PKHA2_HUMAN - dbPTM
PKHA2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PKHA2_HUMAN
UniProt AC Q9HB19
Protein Name Pleckstrin homology domain-containing family A member 2
Gene Name PLEKHA2
Organism Homo sapiens (Human).
Sequence Length 425
Subcellular Localization Cytoplasm. Cell membrane
Peripheral membrane protein. Nucleus. Locates to the plasma membrane after treatments that stimulate the production of PtdIns3,4P2..
Protein Description Binds specifically to phosphatidylinositol 3,4-diphosphate (PtdIns3,4P2), but not to other phosphoinositides. May recruit other proteins to the plasma membrane (By similarity)..
Protein Sequence MPYVDRQNRICGFLDIEEHENSGKFLRRYFILDTQANCLLWYMDNPQNLAMGAGAVGALQLTYISKVSIATPKQKPKTPFCFVINALSQRYFLQANDQKDMKDWVEALNQASKITVPKGGGLPMTTEVLKSLAAPPALEKKPQVAYKTEIIGGVVVHTPISQNGGDGQEGSEPGSHTILRRSQSYIPTSGCRASTGPPLIKSGYCVKQGNVRKSWKRRFFALDDFTICYFKCEQDREPLRTIFLKDVLKTHECLVKSGDLLMRDNLFEIITSSRTFYVQADSPEDMHSWIKEIGAAVQALKCHPRETSFSRSISLTRPGSSSLSSGPNSILCRGRPPLEEKKALCKAPSVASSWQPWTPVPQAGEKLLPPGDTSEDSLFTPRPGEGAPPGVLPSSRIRHRSEPQHPKEKPFMFNLDDENIRTSDV
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
29PhosphorylationSGKFLRRYFILDTQA
CCCHHHHEEEEECCC		6.6322817900
73UbiquitinationKVSIATPKQKPKTPF
EEEECCCCCCCCCCC		67.60-
99UbiquitinationFLQANDQKDMKDWVE
HHCCCCCHHHHHHHH		63.75-
102SumoylationANDQKDMKDWVEALN
CCCCHHHHHHHHHHH		59.58-
102SumoylationANDQKDMKDWVEALN
CCCCHHHHHHHHHHH		59.58-
102UbiquitinationANDQKDMKDWVEALN
CCCCHHHHHHHHHHH		59.58-
113UbiquitinationEALNQASKITVPKGG
HHHHHHHCCCCCCCC		45.47-
115PhosphorylationLNQASKITVPKGGGL
HHHHHCCCCCCCCCC		34.2024719451
118SumoylationASKITVPKGGGLPMT
HHCCCCCCCCCCCCC		66.89-
118UbiquitinationASKITVPKGGGLPMT
HHCCCCCCCCCCCCC		66.89-
118SumoylationASKITVPKGGGLPMT
HHCCCCCCCCCCCCC		66.89-
126PhosphorylationGGGLPMTTEVLKSLA
CCCCCCCHHHHHHCC		20.18-
130UbiquitinationPMTTEVLKSLAAPPA
CCCHHHHHHCCCCHH		48.91-
131PhosphorylationMTTEVLKSLAAPPAL
CCHHHHHHCCCCHHH		21.0528555341
140UbiquitinationAAPPALEKKPQVAYK
CCCHHHHCCCCEEEE		71.28-
141SumoylationAPPALEKKPQVAYKT
CCHHHHCCCCEEEEE		31.1625218447
141UbiquitinationAPPALEKKPQVAYKT
CCHHHHCCCCEEEEE		31.16-
141SumoylationAPPALEKKPQVAYKT
CCHHHHCCCCEEEEE		31.16-
158PhosphorylationIGGVVVHTPISQNGG
ECEEEEECCCCCCCC		15.6528555341
161PhosphorylationVVVHTPISQNGGDGQ
EEEECCCCCCCCCCC		20.8528857561
175PhosphorylationQEGSEPGSHTILRRS
CCCCCCCCCCEEECC		28.3328555341
182PhosphorylationSHTILRRSQSYIPTS
CCCEEECCCCCCCCC		19.6221945579
184PhosphorylationTILRRSQSYIPTSGC
CEEECCCCCCCCCCC		26.6922167270
185PhosphorylationILRRSQSYIPTSGCR
EEECCCCCCCCCCCC		11.8621945579
188PhosphorylationRSQSYIPTSGCRAST
CCCCCCCCCCCCCCC		28.3521945579
189PhosphorylationSQSYIPTSGCRASTG
CCCCCCCCCCCCCCC		30.4621945579
194PhosphorylationPTSGCRASTGPPLIK
CCCCCCCCCCCCEEE		17.9726657352
195PhosphorylationTSGCRASTGPPLIKS
CCCCCCCCCCCEEEC		53.3626552605
201SumoylationSTGPPLIKSGYCVKQ
CCCCCEEECCEEEEC		45.57-
201UbiquitinationSTGPPLIKSGYCVKQ
CCCCCEEECCEEEEC		45.57-
201SumoylationSTGPPLIKSGYCVKQ
CCCCCEEECCEEEEC		45.57-
207UbiquitinationIKSGYCVKQGNVRKS
EECCEEEECCCCCHH		49.26-
245SumoylationPLRTIFLKDVLKTHE
CCHHHHHHHHHHHCH		34.73-
245UbiquitinationPLRTIFLKDVLKTHE
CCHHHHHHHHHHHCH		34.73-
249UbiquitinationIFLKDVLKTHECLVK
HHHHHHHHHCHHHHH		47.92-
262SulfoxidationVKSGDLLMRDNLFEI
HHCCCEEECCCCCHH		7.0421406390
272PhosphorylationNLFEIITSSRTFYVQ
CCCHHHCCCCEEEEE		13.8621712546
273PhosphorylationLFEIITSSRTFYVQA
CCHHHCCCCEEEEEC		27.0425627689
291UbiquitinationEDMHSWIKEIGAAVQ
HHHHHHHHHHHHHHH		36.70-
301UbiquitinationGAAVQALKCHPRETS
HHHHHHHHCCCCCCC		33.25-
308PhosphorylationKCHPRETSFSRSISL
HCCCCCCCCCCEEEE		19.2430576142
312PhosphorylationRETSFSRSISLTRPG
CCCCCCCEEEEECCC		18.4823927012
314PhosphorylationTSFSRSISLTRPGSS
CCCCCEEEEECCCCC		25.5725463755
316PhosphorylationFSRSISLTRPGSSSL
CCCEEEEECCCCCCC		28.2025463755
320PhosphorylationISLTRPGSSSLSSGP
EEEECCCCCCCCCCC		21.3123927012
321PhosphorylationSLTRPGSSSLSSGPN
EEECCCCCCCCCCCC		41.0123927012
322PhosphorylationLTRPGSSSLSSGPNS
EECCCCCCCCCCCCC		33.6923927012
324PhosphorylationRPGSSSLSSGPNSIL
CCCCCCCCCCCCCCC		34.8923927012
325PhosphorylationPGSSSLSSGPNSILC
CCCCCCCCCCCCCCC		64.6623927012
329PhosphorylationSLSSGPNSILCRGRP
CCCCCCCCCCCCCCC		21.7728450419
333MethylationGPNSILCRGRPPLEE
CCCCCCCCCCCCHHH		40.4880702641
346SumoylationEEKKALCKAPSVASS
HHHHHHHCCCCCHHC		65.27-
346UbiquitinationEEKKALCKAPSVASS
HHHHHHHCCCCCHHC		65.27-
346SumoylationEEKKALCKAPSVASS
HHHHHHHCCCCCHHC		65.27-
349PhosphorylationKALCKAPSVASSWQP
HHHHCCCCCHHCCCC		34.8628355574
352PhosphorylationCKAPSVASSWQPWTP
HCCCCCHHCCCCCCC		29.9221712546
353PhosphorylationKAPSVASSWQPWTPV
CCCCCHHCCCCCCCC		21.7230576142
358PhosphorylationASSWQPWTPVPQAGE
HHCCCCCCCCCCCCC		22.5326552605
377PhosphorylationPGDTSEDSLFTPRPG
CCCCCCCCCCCCCCC		22.72-
380PhosphorylationTSEDSLFTPRPGEGA
CCCCCCCCCCCCCCC		24.55-
401PhosphorylationSSRIRHRSEPQHPKE
HHHCCCCCCCCCCCC		47.7221955146
409UbiquitinationEPQHPKEKPFMFNLD
CCCCCCCCCCCCCCC		50.08-
409AcetylationEPQHPKEKPFMFNLD
CCCCCCCCCCCCCCC		50.0825953088
412SulfoxidationHPKEKPFMFNLDDEN
CCCCCCCCCCCCCCC		2.7121406390
422PhosphorylationLDDENIRTSDV----
CCCCCCCCCCC----		26.0221712546
423PhosphorylationDDENIRTSDV-----
CCCCCCCCCC-----		26.9121712546
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 PKHA2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PKHA2_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 PKHA2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MPDZ_HUMANMPDZphysical
11802782
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 PKHA2_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-184, AND MASSSPECTROMETRY.
"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-184 AND SER-349, ANDMASS SPECTROMETRY.

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