EEPD1_HUMAN - dbPTM
EEPD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EEPD1_HUMAN
UniProt AC Q7L9B9
Protein Name Endonuclease/exonuclease/phosphatase family domain-containing protein 1
Gene Name EEPD1
Organism Homo sapiens (Human).
Sequence Length 569
Subcellular Localization
Protein Description
Protein Sequence MGSTLGCHRSIPRDPSDLSHSRKFSAACNFSNILVNQERLNINTATEEELMTLPGVTRAVARSIVEYREYIGGFKKVEDLALVSGVGATKLEQVKFEICVSSKGSSAQHSPSSLRRDLLAEQQPHHLATAVPLTPRVNINTATPAQLMSVRGLSEKMALSIVDFRREHGPFRSVEDLVRMDGINAAFLDRIRHQVFAERSRPPSTHTNGGLTFTAKPHPSPTSLSLQSEDLDLPPGGPTQIISTRPSVEAFGGTRDGRPVLRLATWNLQGCSVEKANNPGVREVVCMTLLENSIKLLAVQELLDREALEKFCTELNQPTLPNIRKWKGPRGCWKAVVAEKPSSQLQKGAGYAGFLWDAAAGMELRDAGSQESSPSNGHGKLAGPSPYLGRFKVGSHDLTLVNLHLAALTLLGSENPSKNHSDGHRLASFAQTLQETLKGEKDVIILGDFGQGPDSNDYDILRKEKFHHLIPAHTFTNISTKNPQGSKSLDNIWISKSLKKVFTGHWAVVREGLTNPWIPDNWSWGGVASEHCPVLAEFYTEKDWSKKDAPRNGSGVALERSEANIKHER
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
2N-myristoyl glycine------MGSTLGCHR
------CCCCCCCCC
29.36-
2Myristoylation------MGSTLGCHR
------CCCCCCCCC
29.3620213681
7S-palmitoylation-MGSTLGCHRSIPRD
-CCCCCCCCCCCCCC
2.4427480498
10PhosphorylationSTLGCHRSIPRDPSD
CCCCCCCCCCCCHHH
17.1826657352
16PhosphorylationRSIPRDPSDLSHSRK
CCCCCCHHHCCCCHH
56.3124670416
19PhosphorylationPRDPSDLSHSRKFSA
CCCHHHCCCCHHHHH
25.1424670416
21PhosphorylationDPSDLSHSRKFSAAC
CHHHCCCCHHHHHHC
33.5123401153
25PhosphorylationLSHSRKFSAACNFSN
CCCCHHHHHHCCCHH
20.2823401153
31PhosphorylationFSAACNFSNILVNQE
HHHHCCCHHHEECHH
14.6830266825
70PhosphorylationSIVEYREYIGGFKKV
HHHHHHHHHCCCCCH
8.89-
101PhosphorylationVKFEICVSSKGSSAQ
EEEEEEECCCCCCCC
23.1728450419
102PhosphorylationKFEICVSSKGSSAQH
EEEEEECCCCCCCCC
22.1928450419
105PhosphorylationICVSSKGSSAQHSPS
EEECCCCCCCCCCCH
26.6621712546
106PhosphorylationCVSSKGSSAQHSPSS
EECCCCCCCCCCCHH
40.3930631047
110PhosphorylationKGSSAQHSPSSLRRD
CCCCCCCCCHHHHHH
17.8824972180
112PhosphorylationSSAQHSPSSLRRDLL
CCCCCCCHHHHHHHH
45.0521712546
113PhosphorylationSAQHSPSSLRRDLLA
CCCCCCHHHHHHHHH
29.3122115753
129PhosphorylationQQPHHLATAVPLTPR
HCCCCEECCCCCCCC
34.2530266825
134PhosphorylationLATAVPLTPRVNINT
EECCCCCCCCCCCCC
11.7223401153
143PhosphorylationRVNINTATPAQLMSV
CCCCCCCCHHHHHHH
19.6728555341
149PhosphorylationATPAQLMSVRGLSEK
CCHHHHHHHCCCCHH
19.7724719451
154PhosphorylationLMSVRGLSEKMALSI
HHHHCCCCHHHCHHH
37.6924719451
156UbiquitinationSVRGLSEKMALSIVD
HHCCCCHHHCHHHHH
26.5432015554
160PhosphorylationLSEKMALSIVDFRRE
CCHHHCHHHHHHHHH
15.8424670416
173PhosphorylationREHGPFRSVEDLVRM
HHHCCCCCHHHHHHC
30.1829255136
200PhosphorylationHQVFAERSRPPSTHT
HHHHHCCCCCCCCCC
40.4120363803
204PhosphorylationAERSRPPSTHTNGGL
HCCCCCCCCCCCCCE
35.1926657352
205PhosphorylationERSRPPSTHTNGGLT
CCCCCCCCCCCCCEE
38.1920363803
207PhosphorylationSRPPSTHTNGGLTFT
CCCCCCCCCCCEEEE
35.3326657352
212PhosphorylationTHTNGGLTFTAKPHP
CCCCCCEEEECCCCC
23.3929052541
214PhosphorylationTNGGLTFTAKPHPSP
CCCCEEEECCCCCCC
28.6529052541
220PhosphorylationFTAKPHPSPTSLSLQ
EECCCCCCCCCEEEE
37.4627732954
222PhosphorylationAKPHPSPTSLSLQSE
CCCCCCCCCEEEEEC
46.7927732954
223PhosphorylationKPHPSPTSLSLQSED
CCCCCCCCEEEEECC
21.2427732954
225PhosphorylationHPSPTSLSLQSEDLD
CCCCCCEEEEECCCC
24.9127732954
228PhosphorylationPTSLSLQSEDLDLPP
CCCEEEEECCCCCCC
38.0727732954
239PhosphorylationDLPPGGPTQIISTRP
CCCCCCCCEEEEECC
35.3626074081
243PhosphorylationGGPTQIISTRPSVEA
CCCCEEEEECCCEEC
21.7226074081
244PhosphorylationGPTQIISTRPSVEAF
CCCEEEEECCCEECC
35.8726074081
247PhosphorylationQIISTRPSVEAFGGT
EEEEECCCEECCCCC
29.3326074081
254PhosphorylationSVEAFGGTRDGRPVL
CEECCCCCCCCCEEE
26.4326471730
265PhosphorylationRPVLRLATWNLQGCS
CEEEEEEEEECCCCC
21.34-
313PhosphorylationEALEKFCTELNQPTL
HHHHHHHHHHCCCCC
46.7926270265
319PhosphorylationCTELNQPTLPNIRKW
HHHHCCCCCCCCCCC
45.1226270265
385PhosphorylationHGKLAGPSPYLGRFK
CCCCCCCCCCCCCEE
25.8422985185
387PhosphorylationKLAGPSPYLGRFKVG
CCCCCCCCCCCEECC
26.5723312004
421PhosphorylationENPSKNHSDGHRLAS
CCCCCCCCCHHHHHH
55.4720068231
428PhosphorylationSDGHRLASFAQTLQE
CCHHHHHHHHHHHHH
26.2111214970
432PhosphorylationRLASFAQTLQETLKG
HHHHHHHHHHHHHCC
27.2920068231
436PhosphorylationFAQTLQETLKGEKDV
HHHHHHHHHCCCCCE
22.3220068231
487UbiquitinationTKNPQGSKSLDNIWI
CCCCCCCCCCCEEEE
62.9632015554
496UbiquitinationLDNIWISKSLKKVFT
CCEEEECHHHHHHHC
51.1521890473
499UbiquitinationIWISKSLKKVFTGHW
EEECHHHHHHHCCCE
54.7222817900
500UbiquitinationWISKSLKKVFTGHWA
EECHHHHHHHCCCEE
48.1222817900
554PhosphorylationKDAPRNGSGVALERS
CCCCCCCCCCCCCCH
33.3722617229
560MethylationGSGVALERSEANIKH
CCCCCCCCHHHCCCC
40.42-
561PhosphorylationSGVALERSEANIKHE
CCCCCCCHHHCCCCC
31.5228634120
569MethylationEANIKHER-------
HHCCCCCC-------
52.11-

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 EEPD1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EEPD1_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 EEPD1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049

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 EEPD1_HUMAN

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Related Literatures of Post-Translational Modification
Myristoylation
ReferencePubMed
"Strategy for comprehensive identification of human N-myristoylatedproteins using an insect cell-free protein synthesis system.";
Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,Tsunasawa S., Utsumi T.;
Proteomics 10:1780-1793(2010).
Cited for: MYRISTOYLATION AT GLY-2.

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