ELL3_HUMAN - dbPTM
ELL3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ELL3_HUMAN
UniProt AC Q9HB65
Protein Name RNA polymerase II elongation factor ELL3
Gene Name ELL3
Organism Homo sapiens (Human).
Sequence Length 397
Subcellular Localization Nucleus .
Protein Description Enhancer-binding elongation factor that specifically binds enhancers in embryonic stem cells (ES cells), marks them, and is required for their future activation during stem cell specification. Does not only bind to enhancer regions of active genes, but also marks the enhancers that are in a poised or inactive state in ES cells and is required for establishing proper RNA polymerase II occupancy at developmentally regulated genes in a cohesin-dependent manner. Probably required for priming developmentally regulated genes for later recruitment of the super elongation complex (SEC), for transcriptional activation during differentiation. Required for recruitment of P-TEFb within SEC during differentiation. Probably preloaded on germ cell chromatin, suggesting that it may prime gene activation by marking enhancers as early as in the germ cells. Promoting epithelial-mesenchymal transition (EMT) (By similarity). Elongation factor component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III. [PubMed: 22195968]
Protein Sequence MEELQEPLRGQLRLCFTQAARTSLLLLRLNDAALRALQECQRQQVRPVIAFQGHRGYLRLPGPGWSCLFSFIVSQCCQEGAGGSLDLVCQRFLRSGPNSLHCLGSLRERLIIWAAMDSIPAPSSVQGHNLTEDARHPESWQNTGGYSEGDAVSQPQMALEEVSVSDPLASNQGQSLPGSSREHMAQWEVRSQTHVPNREPVQALPSSASRKRLDKKRSVPVATVELEEKRFRTLPLVPSPLQGLTNQDLQEGEDWEQEDEDMDPRLEHSSSVQEDSESPSPEDIPDYLLQYRAIHSAEQQHAYEQDFETDYAEYRILHARVGTASQRFIELGAEIKRVRRGTPEYKVLEDKIIQEYKKFRKQYPSYREEKRRCEYLHQKLSHIKGLILEFEEKNRGS
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
105PhosphorylationNSLHCLGSLRERLII
CHHHHHHHHHHHHHH
16.0024719451
207PhosphorylationPVQALPSSASRKRLD
CCCCCCCCHHHHHHH
28.4628555341
209PhosphorylationQALPSSASRKRLDKK
CCCCCCHHHHHHHCC
40.0428555341
218PhosphorylationKRLDKKRSVPVATVE
HHHHCCCCCCCEEEE
39.3928674151
229UbiquitinationATVELEEKRFRTLPL
EEEEEEHHHHCCCCC
47.68-
239PhosphorylationRTLPLVPSPLQGLTN
CCCCCCCCCCCCCCC
30.6625954137
245PhosphorylationPSPLQGLTNQDLQEG
CCCCCCCCCCCHHCC
37.3428348404
269PhosphorylationMDPRLEHSSSVQEDS
CCHHHCCCCCCCCCC
18.2226714015
270PhosphorylationDPRLEHSSSVQEDSE
CHHHCCCCCCCCCCC
36.1126714015
271PhosphorylationPRLEHSSSVQEDSES
HHHCCCCCCCCCCCC
30.7326714015
276PhosphorylationSSSVQEDSESPSPED
CCCCCCCCCCCCCCC
38.9426714015
278PhosphorylationSVQEDSESPSPEDIP
CCCCCCCCCCCCCCC
34.3325849741
280PhosphorylationQEDSESPSPEDIPDY
CCCCCCCCCCCCCHH
50.6426714015
287PhosphorylationSPEDIPDYLLQYRAI
CCCCCCHHHHHHHHH
12.1726714015
351UbiquitinationEYKVLEDKIIQEYKK
CHHHHHHHHHHHHHH
32.1229967540
363PhosphorylationYKKFRKQYPSYREEK
HHHHHHHCCCHHHHH
9.3628509920
365PhosphorylationKFRKQYPSYREEKRR
HHHHHCCCHHHHHHH
31.7128509920
366PhosphorylationFRKQYPSYREEKRRC
HHHHCCCHHHHHHHH
19.9628509920

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 ELL3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ELL3_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 ELL3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FRIH_HUMANFTH1physical
16169070
ICE2_HUMANICE2physical
26186194
AFF1_HUMANAFF1physical
26186194
ICE1_HUMANICE1physical
26186194
AF9_HUMANMLLT3physical
26186194
ENL_HUMANMLLT1physical
26186194
EAF2_HUMANEAF2physical
26186194
ADDG_HUMANADD3physical
26186194
CCNT2_HUMANCCNT2physical
26186194
CCNT1_HUMANCCNT1physical
26186194
CDK14_HUMANCDK14physical
26186194
ELL_HUMANELLphysical
26186194
ENL_HUMANMLLT1physical
28514442
ICE1_HUMANICE1physical
28514442
AFF1_HUMANAFF1physical
28514442
ICE2_HUMANICE2physical
28514442
AF9_HUMANMLLT3physical
28514442
CCNT1_HUMANCCNT1physical
28514442
CDK14_HUMANCDK14physical
28514442
CCNT2_HUMANCCNT2physical
28514442
ELL_HUMANELLphysical
28514442
EAF2_HUMANEAF2physical
28514442
ADDG_HUMANADD3physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ELL3_HUMAN

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Related Literatures of Post-Translational Modification

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