dbPTM

FKBP3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FKBP3_HUMAN
UniProt AC	Q00688
Protein Name	Peptidyl-prolyl cis-trans isomerase FKBP3
Gene Name	FKBP3
Organism	Homo sapiens (Human).
Sequence Length	224
Subcellular Localization	Nucleus.
Protein Description	FK506- and rapamycin-binding proteins (FKBPs) constitute a family of receptors for the two immunosuppressants which inhibit T-cell proliferation by arresting two distinct cytoplasmic signal transmission pathways. PPIases accelerate the folding of proteins..
Protein Sequence	MAAAVPQRAWTVEQLRSEQLPKKDIIKFLQEHGSDSFLAEHKLLGNIKNVAKTANKDHLVTAYNHLFETKRFKGTESISKVSEQVKNVKLNEDKPKETKSEETLDEGPPKYTKSVLKKGDKTNFPKKGDVVHCWYTGTLQDGTVFDTNIQTSAKKKKNAKPLSFKVGVGKVIRGWDEALLTMSKGEKARLEIEPEWAYGKKGQPDAKIPPNAKLTFEVELVDID

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAAVPQRA ------CCCCCCCCC	12.25	25944712
9	Ubiquitination	AAAVPQRAWTVEQLR CCCCCCCCCCHHHHH	10.88	23000965
11	Phosphorylation	AVPQRAWTVEQLRSE CCCCCCCCHHHHHHC	17.12	27251275
15	Ubiquitination	RAWTVEQLRSEQLPK CCCCHHHHHHCCCCH	4.04	23000965
16	Methylation	AWTVEQLRSEQLPKK CCCHHHHHHCCCCHH	37.53	-
19	Ubiquitination	VEQLRSEQLPKKDII HHHHHHCCCCHHHHH	65.40	23000965
22	2-Hydroxyisobutyrylation	LRSEQLPKKDIIKFL HHHCCCCHHHHHHHH	72.21	-
22	Ubiquitination	LRSEQLPKKDIIKFL HHHCCCCHHHHHHHH	72.21	22817900
23	Ubiquitination	RSEQLPKKDIIKFLQ HHCCCCHHHHHHHHH	52.82	22817900
27	Ubiquitination	LPKKDIIKFLQEHGS CCHHHHHHHHHHHCC	40.11	22817900
34	Phosphorylation	KFLQEHGSDSFLAEH HHHHHHCCCCHHHHH	31.80	23401153
36	Phosphorylation	LQEHGSDSFLAEHKL HHHHCCCCHHHHHHH	24.69	29255136
42	Ubiquitination	DSFLAEHKLLGNIKN CCHHHHHHHHHHHHH	36.59	23000965
48	Malonylation	HKLLGNIKNVAKTAN HHHHHHHHHHHHHCC	49.74	26320211
48	Ubiquitination	HKLLGNIKNVAKTAN HHHHHHHHHHHHHCC	49.74	23000965
48	Succinylation	HKLLGNIKNVAKTAN HHHHHHHHHHHHHCC	49.74	23954790
52	Ubiquitination	GNIKNVAKTANKDHL HHHHHHHHHCCHHHH	43.84	23000965
56	Acetylation	NVAKTANKDHLVTAY HHHHHCCHHHHHHHH	44.02	26051181
70	Succinylation	YNHLFETKRFKGTES HHHHHHCCCCCCCHH	48.95	23954790
70	2-Hydroxyisobutyrylation	YNHLFETKRFKGTES HHHHHHCCCCCCCHH	48.95	-
70	Ubiquitination	YNHLFETKRFKGTES HHHHHHCCCCCCCHH	48.95	33845483
70	Acetylation	YNHLFETKRFKGTES HHHHHHCCCCCCCHH	48.95	26051181
73	2-Hydroxyisobutyrylation	LFETKRFKGTESISK HHHCCCCCCCHHHHH	69.80	-
75	Phosphorylation	ETKRFKGTESISKVS HCCCCCCCHHHHHHH	27.44	30108239
77	Phosphorylation	KRFKGTESISKVSEQ CCCCCCHHHHHHHHH	31.81	21712546
79	Phosphorylation	FKGTESISKVSEQVK CCCCHHHHHHHHHHH	35.96	30108239
80	Acetylation	KGTESISKVSEQVKN CCCHHHHHHHHHHHC	48.38	25953088
80	Ubiquitination	KGTESISKVSEQVKN CCCHHHHHHHHHHHC	48.38	33845483
82	Phosphorylation	TESISKVSEQVKNVK CHHHHHHHHHHHCCC	26.50	20068231
86	Ubiquitination	SKVSEQVKNVKLNED HHHHHHHHCCCCCCC	56.57	33845483
86	Acetylation	SKVSEQVKNVKLNED HHHHHHHHCCCCCCC	56.57	25953088
89	Acetylation	SEQVKNVKLNEDKPK HHHHHCCCCCCCCCC	55.80	25953088
98	Phosphorylation	NEDKPKETKSEETLD CCCCCCCCCCHHHCC	46.10	26657352
99	Ubiquitination	EDKPKETKSEETLDE CCCCCCCCCHHHCCC	57.89	33845483
99	Acetylation	EDKPKETKSEETLDE CCCCCCCCCHHHCCC	57.89	26822725
100	Phosphorylation	DKPKETKSEETLDEG CCCCCCCCHHHCCCC	48.35	29255136
103	Phosphorylation	KETKSEETLDEGPPK CCCCCHHHCCCCCCC	35.14	29255136
110	Acetylation	TLDEGPPKYTKSVLK HCCCCCCCCCHHHHH	69.55	23236377
111	Phosphorylation	LDEGPPKYTKSVLKK CCCCCCCCCHHHHHC	25.77	29083192
112	Phosphorylation	DEGPPKYTKSVLKKG CCCCCCCCHHHHHCC	23.99	29083192
114	Phosphorylation	GPPKYTKSVLKKGDK CCCCCCHHHHHCCCC	25.53	29083192
127	Ubiquitination	DKTNFPKKGDVVHCW CCCCCCCCCCEEEEE	61.66	23000965
132	Ubiquitination	PKKGDVVHCWYTGTL CCCCCEEEEEEEEEE	9.02	23000965
133	Glutathionylation	KKGDVVHCWYTGTLQ CCCCEEEEEEEEEEC	1.69	22555962
135	Phosphorylation	GDVVHCWYTGTLQDG CCEEEEEEEEEECCC	10.73	24732914
136	Phosphorylation	DVVHCWYTGTLQDGT CEEEEEEEEEECCCC	10.13	24732914
137	Ubiquitination	VVHCWYTGTLQDGTV EEEEEEEEEECCCCE	14.56	23000965
138	Phosphorylation	VHCWYTGTLQDGTVF EEEEEEEEECCCCEE	17.28	24732914
143	Phosphorylation	TGTLQDGTVFDTNIQ EEEECCCCEEECCCC	26.70	24732914
147	Phosphorylation	QDGTVFDTNIQTSAK CCCCEEECCCCCCCC	23.82	27794612
151	Phosphorylation	VFDTNIQTSAKKKKN EEECCCCCCCCCCCC	27.19	30266825
152	Phosphorylation	FDTNIQTSAKKKKNA EECCCCCCCCCCCCC	23.01	30266825
154	Ubiquitination	TNIQTSAKKKKNAKP CCCCCCCCCCCCCCC	65.96	32015554
154	Acetylation	TNIQTSAKKKKNAKP CCCCCCCCCCCCCCC	65.96	25953088
160	Ubiquitination	AKKKKNAKPLSFKVG CCCCCCCCCCEEEEC	56.75	23000965
160	Acetylation	AKKKKNAKPLSFKVG CCCCCCCCCCEEEEC	56.75	23749302
160	Malonylation	AKKKKNAKPLSFKVG CCCCCCCCCCEEEEC	56.75	26320211
163	Phosphorylation	KKNAKPLSFKVGVGK CCCCCCCEEEECCHH	31.39	28464451
165	Malonylation	NAKPLSFKVGVGKVI CCCCCEEEECCHHHH	34.40	26320211
165	Acetylation	NAKPLSFKVGVGKVI CCCCCEEEECCHHHH	34.40	25953088
165	Ubiquitination	NAKPLSFKVGVGKVI CCCCCEEEECCHHHH	34.40	23000965
170	2-Hydroxyisobutyrylation	SFKVGVGKVIRGWDE EEEECCHHHHCCHHH	31.89	-
170	Acetylation	SFKVGVGKVIRGWDE EEEECCHHHHCCHHH	31.89	19608861
170	Ubiquitination	SFKVGVGKVIRGWDE EEEECCHHHHCCHHH	31.89	23000965
170	Malonylation	SFKVGVGKVIRGWDE EEEECCHHHHCCHHH	31.89	26320211
173	Methylation	VGVGKVIRGWDEALL ECCHHHHCCHHHHHE	43.04	-
181	Phosphorylation	GWDEALLTMSKGEKA CHHHHHEEECCCCCE	21.90	20068231
182	Sulfoxidation	WDEALLTMSKGEKAR HHHHHEEECCCCCEE	3.83	30846556
183	Phosphorylation	DEALLTMSKGEKARL HHHHEEECCCCCEEE	32.07	20068231
187	Methylation	LTMSKGEKARLEIEP EEECCCCCEEEEECC	47.69	23644510
198	Phosphorylation	EIEPEWAYGKKGQPD EECCHHHCCCCCCCC	30.47	20068231
200	2-Hydroxyisobutyrylation	EPEWAYGKKGQPDAK CCHHHCCCCCCCCCC	40.84	-
200	Ubiquitination	EPEWAYGKKGQPDAK CCHHHCCCCCCCCCC	40.84	32015554
200	Malonylation	EPEWAYGKKGQPDAK CCHHHCCCCCCCCCC	40.84	26320211
200	Acetylation	EPEWAYGKKGQPDAK CCHHHCCCCCCCCCC	40.84	23749302
201	Ubiquitination	PEWAYGKKGQPDAKI CHHHCCCCCCCCCCC	59.42	-
207	Ubiquitination	KKGQPDAKIPPNAKL CCCCCCCCCCCCCEE	64.23	33845483

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
-	K	Ubiquitination	E3 ubiquitin ligase	SMURF1	Q9HCE7	PMID:20804422

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of FKBP3_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of FKBP3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MTA2_HUMAN	MTA2	physical	12920132
HDAC1_HUMAN	HDAC1	physical	11532945
HDAC2_HUMAN	HDAC2	physical	11532945
TYY1_HUMAN	YY1	physical	11532945
MDM2_HUMAN	MDM2	physical	19166840
PACN3_HUMAN	PACSIN3	physical	22939629
TIM_HUMAN	TIMELESS	physical	22939629
LRRF1_HUMAN	LRRFIP1	physical	22939629
MYH10_HUMAN	MYH10	physical	22939629
ABCF1_HUMAN	ABCF1	physical	22863883
CN166_HUMAN	C14orf166	physical	22863883
NELFB_HUMAN	NELFB	physical	22863883
DDX1_HUMAN	DDX1	physical	22863883
DIM1_HUMAN	DIMT1	physical	22863883
DYL1_HUMAN	DYNLL1	physical	22863883
EDC4_HUMAN	EDC4	physical	22863883
EI2BB_HUMAN	EIF2B2	physical	22863883
EI2BG_HUMAN	EIF2B3	physical	22863883
ROA2_HUMAN	HNRNPA2B1	physical	22863883
HNRPU_HUMAN	HNRNPU	physical	22863883
IF2B3_HUMAN	IGF2BP3	physical	22863883
ILF2_HUMAN	ILF2	physical	22863883
K1C18_HUMAN	KRT18	physical	22863883
MAP1S_HUMAN	MAP1S	physical	22863883
NMT1_HUMAN	NMT1	physical	22863883
RFC4_HUMAN	RFC4	physical	22863883
SC16A_HUMAN	SEC16A	physical	22863883
HNRPQ_HUMAN	SYNCRIP	physical	22863883
YBOX1_HUMAN	YBX1	physical	22863883
CGBP1_HUMAN	CGGBP1	physical	26344197

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.

Regulatory Network of FKBP3_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-160 AND LYS-170, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-152, AND MASSSPECTROMETRY.	18669648 [Abstract]