PI51C_HUMAN - dbPTM
PI51C_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PI51C_HUMAN
UniProt AC O60331
Protein Name Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma
Gene Name PIP5K1C
Organism Homo sapiens (Human).
Sequence Length 668
Subcellular Localization Cell membrane
Peripheral membrane protein
Cytoplasmic side. Endomembrane system. Cytoplasm. Cell junction, focal adhesion. Cell junction, adherens junction. Cell projection, ruffle membrane. Cell projection, phagocytic cup. Cell projection, uropodium. N
Protein Description Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). PtdIns(4,5)P2 is involved in a variety of cellular processes and is the substrate to form phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3), another second messenger. The majority of PtdIns(4,5)P2 is thought to occur via type I phosphatidylinositol 4-phosphate 5-kinases given the abundance of PtdIns4P. Participates in a variety of cellular processes such as vesicle mediated transport, cell adhesion, cell polarization and cell migration. Together with PIP5K1A is required for phagocytosis, but they regulate different types of actin remodeling at sequential steps. Promotes particle attachment by generating the pool of PtdIns(4,5)P2 that induces controlled actin depolymerization to facilitate Fc-gamma-R clustering. Mediates RAC1-dependent reorganization of actin filaments. Required for synaptic vesicle transport. Controls the plasma membrane pool of PtdIns(4,5)P2 implicated in synaptic vesicle endocytosis and exocytosis. Plays a role in endocytosis mediated by clathrin and AP-2 (adaptor protein complex 2). Required for clathrin-coated pits assembly at the synapse. Participates in cell junction assembly. Modulates adherens junctions formation by facilitating CDH1 trafficking. Required for focal adhesion dynamics. Modulates the targeting of talins (TLN1 and TLN2) to the plasma membrane and their efficient assembly into focal adhesions. Regulates the interaction between talins (TLN1 and TLN2) and beta-integrins. Required for uropodium formation and retraction of the cell rear during directed migration. Has a role in growth factor- stimulated directional cell migration and adhesion. Required for talin assembly into nascent adhesions forming at the leading edge toward the direction of the growth factor. Negative regulator of T-cell activation and adhesion. Negatively regulates integrin alpha-L/beta-2 (LFA-1) polarization and adhesion induced by T-cell receptor. Together with PIP5K1A has a role during embryogenesis and together with PIP5K1B may have a role immediately after birth..
Protein Sequence MELEVPDEAESAEAGAVPSEAAWAAESGAAAGLAQKKAAPTEVLSMTAQPGPGHGKKLGHRGVDASGETTYKKTTSSTLKGAIQLGIGYTVGHLSSKPERDVLMQDFYVVESIFFPSEGSNLTPAHHFQDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSNPGASGSLFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRVVVMNNILPRVVKMHLKFDLKGSTYKRRASKKEKEKSFPTYKDLDFMQDMPEGLLLDADTFSALVKTLQRDCLVLESFKIMDYSLLLGVHNIDQHERERQAQGAQSTSDEKRPVGQKALYSTAMESIQGGAARGEAIESDDTMGGIPAVNGRGERLLLHIGIIDILQSYRFIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMSNTVFRKNSSLKSSPSKKGRGGALLAVKPLGPTAAFSASQIPSEREEAQYDLRGARSYPTLEDEGRPDLLPCTPPSFEEATTASIATTLSSTSLSIPERSPSETSEQPRYRRRTQSSGQDGRPQEEPPAEEDLQQITVQVEPACSVEIVVPKEEDAGVEASPAGASAAVEVETASQASDEEGAPASQASDEEDAPATDIYFPTDERSWVYSPLHYSAQAPPASDGESDT
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
11PhosphorylationEVPDEAESAEAGAVP
CCCCHHHHHHCCCCC		38.1628348404
38UbiquitinationAGLAQKKAAPTEVLS
HHHHHCCCCCCEEEE		26.2120972266
45PhosphorylationAAPTEVLSMTAQPGP
CCCCEEEEEECCCCC		21.1825159151
47PhosphorylationPTEVLSMTAQPGPGH
CCEEEEEECCCCCCC		20.8225159151
52UbiquitinationSMTAQPGPGHGKKLG
EEECCCCCCCCCCCC		37.9923000965
66PhosphorylationGHRGVDASGETTYKK
CCCCCCCCCCCCCCC		32.4728060719
69PhosphorylationGVDASGETTYKKTTS
CCCCCCCCCCCCCCC		38.6628060719
70PhosphorylationVDASGETTYKKTTSS
CCCCCCCCCCCCCCH		29.1028060719
71PhosphorylationDASGETTYKKTTSST
CCCCCCCCCCCCCHH		20.2228060719
73UbiquitinationSGETTYKKTTSSTLK
CCCCCCCCCCCHHHH		46.7729967540
82UbiquitinationTSSTLKGAIQLGIGY
CCHHHHHHHHCCCCC		5.6920972266
95PhosphorylationGYTVGHLSSKPERDV
CCCHHCCCCCCCCCC		30.5522210691
96PhosphorylationYTVGHLSSKPERDVL
CCHHCCCCCCCCCCC		59.6022210691
97 (in isoform 3)Ubiquitination-47.74-
97UbiquitinationTVGHLSSKPERDVLM
CHHCCCCCCCCCCCC		47.7423000965
134UbiquitinationHFQDFRFKTYAPVAF
CCCCCCCCCHHHHHH		36.05-
135PhosphorylationFQDFRFKTYAPVAFR
CCCCCCCCHHHHHHH		23.3928152594
136PhosphorylationQDFRFKTYAPVAFRY
CCCCCCCHHHHHHHH		14.9728152594
155UbiquitinationFGIRPDDYLYSLCNE
HCCCCCHHHHHHHCC		18.2123000965
200 (in isoform 3)Ubiquitination-54.89-
200UbiquitinationKEAEFLQKLLPGYYM
HHHHHHHHHCCCHHC		54.8923000965
215PhosphorylationNLNQNPRTLLPKFYG
CCCCCCCHHCHHHEE		33.62-
228PhosphorylationYGLYCVQSGGKNIRV
EEEEEEECCCEEEEE		29.17-
255UbiquitinationMHLKFDLKGSTYKRR
EECCCCCCCCHHHCC		53.30-
265AcetylationTYKRRASKKEKEKSF
HHHCCCCHHHHHHCC		65.0620668706
268AcetylationRRASKKEKEKSFPTY
CCCCHHHHHHCCCCH		78.3520668706
270UbiquitinationASKKEKEKSFPTYKD
CCHHHHHHCCCCHHC		69.3529967540
300UbiquitinationDTFSALVKTLQRDCL
HHHHHHHHHHHHHCC		44.3522053931
306UbiquitinationVKTLQRDCLVLESFK
HHHHHHHCCCEEHHH		2.8523503661
341PhosphorylationQAQGAQSTSDEKRPV
HHHCCCCCCCCCCCH		28.28-
345UbiquitinationAQSTSDEKRPVGQKA
CCCCCCCCCCHHHHH		67.9721906983
351UbiquitinationEKRPVGQKALYSTAM
CCCCHHHHHHHHHHH		34.1423503661
351 (in isoform 3)Ubiquitination-34.14-
354PhosphorylationPVGQKALYSTAMESI
CHHHHHHHHHHHHHH		14.6121945579
355PhosphorylationVGQKALYSTAMESIQ
HHHHHHHHHHHHHHH		15.5621945579
356PhosphorylationGQKALYSTAMESIQG
HHHHHHHHHHHHHHC		19.2321945579
360PhosphorylationLYSTAMESIQGGAAR
HHHHHHHHHHCCCCC		13.7121945579
369UbiquitinationQGGAARGEAIESDDT
HCCCCCCCCCCCCCC		40.7020972266
402PhosphorylationGIIDILQSYRFIKKL
HHHHHHHHHHHHHHC		18.16-
403PhosphorylationIIDILQSYRFIKKLE
HHHHHHHHHHHHHCH		9.15-
408UbiquitinationQSYRFIKKLEHTWKA
HHHHHHHHCHHHHHH		55.0529967540
414UbiquitinationKKLEHTWKALVHDGD
HHCHHHHHHHCCCCC		32.7620972266
424PhosphorylationVHDGDTVSVHRPSFY
CCCCCEEEEECCCHH		17.8228857561
442PhosphorylationFFKFMSNTVFRKNSS
HHHHHHCCCCCCCCC		17.4524719451
448PhosphorylationNTVFRKNSSLKSSPS
CCCCCCCCCCCCCCC		39.8329083192
449PhosphorylationTVFRKNSSLKSSPSK
CCCCCCCCCCCCCCC		49.5729083192
452PhosphorylationRKNSSLKSSPSKKGR
CCCCCCCCCCCCCCC		53.4229083192
453PhosphorylationKNSSLKSSPSKKGRG
CCCCCCCCCCCCCCC		31.4429083192
455PhosphorylationSSLKSSPSKKGRGGA
CCCCCCCCCCCCCCE		49.2829083192
459Asymmetric dimethylarginineSSPSKKGRGGALLAV
CCCCCCCCCCEEEEE		49.61-
459MethylationSSPSKKGRGGALLAV
CCCCCCCCCCEEEEE		49.6158858933
472PhosphorylationAVKPLGPTAAFSASQ
EEEECCCCCCCCHHH		28.9028060719
476PhosphorylationLGPTAAFSASQIPSE
CCCCCCCCHHHCCCH		23.4532142685
478PhosphorylationPTAAFSASQIPSERE
CCCCCCHHHCCCHHH		27.6929978859
482PhosphorylationFSASQIPSEREEAQY
CCHHHCCCHHHHHHH		51.4129978859
489PhosphorylationSEREEAQYDLRGARS
CHHHHHHHHCCCCCC		24.8029978859
496PhosphorylationYDLRGARSYPTLEDE
HHCCCCCCCCCCCCC		34.6226074081
497PhosphorylationDLRGARSYPTLEDEG
HCCCCCCCCCCCCCC		8.4926074081
499PhosphorylationRGARSYPTLEDEGRP
CCCCCCCCCCCCCCC		34.2526074081
515PhosphorylationLLPCTPPSFEEATTA
CCCCCCCCHHHCCHH		46.6328348404
520PhosphorylationPPSFEEATTASIATT
CCCHHHCCHHHHHHH		26.6128348404
521PhosphorylationPSFEEATTASIATTL
CCHHHCCHHHHHHHH		26.0028348404
523PhosphorylationFEEATTASIATTLSS
HHHCCHHHHHHHHCC		15.6328348404
526PhosphorylationATTASIATTLSSTSL
CCHHHHHHHHCCCCC		26.9728348404
527PhosphorylationTTASIATTLSSTSLS
CHHHHHHHHCCCCCC		18.6728348404
529PhosphorylationASIATTLSSTSLSIP
HHHHHHHCCCCCCCC		29.4928348404
530PhosphorylationSIATTLSSTSLSIPE
HHHHHHCCCCCCCCC		25.7328348404
531PhosphorylationIATTLSSTSLSIPER
HHHHHCCCCCCCCCC		30.2528348404
532PhosphorylationATTLSSTSLSIPERS
HHHHCCCCCCCCCCC		23.2828348404
539PhosphorylationSLSIPERSPSETSEQ
CCCCCCCCCCCCCCC		30.9925850435
541PhosphorylationSIPERSPSETSEQPR
CCCCCCCCCCCCCCC		55.5429255136
543PhosphorylationPERSPSETSEQPRYR
CCCCCCCCCCCCCCC		41.73-
544PhosphorylationERSPSETSEQPRYRR
CCCCCCCCCCCCCCH		30.13-
553PhosphorylationQPRYRRRTQSSGQDG
CCCCCHHCCCCCCCC		30.8728348404
555PhosphorylationRYRRRTQSSGQDGRP
CCCHHCCCCCCCCCC		35.5027251275
556PhosphorylationYRRRTQSSGQDGRPQ
CCHHCCCCCCCCCCC		30.5627251275
639PhosphorylationDAPATDIYFPTDERS
CCCCCCCCCCCCCCC		13.30-
649PhosphorylationTDERSWVYSPLHYSA
CCCCCEEECCCEEEC		9.7915738269
650PhosphorylationDERSWVYSPLHYSAQ
CCCCEEECCCEEECC		16.0317290217
650DephosphorylationDERSWVYSPLHYSAQ
CCCCEEECCCEEECC		16.0317290217
654PhosphorylationWVYSPLHYSAQAPPA
EEECCCEEECCCCCC		17.2427732954
655PhosphorylationVYSPLHYSAQAPPAS
EECCCEEECCCCCCC		11.8027732954
662PhosphorylationSAQAPPASDGESDT-
ECCCCCCCCCCCCC-		52.5028450419
666PhosphorylationPPASDGESDT-----
CCCCCCCCCC-----		52.6720363803
668PhosphorylationASDGESDT-------
CCCCCCCC-------		50.1920363803
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
448SPhosphorylationKinasePRKD1Q15139
PSP
448SPhosphorylationKinasePDPK1O15530
GPS
453SPhosphorylationKinaseCDK5Q00535
PSP
553TPhosphorylationKinaseRPS6KB1P23443
GPS
555SPhosphorylationKinaseAKT1P31749
PSP
555SPhosphorylationKinaseAKT2P31751
PSP
555SPhosphorylationKinaseRPS6KB1P23443
GPS
639YPhosphorylationKinaseEGFRP00533
Uniprot
649YPhosphorylationKinaseCSKP41240
Uniprot
649YPhosphorylationKinaseSRCP12931
PSP
650SPhosphorylationKinaseCDK1P06493
Uniprot
650SPhosphorylationKinaseCDK5Q00535
Uniprot
650SPhosphorylationKinaseMAPK1P28482
Uniprot
650SPhosphorylationKinaseMAPK3P27361
GPS
-KUbiquitinationE3 ubiquitin ligaseHECTD1Q9ULT8
PMID:23572508
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
265KAcetylation

20668706
268KAcetylation

20668706
650SPhosphorylation

15738269
650SPhosphorylation

15738269
650SPhosphorylation

15738269
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 PI51C_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TLN2_HUMANTLN2physical
12422219
SNX5_HUMANSNX5physical
23602387
TLN1_HUMANTLN1physical
23572508
LAP4B_HUMANLAPTM4Bphysical
25588945
SNX5_HUMANSNX5physical
25588945
NEDD4_HUMANNEDD4physical
27557663
UBC_HUMANUBCphysical
23572508
Drug and Disease Associations
Kegg Disease
H00865 Lethal congenital contractural syndrome (LCCS)
OMIM Disease
611369Lethal congenital contracture syndrome 3 (LCCS3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PI51C_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"SIRT1 regulates thyroid-stimulating hormone release by enhancingPIP5Kgamma activity through deacetylation of specific lysine residuesin mammals.";
Akieda-Asai S., Zaima N., Ikegami K., Kahyo T., Yao I., Hatanaka T.,Iemura S., Sugiyama R., Yokozeki T., Eishi Y., Koike M., Ikeda K.,Chiba T., Yamaza H., Shimokawa I., Song S.Y., Matsuno A., Mizutani A.,Sawabe M., Chao M.V., Tanaka M., Kanaho Y., Natsume T., Sugimura H.,Date Y., McBurney M.W., Guarente L., Setou M.;
PLoS ONE 5:E11755-E11755(2010).
Cited for: ACETYLATION AT LYS-265 AND LYS-268, AND DEACETYLATION BY SIRT1.
Phosphorylation
ReferencePubMed
"Regulation of the interaction between PIPKI gamma and talin byproline-directed protein kinases.";
Lee S.Y., Voronov S., Letinic K., Nairn A.C., Di Paolo G.,De Camilli P.;
J. Cell Biol. 168:789-799(2005).
Cited for: PHOSPHORYLATION AT TYR-649 AND SER-650, AND MUTAGENESIS OF SER-650.

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