ELL1_SCHPO - dbPTM
ELL1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ELL1_SCHPO
UniProt AC Q9P7X2
Protein Name RNA polymerase II elongation factor ell1
Gene Name ell1 {ECO:0000312|EMBL:CAB66442.1}
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 533
Subcellular Localization Nucleus .
Protein Description Activates transcription elongation by RNA polymerase II and pyrophosphorolysis as a complex with eaf1. Elongation factor that can increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA..
Protein Sequence MIRNSSISDALPVALGGNEEESPLLMLVQLPKEFLEGYLSGTITDVSLECSDVGTSILANDRSYKCTSVPETAPHEIYRLVDSNSLQLVGRVSQKLQLRRELDSLTAERVKNRTQEAQKEKEEKRIVTLQNDGGSKNTTARKQKQLKKNGLRPLNTSASRIGLSSSPTNTPSPNLPVSQPSASPHYSGDKNSAKGIDLRTRVIQLLAIAPETEDFLRLRTKASLSKLQALLPEVAWKNNMNQWELLNPVYKDVRVFDWRPYSIADRNAVLSRMSNAFDNMQLPPDAPERSLLVSKQKNITKLNNEKRIPPQLAQPTSHVPSFIDTNSPSMPSISSVSSYQQQHRIPKLNASNYSPLLSPSSHRKTSGNLSRTGSESSAVSLSDTTNLNTPISDIPSPGSSTTCSNLSSPHIKRKSRSPPQSLPSTPFPTSSSSTNGTLEPNANSPKKNEQDAWIAKKRRQQRYTTEEMRALAKRFRETYPRYKNLYLKVSSYYDNNDTNNPNLNKLQDELISLHSQLKSWKNTLYDASSELAL
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
164PhosphorylationSASRIGLSSSPTNTP
CHHHHCCCCCCCCCC
24.4529996109
166PhosphorylationSRIGLSSSPTNTPSP
HHHCCCCCCCCCCCC
32.1629996109
168PhosphorylationIGLSSSPTNTPSPNL
HCCCCCCCCCCCCCC
54.3929996109
181PhosphorylationNLPVSQPSASPHYSG
CCCCCCCCCCCCCCC
33.4729996109
183PhosphorylationPVSQPSASPHYSGDK
CCCCCCCCCCCCCCC
19.2929996109
186PhosphorylationQPSASPHYSGDKNSA
CCCCCCCCCCCCCCC
20.1029996109
325PhosphorylationHVPSFIDTNSPSMPS
CCCCCCCCCCCCCCC
32.5529996109
329PhosphorylationFIDTNSPSMPSISSV
CCCCCCCCCCCCHHC
43.0529996109
351PhosphorylationRIPKLNASNYSPLLS
CCCCCCCCCCCCCCC
34.9228889911
353PhosphorylationPKLNASNYSPLLSPS
CCCCCCCCCCCCCCC
14.7925720772
354PhosphorylationKLNASNYSPLLSPSS
CCCCCCCCCCCCCCC
17.2021712547
358PhosphorylationSNYSPLLSPSSHRKT
CCCCCCCCCCCCCCC
30.3428889911
360PhosphorylationYSPLLSPSSHRKTSG
CCCCCCCCCCCCCCC
35.0921712547
361PhosphorylationSPLLSPSSHRKTSGN
CCCCCCCCCCCCCCC
30.6025720772
415PhosphorylationSPHIKRKSRSPPQSL
CCCCCCCCCCCCCCC
41.8624763107
417PhosphorylationHIKRKSRSPPQSLPS
CCCCCCCCCCCCCCC
48.2828889911
433PhosphorylationPFPTSSSSTNGTLEP
CCCCCCCCCCCCCCC
28.0427738172
444PhosphorylationTLEPNANSPKKNEQD
CCCCCCCCCCCCHHH
35.3727738172

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 ELL1_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ELL1_SCHPO !!

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 ELL1_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPB1_SCHPOrpb1physical
17150956

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ELL1_SCHPO

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Related Literatures of Post-Translational Modification

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