ELL2_HUMAN - dbPTM
ELL2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ELL2_HUMAN
UniProt AC O00472
Protein Name RNA polymerase II elongation factor ELL2
Gene Name ELL2
Organism Homo sapiens (Human).
Sequence Length 640
Subcellular Localization Nucleus.
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. 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 Plays a role in immunoglobulin secretion in plasma cells: directs efficient alternative mRNA processing, influencing both proximal poly(A) site choice and exon skipping, as well as immunoglobulin heavy chain (IgH) alternative processing. Probably acts by regulating histone modifications accompanying transition from membrane-specific to secretory IgH mRNA expression.]
Protein Sequence MAAGGTGGLREEQRYGLSCGRLGQDNITVLHVKLTETAIRALETYQSHKNLIPFRPSIQFQGLHGLVKIPKNDPLNEVHNFNFYLSNVGKDNPQGSFDCIQQTFSSSGASQLNCLGFIQDKITVCATNDSYQMTRERMTQAEEESRNRSTKVIKPGGPYVGKRVQIRKAPQAVSDTVPERKRSTPMNPANTIRKTHSSSTISQRPYRDRVIHLLALKAYKKPELLARLQKDGVNQKDKNSLGAILQQVANLNSKDLSYTLKDYVFKELQRDWPGYSEIDRRSLESVLSRKLNPSQNAAGTSRSESPVCSSRDAVSSPQKRLLDSEFIDPLMNKKARISHLTNRVPPTLNGHLNPTSEKSAAGLPLPPAAAAIPTPPPLPSTYLPISHPPQIVNSNSNSPSTPEGRGTQDLPVDSFSQNDSIYEDQQDKYTSRTSLETLPPGSVLLKCPKPMEENHSMSHKKSKKKSKKHKEKDQIKKHDIETIEEKEEDLKREEEIAKLNNSSPNSSGGVKEDCTASMEPSAIELPDYLIKYIAIVSYEQRQNYKDDFNAEYDEYRALHARMETVARRFIKLDAQRKRLSPGSKEYQNVHEEVLQEYQKIKQSSPNYHEEKYRCEYLHNKLAHIKRLIGEFDQQQAESWS
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
6Phosphorylation--MAAGGTGGLREEQ
--CCCCCCCCCHHHH		27.4520068231
37PhosphorylationLHVKLTETAIRALET
EEEEECHHHHHHHHH		23.3423186163
145PhosphorylationMTQAEEESRNRSTKV
HHHHHHHHHHCCCCE		37.83-
162AcetylationPGGPYVGKRVQIRKA
CCCCCCCCEEEEECC		39.0826051181
178UbiquitinationQAVSDTVPERKRSTP
CCCCCCCCCHHCCCC		37.45-
183PhosphorylationTVPERKRSTPMNPAN
CCCCHHCCCCCCHHH		39.6430619164
184PhosphorylationVPERKRSTPMNPANT
CCCHHCCCCCCHHHH		30.5030619164
191PhosphorylationTPMNPANTIRKTHSS
CCCCHHHHHHHCCCC		25.0230619164
197PhosphorylationNTIRKTHSSSTISQR
HHHHHCCCCCCCCCC		31.0828555341
198PhosphorylationTIRKTHSSSTISQRP
HHHHCCCCCCCCCCC		24.7224114839
206PhosphorylationSTISQRPYRDRVIHL
CCCCCCCCHHHHHHH		27.6024114839
241UbiquitinationNQKDKNSLGAILQQV
CHHCHHHHHHHHHHH		8.21-
258PhosphorylationLNSKDLSYTLKDYVF
CCCCCCHHHHHHHHH		24.32-
282PhosphorylationYSEIDRRSLESVLSR
CCHHCHHHHHHHHHH		37.07-
290UbiquitinationLESVLSRKLNPSQNA
HHHHHHHCCCCCCCC		49.60-
295UbiquitinationSRKLNPSQNAAGTSR
HHCCCCCCCCCCCCC		44.85-
301PhosphorylationSQNAAGTSRSESPVC
CCCCCCCCCCCCCCC		32.6525627689
303PhosphorylationNAAGTSRSESPVCSS
CCCCCCCCCCCCCCC		42.0420068231
305PhosphorylationAGTSRSESPVCSSRD
CCCCCCCCCCCCCCC		24.7125159151
309PhosphorylationRSESPVCSSRDAVSS
CCCCCCCCCCCCCCC		28.7420068231
310PhosphorylationSESPVCSSRDAVSSP
CCCCCCCCCCCCCCH		29.1125159151
315PhosphorylationCSSRDAVSSPQKRLL
CCCCCCCCCHHHHHC		37.7129691806
316PhosphorylationSSRDAVSSPQKRLLD
CCCCCCCCHHHHHCC		25.4225159151
334UbiquitinationIDPLMNKKARISHLT
HHHHCCCHHHHHHHH		37.58-
338PhosphorylationMNKKARISHLTNRVP
CCCHHHHHHHHCCCC		13.5928555341
359PhosphorylationLNPTSEKSAAGLPLP
CCCCCCCCCCCCCCC		21.2120873877
374PhosphorylationPAAAAIPTPPPLPST
CHHHCCCCCCCCCCC		42.1720873877
380PhosphorylationPTPPPLPSTYLPISH
CCCCCCCCCCCCCCC		37.0520873877
381PhosphorylationTPPPLPSTYLPISHP
CCCCCCCCCCCCCCC		27.4320873877
382PhosphorylationPPPLPSTYLPISHPP
CCCCCCCCCCCCCCC		18.1520873877
386PhosphorylationPSTYLPISHPPQIVN
CCCCCCCCCCCCCCC		28.1820873877
394PhosphorylationHPPQIVNSNSNSPST
CCCCCCCCCCCCCCC		30.6428348404
396PhosphorylationPQIVNSNSNSPSTPE
CCCCCCCCCCCCCCC		38.2128348404
398PhosphorylationIVNSNSNSPSTPEGR
CCCCCCCCCCCCCCC		21.7628348404
400PhosphorylationNSNSNSPSTPEGRGT
CCCCCCCCCCCCCCC		57.3128348404
401PhosphorylationSNSNSPSTPEGRGTQ
CCCCCCCCCCCCCCC		28.8328348404
414PhosphorylationTQDLPVDSFSQNDSI
CCCCCCCCCCCCCCC		27.3425159151
416PhosphorylationDLPVDSFSQNDSIYE
CCCCCCCCCCCCCCH		31.8425159151
420PhosphorylationDSFSQNDSIYEDQQD
CCCCCCCCCCHHCCC		34.3221815630
428UbiquitinationIYEDQQDKYTSRTSL
CCHHCCCCCCCCCCC		46.20-
431PhosphorylationDQQDKYTSRTSLETL
HCCCCCCCCCCCCCC		30.3928555341
434PhosphorylationDKYTSRTSLETLPPG
CCCCCCCCCCCCCCC		24.0928674419
446UbiquitinationPPGSVLLKCPKPMEE
CCCCEEEECCCCCCC		44.31-
470AcetylationKKKSKKHKEKDQIKK
HHHHHHHHHHHHHHH		75.297296643
476AcetylationHKEKDQIKKHDIETI
HHHHHHHHHHHHHHH		38.127296655
486SumoylationDIETIEEKEEDLKRE
HHHHHHHHHHHHHHH		54.32-
502PhosphorylationEIAKLNNSSPNSSGG
HHHHHHCCCCCCCCC		46.2121955146
503PhosphorylationIAKLNNSSPNSSGGV
HHHHHCCCCCCCCCC		30.1725159151
506PhosphorylationLNNSSPNSSGGVKED
HHCCCCCCCCCCCCC		33.4721955146
507PhosphorylationNNSSPNSSGGVKEDC
HCCCCCCCCCCCCCC		46.3229116813
515PhosphorylationGGVKEDCTASMEPSA
CCCCCCCCCCCCCHH		33.8029116813
517PhosphorylationVKEDCTASMEPSAIE
CCCCCCCCCCCHHHC		12.9125247763
528PhosphorylationSAIELPDYLIKYIAI
HHHCCCHHHHHHHHH		14.37-
532PhosphorylationLPDYLIKYIAIVSYE
CCHHHHHHHHHEEHH		6.6525278378
537PhosphorylationIKYIAIVSYEQRQNY
HHHHHHEEHHHHHHC		19.4825278378
538PhosphorylationKYIAIVSYEQRQNYK
HHHHHEEHHHHHHCC		12.7525278378
544PhosphorylationSYEQRQNYKDDFNAE
EHHHHHHCCCCCCCH		13.8825278378
580PhosphorylationDAQRKRLSPGSKEYQ
HHHHHCCCCCCHHHH		31.1117192257
584AcetylationKRLSPGSKEYQNVHE
HCCCCCCHHHHHHHH		67.3726051181
584UbiquitinationKRLSPGSKEYQNVHE
HCCCCCCHHHHHHHH		67.37-
586PhosphorylationLSPGSKEYQNVHEEV
CCCCCHHHHHHHHHH		14.7729978859
597PhosphorylationHEEVLQEYQKIKQSS
HHHHHHHHHHHHHCC		11.3529759185
599UbiquitinationEVLQEYQKIKQSSPN
HHHHHHHHHHHCCCC		51.47-
601UbiquitinationLQEYQKIKQSSPNYH
HHHHHHHHHCCCCHH		51.68-
603PhosphorylationEYQKIKQSSPNYHEE
HHHHHHHCCCCHHHH		42.6429214152
604PhosphorylationYQKIKQSSPNYHEEK
HHHHHHCCCCHHHHH		18.0517192257
607PhosphorylationIKQSSPNYHEEKYRC
HHHCCCCHHHHHHHH		17.6229759185
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
-KUbiquitinationE3 ubiquitin ligaseSIAH1Q8IUQ4
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ELL2_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 ELL2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EAF1_HUMANEAF1physical
21729782
EAF2_HUMANEAF2physical
21729782
AFF4_HUMANAFF4physical
21729782
AFF1_HUMANAFF1physical
21729782
ENL_HUMANMLLT1physical
21729782
AF9_HUMANMLLT3physical
21729782
CDK9_HUMANCDK9physical
21729782
CCNT1_HUMANCCNT1physical
21729782
CCNT2_HUMANCCNT2physical
21729782
ICE1_HUMANICE1physical
21729782
ENL_HUMANMLLT1physical
26496610
AFF1_HUMANAFF1physical
26496610
AF9_HUMANMLLT3physical
26496610
B3A2_HUMANSLC4A2physical
26496610
TIA1_HUMANTIA1physical
26496610
AFG32_HUMANAFG3L2physical
26496610
EFR3A_HUMANEFR3Aphysical
26496610
NBEL2_HUMANNBEAL2physical
26496610
AFF4_HUMANAFF4physical
26496610
ESYT2_HUMANESYT2physical
26496610
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 ELL2_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503; SER-580 ANDSER-604, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory