PI51A_HUMAN - dbPTM
PI51A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PI51A_HUMAN
UniProt AC Q99755
Protein Name Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha
Gene Name PIP5K1A
Organism Homo sapiens (Human).
Sequence Length 562
Subcellular Localization Cell membrane. Cytoplasm. Nucleus speckle. Cell projection, ruffle. Colocalizes with RAC1 at actin-rich membrane ruffles. Localizes to nuclear speckles and associates with TUT1 to regulate polyadenylation of selected mRNAs.
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 actin cytoskeleton organization, cell adhesion, migration and phagocytosis. Required for membrane ruffling formation, actin organization and focal adhesion formation during directional cell migration by controlling integrin-induced translocation of RAC1 to the plasma membrane. Together with PIP5K1C is required for phagocytosis, but they regulate different types of actin remodeling at sequential steps. Promotes particle ingestion by activating WAS that induces Arp2/3 dependent actin polymerization at the nascent phagocytic cup. Together with PIP5K1B is required after stimulation of G-protein coupled receptors for stable platelet adhesion. Plays a role during calcium-induced keratinocyte differentiation. Recruited to the plasma membrane by the E-cadherin/beta-catenin complex where it provides the substrate PtdIns(4,5)P2 for the production of PtdIns(3,4,5)P3, diacylglycerol and inositol 1,4,5-trisphosphate that mobilize internal calcium and drive keratinocyte differentiation. Together with PIP5K1C have a role during embryogenesis. Functions also in the nucleus where acts as an activator of TUT1 adenylyltransferase activity in nuclear speckles, thereby regulating mRNA polyadenylation of a select set of mRNAs..
Protein Sequence MASASSGPSSSVGFSSFDPAVPSCTLSSAASGIKRPMASEVLEARQDSYISLVPYASGMPIKKIGHRSVDSSGETTYKKTTSSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCSEPLIELCSSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNIRIVVMNNLLPRSVKMHIKYDLKGSTYKRRASQKEREKPLPTFKDLDFLQDIPDGLFLDADMYNALCKTLQRDCLVLQSFKIMDYSLLMSIHNIDHAQREPLSSETQYSVDTRRPAPQKALYSTAMESIQGEARRGGTMETDDHMGGIPARNSKGERLLLYIGIIDILQSYRFVKKLEHSWKALVHDGDTVSVHRPGFYAERFQRFMCNTVFKKIPLKPSPSKKFRSGSSFSRRAGSSGNSCITYQPSVSGEHKAQVTTKAEVEPGVHLGRPDVLPQTPPLEEISEGSPIPDPSFSPLVGETLQMLTTSTTLEKLEVAESEFTH
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
3 (in isoform 2)Phosphorylation-27.6424043423
3 (in isoform 3)Phosphorylation-27.6424043423
5 (in isoform 2)Phosphorylation-33.0824043423
5 (in isoform 3)Phosphorylation-33.0824043423
6 (in isoform 2)Phosphorylation-55.2124043423
6 (in isoform 3)Phosphorylation-55.2124043423
9 (in isoform 2)Phosphorylation-38.4824043423
9 (in isoform 3)Phosphorylation-38.4824043423
10 (in isoform 2)Phosphorylation-31.9824043423
10 (in isoform 3)Phosphorylation-31.9824043423
11 (in isoform 2)Phosphorylation-30.5124043423
11 (in isoform 3)Phosphorylation-30.5124043423
15 (in isoform 2)Phosphorylation-24.9424043423
15 (in isoform 3)Phosphorylation-24.9424043423
16 (in isoform 2)Phosphorylation-31.2624043423
16 (in isoform 3)Phosphorylation-31.2624043423
23 (in isoform 2)Phosphorylation-17.0924043423
23 (in isoform 3)Phosphorylation-17.0924043423
25 (in isoform 2)Phosphorylation-33.7324043423
25 (in isoform 3)Phosphorylation-33.7324043423
27 (in isoform 2)Phosphorylation-10.3624043423
27 (in isoform 3)Phosphorylation-10.3624043423
28 (in isoform 2)Phosphorylation-30.8524043423
28 (in isoform 3)Phosphorylation-30.8524043423
30 (in isoform 2)Phosphorylation-15.3924043423
30 (in isoform 3)Phosphorylation-15.3924043423
38 (in isoform 2)Phosphorylation-12.77-
38 (in isoform 3)Phosphorylation-12.77-
39 (in isoform 4)Phosphorylation-23.22-
42 (in isoform 2)Phosphorylation-3.6029978859
42 (in isoform 3)Phosphorylation-3.6029978859
43 (in isoform 4)Phosphorylation-47.1629978859
44 (in isoform 2)Phosphorylation-15.4127307780
44 (in isoform 3)Phosphorylation-15.4127307780
45 (in isoform 4)Phosphorylation-31.3127307780
48PhosphorylationVLEARQDSYISLVPY
HHHHHHHCCEEEEEC		18.9421406692
49PhosphorylationLEARQDSYISLVPYA
HHHHHHCCEEEEECC		11.6525072903
51PhosphorylationARQDSYISLVPYASG
HHHHCCEEEEECCCC		18.3225072903
55PhosphorylationSYISLVPYASGMPIK
CCEEEEECCCCCCCE		13.1121406692
57PhosphorylationISLVPYASGMPIKKI
EEEEECCCCCCCEEC		29.7625072903
68PhosphorylationIKKIGHRSVDSSGET
CEECCCCCCCCCCCC		25.3025159151
71PhosphorylationIGHRSVDSSGETTYK
CCCCCCCCCCCCCCE		37.7825159151
72PhosphorylationGHRSVDSSGETTYKK
CCCCCCCCCCCCCEE		35.8625159151
75PhosphorylationSVDSSGETTYKKTTS
CCCCCCCCCCEECCH		38.6623312004
76PhosphorylationVDSSGETTYKKTTSS
CCCCCCCCCEECCHH		29.1023312004
77PhosphorylationDSSGETTYKKTTSSA
CCCCCCCCEECCHHH		20.2223312004
78UbiquitinationSSGETTYKKTTSSAL
CCCCCCCEECCHHHH		41.36-
79UbiquitinationSGETTYKKTTSSALK
CCCCCCEECCHHHHH		46.77-
86MethylationKTTSSALKGAIQLGI
ECCHHHHHHHHHHCC		46.11115975041
90 (in isoform 2)Ubiquitination-32.8621890473
90 (in isoform 3)Ubiquitination-32.8621890473
91UbiquitinationALKGAIQLGITHTVG
HHHHHHHHCCCEECC		4.3521890473
103UbiquitinationTVGSLSTKPERDVLM
ECCCCCCCCCHHCCC		41.3221890473
103 (in isoform 1)Ubiquitination-41.3221890473
140UbiquitinationHYNDFRFKTYAPVAF
CCCCCCCCCCHHHHH		36.05-
141PhosphorylationYNDFRFKTYAPVAFR
CCCCCCCCCHHHHHH		23.3928152594
142PhosphorylationNDFRFKTYAPVAFRY
CCCCCCCCHHHHHHH		14.9728152594
193 (in isoform 2)Ubiquitination-3.5721890473
193 (in isoform 3)Ubiquitination-3.5721890473
199UbiquitinationIIKTVQHKEAEFLQK
EEEECCHHHHHHHHH		41.34-
206UbiquitinationKEAEFLQKLLPGYYM
HHHHHHHHHCCCHHC		54.8920639865
206 (in isoform 1)Ubiquitination-54.8921890473
221PhosphorylationNLNQNPRTLLPKFYG
CCCCCCCHHCHHHHE		33.62-
237UbiquitinationYCVQAGGKNIRIVVM
EEEEECCEEEEEEEE		48.56-
261UbiquitinationMHIKYDLKGSTYKRR
EEEEECCCCCHHHCC		48.17-
276AcetylationASQKEREKPLPTFKD
CCHHHHCCCCCCCCC		59.0625953088
276UbiquitinationASQKEREKPLPTFKD
CCHHHHCCCCCCCCC		59.06-
301PhosphorylationLFLDADMYNALCKTL
CCCCHHHHHHHHHHH		9.6124114839
307PhosphorylationMYNALCKTLQRDCLV
HHHHHHHHHHHHHHH		27.4228348404
341PhosphorylationHAQREPLSSETQYSV
HHHHCCCCCCCCCCC		36.5221945579
342PhosphorylationAQREPLSSETQYSVD
HHHCCCCCCCCCCCC		52.9621945579
344PhosphorylationREPLSSETQYSVDTR
HCCCCCCCCCCCCCC		34.4521945579
346PhosphorylationPLSSETQYSVDTRRP
CCCCCCCCCCCCCCC		20.3421945579
347PhosphorylationLSSETQYSVDTRRPA
CCCCCCCCCCCCCCC		12.0521945579
350PhosphorylationETQYSVDTRRPAPQK
CCCCCCCCCCCCCHH		26.8221945579
360PhosphorylationPAPQKALYSTAMESI
CCCHHHHHHHHHHHH		14.6121945579
361PhosphorylationAPQKALYSTAMESIQ
CCHHHHHHHHHHHHH		15.5621945579
362PhosphorylationPQKALYSTAMESIQG
CHHHHHHHHHHHHHC		19.2321945579
366PhosphorylationLYSTAMESIQGEARR
HHHHHHHHHHCHHHC		13.7121945579
373MethylationSIQGEARRGGTMETD
HHHCHHHCCCCCCCC		55.74115487579
373 (in isoform 4)Ubiquitination-55.74-
376PhosphorylationGEARRGGTMETDDHM
CHHHCCCCCCCCCCC		18.0423898821
379PhosphorylationRRGGTMETDDHMGGI
HCCCCCCCCCCCCCC		35.5928348404
414UbiquitinationQSYRFVKKLEHSWKA
HHHHHHHHCHHHHEE		54.53-
418PhosphorylationFVKKLEHSWKALVHD
HHHHCHHHHEEEEEC		22.39-
452UbiquitinationMCNTVFKKIPLKPSP
HHCCCHHHCCCCCCC		37.78-
456UbiquitinationVFKKIPLKPSPSKKF
CHHHCCCCCCCCCCC		37.79-
458PhosphorylationKKIPLKPSPSKKFRS
HHCCCCCCCCCCCCC		39.9729255136
460PhosphorylationIPLKPSPSKKFRSGS
CCCCCCCCCCCCCCC		53.4629255136
465PhosphorylationSPSKKFRSGSSFSRR
CCCCCCCCCCCCCCC		46.2728450419
467PhosphorylationSKKFRSGSSFSRRAG
CCCCCCCCCCCCCCC		29.4728450419
468PhosphorylationKKFRSGSSFSRRAGS
CCCCCCCCCCCCCCC		30.6625159151
470PhosphorylationFRSGSSFSRRAGSSG
CCCCCCCCCCCCCCC		23.8628450419
475PhosphorylationSFSRRAGSSGNSCIT
CCCCCCCCCCCCCEE		33.8021945579
476PhosphorylationFSRRAGSSGNSCITY
CCCCCCCCCCCCEEE		40.8721945579
479PhosphorylationRAGSSGNSCITYQPS
CCCCCCCCCEEECCC		15.4921945579
482PhosphorylationSSGNSCITYQPSVSG
CCCCCCEEECCCCCC		22.0421945579
483PhosphorylationSGNSCITYQPSVSGE
CCCCCEEECCCCCCC		9.8721945579
486PhosphorylationSCITYQPSVSGEHKA
CCEEECCCCCCCCEE		17.2521945579
488PhosphorylationITYQPSVSGEHKAQV
EEECCCCCCCCEEEE		42.6821945579
492UbiquitinationPSVSGEHKAQVTTKA
CCCCCCCEEEEEEEE		35.89-
516PhosphorylationRPDVLPQTPPLEEIS
CCCCCCCCCCHHHHC		25.5720068231
523PhosphorylationTPPLEEISEGSPIPD
CCCHHHHCCCCCCCC		38.9020068231
526PhosphorylationLEEISEGSPIPDPSF
HHHHCCCCCCCCCCC		18.6622468782
532PhosphorylationGSPIPDPSFSPLVGE
CCCCCCCCCCHHHHH		45.8220068231
534PhosphorylationPIPDPSFSPLVGETL
CCCCCCCCHHHHHHH		22.9720068231
540PhosphorylationFSPLVGETLQMLTTS
CCHHHHHHHHHHHHC		19.1620068231
545PhosphorylationGETLQMLTTSTTLEK
HHHHHHHHHCCHHHH		17.2326074081
546PhosphorylationETLQMLTTSTTLEKL
HHHHHHHHCCHHHHH		21.8026074081
547PhosphorylationTLQMLTTSTTLEKLE
HHHHHHHCCHHHHHH		17.7326074081
548PhosphorylationLQMLTTSTTLEKLEV
HHHHHHCCHHHHHHH		33.0526074081
549PhosphorylationQMLTTSTTLEKLEVA
HHHHHCCHHHHHHHH		32.4626074081
561PhosphorylationEVAESEFTH------
HHHHHHCCC------		23.7121815630
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
-KUbiquitinationE3 ubiquitin ligaseNEDD4P46934
PMID:29851245
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PI51A_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 PI51A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
FLNC_HUMANFLNCphysical
26186194
PI51C_HUMANPIP5K1Cphysical
26186194
DCAF5_HUMANDCAF5physical
26186194
NRP1_HUMANNRP1physical
26186194
RAD21_HUMANRAD21physical
26186194
CENPB_HUMANCENPBphysical
26186194
NRX3B_HUMANNRXN3physical
26186194
NRX3A_HUMANNRXN3physical
26186194
PELP1_HUMANPELP1physical
26186194
HTSF1_HUMANHTATSF1physical
26186194
STAG2_HUMANSTAG2physical
26186194
GPC3_HUMANGPC3physical
26186194
TRI41_HUMANTRIM41physical
26186194
TGBR3_HUMANTGFBR3physical
26186194
PI51C_HUMANPIP5K1Cphysical
28514442
NRX3B_HUMANNRXN3physical
28514442
NRX3A_HUMANNRXN3physical
28514442
TRI41_HUMANTRIM41physical
28514442
RAD21_HUMANRAD21physical
28514442
NRP1_HUMANNRP1physical
28514442
TGBR3_HUMANTGFBR3physical
28514442
DCAF5_HUMANDCAF5physical
28514442
CENPB_HUMANCENPBphysical
28514442
GPC3_HUMANGPC3physical
28514442
STAG2_HUMANSTAG2physical
28514442
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 PI51A_HUMAN

loading...

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-68; SER-71; SER-72 ANDSER-458, 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 SER-458, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry.";
Meierhofer D., Wang X., Huang L., Kaiser P.;
J. Proteome Res. 7:4566-4576(2008).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-103, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory