dbPTM

FAF1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FAF1_MOUSE
UniProt AC	P54731
Protein Name	FAS-associated factor 1
Gene Name	Faf1
Organism	Mus musculus (Mouse).
Sequence Length	649
Subcellular Localization	Nucleus .
Protein Description	Ubiquitin-binding protein (By similarity). Required for the progression of DNA replication forks by targeting DNA replication licensing factor CDT1 for degradation (By similarity). Potentiates but cannot initiate FAS-induced apoptosis. [PubMed: 8524870]
Protein Sequence	MASNMDREMILADFQACTGIENIDEAITLLEQNNWDLVAAINGVIPQENGILQSDFGGETMPGPTFDPASHPAPASTPSSSAFRPVMPSRQIVERQPRMLDFRVEYRDRNVDVVLEDSCTVGEIKQILENELQIPVPKMLLKGWKTGDVEDSTVLKSLHLPKNNSLYVLTPDLPPPSSSSHAGALQESLNQNFMLIITHREVQREYNLNFSGSSTVQEVKRNVYDLTSIPVRHQLWEGWPASATDDSMCLAESGLSYPCHRLTVGRRTSPVQTREQSEEQSTDVHMVSDSDGDDFEDASEFGVDDGEVFGMASSTLRKSPMMPENAENEGDALLQFTAEFSSRYGDCHPVFFIGSLEAAFQEAFYVKARDRKLLAIYLHHDESVLTNVFCSQMLCAESIVSYLSQNFITWAWDLTKDTNRARFLTMCNRHFGSVIAQTIRTQKTDQFPLFLIIMGKRSSNEVLNVIQGNTTVDELMMRLMAAMEIFSAQQQEDIKDEDEREARENVKREQDEAYRLSLEADRAKREAHEREMAEQFRLEQIRKEQEEEREAIRLSLEQALPPEPKEENAEPVSKLRIRTPSGEFLERRFLASNKLQIVFDFVASKGFPWDEFKLLSTFPRRDVTQLDPNKSLLEVNLFPQETLFLQAKE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
138	Ubiquitination	ELQIPVPKMLLKGWK CCCCCCCCHHHCCCC	42.27	22790023
142	Ubiquitination	PVPKMLLKGWKTGDV CCCCHHHCCCCCCCC	59.78	22790023
145	Ubiquitination	KMLLKGWKTGDVEDS CHHHCCCCCCCCCCC	51.83	22790023
156	Ubiquitination	VEDSTVLKSLHLPKN CCCCCHHEEEECCCC	46.78	22790023
206	Phosphorylation	HREVQREYNLNFSGS EHHHHHHHCCCCCCC	27.43	18779572
211	Phosphorylation	REYNLNFSGSSTVQE HHHCCCCCCCHHHHH	36.37	18779572
214	Phosphorylation	NLNFSGSSTVQEVKR CCCCCCCHHHHHHHH	35.80	18779572
215	Phosphorylation	LNFSGSSTVQEVKRN CCCCCCHHHHHHHHH	28.10	18779572
220	Ubiquitination	SSTVQEVKRNVYDLT CHHHHHHHHHHCCCC	37.19	22790023
224	Phosphorylation	QEVKRNVYDLTSIPV HHHHHHHCCCCCCCC	14.58	25195567
268	Phosphorylation	RLTVGRRTSPVQTRE ECCCCCCCCCCCCHH	35.70	25521595
269	Phosphorylation	LTVGRRTSPVQTREQ CCCCCCCCCCCCHHH	22.66	25521595
273	Phosphorylation	RRTSPVQTREQSEEQ CCCCCCCCHHHCCCC	36.09	22817900
319	Phosphorylation	ASSTLRKSPMMPENA CCCCCCCCCCCCCCC	16.17	21082442
443	Ubiquitination	AQTIRTQKTDQFPLF HHHHHCCCCCCCCEE	54.15	-
517	Phosphorylation	QDEAYRLSLEADRAK HHHHHHHHHHHHHHH	18.37	25338131
555	Phosphorylation	EREAIRLSLEQALPP HHHHHHHHHHHHCCC	21.73	23567750
574	Ubiquitination	ENAEPVSKLRIRTPS CCCCCCCCCEEECCC	41.86	27667366
579	Phosphorylation	VSKLRIRTPSGEFLE CCCCEEECCCHHHHH	21.31	26824392
581	Phosphorylation	KLRIRTPSGEFLERR CCEEECCCHHHHHHH	50.79	26824392
616	Phosphorylation	WDEFKLLSTFPRRDV HHHHHHHHCCCCCCC	38.14	25338131
617	Phosphorylation	DEFKLLSTFPRRDVT HHHHHHHCCCCCCCC	37.31	25338131

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 FAF1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of FAF1_MOUSE !!

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 FAF1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
TERA_MOUSE	Vcp	physical	24619421
FAF1_MOUSE	Faf1	physical	24619421

Drug and Disease Associations

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

Regulatory Network of FAF1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, AND MASSSPECTROMETRY.	19367708 [Abstract]
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells."; Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.; J. Proteome Res. 6:3174-3186(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-579, AND MASSSPECTROMETRY.	17622165 [Abstract]