FAF2_MOUSE - dbPTM
FAF2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FAF2_MOUSE
UniProt AC Q3TDN2
Protein Name FAS-associated factor 2
Gene Name Faf2
Organism Mus musculus (Mouse).
Sequence Length 445
Subcellular Localization Cytoplasm . Lipid droplet . Endoplasmic reticulum .
Protein Description Plays an important role in endoplasmic reticulum-associated degradation (ERAD) that mediates ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway. Involved in inhibition of lipid droplet degradation by binding to phospholipase PNPL2 and inhibiting its activity by promoting dissociation of PNPL2 from its endogenous activator, ABHD5 which inhibits the rate of triacylglycerol hydrolysis..
Protein Sequence MAAPEEQDLTQEQTEKLLQFQDLTGIESMEQCRLALEQHNWNMEAAVQDRLNEQEGVPSVFNPPPARPLQVNTADHRIYSYVVSRPQPRGLLGWGYYLIMLPFRFTYYTILDIFRFALRFIRPDPRSRVTDPVGDIVSFMHSFEEKYGRAHPVFYQGTYSQALNDAKRELRFLLVYLHGDDHQDSDEFCRNALCAPEVISLINSRMLFWACSTNKPEGYRVSQALRENTYPFLAMIMLKDRRMTVVGRLEGLIQPDDLINQLTFIMDANQTYLVSERLEREERNQTQVLRQQQDEAYLASLRADQEKERKKREEKERKRRKEEEVQQQKLAEERRRQNLQEEKERKLECLPPEPSPDDPESVKIIFKLPNDSRVERRFHFSQSLTVIHDFLFSLKESPEKFQIEANFPRRVLPCVPSEEWPNPPTLQEAGLSHTEVLFVQDLTDE
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 Orthologous
Protein Cluster
2Acetylation------MAAPEEQDL
------CCCHHHCCC
31.55-
10PhosphorylationAPEEQDLTQEQTEKL
CHHHCCCCHHHHHHH
38.0527841257
79PhosphorylationNTADHRIYSYVVSRP
ECCCCEEEEEECCCC
8.2325159016
80PhosphorylationTADHRIYSYVVSRPQ
CCCCEEEEEECCCCC
14.7425367039
124UbiquitinationALRFIRPDPRSRVTD
HHHHHCCCCCCCCCC
41.2027667366
146UbiquitinationFMHSFEEKYGRAHPV
HHHHHHHHHCCCCCE
45.89-
162UbiquitinationYQGTYSQALNDAKRE
ECCCHHHHHHHHHHH
11.4627667366
167AcetylationSQALNDAKRELRFLL
HHHHHHHHHHHHHEE
49.6323954790
167UbiquitinationSQALNDAKRELRFLL
HHHHHHHHHHHHHEE
49.63-
167MalonylationSQALNDAKRELRFLL
HHHHHHHHHHHHHEE
49.6326320211
194S-palmitoylationEFCRNALCAPEVISL
HHHHHCCCHHHHHHH
5.7328526873
215AcetylationFWACSTNKPEGYRVS
HHHHCCCCCCCCCHH
44.5322826441
239AcetylationFLAMIMLKDRRMTVV
EEEEEECCCCCEEEH
31.6319852023
244PhosphorylationMLKDRRMTVVGRLEG
ECCCCCEEEHHEHHC
15.3819060867
297PhosphorylationRQQQDEAYLASLRAD
HHHHCHHHHHHHHHH
10.7625159016
301UbiquitinationDEAYLASLRADQEKE
CHHHHHHHHHHHHHH
4.3227667366
307UbiquitinationSLRADQEKERKKREE
HHHHHHHHHHHHHHH
58.1322790023
321UbiquitinationEKERKRRKEEEVQQQ
HHHHHHHHHHHHHHH
73.78-
329UbiquitinationEEEVQQQKLAEERRR
HHHHHHHHHHHHHHH
45.3822790023
339UbiquitinationEERRRQNLQEEKERK
HHHHHHHHHHHHHHH
5.2627667366
355PhosphorylationECLPPEPSPDDPESV
CCCCCCCCCCCHHHC
39.0221930439
367MalonylationESVKIIFKLPNDSRV
HHCEEEEECCCCCCH
53.2626320211
367UbiquitinationESVKIIFKLPNDSRV
HHCEEEEECCCCCCH
53.2627667366
400UbiquitinationSLKESPEKFQIEANF
HCCCCCCCCCEEECC
46.0522790023

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 FAF2_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FAF2_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 FAF2_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of FAF2_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FAF2_MOUSE

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Related Literatures of Post-Translational Modification

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