DEAF1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DEAF1_HUMAN
• UniProt AC: O75398
• Protein Name: Deformed epidermal autoregulatory factor 1 homolog
• Gene Name: DEAF1
• Organism: Homo sapiens (Human).
• Sequence Length: 565
• Subcellular Localization: Isoform 1: Nucleus. Cytoplasm. Cytoplasmic in non-mucinous colorectal carcinoma. When expressed alone, localized almost exclusively in the nucleus but, when expressed with isoform 4, nuclear expression decreases to 32% and cytoplasmic expression incr
• Protein Description: Transcription factor that binds to sequence with multiple copies of 5'-TTC[CG]G-3' present in its own promoter and that of the HNRPA2B1 gene. Down-regulates transcription of these genes. Binds to the retinoic acid response element (RARE) 5'-AGGGTTCACCGAAAGTTCA-3'. Activates the proenkephalin gene independently of promoter binding, probably through protein-protein interaction. When secreted, behaves as an inhibitor of cell proliferation, by arresting cells in the G0 or G1 phase. Required for neural tube closure and skeletal patterning. Regulates epithelial cell proliferation and side-branching in the mammary gland. Controls the expression of peripheral tissue antigens in pancreatic lymph nodes. Isoform 1 displays greater transcriptional activity than isoform 4. Isoform 4 may inhibit transcriptional activity of isoform 1 by interacting with isoform 1 and retaining it in the cytoplasm. Transcriptional activator of EIF4G3..
• Protein Sequence: MEDSDSAAKQLGLAEAAAVAAAAAVAAAAAAAAGGEAEEPVLSRDEDSEEDADSEAERETPRVTAVAVMAAEPGHMDMGAEALPGPDEAAAAAAFAEVTTVTVANVGAAADNVFTTSVANAASISGHVLSGRTALQIGDSLNTEKATLIVVHTDGSIVETTGLKGPAAPLTPGPQSPPTPLAPGQEKGGTKYNWDPSVYDSELPVRCRNISGTLYKNRLGSGGRGRCIKQGENWYSPTEFEAMAGRASSKDWKRSIRYAGRPLQCLIQDGILNPHAASCTCAACCDDMTLSGPVRLFVPYKRRKKENELPTTPVKKDSPKNITLLPATAATTFTVTPSGQITTSGALTFDRASTVEATAVISESPAQGDVFAGATVQEASVQPPCRASHPEPHYPGYQDSCQIAPFPEAALPTSHPKIVLTSLPALAVPPPTPTKAAPPALVNGLELSEPRSWLYLEEMVNSLLNTAQQLKTLFEQAKHASTYREAATNQAKIHADAERKEQSCVNCGREAMSECTGCHKVNYCSTFCQRKDWKDHQHICGQSAAVTVQADEVHVAESVMEKVTV

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
43	Phosphorylation	EAEEPVLSRDEDSEE CCCCCCCCCCCCCHH	37.61	27732954
48	Phosphorylation	VLSRDEDSEEDADSE CCCCCCCCHHHCCCH	40.62	25850435
54	Phosphorylation	DSEEDADSEAERETP CCHHHCCCHHHHHCC	40.19	25850435
60	Phosphorylation	DSEAERETPRVTAVA CCHHHHHCCCCEEEE	23.71	23909892
130	Phosphorylation	SISGHVLSGRTALQI HHCCCCCCCCCEEEE	25.74	24719451
156	Phosphorylation	IVVHTDGSIVETTGL EEEECCCCEEECCCC	26.69	26074081
160	Phosphorylation	TDGSIVETTGLKGPA CCCCEEECCCCCCCC	18.44	26074081
161	Phosphorylation	DGSIVETTGLKGPAA CCCEEECCCCCCCCC	27.32	26074081
171	Phosphorylation	KGPAAPLTPGPQSPP CCCCCCCCCCCCCCC	25.74	30266825
176	Phosphorylation	PLTPGPQSPPTPLAP CCCCCCCCCCCCCCC	35.66	23401153
179	Phosphorylation	PGPQSPPTPLAPGQE CCCCCCCCCCCCCCC	34.03	30266825
190	Phosphorylation	PGQEKGGTKYNWDPS CCCCCCCCCCCCCHH	38.74	26074081
191	Ubiquitination	GQEKGGTKYNWDPSV CCCCCCCCCCCCHHH	39.60	29967540
192	Phosphorylation	QEKGGTKYNWDPSVY CCCCCCCCCCCHHHC	22.71	26074081
211	Phosphorylation	PVRCRNISGTLYKNR CCEEEECCCCEECCC	29.31	25159151
311	Phosphorylation	KKENELPTTPVKKDS CCCCCCCCCCCCCCC	57.25	30266825
312	Phosphorylation	KENELPTTPVKKDSP CCCCCCCCCCCCCCC	24.93	30266825
318	Phosphorylation	TTPVKKDSPKNITLL CCCCCCCCCCCEEEE	46.80	26055452
343	Phosphorylation	TPSGQITTSGALTFD CCCCCEEECCCEEEC	27.13	32142685
389	Ubiquitination	QPPCRASHPEPHYPG CCCCCCCCCCCCCCC	29.74	29967540
421	Phosphorylation	SHPKIVLTSLPALAV CCCCEEEECCCCCCC	19.81	29396449
422	Phosphorylation	HPKIVLTSLPALAVP CCCEEEECCCCCCCC	28.35	29396449
432	Phosphorylation	ALAVPPPTPTKAAPP CCCCCCCCCCCCCCC	49.73	29255136
434	Phosphorylation	AVPPPTPTKAAPPAL CCCCCCCCCCCCCHH	35.47	29255136
448	Phosphorylation	LVNGLELSEPRSWLY HHCCEECCCCCHHHH	35.86	-
478	Ubiquitination	KTLFEQAKHASTYRE HHHHHHHHHHHHHHH	39.12	29967540
483	Phosphorylation	QAKHASTYREAATNQ HHHHHHHHHHHHHHH	12.17	-
488	Phosphorylation	STYREAATNQAKIHA HHHHHHHHHHHHHHC	34.61	-

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

Oops, there are no upstream regulatory protein records of DEAF1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DEAF1_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 DEAF1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CREB1_HUMAN	CREB1	physical	23846693
RIDA_HUMAN	HRSP12	physical	21988832
PELI2_HUMAN	PELI2	physical	21988832
SP1_HUMAN	SP1	physical	23825960
TCP4_HUMAN	SUB1	physical	23825960
SP3_HUMAN	SP3	physical	23825960

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 615828: Mental retardation, autosomal dominant 24 (MRD24)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176 AND THR-179, ANDMASS SPECTROMETRY.
PubMed: 19413330

"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND MASSSPECTROMETRY.
PubMed: 15302935