FKBP4_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FKBP4_MOUSE
• UniProt AC: P30416
• Protein Name: Peptidyl-prolyl cis-trans isomerase FKBP4
• Gene Name: Fkbp4
• Organism: Mus musculus (Mouse).
• Sequence Length: 458
• Subcellular Localization: Cytoplasm, cytosol . Mitochondrion . Nucleus . Cytoplasm, cytoskeleton. Shuttles from mitochondria to nucleus; co-localizes in mitochondria with the glucocorticoid receptor. Colocalized with MAPT/TAU in the distal part of the primary cortical neurons
• Protein Description: Immunophilin protein with PPIase and co-chaperone activities. Component of steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments. The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May have a protective role against oxidative stress in mitochondria..
• Protein Sequence: MTAEEMKAAENGAQSAPLPLEGVDISPKQDEGVLKVIKREGTGTETPMIGDRVFVHYTGWLLDGTKFDSSLDRKDKFSFDLGKGEVIKAWDIAVATMKVGEVCHITCKPEYAYGAAGSPPKIPPNATLVFEVELFEFKGEDLTEEEDGGIIRRIRTRGEGYARPNDGAMVEVALEGYHKDRLFDQRELCFEVGEGESLDLPCGLEEAIQRMEKGEHSIVYLKPSYAFGSVGKERFQIPPHAELRYEVRLKSFEKAKESWEMSSAEKLEQSNIVKERGTAYFKEGKYKQALLQYKKIVSWLEYESSFSGEEMQKVHALRLASHLNLAMCHLKLQAFSAAIESCNKALELDSNNEKGLFRRGEAHLAVNDFDLARADFQKVLQLYPSNKAAKTQLAVCQQRTRRQLAREKKLYANMFERLAEEEHKVKAEVAAGDHPTDAEMKGERNNVAENQSRVETEA

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
1	Acetylation	-------MTAEEMKA -------CCHHHHHH	7.86	-
2	Acetylation	------MTAEEMKAA ------CCHHHHHHH	42.66	-
15	Phosphorylation	AAENGAQSAPLPLEG HHHCCCCCCCCCCCC	31.18	29514104
28	Ubiquitination	EGVDISPKQDEGVLK CCCCCCCCCCCCCEE	64.69	22790023
35	Ubiquitination	KQDEGVLKVIKREGT CCCCCCEEEEEECCC	39.24	-
35	Acetylation	KQDEGVLKVIKREGT CCCCCCEEEEEECCC	39.24	22826441
38	Acetylation	EGVLKVIKREGTGTE CCCEEEEEECCCCCC	47.59	7609853
42	Phosphorylation	KVIKREGTGTETPMI EEEEECCCCCCCCCC	35.86	26643407
44	Phosphorylation	IKREGTGTETPMIGD EEECCCCCCCCCCCC	36.20	28066266
46	Phosphorylation	REGTGTETPMIGDRV ECCCCCCCCCCCCEE	20.28	26643407
74	Ubiquitination	FDSSLDRKDKFSFDL CCCCCCCCCCCEEEC	66.01	22790023
76	Acetylation	SSLDRKDKFSFDLGK CCCCCCCCCEEECCC	46.04	23806337
78	Phosphorylation	LDRKDKFSFDLGKGE CCCCCCCEEECCCCC	24.48	22817900
83	Ubiquitination	KFSFDLGKGEVIKAW CCEEECCCCCEEEEE	60.23	22790023
108	Acetylation	EVCHITCKPEYAYGA CEEEEEECCCCCCCC	32.03	22826441
143	Phosphorylation	EFKGEDLTEEEDGGI EEECCCCCCCCCCCE	54.39	28066266
217	Phosphorylation	RMEKGEHSIVYLKPS HHHCCCCEEEEEECC	14.94	28285833
220	Phosphorylation	KGEHSIVYLKPSYAF CCCCEEEEEECCEEC	13.82	22817900
222	Ubiquitination	EHSIVYLKPSYAFGS CCEEEEEECCEECCC	17.77	22790023
222	Acetylation	EHSIVYLKPSYAFGS CCEEEEEECCEECCC	17.77	23954790
224	Phosphorylation	SIVYLKPSYAFGSVG EEEEEECCEECCCCC	27.75	26745281
225	Phosphorylation	IVYLKPSYAFGSVGK EEEEECCEECCCCCC	17.93	26745281
229	Phosphorylation	KPSYAFGSVGKERFQ ECCEECCCCCCCCCC	22.65	30352176
232	Ubiquitination	YAFGSVGKERFQIPP EECCCCCCCCCCCCC	43.49	22790023
258	Phosphorylation	SFEKAKESWEMSSAE HHHHHHHHHHCCCHH	27.85	26643407
274	Ubiquitination	LEQSNIVKERGTAYF HHHCCCHHHCCCCHH	37.59	27667366
274	Acetylation	LEQSNIVKERGTAYF HHHCCCHHHCCCCHH	37.59	23806337
274	Malonylation	LEQSNIVKERGTAYF HHHCCCHHHCCCCHH	37.59	26320211
282	Acetylation	ERGTAYFKEGKYKQA HCCCCHHHCCHHHHH	53.53	-
287	Malonylation	YFKEGKYKQALLQYK HHHCCHHHHHHHHHH	32.36	26320211
287	Acetylation	YFKEGKYKQALLQYK HHHCCHHHHHHHHHH	32.36	22826441
328	S-nitrosocysteine	SHLNLAMCHLKLQAF HHHCHHHHHHHHHHH	2.57	-
328	S-nitrosylation	SHLNLAMCHLKLQAF HHHCHHHHHHHHHHH	2.57	21278135
336	Phosphorylation	HLKLQAFSAAIESCN HHHHHHHHHHHHHHH	21.58	-
342	Glutathionylation	FSAAIESCNKALELD HHHHHHHHHHHHCCC	3.82	24333276
350	Phosphorylation	NKALELDSNNEKGLF HHHHCCCCCCCCCCE	54.93	28285833
354	Ubiquitination	ELDSNNEKGLFRRGE CCCCCCCCCCEECCE	64.14	27667366
354	Acetylation	ELDSNNEKGLFRRGE CCCCCCCCCCEECCE	64.14	23806337
354	Malonylation	ELDSNNEKGLFRRGE CCCCCCCCCCEECCE	64.14	26320211
373	Methylation	VNDFDLARADFQKVL ECHHHHHHHHHHHHH	41.82	24129315
387	Malonylation	LQLYPSNKAAKTQLA HHHCCCCHHHHHHHH	54.80	26320211
387	Ubiquitination	LQLYPSNKAAKTQLA HHHCCCCHHHHHHHH	54.80	27667366
390	Malonylation	YPSNKAAKTQLAVCQ CCCCHHHHHHHHHHH	41.48	26320211
390	Ubiquitination	YPSNKAAKTQLAVCQ CCCCHHHHHHHHHHH	41.48	-
396	S-nitrosylation	AKTQLAVCQQRTRRQ HHHHHHHHHHHHHHH	2.07	20925432
396	Glutathionylation	AKTQLAVCQQRTRRQ HHHHHHHHHHHHHHH	2.07	24333276
396	S-nitrosocysteine	AKTQLAVCQQRTRRQ HHHHHHHHHHHHHHH	2.07	-
409	Malonylation	RQLAREKKLYANMFE HHHHHHHHHHHHHHH	41.81	26320211
409	Ubiquitination	RQLAREKKLYANMFE HHHHHHHHHHHHHHH	41.81	-
411	Phosphorylation	LAREKKLYANMFERL HHHHHHHHHHHHHHH	12.57	25367039
424	Ubiquitination	RLAEEEHKVKAEVAA HHHHHHHHHHHEHHC	49.03	-
436	Phosphorylation	VAAGDHPTDAEMKGE HHCCCCCCHHHHHCH	44.41	-
441	Ubiquitination	HPTDAEMKGERNNVA CCCHHHHHCHHCCHH	49.47	22790023
452	Phosphorylation	NNVAENQSRVETEA- CCHHHHHHHHCCCC-	50.29	-

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
143	T	Phosphorylation	Kinase	CK2	-	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of FKBP4_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of FKBP4_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of FKBP4_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.