dbPTM

EAF2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EAF2_HUMAN
UniProt AC	Q96CJ1
Protein Name	ELL-associated factor 2
Gene Name	EAF2
Organism	Homo sapiens (Human).
Sequence Length	260
Subcellular Localization	Nucleus speckle .
Protein Description	Acts as a transcriptional transactivator of TCEA1 elongation activity (By similarity). Acts as a transcriptional transactivator of ELL and ELL2 elongation activities. Potent inducer of apoptosis in prostatic and non-prostatic cell lines. Inhibits prostate tumor growth in vivo..
Protein Sequence	MNSAAGFSHLDRRERVLKLGESFEKQPRCAFHTVRYDFKPASIDTSSEGYLEVGEGEQVTITLPNIEGSTPPVTVFKGSKKPYLKECILIINHDTGECRLEKLSSNITVKKTRVEGSSKIQYRKEQQQQQMWNSARTPNLVKHSPSEDKMSPASPIDDIERELKAEASLMDQMSSCDSSSDSKSSSSSSSEDSSSDSEDEDCKSSTSDTGNCVSGHPTMTQYRIPDIDASHNRFRDNSGLLMNTLRNDLQLSESGSDSDD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
14 (in isoform 2)	Phosphorylation	-	48.30	29116813
18	Ubiquitination	DRRERVLKLGESFEK HHHHHHHHHHHHHHC	52.14	-
22	Phosphorylation	RVLKLGESFEKQPRC HHHHHHHHHHCCCCE	36.59	23401153
25	Ubiquitination	KLGESFEKQPRCAFH HHHHHHHCCCCEEEE	64.69	-
39	Ubiquitination	HTVRYDFKPASIDTS EEEECCCCCCCCCCC	36.45	-
81	Ubiquitination	TVFKGSKKPYLKECI EEECCCCCCCEEEEE	40.36	-
85	Ubiquitination	GSKKPYLKECILIIN CCCCCCEEEEEEEEE	44.70	-
104	Phosphorylation	ECRLEKLSSNITVKK CEEEEECCCCCEEEE	32.19	-
105	Phosphorylation	CRLEKLSSNITVKKT EEEEECCCCCEEEEE	42.56	-
108	Phosphorylation	EKLSSNITVKKTRVE EECCCCCEEEEEEEE	30.44	-
111	Ubiquitination	SSNITVKKTRVEGSS CCCCEEEEEEEECCH	36.91	-
119	Ubiquitination	TRVEGSSKIQYRKEQ EEEECCHHHEEHHHH	35.21	-
134	Phosphorylation	QQQQMWNSARTPNLV HHHHHHHHCCCCCCC	12.01	25627689
137	Phosphorylation	QMWNSARTPNLVKHS HHHHHCCCCCCCCCC	19.08	28450419
144	Phosphorylation	TPNLVKHSPSEDKMS CCCCCCCCCCCCCCC	25.14	30108239
146	Phosphorylation	NLVKHSPSEDKMSPA CCCCCCCCCCCCCCC	62.53	23401153
151	Phosphorylation	SPSEDKMSPASPIDD CCCCCCCCCCCCHHH	24.05	25159151
154	Phosphorylation	EDKMSPASPIDDIER CCCCCCCCCHHHHHH	26.27	23401153
197	Phosphorylation	SEDSSSDSEDEDCKS CCCCCCCCCCCCHHC	49.23	-
204	Phosphorylation	SEDEDCKSSTSDTGN CCCCCHHCCCCCCCC	45.22	28450419
205	Phosphorylation	EDEDCKSSTSDTGNC CCCCHHCCCCCCCCC	19.88	28450419
206	Phosphorylation	DEDCKSSTSDTGNCV CCCHHCCCCCCCCCC	37.40	28450419
207	Phosphorylation	EDCKSSTSDTGNCVS CCHHCCCCCCCCCCC	34.81	28450419
209	Phosphorylation	CKSSTSDTGNCVSGH HHCCCCCCCCCCCCC	30.02	28450419
214	Phosphorylation	SDTGNCVSGHPTMTQ CCCCCCCCCCCCCEE	33.32	28450419
252	Phosphorylation	LRNDLQLSESGSDSD HHHHHHHHHCCCCCC	19.43	23663014
254	Phosphorylation	NDLQLSESGSDSDD- HHHHHHHCCCCCCC-	39.97	23911959
256	Phosphorylation	LQLSESGSDSDD--- HHHHHCCCCCCC---	43.13	23911959
258	Phosphorylation	LSESGSDSDD----- HHHCCCCCCC-----	45.43	25159151

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 EAF2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EAF2_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 EAF2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ELL_HUMAN	ELL	physical	12446457
BEND7_HUMAN	BEND7	physical	25416956
RBBP4_HUMAN	RBBP4	physical	24727455
RBBP7_HUMAN	RBBP7	physical	24727455
SIAH2_HUMAN	SIAH2	physical	27058417
ELL_HUMAN	ELL	physical	27058417
ELL2_HUMAN	ELL2	physical	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 EAF2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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-146; SER-151 ANDSER-154, AND MASS SPECTROMETRY.	18669648 [Abstract]