PI42B_HUMAN - dbPTM
PI42B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PI42B_HUMAN
UniProt AC P78356
Protein Name Phosphatidylinositol 5-phosphate 4-kinase type-2 beta
Gene Name PIP4K2B
Organism Homo sapiens (Human).
Sequence Length 416
Subcellular Localization Endoplasmic reticulum membrane
Peripheral membrane protein. Cell membrane
Peripheral membrane protein. Nucleus . Cytoplasm . Associated with the plasma membrane and the endoplasmic reticulum..
Protein Description Participates in the biosynthesis of phosphatidylinositol 4,5-bisphosphate..
Protein Sequence MSSNCTSTTAVAVAPLSASKTKTKKKHFVCQKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVDRAEQEEMEVEERAEDEECENDGVGGNLLCSYGTPPDSPGNLLSFPRFFGPGEFDPSVDVYAMKSHESSPKKEVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSNILT
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
2Phosphorylation------MSSNCTSTT
------CCCCCCCCC		30.2026552605
2Acetylation------MSSNCTSTT
------CCCCCCCCC		30.2022223895
3Phosphorylation-----MSSNCTSTTA
-----CCCCCCCCCE		34.3329116813
6Phosphorylation--MSSNCTSTTAVAV
--CCCCCCCCCEEEE		33.1029116813
7Phosphorylation-MSSNCTSTTAVAVA
-CCCCCCCCCEEEEE		26.4326552605
8PhosphorylationMSSNCTSTTAVAVAP
CCCCCCCCCEEEEEE		10.7127251275
9PhosphorylationSSNCTSTTAVAVAPL
CCCCCCCCEEEEEEC		20.9227251275
17PhosphorylationAVAVAPLSASKTKTK
EEEEEECCCCCCCCC		29.4525159151
19PhosphorylationAVAPLSASKTKTKKK
EEEECCCCCCCCCCC		37.1725159151
21PhosphorylationAPLSASKTKTKKKHF
EECCCCCCCCCCCCC		41.2625002506
23PhosphorylationLSASKTKTKKKHFVC
CCCCCCCCCCCCCEE		54.0129116813
32UbiquitinationKKHFVCQKVKLFRAS
CCCCEECCCCEEECC		35.8929967540
50UbiquitinationLSVLMWGVNHTINEL
HHHHHHCCCCHHHHH		2.5424816145
59UbiquitinationHTINELSNVPVPVML
CHHHHHCCCCCCEEE		55.5324816145
74PhosphorylationMPDDFKAYSKIKVDN
CCCCCHHHHCCEECC		15.8729978859
75PhosphorylationPDDFKAYSKIKVDNH
CCCCHHHHCCEECCC		32.5329978859
80UbiquitinationAYSKIKVDNHLFNKE
HHHCCEECCCCCCCC		31.6524816145
86UbiquitinationVDNHLFNKENLPSRF
ECCCCCCCCCCCCCC		40.4224816145
94AcetylationENLPSRFKFKEYCPM
CCCCCCCCHHHHHHH		55.18-
96UbiquitinationLPSRFKFKEYCPMVF
CCCCCCHHHHHHHHH		48.65-
96AcetylationLPSRFKFKEYCPMVF
CCCCCCHHHHHHHHH		48.6526051181
98PhosphorylationSRFKFKEYCPMVFRN
CCCCHHHHHHHHHHH		11.4818083107
124PhosphorylationYQNSVTRSAPINSDS
CCCCCCCCCCCCCCC		29.09-
150AcetylationYDRRFVIKTVSSEDV
CCCCEEEEECCHHHH		37.2619608861
154UbiquitinationFVIKTVSSEDVAEMH
EEEEECCHHHHHHHH		33.2224816145
167PhosphorylationMHNILKKYHQFIVEC
HHHHHHHHHHHHHHC		10.1622817900
181UbiquitinationCHGNTLLPQFLGMYR
CCCCCCHHHHHCEEE		26.4524816145
190PhosphorylationFLGMYRLTVDGVETY
HHCEEEEEECCEEEE		13.9320068231
196PhosphorylationLTVDGVETYMVVTRN
EEECCEEEEEEEECC		17.9520068231
197PhosphorylationTVDGVETYMVVTRNV
EECCEEEEEEEECCC		3.7120068231
215PhosphorylationRLTVHRKYDLKGSTV
CCEEEEECCCCCCCC		26.8528509920
218UbiquitinationVHRKYDLKGSTVARE
EEEECCCCCCCCCHH		48.1724816145
220PhosphorylationRKYDLKGSTVAREAS
EECCCCCCCCCHHHC		20.3728509920
221PhosphorylationKYDLKGSTVAREASD
ECCCCCCCCCHHHCC		27.1828509920
227PhosphorylationSTVAREASDKEKAKD
CCCCHHHCCHHHHHC		44.4528509920
237UbiquitinationEKAKDLPTFKDNDFL
HHHHCCCCCCCCCCC		51.0922053931
239UbiquitinationAKDLPTFKDNDFLNE
HHCCCCCCCCCCCCC		59.0929967540
245UbiquitinationFKDNDFLNEGQKLHV
CCCCCCCCCCCCCCC		51.8824816145
246UbiquitinationKDNDFLNEGQKLHVG
CCCCCCCCCCCCCCC		66.2122053931
249UbiquitinationDFLNEGQKLHVGEES
CCCCCCCCCCCCHHH		51.9529967540
256PhosphorylationKLHVGEESKKNFLEK
CCCCCHHHHHHHHHH		44.6321406692
263UbiquitinationSKKNFLEKLKRDVEF
HHHHHHHHHHHHHHH		62.55-
265UbiquitinationKNFLEKLKRDVEFLA
HHHHHHHHHHHHHHH		58.58-
267UbiquitinationFLEKLKRDVEFLAQL
HHHHHHHHHHHHHHH		42.5922053931
273UbiquitinationRDVEFLAQLKIMDYS
HHHHHHHHHHHCCHH		45.4922053931
319PhosphorylationVGGNLLCSYGTPPDS
CCCCEEEECCCCCCC		26.9426657352
320PhosphorylationGGNLLCSYGTPPDSP
CCCEEEECCCCCCCC		24.8328102081
322PhosphorylationNLLCSYGTPPDSPGN
CEEEECCCCCCCCCC		24.3430175587
326PhosphorylationSYGTPPDSPGNLLSF
ECCCCCCCCCCCCCC		40.2428102081
332PhosphorylationDSPGNLLSFPRFFGP
CCCCCCCCCCCCCCC		36.0529691806
341UbiquitinationPRFFGPGEFDPSVDV
CCCCCCCCCCCCCEE		50.4322053931
352UbiquitinationSVDVYAMKSHESSPK
CCEEEEECCCCCCCC		40.2530230243
363PhosphorylationSSPKKEVYFMAIIDI
CCCCCEEEEEEHHHH		6.69-
368UbiquitinationEVYFMAIIDILTPYD
EEEEEEHHHHHCCCC		1.6322053931
385UbiquitinationKKAAHAAKTVKHGAG
HHHHHHHHHHHCCCC		55.4230230243
385AcetylationKKAAHAAKTVKHGAG
HHHHHHHHHHHCCCC		55.4219806649
386PhosphorylationKAAHAAKTVKHGAGA
HHHHHHHHHHCCCCC		30.02-
397PhosphorylationGAGAEISTVNPEQYS
CCCCCEECCCHHHHH		29.9322210691
405UbiquitinationVNPEQYSKRFNEFMS
CCHHHHHHHHHHHHH		56.9532142685
405 (in isoform 1)Ubiquitination-56.9521906983
432Ubiquitination-----------------------
-----------------------		22053931
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
326SPhosphorylationKinaseMAPK14Q16539
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PI42B_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 PI42B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PI42B_HUMANPIP4K2Bphysical
9753329
SPOP_HUMANSPOPphysical
18218622
HMBX1_HUMANHMBOX1physical
25416956
SKP1_HUMANSKP1physical
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 PI42B_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-150, AND MASS SPECTROMETRY.
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-17; THR-322 AND SER-326,AND MASS SPECTROMETRY.
"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 THR-322 AND SER-326, ANDMASS SPECTROMETRY.
"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-98, AND MASSSPECTROMETRY.

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