EAF1_HUMAN - dbPTM
EAF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EAF1_HUMAN
UniProt AC Q96JC9
Protein Name ELL-associated factor 1
Gene Name EAF1
Organism Homo sapiens (Human).
Sequence Length 268
Subcellular Localization Nucleus speckle . Nucleus, Cajal body .
Protein Description Acts as a transcriptional transactivator of ELL and ELL2 elongation activities..
Protein Sequence MNGTANPLLDREEHCLRLGESFEKRPRASFHTIRYDFKPASIDTSCEGELQVGKGDEVTITLPHIPGSTPPMTVFKGNKRPYQKDCVLIINHDTGEYVLEKLSSSIQVKKTRAEGSSKIQARMEQQPTRPPQTSQPPPPPPPMPFRAPTKPPVGPKTSPLKDNPSPEPQLDDIKRELRAEVDIIEQMSSSSGSSSSDSESSSGSDDDSSSSGGEDNGPASPPQPSHQQPYNSRPAVANGTSRPQGSNQLMNTLRNDLQLSESGSDSDD
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
3 (in isoform 2)Phosphorylation-25.5530622161
10 (in isoform 2)Phosphorylation-64.7230622161
15 (in isoform 2)Phosphorylation-2.4030622161
21PhosphorylationHCLRLGESFEKRPRA
HHHHHCHHHHHCCCC
36.5923401153
24UbiquitinationRLGESFEKRPRASFH
HHCHHHHHCCCCEEE
66.7429967540
29PhosphorylationFEKRPRASFHTIRYD
HHHCCCCEEEEEEEC
20.8820068231
32PhosphorylationRPRASFHTIRYDFKP
CCCCEEEEEEECCCC
12.7323186163
49AcetylationIDTSCEGELQVGKGD
CCCCCCCEEEECCCC
17.46-
68PhosphorylationTLPHIPGSTPPMTVF
ECCCCCCCCCCEEEE
32.1725627689
69PhosphorylationLPHIPGSTPPMTVFK
CCCCCCCCCCEEEEC
37.0125627689
73PhosphorylationPGSTPPMTVFKGNKR
CCCCCCEEEECCCCC
28.6728122231
105PhosphorylationVLEKLSSSIQVKKTR
HHHHHHCCCEEEECC
17.4228555341
118AcetylationTRAEGSSKIQARMEQ
CCCCCCHHHHHHHHC
40.3025953088
149PhosphorylationPMPFRAPTKPPVGPK
CCCCCCCCCCCCCCC
56.0223186163
150AcetylationMPFRAPTKPPVGPKT
CCCCCCCCCCCCCCC
46.3923749302
157PhosphorylationKPPVGPKTSPLKDNP
CCCCCCCCCCCCCCC
38.4223927012
158PhosphorylationPPVGPKTSPLKDNPS
CCCCCCCCCCCCCCC
34.0723927012
165PhosphorylationSPLKDNPSPEPQLDD
CCCCCCCCCCCCHHH
48.4219664994
260PhosphorylationLRNDLQLSESGSDSD
HHHHHHHHHCCCCCC
19.4323663014
262PhosphorylationNDLQLSESGSDSDD-
HHHHHHHCCCCCCC-
39.9723911959
264PhosphorylationLQLSESGSDSDD---
HHHHHCCCCCCC---
43.1323911959
266PhosphorylationLSESGSDSDD-----
HHHCCCCCCC-----
45.4325159151

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 EAF1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EAF1_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 EAF1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ELL_HUMANELLphysical
11418481
ELL2_HUMANELL2physical
11418481
A4_HUMANAPPphysical
21832049
ELL_HUMANELLphysical
21729782
ELL2_HUMANELL2physical
21729782
ELL3_HUMANELL3physical
21729782
AFF4_HUMANAFF4physical
21729782
AFF1_HUMANAFF1physical
21729782
ICE2_HUMANICE2physical
21729782
ICE1_HUMANICE1physical
21729782
MIPO1_HUMANMIPOL1physical
25416956
BEND7_HUMANBEND7physical
25416956
EAF2_HUMANEAF2physical
26186194
ASPM_HUMANASPMphysical
26186194
TOP1_HUMANTOP1physical
26186194
FIP1_HUMANFIP1L1physical
26186194
LC7L2_HUMANLUC7L2physical
26186194
LUC7L_HUMANLUC7Lphysical
26186194
TAF1A_HUMANTAF1Aphysical
26186194
ICE2_HUMANICE2physical
26186194
RSBNL_HUMANRSBN1Lphysical
26186194
RSBN1_HUMANRSBN1physical
26186194
ICE1_HUMANICE1physical
26186194
RL26L_HUMANRPL26L1physical
26186194
ELL2_HUMANELL2physical
26186194
CABIN_HUMANCABIN1physical
26186194
PINX1_HUMANPINX1physical
26186194
LC7L3_HUMANLUC7L3physical
26186194
AF9_HUMANMLLT3physical
26186194
ENL_HUMANMLLT1physical
26186194
ELL_HUMANELLphysical
26186194
TAF1B_HUMANTAF1Bphysical
26186194
PI42C_HUMANPIP4K2Cphysical
26186194
PI42B_HUMANPIP4K2Bphysical
26186194
PI42A_HUMANPIP4K2Aphysical
26186194
SNUT1_HUMANSART1physical
26186194
AFF4_HUMANAFF4physical
26186194
T2FA_HUMANGTF2F1physical
26186194
E41L5_HUMANEPB41L5physical
26186194
E41LB_HUMANEPB41L4Bphysical
26186194
CAPON_HUMANNOS1APphysical
26186194
KLDC3_HUMANKLHDC3physical
26186194
CPSF4_HUMANCPSF4physical
26186194
ELL3_HUMANELL3physical
26186194
TAF1D_HUMANTAF1Dphysical
26186194
AFF1_HUMANAFF1physical
26186194
MMTA2_HUMANC1orf35physical
26186194
RBMX2_HUMANRBMX2physical
26186194
TAF1C_HUMANTAF1Cphysical
26186194
PLCD3_HUMANPLCD3physical
26186194
CI114_HUMANC9orf114physical
26186194
SP17_HUMANSPA17physical
26186194
SFSWA_HUMANSFSWAPphysical
26186194
IKBL1_HUMANNFKBIL1physical
26186194
HOME3_HUMANHOMER3physical
21516116
ELL3_HUMANELL3physical
28514442
ELL_HUMANELLphysical
28514442
ELL2_HUMANELL2physical
28514442
ICE1_HUMANICE1physical
28514442
ICE2_HUMANICE2physical
28514442
EAF2_HUMANEAF2physical
28514442
AFF4_HUMANAFF4physical
28514442
AFF1_HUMANAFF1physical
28514442
ENL_HUMANMLLT1physical
28514442
CABIN_HUMANCABIN1physical
28514442
IKBL1_HUMANNFKBIL1physical
28514442
E41L5_HUMANEPB41L5physical
28514442
PI42C_HUMANPIP4K2Cphysical
28514442
PI42A_HUMANPIP4K2Aphysical
28514442
TAC2N_HUMANTC2Nphysical
28514442
PI42B_HUMANPIP4K2Bphysical
28514442
PLCD3_HUMANPLCD3physical
28514442
RSBNL_HUMANRSBN1Lphysical
28514442
CPSF4_HUMANCPSF4physical
28514442
RSBN1_HUMANRSBN1physical
28514442
TOP1_HUMANTOP1physical
28514442
TAF1A_HUMANTAF1Aphysical
28514442
CAPON_HUMANNOS1APphysical
28514442
AF9_HUMANMLLT3physical
28514442
TAF1C_HUMANTAF1Cphysical
28514442
TAF1B_HUMANTAF1Bphysical
28514442
SFSWA_HUMANSFSWAPphysical
28514442
TAF1D_HUMANTAF1Dphysical
28514442
USPL1_HUMANUSPL1physical
28514442
FGRL1_HUMANFGFRL1physical
28514442
T2FA_HUMANGTF2F1physical
28514442
E41LB_HUMANEPB41L4Bphysical
28514442
PINX1_HUMANPINX1physical
28514442
CI114_HUMANC9orf114physical
28514442
LUC7L_HUMANLUC7Lphysical
28514442
LC7L2_HUMANLUC7L2physical
28514442
RL26L_HUMANRPL26L1physical
28514442
KLDC3_HUMANKLHDC3physical
28514442
RBMX2_HUMANRBMX2physical
28514442
NAF1_HUMANNAF1physical
27173435
DPOD1_HUMANPOLD1physical
27173435
CC154_HUMANCCDC154physical
27173435

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 EAF1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-150, AND MASS SPECTROMETRY.
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 THR-157 AND SER-165, ANDMASS SPECTROMETRY.
"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-158 AND SER-165, ANDMASS SPECTROMETRY.
"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-165, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND MASSSPECTROMETRY.

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