dbPTM

EI24_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EI24_HUMAN
UniProt AC	O14681
Protein Name	Etoposide-induced protein 2.4 homolog
Gene Name	EI24
Organism	Homo sapiens (Human).
Sequence Length	340
Subcellular Localization	Nucleus membrane Multi-pass membrane protein . Cytoplasm . Endoplasmic reticulum membrane Multi-pass membrane protein.
Protein Description	Acts as a negative growth regulator via p53-mediated apoptosis pathway. Regulates formation of degradative autolysosomes during autophagy (By similarity)..
Protein Sequence	MADSVKTFLQDLARGIKDSIWGICTISKLDARIQQKREEQRRRRASSVLAQRRAQSIERKQESEPRIVSRIFQCCAWNGGVFWFSLLLFYRVFIPVLQSVTARIIGDPSLHGDVWSWLEFFLTSIFSALWVLPLFVLSKVVNAIWFQDIADLAFEVSGRKPHPFPSVSKIIADMLFNLLLQALFLIQGMFVSLFPIHLVGQLVSLLHMSLLYSLYCFEYRWFNKGIEMHQRLSNIERNWPYYFGFGLPLAFLTAMQSSYIISGCLFSILFPLFIISANEAKTPGKAYLFQLRLFSLVVFLSNRLFHKTVYLQSALSSSTSAEKFPSPHPSPAKLKATAGH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADSVKTFL ------CHHHHHHHH	20.13	22814378
6	Ubiquitination	--MADSVKTFLQDLA --CHHHHHHHHHHHH	37.20	-
17	Ubiquitination	QDLARGIKDSIWGIC HHHHHCHHHHHHHHH	48.52	-
46	Phosphorylation	EQRRRRASSVLAQRR HHHHHHHHHHHHHHH	21.11	23401153
47	Phosphorylation	QRRRRASSVLAQRRA HHHHHHHHHHHHHHH	21.84	30266825
56	Phosphorylation	LAQRRAQSIERKQES HHHHHHHHHHHHHHC	25.98	28355574
166	Phosphorylation	RKPHPFPSVSKIIAD CCCCCCCCHHHHHHH	39.13	26091039
224	Malonylation	FEYRWFNKGIEMHQR HHHHHHHHCHHHHHH	52.36	26320211
308	Phosphorylation	SNRLFHKTVYLQSAL HCCCCCHHHHHHHHH	13.05	28450419
310	Phosphorylation	RLFHKTVYLQSALSS CCCCHHHHHHHHHHC	12.31	28450419
313	Phosphorylation	HKTVYLQSALSSSTS CHHHHHHHHHHCCCC	28.69	23927012
316	Phosphorylation	VYLQSALSSSTSAEK HHHHHHHHCCCCHHH	23.20	30278072
317	Phosphorylation	YLQSALSSSTSAEKF HHHHHHHCCCCHHHC	38.19	30278072
318	Phosphorylation	LQSALSSSTSAEKFP HHHHHHCCCCHHHCC	24.01	30278072
319	Phosphorylation	QSALSSSTSAEKFPS HHHHHCCCCHHHCCC	33.63	25159151
320	Phosphorylation	SALSSSTSAEKFPSP HHHHCCCCHHHCCCC	36.06	30278072
323	Ubiquitination	SSSTSAEKFPSPHPS HCCCCHHHCCCCCCC	63.39	21890473
326	Phosphorylation	TSAEKFPSPHPSPAK CCHHHCCCCCCCHHH	38.69	19664994
330	Phosphorylation	KFPSPHPSPAKLKAT HCCCCCCCHHHCCCC	34.16	19664994
342	Ubiquitination	KATAGH--------- CCCCCC---------		21890473
342	Ubiquitination	KATAGH--------- CCCCCC---------		21890473

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 EI24_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EI24_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 EI24_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
STOM_HUMAN	STOM	physical	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 EI24_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-326 AND SER-330, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"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-56, AND MASSSPECTROMETRY.	19369195 [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-326 AND SER-330, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"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-56; SER-326 AND SER-330,AND MASS SPECTROMETRY.	18691976 [Abstract]
"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-56; SER-326 AND SER-330,AND MASS SPECTROMETRY.	17081983 [Abstract]