dbPTM

CEBPD_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CEBPD_HUMAN
UniProt AC	P49716
Protein Name	CCAAT/enhancer-binding protein delta
Gene Name	CEBPD
Organism	Homo sapiens (Human).
Sequence Length	269
Subcellular Localization	Nucleus .
Protein Description	Transcription activator that recognizes two different DNA motifs: the CCAAT homology common to many promoters and the enhanced core homology common to many enhancers. [PubMed: 16397300 Important transcription factor regulating the expression of genes involved in immune and inflammatory responses]
Protein Sequence	MSAALFSLDGPARGAPWPAEPAPFYEPGRAGKPGRGAEPGALGEPGAAAPAMYDDESAIDFSAYIDSMAAVPTLELCHDELFADLFNSNHKAGGAGPLELLPGGPARPLGPGPAAPRLLKREPDWGDGDAPGSLLPAQVAACAQTVVSLAAAGQPTPPTSPEPPRSSPRQTPAPGPAREKSAGKRGPDRGSPEYRQRRERNNIAVRKSRDKAKRRNQEMQQKLVELSAENEKLHQRVEQLTRDLAGLRQFFKQLPSPPFLPAAGTADCR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSAALFSLD ------CCCCCCCCC	23.42	22814378
25	Phosphorylation	PAEPAPFYEPGRAGK CCCCCCCCCCCCCCC	21.83	21945579
57	Phosphorylation	PAMYDDESAIDFSAY CCCCCCCCCCCHHHH	37.20	-
120	Sumoylation	PAAPRLLKREPDWGD CCCCHHHHCCCCCCC	60.34	-
120	Acetylation	PAAPRLLKREPDWGD CCCCHHHHCCCCCCC	60.34	6993007
120	Sumoylation	PAAPRLLKREPDWGD CCCCHHHHCCCCCCC	60.34	16397300
133	Phosphorylation	GDGDAPGSLLPAQVA CCCCCCCCCHHHHHH	26.18	22210691
156	Phosphorylation	LAAAGQPTPPTSPEP HHHCCCCCCCCCCCC	33.73	22210691
159	Phosphorylation	AGQPTPPTSPEPPRS CCCCCCCCCCCCCCC	59.11	22210691
166	Phosphorylation	TSPEPPRSSPRQTPA CCCCCCCCCCCCCCC	50.93	17081983
167	Phosphorylation	SPEPPRSSPRQTPAP CCCCCCCCCCCCCCC	25.94	17081983
171	Phosphorylation	PRSSPRQTPAPGPAR CCCCCCCCCCCCCCC	23.77	-
191	Phosphorylation	KRGPDRGSPEYRQRR CCCCCCCCHHHHHHH	18.56	23927012
194	Phosphorylation	PDRGSPEYRQRRERN CCCCCHHHHHHHHHH	18.54	24732914
232	Ubiquitination	ELSAENEKLHQRVEQ HHHHHHHHHHHHHHH	63.95	33845483
256	Phosphorylation	QFFKQLPSPPFLPAA HHHHHCCCCCCCCCC	54.52	21815630

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
57	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
167	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
171	T	Phosphorylation	Kinase	GSK3B	P49841	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	FBXW7	Q969H0	PMID:24658274

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMAD3_HUMAN	SMAD3	physical	12524424
SMAD4_HUMAN	SMAD4	physical	12524424
HDAC1_HUMAN	HDAC1	physical	18619497
HDAC3_HUMAN	HDAC3	physical	18619497
CBP_HUMAN	CREBBP	physical	12857754
PIAS4_HUMAN	PIAS4	physical	18477566
FACD2_HUMAN	FANCD2	physical	20805509
IPO4_HUMAN	IPO4	physical	20805509
SPAG5_HUMAN	SPAG5	physical	20805509
TRI26_HUMAN	TRIM26	physical	20805509
UBR5_HUMAN	UBR5	physical	20805509
XPO1_HUMAN	XPO1	physical	20805509
HDAC1_HUMAN	HDAC1	physical	17910034
HDAC3_HUMAN	HDAC3	physical	17910034
HDAC4_HUMAN	HDAC4	physical	17910034
SIAH2_HUMAN	SIAH2	physical	22037769

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 CEBPD_HUMAN

Related Literatures of Post-Translational Modification

Sumoylation
Reference	PubMed
"Functional role of NF-IL6beta and its sumoylation and acetylationmodifications in promoter activation of cyclooxygenase 2 gene."; Wang J.-M., Ko C.-Y., Chen L.-C., Wang W.-L., Chang W.-C.; Nucleic Acids Res. 34:217-231(2006). Cited for: SUMOYLATION AT LYS-120, AND MUTAGENESIS OF LYS-120.	16397300 [Abstract]