRVLESFKIMDYSLLLGIHFLDHSLKEKEEETPQNVPDAKRTGMQKVLYSTAMESIQGPGKSGDGIITENPDTMGGIPAKSHRGEKLLLFMGIIDILQSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMNSRVFKKIQALKASPSKKRCNSIAALKATSQEIVSSISQEWKDEKRDLLTEGQSFSSLDEEALGSRHRPDLVPSTPSLFEAASLATTISSSSLYVNEHYPHDRPTLYSNSKGLPSSSTFTLEEGTIYLTAEPNTLEVQDDNASVLDVYL | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSSAAENGE ------CCCCHHCCC | 28.78 | - | |
| 3 | Phosphorylation | -----MSSAAENGEA -----CCCCHHCCCC | 30.14 | - | |
| 32 (in isoform 2) | Phosphorylation | - | 4.95 | 21964256 | |
| 39 | Phosphorylation | AIQLGIGYTVGNLTS HHHHCCCEEECCCCC | 9.06 | 22210691 | |
| 45 | Phosphorylation | GYTVGNLTSKPERDV CEEECCCCCCCCHHC | 38.41 | 22210691 | |
| 47 | Ubiquitination | TVGNLTSKPERDVLM EECCCCCCCCHHCCC | 45.74 | - | |
| 63 (in isoform 2) | Phosphorylation | - | 3.46 | 25690035 | |
| 64 (in isoform 2) | Phosphorylation | - | 13.30 | 25690035 | |
| 67 (in isoform 2) | Phosphorylation | - | 57.65 | 25690035 | |
| 105 | Phosphorylation | FGIKPDDYLYSICSE HCCCCCCCHHHHHCC | 18.21 | 19553680 | |
| 143 | Ubiquitination | IIKTVQHKEAEFLQK EEEECCHHHHHHHHH | 41.34 | - | |
| 150 (in isoform 1) | Ubiquitination | - | 54.89 | 21906983 | |
| 150 | Ubiquitination | KEAEFLQKLLPGYYM HHHHHHHHHCCCHHC | 54.89 | 2190698 | |
| 165 | Phosphorylation | NLNQNPRTLLPKFYG CCCCCCCHHHHHCCE | 33.62 | - | |
| 190 (in isoform 2) | Ubiquitination | - | 20.71 | 21906983 | |
| 205 | Ubiquitination | MHFTYDLKGSTYKRR EEEEEECCCCHHHHH | 48.17 | - | |
| 301 | Methylation | AKRTGMQKVLYSTAM HHHHCHHHHHHHHHH | 25.89 | - | |
| 301 | Trimethylation | AKRTGMQKVLYSTAM HHHHCHHHHHHHHHH | 25.89 | - | |
| 360 | Ubiquitination | QSYRLMKKLEHSWKA HHHHHHHHCCCCEEE | 45.18 | - | |
| 374 | Phosphorylation | ALVYDGDTVSVHRPS EEEECCCCEEEECCH | 21.88 | 28387310 | |
| 383 | Phosphorylation | SVHRPSFYADRFLKF EEECCHHHHHHHHHH | 16.36 | 28387310 | |
| 393 | Phosphorylation | RFLKFMNSRVFKKIQ HHHHHHHHHHHHHHH | 20.31 | 28387310 | |
| 405 | Phosphorylation | KIQALKASPSKKRCN HHHHHHCCCCCCCCC | 28.28 | 28450419 | |
| 407 | Phosphorylation | QALKASPSKKRCNSI HHHHCCCCCCCCCHH | 48.60 | 30108239 | |
| 413 | Phosphorylation | PSKKRCNSIAALKAT CCCCCCCHHHHHHHH | 19.75 | 26657352 | |
| 420 | Phosphorylation | SIAALKATSQEIVSS HHHHHHHHHHHHHHH | 29.38 | 23186163 | |
| 421 | Phosphorylation | IAALKATSQEIVSSI HHHHHHHHHHHHHHH | 30.58 | 30108239 | |
| 426 | Phosphorylation | ATSQEIVSSISQEWK HHHHHHHHHHCHHHH | 27.84 | 23186163 | |
| 427 | Phosphorylation | TSQEIVSSISQEWKD HHHHHHHHHCHHHHH | 18.50 | 23186163 | |
| 429 | Phosphorylation | QEIVSSISQEWKDEK HHHHHHHCHHHHHHH | 24.80 | 23186163 | |
| 445 | Phosphorylation | DLLTEGQSFSSLDEE HHHCCCCCCHHCCHH | 37.64 | 30108239 | |
| 447 | Phosphorylation | LTEGQSFSSLDEEAL HCCCCCCHHCCHHHH | 34.93 | 30108239 | |
| 448 | Phosphorylation | TEGQSFSSLDEEALG CCCCCCHHCCHHHHC | 37.52 | 26657352 | |
| 485 | Phosphorylation | TISSSSLYVNEHYPH HCCCCCCCCCCCCCC | 11.81 | 19369195 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 105 | Y | Phosphorylation | Kinase | SYK | P43405 | PSP |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PI51B_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 PI51B_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of PI51B_HUMAN !! | ||||
| 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 |
| "Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-445; SER-447AND SER-448, AND MASS SPECTROMETRY. | |
