ELL_HUMAN - dbPTM
ELL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ELL_HUMAN
UniProt AC P55199
Protein Name RNA polymerase II elongation factor ELL
Gene Name ELL
Organism Homo sapiens (Human).
Sequence Length 621
Subcellular Localization Nucleus . Nucleus speckle . Nucleus, Cajal body . Colocalizes with EAF2 to nuclear speckles (PubMed:12446457). Colocalizes with coilin in subnuclear cajal and histone locus bodies (PubMed:12686606). Translocates in the LEC complex to cajal and histon
Protein Description 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. Elongation factor 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 MAALKEDRSYGLSCGRVSDGSKVSVFHVKLTDSALRAFESYRARQDSVSLRPSIRFQGSQGHISIPQPDCPAEARTFSFYLSNIGRDNPQGSFDCIQQYVSSHGEVHLDCLGSIQDKITVCATDDSYQKARQSMAQAEEETRSRSAIVIKAGGRYLGKKVQFRKPAPGATDAVPSRKRATPINLASAIRKSGASAVSGGSGVSQRPFRDRVLHLLALRPYRKAELLLRLQKDGLTQADKDALDGLLQQVANMSAKDGTCTLQDCMYKDVQKDWPGYSEGDQQLLKRVLVRKLCQPQSTGSLLGDPAASSPPGERGRSASPPQKRLQPPDFIDPLANKKPRISHFTQRAQPAVNGKLGVPNGREALLPTPGPPASTDTLSSSTHLPPRLEPPRAHDPLADVSNDLGHSGRDCEHGEAAAPAPTVRLGLPLLTDCAQPSRPHGSPSRSKPKKKSKKHKDKERAAEDKPRAQLPDCAPATHATPGAPADTPGLNGTCSVSSVPTSTSETPDYLLKYAAISSSEQRQSYKNDFNAEYSEYRDLHARIERITRRFTQLDAQLRQLSQGSEEYETTRGQILQEYRKIKKTNTNYSQEKHRCEYLHSKLAHIKRLIAEYDQRQLQAWP
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
2Acetylation------MAALKEDRS
------CCCCCCCCC		22.8522814378
9PhosphorylationAALKEDRSYGLSCGR
CCCCCCCCCCCCCEE		35.5620068231
10PhosphorylationALKEDRSYGLSCGRV
CCCCCCCCCCCCEEC		23.9924719451
13PhosphorylationEDRSYGLSCGRVSDG
CCCCCCCCCEECCCC		15.3420068231
18PhosphorylationGLSCGRVSDGSKVSV
CCCCEECCCCCEEEE		34.5920068231
21PhosphorylationCGRVSDGSKVSVFHV
CEECCCCCEEEEEEE		34.5720068231
29AcetylationKVSVFHVKLTDSALR
EEEEEEEEECHHHHH		36.7826051181
47PhosphorylationSYRARQDSVSLRPSI
HHHHCCCCCCCCCEE		12.7924719451
49PhosphorylationRARQDSVSLRPSIRF
HHCCCCCCCCCEEEE		23.7124719451
119PhosphorylationGSIQDKITVCATDDS
CCCCCCEEEEECCHH		18.44-
123PhosphorylationDKITVCATDDSYQKA
CCEEEEECCHHHHHH		34.9021815630
126PhosphorylationTVCATDDSYQKARQS
EEEECCHHHHHHHHH		32.0729978859
127PhosphorylationVCATDDSYQKARQSM
EEECCHHHHHHHHHH		22.4929978859
129UbiquitinationATDDSYQKARQSMAQ
ECCHHHHHHHHHHHH		36.99-
133PhosphorylationSYQKARQSMAQAEEE
HHHHHHHHHHHHHHH		15.5520068231
141PhosphorylationMAQAEEETRSRSAIV
HHHHHHHHHCCCEEE		36.9120068231
143PhosphorylationQAEEETRSRSAIVIK
HHHHHHHCCCEEEEE		37.7020068231
145PhosphorylationEEETRSRSAIVIKAG
HHHHHCCCEEEEEEC		24.4820068231
150AcetylationSRSAIVIKAGGRYLG
CCCEEEEEECCEECC		30.0425953088
170PhosphorylationRKPAPGATDAVPSRK
CCCCCCCCCCCCCCC		30.3317924679
180PhosphorylationVPSRKRATPINLASA
CCCCCCCCCCCHHHH		28.8325159151
186PhosphorylationATPINLASAIRKSGA
CCCCCHHHHHHHHCC		27.6522210691
191PhosphorylationLASAIRKSGASAVSG
HHHHHHHHCCCCCCC		29.7324719451
194PhosphorylationAIRKSGASAVSGGSG
HHHHHCCCCCCCCCC		32.5020044836
197PhosphorylationKSGASAVSGGSGVSQ
HHCCCCCCCCCCCCC		36.8330206219
200PhosphorylationASAVSGGSGVSQRPF
CCCCCCCCCCCCCCH		39.2820044836
203PhosphorylationVSGGSGVSQRPFRDR
CCCCCCCCCCCHHHH		24.8120044836
258PhosphorylationNMSAKDGTCTLQDCM
HCCCCCCCEEHHHHH		16.6727251789
260PhosphorylationSAKDGTCTLQDCMYK
CCCCCCEEHHHHHCC		27.56-
266PhosphorylationCTLQDCMYKDVQKDW
EEHHHHHCCCCCCCC		15.4627251789
271UbiquitinationCMYKDVQKDWPGYSE
HHCCCCCCCCCCCCH		62.70-
285UbiquitinationEGDQQLLKRVLVRKL
HHHHHHHHHHHHHHH		49.40-
297PhosphorylationRKLCQPQSTGSLLGD
HHHCCCCCCCCCCCC		41.2324732914
298PhosphorylationKLCQPQSTGSLLGDP
HHCCCCCCCCCCCCC		26.0824732914
300PhosphorylationCQPQSTGSLLGDPAA
CCCCCCCCCCCCCHH		22.1023403867
308PhosphorylationLLGDPAASSPPGERG
CCCCCHHCCCCCCCC		45.5530266825
309PhosphorylationLGDPAASSPPGERGR
CCCCHHCCCCCCCCC		30.3229255136
317PhosphorylationPPGERGRSASPPQKR
CCCCCCCCCCCCCHH		35.6026657352
319PhosphorylationGERGRSASPPQKRLQ
CCCCCCCCCCCHHCC		38.0622115753
355AcetylationAQPAVNGKLGVPNGR
CCCCCCCCCCCCCCC		36.5425953088
368PhosphorylationGREALLPTPGPPAST
CCCCCCCCCCCCCCC		40.6326853621
401PhosphorylationHDPLADVSNDLGHSG
CCCHHHCCCCCCCCC		25.7726055452
407PhosphorylationVSNDLGHSGRDCEHG
CCCCCCCCCCCCCCC		33.4528348404
431PhosphorylationRLGLPLLTDCAQPSR
ECCCCCCCCCCCCCC		36.3929255136
437PhosphorylationLTDCAQPSRPHGSPS
CCCCCCCCCCCCCCC		46.4929255136
442PhosphorylationQPSRPHGSPSRSKPK
CCCCCCCCCCCCCCC		19.3729255136
444PhosphorylationSRPHGSPSRSKPKKK
CCCCCCCCCCCCCCC		51.3829255136
446PhosphorylationPHGSPSRSKPKKKSK
CCCCCCCCCCCCCCH		58.6128111955
451"N6,N6-dimethyllysine"SRSKPKKKSKKHKDK
CCCCCCCCCHHHHHH		73.89-
451MethylationSRSKPKKKSKKHKDK
CCCCCCCCCHHHHHH		73.89-
456MethylationKKKSKKHKDKERAAE
CCCCHHHHHHHHHHH		78.39-
456"N6,N6-dimethyllysine"KKKSKKHKDKERAAE
CCCCHHHHHHHHHHH		78.39-
465MethylationKERAAEDKPRAQLPD
HHHHHHCCCHHHCCC		28.10-
465"N6,N6-dimethyllysine"KERAAEDKPRAQLPD
HHHHHHCCCHHHCCC		28.10-
518PhosphorylationLKYAAISSSEQRQSY
HHHHHCCCHHHHHHH		31.6125627689
519PhosphorylationKYAAISSSEQRQSYK
HHHHCCCHHHHHHHC		30.8425159151
551PhosphorylationERITRRFTQLDAQLR
HHHHHHHHHHHHHHH		26.8122210691
561PhosphorylationDAQLRQLSQGSEEYE
HHHHHHHHCCCHHHH		24.9417525332
569PhosphorylationQGSEEYETTRGQILQ
CCCHHHHHHHHHHHH		22.3822210691
570PhosphorylationGSEEYETTRGQILQE
CCHHHHHHHHHHHHH		22.3622210691
578PhosphorylationRGQILQEYRKIKKTN
HHHHHHHHHHHHHCC		12.3022210691
583UbiquitinationQEYRKIKKTNTNYSQ
HHHHHHHHCCCCCHH		50.94-
584PhosphorylationEYRKIKKTNTNYSQE
HHHHHHHCCCCCHHH		42.1220860994
586PhosphorylationRKIKKTNTNYSQEKH
HHHHHCCCCCHHHHH		40.5429449344
588PhosphorylationIKKTNTNYSQEKHRC
HHHCCCCCHHHHHHH		15.0829449344
589PhosphorylationKKTNTNYSQEKHRCE
HHCCCCCHHHHHHHH		33.6529449344
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
309SPhosphorylationKinaseMTORP42345
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ELL_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 ELL_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SIR2_HUMANSIRT2physical
17353931
P53_HUMANTP53physical
10358050
SNF8_HUMANSNF8physical
10419521
RPAB1_RATPolr2ephysical
9268387
RPAB2_RATPolr2fphysical
9268387
RPB7_RATPolr2gphysical
9268387
USPL1_HUMANUSPL1physical
24413172
EAF2_HUMANEAF2physical
27058417
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 ELL_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.
"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.
"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.
"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.
"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.

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