Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  RNA polymerase II elongation factor ELL  

UniProtKB / Swiss-Prot ID :  ELL_HUMAN

Gene Name (Synonyms) : 
ELL, C19orf17  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus speckle. Nucleus, Cajal body. Note=Colocalizes with EAF2 to nuclear speckles. Also localized to Cajal (coiled) bodies. 

Protein Function :  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 MAALKEDRSYGLSCGRVSDGSKVSVFHVKLTDSALRAFESYRARQDSVSLRPSIRFQGSQGHISIPQPDC...
Predicted Secondary Structure CCCCHHHHHHCCCCCCCCCCCCEEEEEEEECHHHHHHHHHHHHHHCCCCCCEEEEEECCCCEEECCCCCC...
Protein Variant
LocationDescription
297S -> N (in dbSNP:rs2303694). VAR_053072
387R -> W (in dbSNP:rs35245196). VAR_053073
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
9PhosphoserineKEDRSYGLS
HHHHHHCCC
35.56HPRD
Link-
133PhosphoserineKARQSMAQA
HHHHHHHHH
15.55HPRD
Link-
145PhosphoserineTRSRSAIVI
HCCCCEEEE
24.48HPRD
Link-
170PhosphothreonineAPGATDAVP
CCCHHHCCC
30.33HPRD
Link-
170Phosphothreonine.APGATDAVP
CCCHHHCCC
30.33UniProtKB
Link-
194PhosphoserineKSGASAVSG
HCCCCCCCC
32.50Phosphositeplus
Link-
200PhosphoserineVSGGSGVSQ
CCCCCCCCC
39.28Phosphositeplus
Link
203PhosphoserineGSGVSQRPF
CCCCCCCCH
24.81Phosphositeplus
Link
308PhosphoserineDPAASSPPG
CCCCCCCCC
45.55Phosphositeplus
Link-
309PhosphoserinePAASSPPGE
CCCCCCCCC
30.32HPRD
Link-
309PhosphoserinePAASSPPGE
CCCCCCCCC
30.32PhosphoELM
Link-
309PhosphoserinePAASSPPGE
CCCCCCCCC
30.32Phosphositeplus
Link-
309PhosphoserinePAASSPPGE
CCCCCCCCC
30.32SysPTM
Link-
309Phosphoserine.PAASSPPGE
CCCCCCCCC
30.32UniProtKB
Link-
317PhosphoserineERGRSASPP
CCCCCCCCC
35.60Phosphositeplus
Link-
319PhosphoserineGRSASPPQK
CCCCCCCCC
38.06Phosphositeplus
Link-
437PhosphoserineCAQPSRPHG
CCCCCCCCC
46.49HPRD
Link-
437PhosphoserineCAQPSRPHG
CCCCCCCCC
46.49PhosphoELM
Link-
437PhosphoserineCAQPSRPHG
CCCCCCCCC
46.49Phosphositeplus
Link-
442PhosphoserineRPHGSPSRS
CCCCCCCCC
19.37HPRD
Link-
442PhosphoserineRPHGSPSRS
CCCCCCCCC
19.37PhosphoELM
Link-
442PhosphoserineRPHGSPSRS
CCCCCCCCC
19.37Phosphositeplus
Link-
442PhosphoserineRPHGSPSRS
CCCCCCCCC
19.37SysPTM
Link-
561PhosphoserineLRQLSQGSE
HHHCCCCCH
24.94HPRD
Link-
561PhosphoserineLRQLSQGSE
HHHCCCCCH
24.94PhosphoELM
Link-
561PhosphoserineLRQLSQGSE
HHHCCCCCH
24.94Phosphositeplus
Link-
561Phosphoserine.LRQLSQGSE
HHHCCCCCH
24.94UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
TFPT_HUMANphysical interaction
physical interaction
EBI-1245897
EBI-1245862
intact17395368
17395368
P53_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:02615HPRD10358050
8016121
RPAB1_HUMANENSP00000262809STRING
RPAB2_HUMANENSP00000262809STRING
RPB3_HUMANENSP00000262809STRING
ERCC2_HUMANENSP00000262809STRING
RPB9_HUMANENSP00000262809STRING
TF2H3_HUMANENSP00000262809STRING
T2FA_HUMANENSP00000262809STRING
ENL_HUMANENSP00000262809STRING
CDK7_HUMANENSP00000262809STRING
CCNH_HUMANENSP00000262809STRING
TF2H4_HUMANENSP00000262809STRING
MAT1_HUMANENSP00000262809STRING
CCNT1_HUMANENSP00000262809STRING
ELOB_HUMANENSP00000262809STRING
CCNT2_HUMANENSP00000262809STRING
TF2H1_HUMANENSP00000262809STRING
RPB4_HUMANENSP00000262809STRING
EAF1_HUMANENSP00000262809STRING
EAF2_HUMANENSP00000262809STRING
TF2H2_HUMANENSP00000262809STRING
SSRP1_HUMANENSP00000262809STRING
ELOC_HUMANENSP00000262809STRING
ERCC3_HUMANENSP00000262809STRING
SNF8_HUMANENSP00000262809STRING
RPAB3_HUMANENSP00000262809STRING
CTDP1_HUMANENSP00000262809STRING
RPB7_HUMANENSP00000262809STRING
RPB2_HUMANENSP00000262809STRING
RPB1_HUMANENSP00000262809STRING
RPAB5_HUMANENSP00000262809STRING
NELFA_HUMANENSP00000262809STRING
NELFB_HUMANENSP00000262809STRING
NELFD_HUMANENSP00000262809STRING
RPAB4_HUMANENSP00000262809STRING
T2FB_HUMANENSP00000262809STRING
HRX_HUMANENSP00000262809STRING
TCEA1_HUMANENSP00000262809STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-170, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-561, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures