EFR3A_HUMAN - dbPTM
EFR3A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EFR3A_HUMAN
UniProt AC Q14156
Protein Name Protein EFR3 homolog A {ECO:0000305}
Gene Name EFR3A {ECO:0000312|HGNC:HGNC:28970}
Organism Homo sapiens (Human).
Sequence Length 821
Subcellular Localization Cell membrane
Lipid-anchor . Cytoplasm, cytosol . Palmitoylation anchors the protein to the plasma membrane (PubMed:23229899, PubMed:25380825, PubMed:26571211). A small amount is observed in the cytosol (PubMed:25380825).
Protein Description Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane. [PubMed: 23229899]
Protein Sequence MPTRVCCCCSALRPRYKRLVDNIFPEDPKDGLVKTDMEKLTFYAVSAPEKLDRIGSYLAERLSRDVVRHRSGYVLIAMEALDQLLMACHSQSIKPFVESFLHMVAKLLESGEPKLQVLGTNSFVKFANIEEDTPSYHRRYDFFVSRFSAMCHSCHSDPEIRTEIRIAGIRGIQGVVRKTVNDELRATIWEPQHMDKIVPSLLFNMQKIEEVDSRIGPPSSPSATDKEENPAVLAENCFRELLGRATFGNMNNAVRPVFAHLDHHKLWDPNEFAVHCFKIIMYSIQAQYSHHVIQEILGHLDARKKDAPRVRAGIIQVLLEAVAIAAKGSIGPTVLEVFNTLLKHLRLSVEFEANDLQGGSVGSVNLNTSSKDNDEKIVQNAIIQTIGFFGSNLPDYQRSEIMMFIMGKVPVFGTSTHTLDISQLGDLGTRRIQIMLLRSLLMVTSGYKAKTIVTALPGSFLDPLLSPSLMEDYELRQLVLEVMHNLMDRHDNRAKLRGIRIIPDVADLKIKREKICRQDTSFMKKNGQQLYRHIYLGCKEEDNVQKNYELLYTSLALITIELANEEVVIDLIRLAIALQDSAIINEDNLPMFHRCGIMALVAAYLNFVSQMIAVPAFCQHVSKVIEIRTMEAPYFLPEHIFRDKCMLPKSLEKHEKDLYFLTNKIAESLGGSGYSVERLSVPYVPQVTDEDRLSRRKSIVDTVSIQVDILSNNVPSDDVVSNTEEITFEALKKAIDTSGMEEQEKEKRRLVIEKFQKAPFEEIAAQCESKANLLHDRLAQILELTIRPPPSPSGTLTITSGHAQYQSVPVYEMKFPDLCVY
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
3Phosphorylation-----MPTRVCCCCS
-----CCCEEECCCH		34.1428270605
6S-palmitoylation--MPTRVCCCCSALR
--CCCEEECCCHHCC		1.0129575903
7S-palmitoylation-MPTRVCCCCSALRP
-CCCEEECCCHHCCH		2.1029575903
8S-palmitoylationMPTRVCCCCSALRPR
CCCEEECCCHHCCHH		1.4129575903
9S-palmitoylationPTRVCCCCSALRPRY
CCEEECCCHHCCHHH		1.3429575903
10PhosphorylationTRVCCCCSALRPRYK
CEEECCCHHCCHHHH		19.2028270605
14 (in isoform 2)Ubiquitination-44.8121890473
14UbiquitinationCCCSALRPRYKRLVD
CCCHHCCHHHHHHHH		44.8121890473
29UbiquitinationNIFPEDPKDGLVKTD
HCCCCCCCCCCCCCC		76.4129967540
34UbiquitinationDPKDGLVKTDMEKLT
CCCCCCCCCCHHHCE		43.8023000965
35PhosphorylationPKDGLVKTDMEKLTF
CCCCCCCCCHHHCEE		32.85-
39 (in isoform 3)Ubiquitination-46.3021890473
39UbiquitinationLVKTDMEKLTFYAVS
CCCCCHHHCEEEEEC		46.3023000965
39 (in isoform 1)Ubiquitination-46.3021890473
41PhosphorylationKTDMEKLTFYAVSAP
CCCHHHCEEEEECCH		26.1828152594
43PhosphorylationDMEKLTFYAVSAPEK
CHHHCEEEEECCHHH		10.8028152594
50 (in isoform 3)Ubiquitination-55.4121890473
50 (in isoform 1)Ubiquitination-55.4121890473
50UbiquitinationYAVSAPEKLDRIGSY
EEECCHHHHHHHHHH		55.4123000965
56PhosphorylationEKLDRIGSYLAERLS
HHHHHHHHHHHHHHC		18.0121082442
57PhosphorylationKLDRIGSYLAERLSR
HHHHHHHHHHHHHCC		12.5223186163
89UbiquitinationDQLLMACHSQSIKPF
HHHHHHHHCCCCHHH		21.2322817900
89 (in isoform 2)Ubiquitination-21.2321890473
90PhosphorylationQLLMACHSQSIKPFV
HHHHHHHCCCCHHHH		26.0522210691
92PhosphorylationLMACHSQSIKPFVES
HHHHHCCCCHHHHHH		35.2822210691
125 (in isoform 1)Ubiquitination-36.4321890473
125UbiquitinationLGTNSFVKFANIEED
EECCCCEEECCCCCC		36.4322817900
125 (in isoform 3)Ubiquitination-36.4321890473
171UbiquitinationIRIAGIRGIQGVVRK
HHHHCCCCCHHEEEH		18.0422817900
171 (in isoform 2)Ubiquitination-18.0421890473
179PhosphorylationIQGVVRKTVNDELRA
CHHEEEHHHCHHHHH		17.6124702127
190UbiquitinationELRATIWEPQHMDKI
HHHHHHCCHHHHHHH		31.0929967540
207 (in isoform 1)Ubiquitination-41.1221890473
207 (in isoform 3)Ubiquitination-41.1221890473
207UbiquitinationSLLFNMQKIEEVDSR
HHHHCHHHHHHHHHC		41.1221906983
219PhosphorylationDSRIGPPSSPSATDK
HHCCCCCCCCCCCCC		59.0030266825
220PhosphorylationSRIGPPSSPSATDKE
HCCCCCCCCCCCCCC		28.7530266825
222PhosphorylationIGPPSSPSATDKEEN
CCCCCCCCCCCCCCC		45.8330266825
224PhosphorylationPPSSPSATDKEENPA
CCCCCCCCCCCCCHH		52.5230266825
226UbiquitinationSSPSATDKEENPAVL
CCCCCCCCCCCHHHH		63.6729967540
360PhosphorylationANDLQGGSVGSVNLN
CCCCCCCCEEEEECC		30.08-
363PhosphorylationLQGGSVGSVNLNTSS
CCCCCEEEEECCCCC		12.99-
414PhosphorylationGKVPVFGTSTHTLDI
CCCCEEECCCCEECH		20.9823186163
415PhosphorylationKVPVFGTSTHTLDIS
CCCEEECCCCEECHH		20.6926657352
416PhosphorylationVPVFGTSTHTLDISQ
CCEEECCCCEECHHH		20.7924732914
418PhosphorylationVFGTSTHTLDISQLG
EEECCCCEECHHHHC		26.6423186163
422PhosphorylationSTHTLDISQLGDLGT
CCCEECHHHHCCCCH		21.0121712546
429PhosphorylationSQLGDLGTRRIQIML
HHHCCCCHHHHHHHH		24.8724732914
439PhosphorylationIQIMLLRSLLMVTSG
HHHHHHHHHHHHCCC		26.3127690223
444PhosphorylationLRSLLMVTSGYKAKT
HHHHHHHCCCCCCEE		11.5027690223
445PhosphorylationRSLLMVTSGYKAKTI
HHHHHHCCCCCCEEH		28.8120068231
447PhosphorylationLLMVTSGYKAKTIVT
HHHHCCCCCCEEHEE		13.9327690223
473 (in isoform 2)Ubiquitination-11.9821890473
473UbiquitinationSPSLMEDYELRQLVL
CHHHCCCHHHHHHHH		11.9822817900
475UbiquitinationSLMEDYELRQLVLEV
HHCCCHHHHHHHHHH		3.2622817900
478UbiquitinationEDYELRQLVLEVMHN
CCHHHHHHHHHHHHH		3.7222817900
488UbiquitinationEVMHNLMDRHDNRAK
HHHHHHHHCCCHHHH		48.1827667366
489UbiquitinationVMHNLMDRHDNRAKL
HHHHHHHCCCHHHHH		25.7027667366
503UbiquitinationLRGIRIIPDVADLKI
HCCEEECCCHHHCCC		27.8729967540
509 (in isoform 1)Ubiquitination-46.8821890473
509 (in isoform 3)Ubiquitination-46.8821890473
509UbiquitinationIPDVADLKIKREKIC
CCCHHHCCCCHHHHH		46.8822817900
511UbiquitinationDVADLKIKREKICRQ
CHHHCCCCHHHHHCC		53.5722817900
514UbiquitinationDLKIKREKICRQDTS
HCCCCHHHHHCCCCH		51.6522817900
521PhosphorylationKICRQDTSFMKKNGQ
HHHCCCCHHHHHHHH		31.4725627689
524UbiquitinationRQDTSFMKKNGQQLY
CCCCHHHHHHHHHHH		40.8727667366
525UbiquitinationQDTSFMKKNGQQLYR
CCCHHHHHHHHHHHH		55.3027667366
539UbiquitinationRHIYLGCKEEDNVQK
HHHHCCCCCHHCHHH		63.4429967540
628UbiquitinationVSKVIEIRTMEAPYF
HHHHHEEEECCCCCC		18.4122817900
628 (in isoform 2)Ubiquitination-18.4121890473
650PhosphorylationDKCMLPKSLEKHEKD
CCCCCCHHHHHHHHH		39.5618669648
658PhosphorylationLEKHEKDLYFLTNKI
HHHHHHHHHHHHHHH		4.8932142685
659PhosphorylationEKHEKDLYFLTNKIA
HHHHHHHHHHHHHHH		13.4830301811
662PhosphorylationEKDLYFLTNKIAESL
HHHHHHHHHHHHHHH		25.2730301811
664 (in isoform 1)Ubiquitination-37.7521890473
664UbiquitinationDLYFLTNKIAESLGG
HHHHHHHHHHHHHCC		37.7522817900
680PhosphorylationGYSVERLSVPYVPQV
CCCEEEECCCCCCCC		27.5423927012
683PhosphorylationVERLSVPYVPQVTDE
EEEECCCCCCCCCCH		23.7023927012
688PhosphorylationVPYVPQVTDEDRLSR
CCCCCCCCCHHHHHH		28.5530266825
694PhosphorylationVTDEDRLSRRKSIVD
CCCHHHHHHCCHHCC		30.8229255136
698PhosphorylationDRLSRRKSIVDTVSI
HHHHHCCHHCCEEEE		26.4926074081
711PhosphorylationSIQVDILSNNVPSDD
EEEHHHHHCCCCCCC		27.0532142685
721UbiquitinationVPSDDVVSNTEEITF
CCCCCCCCCCCHHCH		37.5729967540
737PhosphorylationALKKAIDTSGMEEQE
HHHHHHHCCCCCHHH		22.5221712546
738PhosphorylationLKKAIDTSGMEEQEK
HHHHHHCCCCCHHHH		32.1821815630
757UbiquitinationLVIEKFQKAPFEEIA
HHHHHHHCCCHHHHH		62.2529967540
774UbiquitinationCESKANLLHDRLAQI
CHHHHHHHHHHHHHH		3.8629967540
791PhosphorylationLTIRPPPSPSGTLTI
HEECCCCCCCCEEEE		37.1628348404
793PhosphorylationIRPPPSPSGTLTITS
ECCCCCCCCEEEEEE		49.0728348404
795PhosphorylationPPPSPSGTLTITSGH
CCCCCCCEEEEEECC		25.6828348404
797PhosphorylationPSPSGTLTITSGHAQ
CCCCCEEEEEECCCE		23.2628348404
799PhosphorylationPSGTLTITSGHAQYQ
CCCEEEEEECCCEEE		24.3428348404
800PhosphorylationSGTLTITSGHAQYQS
CCEEEEEECCCEEEE		25.4028348404
805PhosphorylationITSGHAQYQSVPVYE
EEECCCEEEECCEEE		11.98-
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 EFR3A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EFR3A_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 EFR3A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of EFR3A_HUMAN !!
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 EFR3A_HUMAN

loading...

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-56, 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-694, AND MASSSPECTROMETRY.
"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-422 AND SER-694, ANDMASS 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-694, AND MASSSPECTROMETRY.

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