EHF_HUMAN - dbPTM
EHF_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EHF_HUMAN
UniProt AC Q9NZC4
Protein Name ETS homologous factor
Gene Name EHF {ECO:0000312|HGNC:HGNC:3246}
Organism Homo sapiens (Human).
Sequence Length 300
Subcellular Localization Nucleus .
Protein Description Transcriptional activator that may play a role in regulating epithelial cell differentiation and proliferation. May act as a repressor for a specific subset of ETS/AP-1-responsive genes and as a modulator of the nuclear response to mitogen-activated protein kinase signaling cascades. Binds to DNA sequences containing the consensus nucleotide core sequence GGAA. Involved in regulation of TNFRSF10B/DR5 expression through Ets-binding sequences on the TNFRSF10B/DR5 promoter. May contribute to development and carcinogenesis by acting as a tumor suppressor gene or anti-oncogene..
Protein Sequence MILEGGGVMNLNPGNNLLHQPPAWTDSYSTCNVSSGFFGGQWHEIHPQYWTKYQVWEWLQHLLDTNQLDANCIPFQEFDINGEHLCSMSLQEFTRAAGTAGQLLYSNLQHLKWNGQCSSDLFQSTHNVIVKTEQTEPSIMNTWKDENYLYDTNYGSTVDLLDSKTFCRAQISMTTTSHLPVAESPDMKKEQDPPAKCHTKKHNPRGTHLWEFIRDILLNPDKNPGLIKWEDRSEGVFRFLKSEAVAQLWGKKKNNSSMTYEKLSRAMRYYYKREILERVDGRRLVYKFGKNARGWRENEN
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
127PhosphorylationDLFQSTHNVIVKTEQ
HHHHHCCCEEEEECC
25.8727642862
148 (in isoform 2)Phosphorylation-12.4626552605
150 (in isoform 2)Phosphorylation-15.4526552605
152 (in isoform 2)Phosphorylation-19.4526552605
154 (in isoform 2)Phosphorylation-17.9726552605
156 (in isoform 2)Phosphorylation-18.2026552605
157 (in isoform 2)Phosphorylation-17.4226552605
161 (in isoform 2)Phosphorylation-6.3826552605
164AcetylationTVDLLDSKTFCRAQI
CEEEECCCCEEEEEE
45.3320167786
184PhosphorylationSHLPVAESPDMKKEQ
CCCCCCCCCCCCCCC
19.2322617229
188AcetylationVAESPDMKKEQDPPA
CCCCCCCCCCCCCCC
61.6120167786
196AcetylationKEQDPPAKCHTKKHN
CCCCCCCCCCCCCCC
32.1120167786
199PhosphorylationDPPAKCHTKKHNPRG
CCCCCCCCCCCCCCC
51.78-
206PhosphorylationTKKHNPRGTHLWEFI
CCCCCCCCCCHHHHH
20.8124719451
242PhosphorylationGVFRFLKSEAVAQLW
CHHHHHHHHHHHHHH
32.7022817900
256PhosphorylationWGKKKNNSSMTYEKL
HCCCCCCCCCCHHHH
30.7729083192
257PhosphorylationGKKKNNSSMTYEKLS
CCCCCCCCCCHHHHH
19.7829083192
259PhosphorylationKKNNSSMTYEKLSRA
CCCCCCCCHHHHHHH
30.4029083192
260PhosphorylationKNNSSMTYEKLSRAM
CCCCCCCHHHHHHHH
11.4829759185
262UbiquitinationNSSMTYEKLSRAMRY
CCCCCHHHHHHHHHH
41.15-

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 EHF_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EHF_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 EHF_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XRCC6_HUMANXRCC6physical
15075319
XRCC5_HUMANXRCC5physical
15075319
CYTM_HUMANCST6physical
26186194
KPRP_HUMANKPRPphysical
26186194
KPRP_HUMANKPRPphysical
28514442
CYTM_HUMANCST6physical
28514442
ARGI1_HUMANARG1physical
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 EHF_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-242, AND MASSSPECTROMETRY.

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