PI4KB_HUMAN - dbPTM
PI4KB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PI4KB_HUMAN
UniProt AC Q9UBF8
Protein Name Phosphatidylinositol 4-kinase beta
Gene Name PI4KB
Organism Homo sapiens (Human).
Sequence Length 816
Subcellular Localization Endomembrane system. Mitochondrion outer membrane
Peripheral membrane protein. Rough endoplasmic reticulum membrane
Peripheral membrane protein. Golgi apparatus. Golgi apparatus membrane . Cytoplasm, perinuclear region. Found in the outer membrane
Protein Description Phosphorylates phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate (PIP). May regulate Golgi disintegration/reorganization during mitosis, possibly via its phosphorylation. Involved in Golgi-to-plasma membrane trafficking (By similarity)..
Protein Sequence MGDTVVEPAPLKPTSEPTSGPPGNNGGSLLSVITEGVGELSVIDPEVAQKACQEVLEKVKLLHGGVAVSSRGTPLELVNGDGVDSEIRCLDDPPAQIREEEDEMGAAVASGTAKGARRRRQNNSAKQSWLLRLFESKLFDISMAISYLYNSKEPGVQAYIGNRLFCFRNEDVDFYLPQLLNMYIHMDEDVGDAIKPYIVHRCRQSINFSLQCALLLGAYSSDMHISTQRHSRGTKLRKLILSDELKPAHRKRELPSLSPAPDTGLSPSKRTHQRSKSDATASISLSSNLKRTASNPKVENEDEELSSSTESIDNSFSSPVRLAPEREFIKSLMAIGKRLATLPTKEQKTQRLISELSLLNHKLPARVWLPTAGFDHHVVRVPHTQAVVLNSKDKAPYLIYVEVLECENFDTTSVPARIPENRIRSTRSVENLPECGITHEQRAGSFSTVPNYDNDDEAWSVDDIGELQVELPEVHTNSCDNISQFSVDSITSQESKEPVFIAAGDIRRRLSEQLAHTPTAFKRDPEDPSAVALKEPWQEKVRRIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQLSLLDYFLQEHGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGFETSAFKLTTEFVDVMGGLDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGSQLPCFHGSSTIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLTNGIM
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
2Acetylation------MGDTVVEPA
------CCCCEEECC		39.0223572552
58UbiquitinationACQEVLEKVKLLHGG
HHHHHHHHHHHHHCC		40.27-
72UbiquitinationGVAVSSRGTPLELVN
CEEECCCCCCEEEEC		33.36-
128PhosphorylationQNNSAKQSWLLRLFE
HCCHHHHHHHHHHHH		20.9823532336
147PhosphorylationDISMAISYLYNSKEP
CHHHHHHHHHHCCCC		13.69-
175PhosphorylationRNEDVDFYLPQLLNM
ECCCCCCHHHHHHHH		17.0127251275
183PhosphorylationLPQLLNMYIHMDEDV
HHHHHHHHHCCCCCC		6.1327251275
187PhosphorylationLNMYIHMDEDVGDAI
HHHHHCCCCCCHHHH		34.48-
195PhosphorylationEDVGDAIKPYIVHRC
CCCHHHHHHHHHHHH		33.23-
205PhosphorylationIVHRCRQSINFSLQC
HHHHHHHHHCHHHHH		10.51-
209PhosphorylationCRQSINFSLQCALLL
HHHHHCHHHHHHHHH		17.03-
242PhosphorylationKLRKLILSDELKPAH
HHHHHHHCCCCCHHH		23.2628555341
256PhosphorylationHRKRELPSLSPAPDT
HHCCCCCCCCCCCCC		54.8522322096
258 (in isoform 2)Phosphorylation-24.2918669648
258PhosphorylationKRELPSLSPAPDTGL
CCCCCCCCCCCCCCC		24.2930266825
263PhosphorylationSLSPAPDTGLSPSKR
CCCCCCCCCCCCCCC		38.6823401153
263 (in isoform 2)Phosphorylation-38.6818669648
266 (in isoform 2)Phosphorylation-28.5918220336
266PhosphorylationPAPDTGLSPSKRTHQ
CCCCCCCCCCCCCCC		28.5929255136
268PhosphorylationPDTGLSPSKRTHQRS
CCCCCCCCCCCCCCC		31.2430266825
270PhosphorylationTGLSPSKRTHQRSKS
CCCCCCCCCCCCCCC		41.6011277933
275PhosphorylationSKRTHQRSKSDATAS
CCCCCCCCCCCCCCE		29.9130278072
275 (in isoform 2)Phosphorylation-29.9118669648
277PhosphorylationRTHQRSKSDATASIS
CCCCCCCCCCCCEEE		33.4523927012
277 (in isoform 2)Phosphorylation-33.4518669648
278PhosphorylationTHQRSKSDATASISL
CCCCCCCCCCCEEEC		52.2318220336
280PhosphorylationQRSKSDATASISLSS
CCCCCCCCCEEECCH		26.4023927012
282PhosphorylationSKSDATASISLSSNL
CCCCCCCEEECCHHH		14.3523927012
284PhosphorylationSDATASISLSSNLKR
CCCCCEEECCHHHHH		21.5023927012
286PhosphorylationATASISLSSNLKRTA
CCCEEECCHHHHHCC		15.4723927012
287PhosphorylationTASISLSSNLKRTAS
CCEEECCHHHHHCCC		52.0223927012
289PhosphorylationSISLSSNLKRTASNP
EEECCHHHHHCCCCC		4.2518669648
290MethylationISLSSNLKRTASNPK
EECCHHHHHCCCCCC		52.53-
290"N6,N6-dimethyllysine"ISLSSNLKRTASNPK
EECCHHHHHCCCCCC		52.53-
292 (in isoform 2)Phosphorylation-32.6123927012
292PhosphorylationLSSNLKRTASNPKVE
CCHHHHHCCCCCCCC		32.6122496350
294PhosphorylationSNLKRTASNPKVENE
HHHHHCCCCCCCCCC		53.7228731282
294 (in isoform 2)Phosphorylation-53.7220201521
296PhosphorylationLKRTASNPKVENEDE
HHHCCCCCCCCCCCH		39.3018767875
298PhosphorylationRTASNPKVENEDEEL
HCCCCCCCCCCCHHH		11.43-
304PhosphorylationKVENEDEELSSSTES
CCCCCCHHHHCCCHH		67.2927251275
306PhosphorylationENEDEELSSSTESID
CCCCHHHHCCCHHCC		26.0618669648
307PhosphorylationNEDEELSSSTESIDN
CCCHHHHCCCHHCCC		54.6327251275
308PhosphorylationEDEELSSSTESIDNS
CCHHHHCCCHHCCCC		32.5827251275
309PhosphorylationDEELSSSTESIDNSF
CHHHHCCCHHCCCCC		35.3827251275
319PhosphorylationIDNSFSSPVRLAPER
CCCCCCCCCCCCCHH		17.6627251275
320PhosphorylationDNSFSSPVRLAPERE
CCCCCCCCCCCCHHH		9.4027251275
321PhosphorylationNSFSSPVRLAPEREF
CCCCCCCCCCCHHHH		28.6327251275
337UbiquitinationKSLMAIGKRLATLPT
HHHHHHHHHHHCCCC		37.82-
337AcetylationKSLMAIGKRLATLPT
HHHHHHHHHHHCCCC		37.8225953088
341PhosphorylationAIGKRLATLPTKEQK
HHHHHHHCCCCHHHH		37.5518077418
345UbiquitinationRLATLPTKEQKTQRL
HHHCCCCHHHHHHHH		57.09-
348UbiquitinationTLPTKEQKTQRLISE
CCCCHHHHHHHHHHH		47.95-
349PhosphorylationLPTKEQKTQRLISEL
CCCHHHHHHHHHHHH		20.7218077418
349UbiquitinationLPTKEQKTQRLISEL
CCCHHHHHHHHHHHH		20.72-
353PhosphorylationEQKTQRLISELSLLN
HHHHHHHHHHHHHHC		3.0718077418
357UbiquitinationQRLISELSLLNHKLP
HHHHHHHHHHCCCCC		27.10-
361PhosphorylationSELSLLNHKLPARVW
HHHHHHCCCCCCCEE		32.7618077418
362UbiquitinationELSLLNHKLPARVWL
HHHHHCCCCCCCEEE		55.91-
374UbiquitinationVWLPTAGFDHHVVRV
EEEECCCCCCEEEEC		8.18-
398 (in isoform 2)Phosphorylation-1.9118669648
404UbiquitinationYLIYVEVLECENFDT
EEEEEEEEEECCCCC		3.84-
413PhosphorylationCENFDTTSVPARIPE
ECCCCCCCCCCCCCC		28.3518220336
425PhosphorylationIPENRIRSTRSVENL
CCCCCCCCCCCCCCC		26.2920201521
426PhosphorylationPENRIRSTRSVENLP
CCCCCCCCCCCCCCC		19.6726503892
428PhosphorylationNRIRSTRSVENLPEC
CCCCCCCCCCCCCCC		33.5929255136
437PhosphorylationENLPECGITHEQRAG
CCCCCCCCCCCCCCC		5.5527251275
438PhosphorylationNLPECGITHEQRAGS
CCCCCCCCCCCCCCC		12.4923927012
440PhosphorylationPECGITHEQRAGSFS
CCCCCCCCCCCCCCC		32.8620166139
445PhosphorylationTHEQRAGSFSTVPNY
CCCCCCCCCCCCCCC		18.2926074081
447PhosphorylationEQRAGSFSTVPNYDN
CCCCCCCCCCCCCCC		30.1426074081
448PhosphorylationQRAGSFSTVPNYDND
CCCCCCCCCCCCCCC		37.6626074081
450PhosphorylationAGSFSTVPNYDNDDE
CCCCCCCCCCCCCCC		33.4811277933
511PhosphorylationGDIRRRLSEQLAHTP
HHHHHHHHHHHCCCC		22.8329255136
517PhosphorylationLSEQLAHTPTAFKRD
HHHHHCCCCCCCCCC		19.4123927012
519PhosphorylationEQLAHTPTAFKRDPE
HHHCCCCCCCCCCCC		45.979405935
523PhosphorylationHTPTAFKRDPEDPSA
CCCCCCCCCCCCCCC		59.2620068231
529PhosphorylationKRDPEDPSAVALKEP
CCCCCCCCCCCCCCH		47.9318220336
531PhosphorylationDPEDPSAVALKEPWQ
CCCCCCCCCCCCHHH		8.2211277933
546UbiquitinationEKVRRIREGSPYGHL
HHHHHHHCCCCCCCC		62.75-
596UbiquitinationERVPLWIKPYKILVI
HCCCCEECCEEEEEE		30.61-
608UbiquitinationLVISADSGMIEPVVN
EEEECCCCCCHHCCH		22.95-
623UbiquitinationAVSIHQVKKQSQLSL
HCCHHHHHHHHHHHH		38.23-
711PhosphorylationETSAFKLTTEFVDVM
CCCEEEEEHHHHHHH		25.5221955146
712PhosphorylationTSAFKLTTEFVDVMG
CCEEEEEHHHHHHHC		37.5521955146
728PhosphorylationLDGDMFNYYKMLMLQ
CCCHHHHHHHHHHHH		8.0021955146
729PhosphorylationDGDMFNYYKMLMLQG
CCHHHHHHHHHHHHH		7.3321955146
742AcetylationQGLIAARKHMDKVVQ
HHHHHHHHHHHHHHH		38.267671101
779PhosphorylationLKERFHMSMTEEQLQ
HHHHHCCCCCHHHHH		17.6227732954
781PhosphorylationERFHMSMTEEQLQLL
HHHCCCCCHHHHHHH		29.1227732954
796PhosphorylationVEQMVDGSMRSITTK
HHHHCCCCCHHHHHH		13.4227732954
805PhosphorylationRSITTKLYDGFQYLT
HHHHHHHHCHHHHHH		18.6425159151
810PhosphorylationKLYDGFQYLTNGIM-
HHHCHHHHHHCCCC-		17.15-
817PhosphorylationYLTNGIM--------
HHHCCCC--------		-
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
266SPhosphorylationKinaseCDK1P06493
PSP
277SPhosphorylationKinaseSTK38Q91VJ4
GPS
294SPhosphorylationKinasePRKD1Q15139
PSP
294SPhosphorylationKinasePRKD2Q9BZL6
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PI4KB_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 PI4KB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NCS1_HUMANNCS1physical
11526106
UTRO_HUMANUTRNphysical
26496610
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 PI4KB_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, AND MASSSPECTROMETRY.
"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-258; THR-263; SER-277;SER-294; SER-428 AND SER-511, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266; SER-511 ANDTHR-517, AND MASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, AND MASSSPECTROMETRY.
"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-428 AND SER-511, ANDMASS SPECTROMETRY.
"Human phosphatidylinositol 4-kinase isoform PI4K92. Expression of therecombinant enzyme and determination of multiple phosphorylationsites.";
Suer S., Sickmann A., Meyer H.E., Herberg F.W., Heilmeyer L.M.G. Jr.;
Eur. J. Biochem. 268:2099-2106(2001).
Cited for: PHOSPHORYLATION AT SER-258; THR-263; SER-266; SER-277; SER-294;THR-438; SER-511 AND THR-519.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-280, AND MASSSPECTROMETRY.

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