dbPTM

EID1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EID1_HUMAN
UniProt AC	Q9Y6B2
Protein Name	EP300-interacting inhibitor of differentiation 1
Gene Name	EID1 {ECO:0000312\|EMBL:AAI14947.1}
Organism	Homo sapiens (Human).
Sequence Length	187
Subcellular Localization	Nucleus . Cytoplasm . May shuttle between nucleus and cytoplasm.
Protein Description	Interacts with RB1 and EP300 and acts as a repressor of MYOD1 transactivation. Inhibits EP300 and CBP histone acetyltransferase activity. May be involved in coupling cell cycle exit to the transcriptional activation of genes required for cellular differentiation. May act as a candidate coinhibitory factor for NR0B2 that can be directly linked to transcription inhibitory mechanisms..
Protein Sequence	MSEMAELSELYEESSDLQMDVMPGEGDLPQMEVGSGSRELSLRPSRSGAQQLEEEGPMEEEEAQPMAAPEGKRSLANGPNAGEQPGQVAGADFESEDEGEEFDDWEDDYDYPEEEQLSGAGYRVSAALEEADKMFLRTREPALDGGFQMHYEKTPFDQLAFIEELFSLMVVNRLTEELGCDEIIDRE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSEMAELSE ------CCHHHHHHH	35.76	18187866
8	Phosphorylation	MSEMAELSELYEESS CCHHHHHHHHHHHCC	19.63	18187866
41	Phosphorylation	GSGSRELSLRPSRSG CCCCCEEECCCCCHH	19.99	24719451
45	Phosphorylation	RELSLRPSRSGAQQL CEEECCCCCHHHHHH	32.42	24719451
72	Ubiquitination	PMAAPEGKRSLANGP CCCCCCCHHHHCCCC	36.83	21906983
72 (in isoform 1)	Ubiquitination	-	36.83	21890473
110 (in isoform 2)	Ubiquitination	-	60.55	21890473
133	Ubiquitination	AALEEADKMFLRTRE HHHHHHHHHHHHCCC	38.30	23000965
133 (in isoform 1)	Ubiquitination	-	38.30	21890473
151	Phosphorylation	DGGFQMHYEKTPFDQ CCCCEEECCCCCHHH	17.49	27642862

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
-	K	Ubiquitination	E3 ubiquitin ligase	FBXO21	O94952	PMID:26085330
-	K	Ubiquitination	E3 ubiquitin ligase	MDM2	Q00987	PMID:11073989

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EID1_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 EID1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RB_HUMAN	RB1	physical	11073989
MDM2_HUMAN	MDM2	physical	11073989
RB_HUMAN	RB1	physical	11073990
EP300_HUMAN	EP300	physical	11073990
RB_HUMAN	RB1	physical	11964378
EP300_HUMAN	EP300	physical	11964378
KAT2A_HUMAN	KAT2A	physical	11964378
NCOA2_HUMAN	NCOA2	physical	11964378
H2A1B_HUMAN	HIST1H2AE	physical	11964378
H2B1B_HUMAN	HIST1H2BB	physical	11964378
H31_HUMAN	HIST1H3A	physical	11964378
NR0B2_HUMAN	NR0B2	physical	20516075
NR0B2_HUMAN	NR0B2	physical	14963109
RB_HUMAN	RB1	physical	15806172
PCID2_HUMAN	PCID2	physical	24167073
EP300_HUMAN	EP300	physical	24167073
CBP_HUMAN	CREBBP	physical	24167073
JAK1_HUMAN	JAK1	physical	26631746
IQGA1_HUMAN	IQGAP1	physical	26631746
CAMP3_HUMAN	CAMSAP3	physical	26631746
DNJA1_HUMAN	DNAJA1	physical	26631746
TESK2_HUMAN	TESK2	physical	26631746
PFKAP_HUMAN	PFKP	physical	26631746
SCAFB_HUMAN	SCAF11	physical	26631746
SLIRP_HUMAN	SLIRP	physical	26631746
DMBT1_HUMAN	DMBT1	physical	26631746
FBX21_HUMAN	FBXO21	physical	26631746
RL21_HUMAN	RPL21	physical	26631746
DISP1_HUMAN	DISP1	physical	26631746
RASA3_HUMAN	RASA3	physical	26631746
RCN2_HUMAN	RCN2	physical	26631746
RL37A_HUMAN	RPL37A	physical	26631746
PCNT_HUMAN	PCNT	physical	26631746
UBB_HUMAN	UBB	physical	28514442
FBX21_HUMAN	FBXO21	physical	28514442
ASPM_HUMAN	ASPM	physical	28514442
BDH2_HUMAN	BDH2	physical	28514442
MYO5A_HUMAN	MYO5A	physical	28514442
MYO9B_HUMAN	MYO9B	physical	28514442
MYO1D_HUMAN	MYO1D	physical	28514442
KLC2_HUMAN	KLC2	physical	28514442
CUL1_HUMAN	CUL1	physical	28514442
PAPD1_HUMAN	MTPAP	physical	28514442

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 EID1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-8, AND MASSSPECTROMETRY.	18187866 [Abstract]