P4K2B_HUMAN - dbPTM
P4K2B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID P4K2B_HUMAN
UniProt AC Q8TCG2
Protein Name Phosphatidylinositol 4-kinase type 2-beta
Gene Name PI4K2B
Organism Homo sapiens (Human).
Sequence Length 481
Subcellular Localization Cytoplasm. Membrane. Mostly cytoplasmic but also found associated with the plasma membrane, the Golgi and endosomes. Compared to PI4K2A, a larger fraction of PI4K2B is cytosolic due to a smaller extent of palmitoylation. Translocates to membranes whe
Protein Description Together with PI4K2A and the type III PI4Ks (PIK4CA and PIK4CB) it contributes to the overall PI4-kinase activity of the cell. This contribution may be especially significant in plasma membrane, endosomal and Golgi compartments. The phosphorylation of phosphatidylinositol (PI) to PI4P is the first committed step in the generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor of the second messenger inositol 1,4,5-trisphosphate (InsP3). Contributes to the production of InsP3 in stimulated cells and is likely to be involved in the regulation of vesicular trafficking..
Protein Sequence MEDPSEPDRLASADGGSPEEEEDGEREPLLPRIAWAHPRRGAPGSAVRLLDAAGEEGEAGDEELPLPPGDVGVSRSSSAELDRSRPAVSVTIGTSEMNAFLDDPEFADIMLRAEQAIEVGIFPERISQGSSGSYFVKDPKRKIIGVFKPKSEEPYGQLNPKWTKYVHKVCCPCCFGRGCLIPNQGYLSEAGAYLVDNKLHLSIVPKTKVVWLVSETFNYNAIDRAKSRGKKYALEKVPKVGRKFHRIGLPPKIGSFQLFVEGYKEAEYWLRKFEADPLPENIRKQFQSQFERLVILDYIIRNTDRGNDNWLVRYEKQKCEKEIDHKESKWIDDEEFLIKIAAIDNGLAFPFKHPDEWRAYPFHWAWLPQAKVPFSEEIRNLILPYISDMNFVQDLCEDLYELFKTDKGFDKATFESQMSVMRGQILNLTQALRDGKSPFQLVQIPCVIVERSQGGSQGRIVHLSNSFTQTVNCRKPFFSSW
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
12PhosphorylationSEPDRLASADGGSPE
CCCCHHHCCCCCCHH
31.3330278072
17PhosphorylationLASADGGSPEEEEDG
HHCCCCCCHHHCCCC
34.3723401153
45PhosphorylationPRRGAPGSAVRLLDA
CCCCCCCHHHHHHHH
23.6428102081
78PhosphorylationVGVSRSSSAELDRSR
CCCCCCCCCCCCCCC
27.3228857561
133PhosphorylationISQGSSGSYFVKDPK
CCCCCCCCEECCCCC
19.8325884760
134PhosphorylationSQGSSGSYFVKDPKR
CCCCCCCEECCCCCC
18.8622817900
137UbiquitinationSSGSYFVKDPKRKII
CCCCEECCCCCCCEE
59.4221890473
140UbiquitinationSYFVKDPKRKIIGVF
CEECCCCCCCEEEEE
76.18-
142UbiquitinationFVKDPKRKIIGVFKP
ECCCCCCCEEEEECC
44.81-
148UbiquitinationRKIIGVFKPKSEEPY
CCEEEEECCCCCCCC
49.48-
150UbiquitinationIIGVFKPKSEEPYGQ
EEEEECCCCCCCCCC
71.71-
155PhosphorylationKPKSEEPYGQLNPKW
CCCCCCCCCCCCHHH
22.3028102081
161UbiquitinationPYGQLNPKWTKYVHK
CCCCCCHHHHHHHHH
67.4321890473
164UbiquitinationQLNPKWTKYVHKVCC
CCCHHHHHHHHHCCC
44.13-
168UbiquitinationKWTKYVHKVCCPCCF
HHHHHHHHCCCCCCC
27.24-
170S-palmitoylationTKYVHKVCCPCCFGR
HHHHHHCCCCCCCCC
2.2717927563
171S-palmitoylationKYVHKVCCPCCFGRG
HHHHHCCCCCCCCCC
3.0217927563
173S-palmitoylationVHKVCCPCCFGRGCL
HHHCCCCCCCCCCCC
1.5517927563
174S-palmitoylationHKVCCPCCFGRGCLI
HHCCCCCCCCCCCCC
2.1517927563
198UbiquitinationGAYLVDNKLHLSIVP
CEEEECCCEEEEECC
32.59-
232PhosphorylationAKSRGKKYALEKVPK
HHHCCCCHHHHHCCC
21.6529496907
236UbiquitinationGKKYALEKVPKVGRK
CCCHHHHHCCCCCCC
65.76-
272UbiquitinationEAEYWLRKFEADPLP
HHHHHHHHCCCCCCC
45.4421890473
284UbiquitinationPLPENIRKQFQSQFE
CCCHHHHHHHHHHHH
52.22-
298PhosphorylationERLVILDYIIRNTDR
HHHHHHHHHHHCCCC
8.5324670416
326UbiquitinationCEKEIDHKESKWIDD
CHHHCCCCHHCCCCC
60.99-
329UbiquitinationEIDHKESKWIDDEEF
HCCCCHHCCCCCHHH
49.62-
352UbiquitinationNGLAFPFKHPDEWRA
CCEEECCCCCCCCCC
55.2421890473
411UbiquitinationKTDKGFDKATFESQM
HHCCCCCHHHHHHHH
47.2521890473
436UbiquitinationTQALRDGKSPFQLVQ
HHHHHCCCCCCEEEE
60.28-
464PhosphorylationQGRIVHLSNSFTQTV
CCEEEEECCCCCCEE
18.6221712546
466PhosphorylationRIVHLSNSFTQTVNC
EEEEECCCCCCEECC
26.7123401153
468PhosphorylationVHLSNSFTQTVNCRK
EEECCCCCCEECCCC
24.1323911959
470PhosphorylationLSNSFTQTVNCRKPF
ECCCCCCEECCCCCC
15.6123403867
475UbiquitinationTQTVNCRKPFFSSW-
CCEECCCCCCCCCC-
48.67-
480PhosphorylationCRKPFFSSW------
CCCCCCCCC------
31.48-

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 P4K2B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of P4K2B_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 P4K2B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HS90A_HUMANHSP90AA1physical
21330372

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 P4K2B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-12; SER-17 AND SER-45,AND MASS SPECTROMETRY.

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