EFCB3_HUMAN - dbPTM
EFCB3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EFCB3_HUMAN
UniProt AC Q8N7B9
Protein Name EF-hand calcium-binding domain-containing protein 3
Gene Name EFCAB3
Organism Homo sapiens (Human).
Sequence Length 438
Subcellular Localization
Protein Description
Protein Sequence MAVSEIKPKLKLNPLTKVPISHNKRDRDLPGSLQCQLQHKEKKLSASQMAAFQDAYNFFYKDKTGCIDFHGLMCTVAKLGMNLTKHDVYNELKCADIDRDGKVNFSDFIKVLTDKNLFLKAVVPEKETCLDLAGNPGILLFEILSRLLETSALPRKSIIEIVSYFQRKFQHTGPGMLWSPYTMGYGKRTLKPDICTPPSSSMAAFANAARIAIMKEKDLFKFLEELKRCNSGSDSPYSKIPIFPLFPNVDGVVMGKPFKDMQKLEMLRIKEPLHFFEDYFFHKRDWKTQAANIKSMDPASGYSNNIFTIDQMLKKKQTCTVADATAIKQHVKRATDTYNLGIALEHRKEMLNLWQKIRGDLIGMDSRNESFYDTFSTYTWSWNVCQELLSPKDLRLYDAYVNRNSSHNSRSSSSSDTSECYTDSGRKRKRKGLKGFQQ
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
4Phosphorylation----MAVSEIKPKLK
----CCHHHCCCCCC
24.8618187866
9 (in isoform 2)Phosphorylation-53.9325999147
32PhosphorylationRDRDLPGSLQCQLQH
CCCCCCCCHHHHHHH
17.2130622161
145PhosphorylationILLFEILSRLLETSA
HHHHHHHHHHHHCCC
26.9224719451
151PhosphorylationLSRLLETSALPRKSI
HHHHHHCCCCCHHHH
20.5924719451
157PhosphorylationTSALPRKSIIEIVSY
CCCCCHHHHHHHHHH
30.0327174698
163PhosphorylationKSIIEIVSYFQRKFQ
HHHHHHHHHHHHHCC
26.3727174698
164PhosphorylationSIIEIVSYFQRKFQH
HHHHHHHHHHHHCCC
7.8827174698
189PhosphorylationTMGYGKRTLKPDICT
CCCCCCCCCCCCCCC
42.4924719451
196PhosphorylationTLKPDICTPPSSSMA
CCCCCCCCCCCHHHH
38.2724719451
199PhosphorylationPDICTPPSSSMAAFA
CCCCCCCCHHHHHHH
35.9325693802
200PhosphorylationDICTPPSSSMAAFAN
CCCCCCCHHHHHHHH
29.8825693802
201PhosphorylationICTPPSSSMAAFANA
CCCCCCHHHHHHHHH
19.4425693802
241PhosphorylationDSPYSKIPIFPLFPN
CCCCCCCCCCCCCCC
26.3824719451
248PhosphorylationPIFPLFPNVDGVVMG
CCCCCCCCCCEEEEC
36.8624719451
279PhosphorylationPLHFFEDYFFHKRDW
CHHHHHHHHHHCCCH
10.8430622161
300PhosphorylationIKSMDPASGYSNNIF
CCCCCCCCCCCCCCE
43.59-
372PhosphorylationDSRNESFYDTFSTYT
CCCCCCHHHHCHHHE
24.29-
390PhosphorylationNVCQELLSPKDLRLY
HHHHHHCCHHHHHHH
42.3924719451
406PhosphorylationAYVNRNSSHNSRSSS
HHCCCCCCCCCCCCC
30.1816964243
409PhosphorylationNRNSSHNSRSSSSSD
CCCCCCCCCCCCCCC
28.2816964243
418PhosphorylationSSSSSDTSECYTDSG
CCCCCCCHHCCCCCC
30.57-
422PhosphorylationSDTSECYTDSGRKRK
CCCHHCCCCCCHHHC
35.03-

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 EFCB3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EFCB3_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 EFCB3_HUMAN !!

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

Oops, there are no PPI records of EFCB3_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 EFCB3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND MASSSPECTROMETRY.

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