EID3_HUMAN - dbPTM
EID3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EID3_HUMAN
UniProt AC Q8N140
Protein Name EP300-interacting inhibitor of differentiation 3
Gene Name EID3 {ECO:0000312|EMBL:AAH27612.1}
Organism Homo sapiens (Human).
Sequence Length 333
Subcellular Localization Nucleus . Cytoplasm . Chromosome, telomere . May shuttle between nucleus and cytoplasm.
Protein Description Tissue-specific component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination and mediates sumoylation of shelterin complex (telosome) components.; Acts as a repressor of nuclear receptor-dependent transcription possibly by interfering with CREBBP-dependent coactivation. May function as a coinhibitor of other CREBBP/EP300-dependent transcription factors..
Protein Sequence MKMDVSVRAAGCSDDLSSGEADVDPKLLELTADEEKCRSIRRQYRQLMYCVRQNREDIVSSANNSLTEALEEANVLFDGVSRTREAALDARFLVMASDLGKEKAKQLNSDMNFFNQLAFCDFLFLFVGLNWMEGDPDKLSDCDDSIALSFWKAIEKEATSWMVKAETFHFVFGSFKLERSAPKPRLEHQKKVRKMEENGNMPTKLQKLDLSSYPEATEKNVERILGLLQTYFRKYPDTPVSYFEFVIDPNSFSRTVENIFYVSFIVRDGFARIRLDEDRLPILEPMNVNQMGEGNDSSCHGRKQGVISLTLQEWKNIVAAFEISEAMITYSSY
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
6Phosphorylation--MKMDVSVRAAGCS
--CCCCEEECCCCCC
11.1320068231
13PhosphorylationSVRAAGCSDDLSSGE
EECCCCCCCCCCCCC
32.9920068231
17PhosphorylationAGCSDDLSSGEADVD
CCCCCCCCCCCCCCC
43.2020068231
18PhosphorylationGCSDDLSSGEADVDP
CCCCCCCCCCCCCCH
48.2020068231
207UbiquitinationNMPTKLQKLDLSSYP
CCCCHHHHCCHHHCH
55.17-
230PhosphorylationRILGLLQTYFRKYPD
HHHHHHHHHHHHCCC
25.2920068231
231PhosphorylationILGLLQTYFRKYPDT
HHHHHHHHHHHCCCC
6.6020068231
235PhosphorylationLQTYFRKYPDTPVSY
HHHHHHHCCCCCCEE
11.3320068231
238PhosphorylationYFRKYPDTPVSYFEF
HHHHCCCCCCEEEEE
22.5320068231
241PhosphorylationKYPDTPVSYFEFVID
HCCCCCCEEEEEEEC
25.8820068231
242PhosphorylationYPDTPVSYFEFVIDP
CCCCCCEEEEEEECC
13.8320068231

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 EID3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EID3_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 EID3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NSE1_HUMANNSMCE1physical
18086888
SMC6_HUMANSMC6physical
18086888
MAGA1_HUMANMAGEA1physical
21364888
NSE1_HUMANNSMCE1physical
21364888
HDAC1_HUMANHDAC1physical
15970276
EID3_HUMANEID3physical
15970276
EID2_HUMANEID2physical
15970276
NMT1_HUMANNMT1physical
26186194
TLK2_HUMANTLK2physical
26186194
SMC6_HUMANSMC6physical
26186194
AKA12_HUMANAKAP12physical
26186194
ACSL4_HUMANACSL4physical
26186194
NSE2_HUMANNSMCE2physical
26186194
S27A2_HUMANSLC27A2physical
26186194
NSE3_HUMANNDNL2physical
26186194
SMC5_HUMANSMC5physical
26186194
CND2_HUMANNCAPHphysical
26186194
NSE1_HUMANNSMCE1physical
26186194
PGES2_HUMANPTGES2physical
26186194
APOL2_HUMANAPOL2physical
26186194
T22D3_HUMANTSC22D3physical
26186194
EMRE_HUMANSMDT1physical
26186194
NSE1_HUMANNSMCE1physical
28514442
NSE3_HUMANNDNL2physical
28514442
SMC5_HUMANSMC5physical
28514442
SMC6_HUMANSMC6physical
28514442
NSE2_HUMANNSMCE2physical
28514442
EMRE_HUMANSMDT1physical
28514442
PGES2_HUMANPTGES2physical
28514442
TLK2_HUMANTLK2physical
28514442
ACSL4_HUMANACSL4physical
28514442
RRP44_HUMANDIS3physical
28514442

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 EID3_HUMAN

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Related Literatures of Post-Translational Modification

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