CITE1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CITE1_HUMAN
• UniProt AC: Q99966
• Protein Name: Cbp/p300-interacting transactivator 1
• Gene Name: CITED1
• Organism: Homo sapiens (Human).
• Sequence Length: 193
• Subcellular Localization: Nucleus . Cytoplasm . Shuttles between the nucleus and the cytoplasm by a nuclear export signal and (NES) in a CRM1-dependent manner.
• Protein Description: Transcriptional coactivator of the p300/CBP-mediated transcription complex. Enhances SMAD-mediated transcription by strengthening the functional link between the DNA-binding SMAD transcription factors and the p300/CBP transcription coactivator complex. Stimulates estrogen-dependent transactivation activity mediated by estrogen receptors signaling; stabilizes the interaction of estrogen receptor ESR1 and histone acetyltransferase EP300. Positively regulates TGF-beta signaling through its association with the SMAD/p300/CBP-mediated transcriptional coactivator complex. Induces transcription from estrogen-responsive promoters and protection against cell death. Potentiates EGR2-mediated transcriptional activation activity from the ERBB2 promoter. Acts as an inhibitor of osteoblastic mineralization through a cAMP-dependent parathyroid hormone receptor signaling. May play a role in pigmentation of melanocytes. Associates with chromatin to the estrogen-responsive TGF-alpha promoter region in a estrogen-dependent manner..
• Protein Sequence: MPTTSRPALDVKGGTSPAKEDANQEMSSVAYSNLAVKDRKAVAILHYPGVASNGTKASGAPTSSSGSPIGSPTTTPPTKPPSFNLHPAPHLLASMHLQKLNSQYQGMAAATPGQPGEAGPLQNWDFGAQAGGAESLSPSAGAQSPAIIDSDPVDEEVLMSLVVELGLDRANELPELWLGQNEFDFTADFPSSC

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
3	Phosphorylation	-----MPTTSRPALD -----CCCCCCCCCC	35.78	23186163
4	Phosphorylation	----MPTTSRPALDV ----CCCCCCCCCCC	19.50	23186163
5	Phosphorylation	---MPTTSRPALDVK ---CCCCCCCCCCCC	38.45	23186163
12	Sumoylation	SRPALDVKGGTSPAK CCCCCCCCCCCCCCH	51.82	-
15	Phosphorylation	ALDVKGGTSPAKEDA CCCCCCCCCCCHHHC	39.96	30278072
16	Phosphorylation	LDVKGGTSPAKEDAN CCCCCCCCCCHHHCH	26.57	23186163
27	Phosphorylation	EDANQEMSSVAYSNL HHCHHHHHHHHHHCC	22.40	27251275
28	Phosphorylation	DANQEMSSVAYSNLA HCHHHHHHHHHHCCC	14.95	23186163
32	Phosphorylation	EMSSVAYSNLAVKDR HHHHHHHHCCCCCCC	18.68	30631047
37	Acetylation	AYSNLAVKDRKAVAI HHHCCCCCCCCEEEE	46.32	23954790
42	Phosphorylation	AVKDRKAVAILHYPG CCCCCCEEEEEECCC	3.69	27251275
52	Phosphorylation	LHYPGVASNGTKASG EECCCCCCCCCCCCC	33.13	18669648
55	Phosphorylation	PGVASNGTKASGAPT CCCCCCCCCCCCCCC	27.90	18669648
64	Phosphorylation	ASGAPTSSSGSPIGS CCCCCCCCCCCCCCC	40.99	18669648
67	Phosphorylation	APTSSSGSPIGSPTT CCCCCCCCCCCCCCC	18.45	29507054

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of CITE1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CITE1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of CITE1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMAD4_HUMAN	SMAD4	physical	9707553
AP2B_HUMAN	TFAP2B	physical	11744733
HSP7C_HUMAN	HSPA8	physical	10722728
HSP7C_HUMAN	HSPA8	genetic	10722728
ESR1_HUMAN	ESR1	physical	11581164
CTNB1_HUMAN	CTNNB1	physical	15843474
EP300_HUMAN	EP300	physical	16864582

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.