EFR3B_HUMAN - dbPTM
EFR3B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EFR3B_HUMAN
UniProt AC Q9Y2G0
Protein Name Protein EFR3 homolog B {ECO:0000305}
Gene Name EFR3B {ECO:0000312|HGNC:HGNC:29155}
Organism Homo sapiens (Human).
Sequence Length 817
Subcellular Localization Cell membrane
Lipid-anchor . Cytoplasm, cytosol . Palmitoylation anchors the protein to the plasma membrane (PubMed:23229899, PubMed:25380825). 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 MYGVCGCCGALRPRYKRLVDNIFPEDPEDGLVKTNMEKLTFYALSAPEKLDRIGAYLSERLIRDVGRHRYGYVCIAMEALDQLLMACHCQSINLFVESFLKMVAKLLESEKPNLQILGTNSFVKFANIEEDTPSYHRSYDFFVSRFSEMCHSSHDDLEIKTKIRMSGIKGLQGVVRKTVNDELQANIWDPQHMDKIVPSLLFNLQHVEEAESRSPSPLQAPEKEKESPAELAERCLRELLGRAAFGNIKNAIKPVLIHLDNHSLWEPKVFAIRCFKIIMYSIQPQHSHLVIQQLLGHLDANSRSAATVRAGIVEVLSEAAVIAATGSVGPTVLEMFNTLLRQLRLSIDYALTGSYDGAVSLGTKIIKEHEERMFQEAVIKTVGSFASTLPTYQRSEVILFIMSKVPRPSLHQAVDTGRTGENRNRLTQIMLLKSLLQVSTGFQCNNMMSALPSNFLDRLLSTALMEDAEIRLFVLEILISFIDRHGNRHKFSTISTLSDISVLKLKVDKCSRQDTVFMKKHSQQLYRHIYLSCKEETNVQKHYEALYGLLALISIELANEEVVVDLIRLVLAVQDVAQVNEENLPVYNRCALYALGAAYLNLISQLTTVPAFCQHIHEVIETRKKEAPYMLPEDVFVERPRLSQNLDGVVIELLFRQSKISEVLGGSGYNSDRLCLPYIPQLTDEDRLSKRRSIGETISLQVEVESRNSPEKEERVPAEEITYETLKKAIVDSVAVEEQERERRRQVVEKFQKAPFEEIAAHCGARASLLQSKLNQIFEITIRPPPSPSGTITAAYGQPQNHSIPVYEMKFPDLCVY
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
15PhosphorylationCGALRPRYKRLVDNI
CHHHCHHHHHHHHHC
11.8018083107
38 (in isoform 3)Ubiquitination-41.9021890473
38 (in isoform 1)Ubiquitination-41.9021890473
38UbiquitinationLVKTNMEKLTFYALS
CEECCHHHEEEEECC
41.9021890473
42PhosphorylationNMEKLTFYALSAPEK
CHHHEEEEECCCHHH
11.0327050516
56PhosphorylationKLDRIGAYLSERLIR
HHHHHHHHHHHHHHH
12.92-
70PhosphorylationRDVGRHRYGYVCIAM
HHHCCCCCHHHHHCH
13.4924043423
72PhosphorylationVGRHRYGYVCIAMEA
HCCCCCHHHHHCHHH
5.3424043423
91PhosphorylationLMACHCQSINLFVES
HHHHCCCHHHHHHHH
20.8824043423
98PhosphorylationSINLFVESFLKMVAK
HHHHHHHHHHHHHHH
30.4924719451
105AcetylationSFLKMVAKLLESEKP
HHHHHHHHHHHCCCC
42.0420167786
111AcetylationAKLLESEKPNLQILG
HHHHHCCCCCEEEEE
48.7820167786
199PhosphorylationHMDKIVPSLLFNLQH
HHHHHHHHHHHHHHC
27.1529514088
212PhosphorylationQHVEEAESRSPSPLQ
HCHHHHHHCCCCCCC
45.1425849741
214PhosphorylationVEEAESRSPSPLQAP
HHHHHHCCCCCCCCC
38.7230266825
216PhosphorylationEAESRSPSPLQAPEK
HHHHCCCCCCCCCHH
39.2230266825
223UbiquitinationSPLQAPEKEKESPAE
CCCCCCHHHCCCHHH
73.38-
338PhosphorylationTVLEMFNTLLRQLRL
HHHHHHHHHHHHHHH
18.86-
352PhosphorylationLSIDYALTGSYDGAV
HHCCHHHHCCCCCCH
18.8619690332
360PhosphorylationGSYDGAVSLGTKIIK
CCCCCCHHHCCHHHH
22.1319690332
363PhosphorylationDGAVSLGTKIIKEHE
CCCHHHCCHHHHHHH
25.1019690332
416PhosphorylationSLHQAVDTGRTGENR
CHHHHHHCCCCCCCH
23.2024719451
522PhosphorylationTVFMKKHSQQLYRHI
CEEEHHHHHHHHHHH
28.6224719451
643PhosphorylationFVERPRLSQNLDGVV
CCCCCCCCCCCCHHH
20.5027732954
678PhosphorylationSDRLCLPYIPQLTDE
CCCCCCCCCCCCCCH
16.5728122231
683PhosphorylationLPYIPQLTDEDRLSK
CCCCCCCCCHHHHHH
31.9026657352
689PhosphorylationLTDEDRLSKRRSIGE
CCCHHHHHHCCCCCC
25.6325849741
693PhosphorylationDRLSKRRSIGETISL
HHHHHCCCCCCEEEE
38.6926471730
697PhosphorylationKRRSIGETISLQVEV
HCCCCCCEEEEEEEE
15.6226471730
699PhosphorylationRSIGETISLQVEVES
CCCCCEEEEEEEEEC
21.8426471730
722PhosphorylationRVPAEEITYETLKKA
CCCHHHCCHHHHHHH
20.7025884760
723PhosphorylationVPAEEITYETLKKAI
CCHHHCCHHHHHHHH
16.7525884760
725PhosphorylationAEEITYETLKKAIVD
HHHCCHHHHHHHHHH
33.2026074081
727UbiquitinationEITYETLKKAIVDSV
HCCHHHHHHHHHHHH
47.80-
733PhosphorylationLKKAIVDSVAVEEQE
HHHHHHHHHHHHHHH
10.9026074081
768PhosphorylationAHCGARASLLQSKLN
HHHCHHHHHHHHHHH
24.8627251275
787PhosphorylationITIRPPPSPSGTITA
EEECCCCCCCCCEEE
37.1622468782

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 EFR3B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EFR3B_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 EFR3B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of EFR3B_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 EFR3B_HUMAN

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Related Literatures of Post-Translational Modification

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