MDFIC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MDFIC_HUMAN
• UniProt AC: Q9P1T7
• Protein Name: MyoD family inhibitor domain-containing protein
• Gene Name: MDFIC {ECO:0000312|HGNC:HGNC:28870}
• Organism: Homo sapiens (Human).
• Sequence Length: 246
• Subcellular Localization: Isoform 1: Nucleus, nucleolus. Also shows a granular distribution in the cytoplasm.; Isoform 2: Cytoplasm . Weak expression in the nucleus.
• Protein Description: Acts as a transcriptional activator or repressor. Inhibits the transcriptional activation of Zic family proteins ZIC1, ZIC2 and ZIC3. Retains nuclear Zic proteins ZIC1, ZIC2 and ZIC3 in the cytoplasm. Modulates the expression from both cellular and viral promoters. Down-regulates Tat-dependent transcription of the human immunodeficiency virus type 1 (HIV-1) LTR by interacting with HIV-1 Tat and Rev and impairing their nuclear import, probably by rendering the NLS domains inaccessible to importin-beta. Also stimulates activation of human T-cell leukemia virus type I (HTLV-I) LTR. Binds to the axin complex, resulting in an increase in the level of free beta-catenin. Affects axin regulation of the WNT and JNK signaling pathways..
• Protein Sequence: MSGAGEALAPGPVGPQRVAEAGGGQLGSTAQGKCDKDNTEKDITQATNSHFTHGEMQDQSIWGNPSDGELIRTQPQRLPQLQTSAQVPSGEEIGKIKNGHTGLSNGNGIHHGAKHGSADNRKLSAPVSQKMHRKIQSSLSVNSDISKKSKVNAVFSQKTGSSPEDCCVHCILACLFCEFLTLCNIVLGQASCGICTSEACCCCCGDEMGDDCNCPCDMDCGIMDACCESSDCLEICMECCGICFPS

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
8 (in isoform 1)	Phosphorylation	-	5.27	-
15 (in isoform 1)	Phosphorylation	-	21.02	-
18 (in isoform 1)	Phosphorylation	-	4.80	18767875
18	Phosphorylation	GPVGPQRVAEAGGGQ CCCCHHHHHHCCCCC	4.80	18767875
28	Phosphorylation	AGGGQLGSTAQGKCD CCCCCCCCCCCCCCC	29.21	-
29	Phosphorylation	GGGQLGSTAQGKCDK CCCCCCCCCCCCCCC	22.62	-
33	Ubiquitination	LGSTAQGKCDKDNTE CCCCCCCCCCCCCCC	27.46	33845483
89	Phosphorylation	QTSAQVPSGEEIGKI CCCCCCCCHHHHCCC	61.04	28555341
95	Ubiquitination	PSGEEIGKIKNGHTG CCHHHHCCCCCCCCC	57.05	33845483
117	Phosphorylation	HHGAKHGSADNRKLS CCCCCCCCCCCCCCC	31.97	29514088
122	Ubiquitination	HGSADNRKLSAPVSQ CCCCCCCCCCCCHHH	53.71	29967540
124	Phosphorylation	SADNRKLSAPVSQKM CCCCCCCCCCHHHHH	33.30	25159151
128	Phosphorylation	RKLSAPVSQKMHRKI CCCCCCHHHHHHHHH	24.03	29255136
130	Ubiquitination	LSAPVSQKMHRKIQS CCCCHHHHHHHHHHH	29.21	32015554
134	Ubiquitination	VSQKMHRKIQSSLSV HHHHHHHHHHHHHCC	30.34	33845483
137	Phosphorylation	KMHRKIQSSLSVNSD HHHHHHHHHHCCCCC	36.40	30108239
138	Phosphorylation	MHRKIQSSLSVNSDI HHHHHHHHHCCCCCC	14.32	30108239
140	Phosphorylation	RKIQSSLSVNSDISK HHHHHHHCCCCCCCH	22.62	30266825
142	Ubiquitination	IQSSLSVNSDISKKS HHHHHCCCCCCCHHH	30.50	33845483
143	Phosphorylation	QSSLSVNSDISKKSK HHHHCCCCCCCHHHH	33.88	30266825
146	Phosphorylation	LSVNSDISKKSKVNA HCCCCCCCHHHHHEE	38.73	30266825
147	Ubiquitination	SVNSDISKKSKVNAV CCCCCCCHHHHHEEE	62.49	33845483
147	Acetylation	SVNSDISKKSKVNAV CCCCCCCHHHHHEEE	62.49	19819213
148	Acetylation	VNSDISKKSKVNAVF CCCCCCHHHHHEEEE	49.03	19819221
149	Phosphorylation	NSDISKKSKVNAVFS CCCCCHHHHHEEEEC	45.64	24719451
150	Ubiquitination	SDISKKSKVNAVFSQ CCCCHHHHHEEEECC	48.68	29967540
204	Ubiquitination	SEACCCCCGDEMGDD CCCCCCCCCCCCCCC	4.86	33845483
231	Ubiquitination	DACCESSDCLEICME HHHCCCCHHHHHHHH	50.75	29967540
239	Ubiquitination	CLEICMECCGICFPS HHHHHHHHHCCCCCC	0.74	32015554
243	Ubiquitination	CMECCGICFPS---- HHHHHCCCCCC----	2.20	33845483
249	Phosphorylation	ICFPS---------- CCCCC----------		19651622
252	Phosphorylation	PS------------- CC-------------		19651622
255	Phosphorylation	---------------- ----------------		18578522
256	Ubiquitination	----------------- -----------------		33845483
259	Ubiquitination	-------------------- --------------------		29967540

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MDFIC_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 MDFIC_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CCNT1_HUMAN	CCNT1	physical	12944466
MDFIC_HUMAN	MDFIC	physical	12944466
CDK9_HUMAN	CDK9	physical	12944466
TAT_HV1H2	tat	physical	12944466
KS6A5_HUMAN	RPS6KA5	physical	21988832
SOCS4_HUMAN	SOCS4	physical	21988832

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-140 AND SER-143, ANDMASS SPECTROMETRY.
PubMed: 18669648