FANCI_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FANCI_MOUSE
• UniProt AC: Q8K368
• Protein Name: Fanconi anemia group I protein homolog
• Gene Name: Fanci
• Organism: Mus musculus (Mouse).
• Sequence Length: 1330
• Subcellular Localization: Nucleus. Observed in spots localized in pairs on the sister chromatids of mitotic chromosome arms and not centromeres, one on each chromatids. These foci coincide with common fragile sites. They are frequently interlinked through BLM-associated ultra
• Protein Description: Plays an essential role in the repair of DNA double-strand breaks by homologous recombination and in the repair of interstrand DNA cross-links (ICLs) by promoting FANCD2 monoubiquitination by FANCL and participating in recruitment to DNA repair sites. Required for maintenance of chromosomal stability. Specifically binds branched DNA: binds both single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA). Participates in S phase and G2 phase checkpoint activation upon DNA damage..
• Protein Sequence: MDLKILSLATDKTTDKLQEFLQTLKDDDLASLLQNQAVKGRAVGTLLRAVLKGSPCSEEDGALRRYKIYSCCIQLVESGDLQQDVASEIIGLLMLEVHHFPGPLLVDLASDFVGAVREDRLVNGKSLELLPIILTALATKKEVLACGKGDLNGEEYKRQLIDTLCSVRWPQRYMIQLTSVFKDVCLTPEEMNLVVAKVLTMFSKLNLQEIPPLVYQLLVLSSKGSRRSVLDGIIAFFRELDKQHREEQSSDELSELITAPADELYHVEGTVILHIVFAIKLDCELGRELLKHLKAGQQGDPSKCLCPFSIALLLSLTRIQRFEEQVFDLLKTSVVKSFKDLQLLQGSKFLQTLVPQRTCVSTMILEVVRNSVHSWDHVTQGLIEFGFILMDSYGPKKILDGKAVEIGTSLSKMTNQHACKLGANILLETFKIHEMIRQEILEQVLNRVVTRTSSPINHFLDLFSDIIMYAPLILQNCSKVTETFDYLTFLPLQTVQGLLKAVQPLLKISMSMRDSLILVLRKAMFASQLDARKSAVAGFLLLLKNFKVLGSLPSSQCTQSIGVTQVRVDVHSRYSAVANETFCLEIIDSLKRSLGQQADIRLMLYDGFYDVLRRNSQLASSIMQTLFSQLKQFYEPEPDLLPPLKLGACVLTQGSQIFLQEPLDHLLSCIQHCLAWYKSRVVPLQQGDEGEEEEEELYSELDDMLESITVRMIKSELEDFELDKSADFSQNTNVGIKNNICACLIMGVCEVLMEYNFSISNFSKSKFEEILSLFTCYKKFSDILSEKAGKGKAKMTSKVSDSLLSLKFVSDLLTALFRDSIQSHEESLSVLRSSGEFMHYAVNVTLQKIQQLIRTGHVSGPDGQNPDKIFQNLCDITRVLLWRYTSIPTSVEESGKKEKGKSISLLCLEGLQKTFSVVLQFYQPKVQQFLQALDVMGTEEEEAGVTVTQRASFQIRQFQRSLLNLLSSEEDDFNSKEALLLIAVLSTLSRLLEPTSPQFVQMLSWTSKICKEYSQEDASFCKSLMNLFFSLHVLYKSPVTLLRDLSQDIHGQLGDIDQDVEIEKTDHFAVVNLRTAAPTVCLLVLSQAEKVLEEVDWLIAKIKGSANQETLSDKVTPEDASSQAVPPTLLIEKAIVMQLGTLVTFFHELVQTALPSGSCVDTLLKGLSKIYSTLTAFVKYYLQVCQSSRGIPNTVEKLVKLSGSHLTPVCYSFISYVQNKSSDAPKCSEKEKAAVSTTMAKVLRETKPIPNLVFAIEQYEKFLIQLSKKSKVNLMQHMKLSTSRDFKIKGSVLDMVLREDEEDENEEGTASAHTQQDREPAKKRRKKCLS

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
7	Phosphorylation	-MDLKILSLATDKTT -CCCCHHHHHCCCCH	21.30	-
148	Acetylation	KEVLACGKGDLNGEE HHHHHCCCCCCCHHH	49.49	19853525
157	Acetylation	DLNGEEYKRQLIDTL CCCHHHHHHHHHHHH	36.63	19853533
452	Phosphorylation	LNRVVTRTSSPINHF HHHHHHCCCCHHHHH	24.96	25777480
453	Phosphorylation	NRVVTRTSSPINHFL HHHHHCCCCHHHHHH	30.72	25777480
454	Phosphorylation	RVVTRTSSPINHFLD HHHHCCCCHHHHHHH	29.23	25777480
464	Phosphorylation	NHFLDLFSDIIMYAP HHHHHHHHHHHHHHH	34.89	25777480
469	Phosphorylation	LFSDIIMYAPLILQN HHHHHHHHHHHHHHC	8.48	25777480
478	Phosphorylation	PLILQNCSKVTETFD HHHHHCCCCCCCCCC	37.40	25777480
522	Ubiquitination	SLILVLRKAMFASQL HHHHHHHHHHHHHHH	39.79	-
527	Phosphorylation	LRKAMFASQLDARKS HHHHHHHHHHHHHHH	21.73	-
551	Phosphorylation	KNFKVLGSLPSSQCT HHCEEECCCCHHHCC	32.71	25293948
554	Phosphorylation	KVLGSLPSSQCTQSI EEECCCCHHHCCCCC	38.03	26643407
555	Phosphorylation	VLGSLPSSQCTQSIG EECCCCHHHCCCCCC	27.60	17525332
558	Phosphorylation	SLPSSQCTQSIGVTQ CCCHHHCCCCCCCEE	20.08	17525332
560	Phosphorylation	PSSQCTQSIGVTQVR CHHHCCCCCCCEEEE	11.80	28066266
564	Phosphorylation	CTQSIGVTQVRVDVH CCCCCCCEEEEEEEC	19.01	25777480
729	Phosphorylation	LDKSADFSQNTNVGI CCCCCCCCCCCCCCC	24.06	-
823	Phosphorylation	LFRDSIQSHEESLSV HHHHHHHHCHHHHHH	31.06	26370283
948	Phosphorylation	EEAGVTVTQRASFQI HHCCCEEEHHHHHHH	11.72	-
967	Phosphorylation	RSLLNLLSSEEDDFN HHHHHHHCCCCCCCC	38.58	24759943
975	Phosphorylation	SEEDDFNSKEALLLI CCCCCCCCHHHHHHH	31.69	24759943
1122	Phosphorylation	VTPEDASSQAVPPTL CCHHHHHCCCCCCCH	24.71	-
1291	Phosphorylation	RDFKIKGSVLDMVLR CCCEECCCCEEHEEC	17.95	28059163

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

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

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
522	K	ubiquitylation	Monoubiquitinated by FANCL on Lys-522 during S phase and upon genotoxic stress.	-

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FACD2_MOUSE	Fancd2	physical	21764741

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-555 AND THR-558, ANDMASS SPECTROMETRY.
PubMed: 17525332

"Identification of the FANCI protein, a monoubiquitinated FANCD2paralog required for DNA repair.";
Smogorzewska A., Matsuoka S., Vinciguerra P., McDonald E.R. III,Hurov K.E., Luo J., Ballif B.A., Gygi S.P., Hofmann K., D'Andrea A.D.,Elledge S.J.;
Cell 129:289-301(2007).
Cited for: PHOSPHORYLATION AT SER-555 AND THR-558.
PubMed: 17412408