dbPTM

FABP5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FABP5_HUMAN
UniProt AC	Q01469
Protein Name	Fatty acid-binding protein 5
Gene Name	FABP5
Organism	Homo sapiens (Human).
Sequence Length	135
Subcellular Localization	Cytoplasm . Nucleus . Cell junction, synapse . Cell junction, synapse, postsynaptic cell membrane, postsynaptic density . Secreted . Localizes primarily to the cytoplasm. Upon certain ligand binding, a conformation change exposes a nuclear localizati
Protein Description	Intracellular carrier for long-chain fatty acids and related active lipids, such as the endocannabinoid, that regulates the metabolism and actions of the ligands they bind. In addition to the cytosolic transport, selectively delivers specific fatty acids from the cytosol to the nucleus, wherein they activate nuclear receptors. [PubMed: 22170058 Delivers retinoic acid to the nuclear receptor peroxisome proliferator-activated receptor delta; which promotes proliferation and survival. May also serve as a synaptic carrier of endocannabinoid at central synapses and thus controls retrograde endocannabinoid signaling. Modulates inflammation by regulating PTGES induction via NF-kappa-B activation, and prostaglandin E2 (PGE2) biosynthesis during inflammation (By similarity May be involved in keratinocyte differentiation]
Protein Sequence	MATVQQLEGRWRLVDSKGFDEYMKELGVGIALRKMGAMAKPDCIITCDGKNLTIKTESTLKTTQFSCTLGEKFEETTADGRKTQTVCNFTDGALVQHQEWDGKESTITRKLKDGKLVVECVMNNVTCTRIYEKVE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MATVQQLEG ------CCCCEEEEC	19.24	19413330
3	Phosphorylation	-----MATVQQLEGR -----CCCCEEEECC	19.97	23532336
10	Methylation	TVQQLEGRWRLVDSK CCEEEECCEEEECCC	13.13	-
16	Phosphorylation	GRWRLVDSKGFDEYM CCEEEECCCCHHHHH	27.48	25159151
17	Acetylation	RWRLVDSKGFDEYMK CEEEECCCCHHHHHH	60.16	19608861
17	Ubiquitination	RWRLVDSKGFDEYMK CEEEECCCCHHHHHH	60.16	21890473
17	Succinylation	RWRLVDSKGFDEYMK CEEEECCCCHHHHHH	60.16	23954790
17	Malonylation	RWRLVDSKGFDEYMK CEEEECCCCHHHHHH	60.16	32601280
17	2-Hydroxyisobutyrylation	RWRLVDSKGFDEYMK CEEEECCCCHHHHHH	60.16	-
22	Phosphorylation	DSKGFDEYMKELGVG CCCCHHHHHHHHCHH	18.48	-
24	Methylation	KGFDEYMKELGVGIA CCHHHHHHHHCHHHH	49.22	-
24	Ubiquitination	KGFDEYMKELGVGIA CCHHHHHHHHCHHHH	49.22	21906983
34	Ubiquitination	GVGIALRKMGAMAKP CHHHHHHHCCCCCCC	42.40	-
35	Sulfoxidation	VGIALRKMGAMAKPD HHHHHHHCCCCCCCC	3.15	21406390
40	Ubiquitination	RKMGAMAKPDCIITC HHCCCCCCCCEEEEE	28.44	-
40	Acetylation	RKMGAMAKPDCIITC HHCCCCCCCCEEEEE	28.44	23749302
46	Phosphorylation	AKPDCIITCDGKNLT CCCCEEEEECCCEEE	5.66	-
50	2-Hydroxyisobutyrylation	CIITCDGKNLTIKTE EEEEECCCEEEEEEC	35.22	-
50	Acetylation	CIITCDGKNLTIKTE EEEEECCCEEEEEEC	35.22	25038526
50	Ubiquitination	CIITCDGKNLTIKTE EEEEECCCEEEEEEC	35.22	-
55	Ubiquitination	DGKNLTIKTESTLKT CCCEEEEEECCCEEE	40.79	19608861
55	Acetylation	DGKNLTIKTESTLKT CCCEEEEEECCCEEE	40.79	19608861
61	Ubiquitination	IKTESTLKTTQFSCT EEECCCEEEEEEEEE	50.00	21890473
61	Malonylation	IKTESTLKTTQFSCT EEECCCEEEEEEEEE	50.00	26320211
61	Acetylation	IKTESTLKTTQFSCT EEECCCEEEEEEEEE	50.00	23236377
63	Phosphorylation	TESTLKTTQFSCTLG ECCCEEEEEEEEECC	26.48	23312004
67	S-nitrosylation	LKTTQFSCTLGEKFE EEEEEEEEECCCCEE	3.72	2212679
67	S-palmitoylation	LKTTQFSCTLGEKFE EEEEEEEEECCCCEE	3.72	29575903
72	Ubiquitination	FSCTLGEKFEETTAD EEEECCCCEEEECCC	57.17	-
72	Acetylation	FSCTLGEKFEETTAD EEEECCCCEEEECCC	57.17	23749302
76	Phosphorylation	LGEKFEETTADGRKT CCCCEEEECCCCCEE	21.78	20068231
82	Ubiquitination	ETTADGRKTQTVCNF EECCCCCEEEEEEEC	50.98	21906983
103	Ubiquitination	QHQEWDGKESTITRK EECEECCCCCEEEEE	46.12	-
103	2-Hydroxyisobutyrylation	QHQEWDGKESTITRK EECEECCCCCEEEEE	46.12	-
103	Acetylation	QHQEWDGKESTITRK EECEECCCCCEEEEE	46.12	25038526
122	Sulfoxidation	KLVVECVMNNVTCTR CEEEEEEECCCEEEE	4.58	21406390
131	Phosphorylation	NVTCTRIYEKVE--- CCEEEEEEEECC---	13.35	10493790

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
Oops, there are no upstream regulatory protein records of FABP5_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of FABP5_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 FABP5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ALDR_HUMAN	AKR1B1	physical	26344197
ECI1_HUMAN	ECI1	physical	26344197
FKB1A_HUMAN	FKBP1A	physical	26344197
FKB1B_HUMAN	FKBP1B	physical	26344197
GRB2_HUMAN	GRB2	physical	26344197
CH10_HUMAN	HSPE1	physical	26344197
PIN1_HUMAN	PIN1	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 FABP5_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]
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides."; Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.; Nat. Biotechnol. 21:566-569(2003). Cited for: PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT ALA-2.	12665801 [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-17, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-131, AND MASSSPECTROMETRY.	15592455 [Abstract]