PO3F2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PO3F2_HUMAN
• UniProt AC: P20265
• Protein Name: POU domain, class 3, transcription factor 2
• Gene Name: POU3F2
• Organism: Homo sapiens (Human).
• Sequence Length: 443
• Subcellular Localization: Nucleus.
• Protein Description: Transcription factor that plays a key role in neuronal differentiation (By similarity). Binds preferentially to the recognition sequence which consists of two distinct half-sites, ('GCAT') and ('TAAT'), separated by a non-conserved spacer region of 0, 2, or 3 nucleotides (By similarity). The combination of three transcription factors, ASCL1, POU3F2/BRN2 and MYT1L, is sufficient to reprogram fibroblasts and other somatic cells into induced neuronal (iN) cells in vitro. Acts downstream of ASCL1, accessing chromatin that has been opened by ASCL1, and promotes transcription of neuronal genes (By similarity)..
• Protein Sequence: MATAASNHYSLLTSSASIVHAEPPGGMQQGAGGYREAQSLVQGDYGALQSNGHPLSHAHQWITALSHGGGGGGGGGGGGGGGGGGGGGDGSPWSTSPLGQPDIKPSVVVQQGGRGDELHGPGALQQQHQQQQQQQQQQQQQQQQQQQQQRPPHLVHHAANHHPGPGAWRSAAAAAHLPPSMGASNGGLLYSQPSFTVNGMLGAGGQPAGLHHHGLRDAHDEPHHADHHPHPHSHPHQQPPPPPPPQGPPGHPGAHHDPHSDEDTPTSDDLEQFAKQFKQRRIKLGFTQADVGLALGTLYGNVFSQTTICRFEALQLSFKNMCKLKPLLNKWLEEADSSSGSPTSIDKIAAQGRKRKKRTSIEVSVKGALESHFLKCPKPSAQEITSLADSLQLEKEVVRVWFCNRRQKEKRMTPPGGTLPGAEDVYGGSRDTPPHHGVQTPVQ

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	-----MATAASNHYS -----CCCCHHCCHH	22.81	25693802
6	Phosphorylation	--MATAASNHYSLLT --CCCCHHCCHHHCC	22.98	25693802
9	Phosphorylation	ATAASNHYSLLTSSA CCCHHCCHHHCCCCC	12.79	25693802
10	Phosphorylation	TAASNHYSLLTSSAS CCHHCCHHHCCCCCE	14.89	25693802
13	Phosphorylation	SNHYSLLTSSASIVH HCCHHHCCCCCEEEE	26.40	25693802
14	Phosphorylation	NHYSLLTSSASIVHA CCHHHCCCCCEEEEC	24.71	25693802
15	Phosphorylation	HYSLLTSSASIVHAE CHHHCCCCCEEEECC	22.32	25693802
17	Phosphorylation	SLLTSSASIVHAEPP HHCCCCCEEEECCCC	27.39	25693802
34	Phosphorylation	MQQGAGGYREAQSLV CCCCCCCHHHHHHHH	12.36	25693802
91	Phosphorylation	GGGGGDGSPWSTSPL CCCCCCCCCCCCCCC	28.12	-
131 (in isoform 3)	Ubiquitination	-	36.16	21890473
150 (in isoform 2)	Ubiquitination	-	42.24	21890473
304	Phosphorylation	TLYGNVFSQTTICRF HHHCCCCCHHHHHHH	23.49	22817900
306	Phosphorylation	YGNVFSQTTICRFEA HCCCCCHHHHHHHHH	19.55	22817900
307	Phosphorylation	GNVFSQTTICRFEAL CCCCCHHHHHHHHHH	15.50	22817900
317	Phosphorylation	RFEALQLSFKNMCKL HHHHHHHHHHHHHHH	22.63	24719451
325	Ubiquitination	FKNMCKLKPLLNKWL HHHHHHHHHHHHHHH	21.08	32142685
330	Ubiquitination	KLKPLLNKWLEEADS HHHHHHHHHHHHHHC	53.80	21890473
330 (in isoform 1)	Ubiquitination	-	53.80	21890473
337	Phosphorylation	KWLEEADSSSGSPTS HHHHHHHCCCCCCCH	33.19	28122231
338	Phosphorylation	WLEEADSSSGSPTSI HHHHHHCCCCCCCHH	38.99	29978859
339	Phosphorylation	LEEADSSSGSPTSID HHHHHCCCCCCCHHH	47.44	21082442
341	Phosphorylation	EADSSSGSPTSIDKI HHHCCCCCCCHHHHH	27.27	19413330
343	Phosphorylation	DSSSGSPTSIDKIAA HCCCCCCCHHHHHHH	39.76	30576142
344	Phosphorylation	SSSGSPTSIDKIAAQ CCCCCCCHHHHHHHC	31.97	29978859
347	Ubiquitination	GSPTSIDKIAAQGRK CCCCHHHHHHHCCCC	32.35	29967540
359	Phosphorylation	GRKRKKRTSIEVSVK CCCCCCCCCEEEEHH	42.83	29978859
360	Phosphorylation	RKRKKRTSIEVSVKG CCCCCCCCEEEEHHH	22.30	28857561
364	Phosphorylation	KRTSIEVSVKGALES CCCCEEEEHHHHHHH	12.81	29978859
371	Phosphorylation	SVKGALESHFLKCPK EHHHHHHHHHCCCCC	22.01	23898821
413	Phosphorylation	RQKEKRMTPPGGTLP CCCCCCCCCCCCCCC	30.30	25850435
418	Phosphorylation	RMTPPGGTLPGAEDV CCCCCCCCCCCCHHC	35.38	25954137
426	Phosphorylation	LPGAEDVYGGSRDTP CCCCHHCCCCCCCCC	28.26	28555341
429	Phosphorylation	AEDVYGGSRDTPPHH CHHCCCCCCCCCCCC	23.71	26074081
432	Phosphorylation	VYGGSRDTPPHHGVQ CCCCCCCCCCCCCCC	37.29	22496350
440	Phosphorylation	PPHHGVQTPVQ---- CCCCCCCCCCC----	24.03	28555341

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
91	S	Phosphorylation	Kinase	P38A	Q16539	PSP
96	S	Phosphorylation	Kinase	P38A	Q16539	PSP
360	S	Phosphorylation	Kinase	PRKACA	P00517	GPS
360	S	Phosphorylation	Kinase	PKACA	P17612	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PO3F2_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 PO3F2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PQBP1_HUMAN	PQBP1	physical	10332029
PO3F2_HUMAN	POU3F2	physical	11029584
EP300_HUMAN	EP300	physical	11029584
TBP_HUMAN	TBP	physical	11029584
SOX10_HUMAN	SOX10	physical	11029584
PAX3_HUMAN	PAX3	physical	11029584
TF2B_HUMAN	GTF2B	physical	11029584

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

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341, AND MASSSPECTROMETRY.
PubMed: 19690332

"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-341, AND MASSSPECTROMETRY.
PubMed: 19413330