FHIT_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FHIT_HUMAN
• UniProt AC: P49789
• Protein Name: Bis(5'-adenosyl)-triphosphatase
• Gene Name: FHIT
• Organism: Homo sapiens (Human).
• Sequence Length: 147
• Subcellular Localization: Cytoplasm. Mitochondrion. Nucleus.
• Protein Description: Cleaves P(1)-P(3)-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP. Can also hydrolyze P(1)-P(4)-bis(5'-adenosyl) tetraphosphate (Ap4A), but has extremely low activity with ATP. Modulates transcriptional activation by CTNNB1 and thereby contributes to regulate the expression of genes essential for cell proliferation and survival, such as CCND1 and BIRC5. Plays a role in the induction of apoptosis via SRC and AKT1 signaling pathways. Inhibits MDM2-mediated proteasomal degradation of p53/TP53 and thereby plays a role in p53/TP53-mediated apoptosis. Induction of apoptosis depends on the ability of FHIT to bind P(1)-P(3)-bis(5'-adenosyl) triphosphate or related compounds, but does not require its catalytic activity, it may in part come from the mitochondrial form, which sensitizes the low-affinity Ca(2+) transporters, enhancing mitochondrial calcium uptake. Functions as tumor suppressor..
• Protein Sequence: MSFRFGQHLIKPSVVFLKTELSFALVNRKPVVPGHVLVCPLRPVERFHDLRPDEVADLFQTTQRVGTVVEKHFHGTSLTFSMQDGPEAGQTVKHVHVHVLPRKAGDFHRNDSIYEELQKHDKEDFPASWRSEEEMAAEAAALRVYFQ

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
2	Phosphorylation	------MSFRFGQHL ------CCCCCCCCC	25.73	24719451
61	Phosphorylation	EVADLFQTTQRVGTV HHHHHHHHHCHHCCE	19.98	22210691
62	Phosphorylation	VADLFQTTQRVGTVV HHHHHHHHCHHCCEE	12.00	22210691
67	Phosphorylation	QTTQRVGTVVEKHFH HHHCHHCCEEEECCC	20.65	22210691
112	Phosphorylation	GDFHRNDSIYEELQK CCCCCCCHHHHHHHH	30.53	28857561
114	Phosphorylation	FHRNDSIYEELQKHD CCCCCHHHHHHHHCC	13.80	15835917
145	Phosphorylation	EAAALRVYFQ----- HHHHHHHHCC-----	6.99	16407838

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
114	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of FHIT_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 FHIT_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FHIT_HUMAN	FHIT	physical	16189514
UBC9_HUMAN	UBE2I	physical	11085938
TRI23_HUMAN	TRIM23	physical	21988832
RB40B_HUMAN	RAB40B	physical	21988832
FHIT_HUMAN	FHIT	physical	24722188
REL_HUMAN	REL	physical	24722188
FHIT_HUMAN	FHIT	physical	25416956
MTMR6_HUMAN	MTMR6	physical	28514442

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

"Fhit is a physiological target of the protein kinase Src.";
Pekarsky Y., Garrison P.N., Palamarchuk A., Zanesi N., Aqeilan R.I.,Huebner K., Barnes L.D., Croce C.M.;
Proc. Natl. Acad. Sci. U.S.A. 101:3775-3779(2004).
Cited for: PHOSPHORYLATION BY C-SRC, SUBUNIT, SUBCELLULAR LOCATION, MASSSPECTROMETRY, DISEASE, PHOSPHORYLATION AT TYR-114 AND TYR-145, ANDMUTAGENESIS OF TYR-114 AND TYR-145.
PubMed: 15007172