FYB1_MOUSE - dbPTM
FYB1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FYB1_MOUSE
UniProt AC O35601
Protein Name FYN-binding protein 1
Gene Name Fyb1
Organism Mus musculus (Mouse).
Sequence Length 819
Subcellular Localization Cytoplasm. Nucleus. Cell junction . Colocalizes with TMEM47 at cell-cell contacts in podocytes.
Protein Description May play a role in linking T-cell signaling to remodeling of the actin cytoskeleton (By similarity). Acts as an adapter protein of the FYN and LCP2 signaling cascades in T-cells. Modulates the expression of interleukin-2 (IL-2). Involved in platelet activation. Prevents the degradation of SKAP1 and SKAP2..
Protein Sequence MAKFNTGSNPTEEAATSSRPFKVAGQSSPSGIQSRKNLFDNQGNASPPAGPSSMPKFGTTKPPLAAKPTYEEKPEKEPKPPFLKPTGGSPRFGTQPNSVSRDPEVKVGFLKPVSPKPTSLTKEDSKPVVLRPPGNKLHNLNQESDLKTPGPKPGPAPPVPENELKPGFSKVAGAKSKFMPAAQDTDSKPRFPRHTFGQKPSLSTEDSQEENTSKNVPVQKGSPVQLGAKSKGAPFKPPKEDPEDKDHGAPSSPFPGVVLKPAASRGSPGLSKNFEEKKEDRKTDLAKNIFLNKLNQEEPARFPKAPSKLTAGTPWGQSQEKEGDKNSATPKQKALPPLSVLGPPPPKPNRPPNVDLTRFRKADSANSATKSQTPYSTTSLPPPPPTHPASQPPLPASHPAHPPVPSLPPRNIKPPLDLKHPINDENQDGVMHSDGTGNLEEEQESEGETYEDIDSSKERDKKREKEEKKRLELERKEQKEREKKEQELKKKFKLTGPIQVIHHAKACCDVKGGKNELSFKQGEDIEIIRITDNPEGKWLGRTARGSYGYIKTTAVEIDYDSLKRKKNSLNAVPPRLVEDDQDVYDDVAEQDAPNSHGQSGSGGMFPPPPTDDEIYDGIEEEDDDDGSVPQVDEKTNAWSWGILKMLKGKDDRKKSIREKPKVSESDNNEGSSLPSQHKQLDVGEEVYDDVDASDFPPPPAEMSQGMSVGRAKTEEKDPKKLKKQEKEEKDLRKKFKYDGEIRVLYSTKVASSLTSKKWGARDLQIKPGESLEVIQSTDDTKVLCRNEEGKYGYVLRSYLVDNDGEIYDDIADGCIYDND
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
3Acetylation-----MAKFNTGSNP
-----CCCCCCCCCC
-
11PhosphorylationFNTGSNPTEEAATSS
CCCCCCCCHHHHHCC
25266776
16PhosphorylationNPTEEAATSSRPFKV
CCCHHHHHCCCCEEE
25367039
17PhosphorylationPTEEAATSSRPFKVA
CCHHHHHCCCCEEEC
25367039
18PhosphorylationTEEAATSSRPFKVAG
CHHHHHCCCCEEECC
25367039
27PhosphorylationPFKVAGQSSPSGIQS
CEEECCCCCCCCCHH
23527152
28PhosphorylationFKVAGQSSPSGIQSR
EEECCCCCCCCCHHH
25521595
30PhosphorylationVAGQSSPSGIQSRKN
ECCCCCCCCCHHHHC
28833060
34PhosphorylationSSPSGIQSRKNLFDN
CCCCCCHHHHCCCCC
28833060
46PhosphorylationFDNQGNASPPAGPSS
CCCCCCCCCCCCCCC
22942356
52PhosphorylationASPPAGPSSMPKFGT
CCCCCCCCCCCCCCC
28285833
53PhosphorylationSPPAGPSSMPKFGTT
CCCCCCCCCCCCCCC
28285833
86PhosphorylationKPPFLKPTGGSPRFG
CCCCCCCCCCCCCCC
22817900
89PhosphorylationFLKPTGGSPRFGTQP
CCCCCCCCCCCCCCC
29472430
114PhosphorylationVGFLKPVSPKPTSLT
EEEECCCCCCCCCCC
26824392
118PhosphorylationKPVSPKPTSLTKEDS
CCCCCCCCCCCCCCC
25159016
119PhosphorylationPVSPKPTSLTKEDSK
CCCCCCCCCCCCCCC
25159016
121PhosphorylationSPKPTSLTKEDSKPV
CCCCCCCCCCCCCCE
25159016
195PhosphorylationKPRFPRHTFGQKPSL
CCCCCCCCCCCCCCC
25619855
201PhosphorylationHTFGQKPSLSTEDSQ
CCCCCCCCCCCCCCC
27742792
203PhosphorylationFGQKPSLSTEDSQEE
CCCCCCCCCCCCCCC
26824392
204PhosphorylationGQKPSLSTEDSQEEN
CCCCCCCCCCCCCCC
27742792
207PhosphorylationPSLSTEDSQEENTSK
CCCCCCCCCCCCCCC
25619855
212PhosphorylationEDSQEENTSKNVPVQ
CCCCCCCCCCCCCCC
25619855
213PhosphorylationDSQEENTSKNVPVQK
CCCCCCCCCCCCCCC
25619855
222PhosphorylationNVPVQKGSPVQLGAK
CCCCCCCCCCCCCCC
26824392
251PhosphorylationDKDHGAPSSPFPGVV
CCCCCCCCCCCCCEE
30387612
252PhosphorylationKDHGAPSSPFPGVVL
CCCCCCCCCCCCEEE
27600695
264PhosphorylationVVLKPAASRGSPGLS
EEEECCHHCCCCCCC
22817900
267PhosphorylationKPAASRGSPGLSKNF
ECCHHCCCCCCCCCH
28285833
318PhosphorylationAGTPWGQSQEKEGDK
CCCCCCCCCCCCCCC
24719451
367PhosphorylationRKADSANSATKSQTP
EECCCCCCCCCCCCC
-
371PhosphorylationSANSATKSQTPYSTT
CCCCCCCCCCCCCCC
25367039
373PhosphorylationNSATKSQTPYSTTSL
CCCCCCCCCCCCCCC
25367039
375PhosphorylationATKSQTPYSTTSLPP
CCCCCCCCCCCCCCC
25367039
376PhosphorylationTKSQTPYSTTSLPPP
CCCCCCCCCCCCCCC
25367039
377PhosphorylationKSQTPYSTTSLPPPP
CCCCCCCCCCCCCCC
25367039
378PhosphorylationSQTPYSTTSLPPPPP
CCCCCCCCCCCCCCC
25367039
379PhosphorylationQTPYSTTSLPPPPPT
CCCCCCCCCCCCCCC
25367039
386PhosphorylationSLPPPPPTHPASQPP
CCCCCCCCCCCCCCC
25367039
390PhosphorylationPPPTHPASQPPLPAS
CCCCCCCCCCCCCCC
25367039
397PhosphorylationSQPPLPASHPAHPPV
CCCCCCCCCCCCCCC
25367039
433PhosphorylationNQDGVMHSDGTGNLE
CCCCCCCCCCCCCCH
25159016
436PhosphorylationGVMHSDGTGNLEEEQ
CCCCCCCCCCCHHHH
25159016
445PhosphorylationNLEEEQESEGETYED
CCHHHHHHCCCCHHH
25521595
449PhosphorylationEQESEGETYEDIDSS
HHHHCCCCHHHCCCH
25159016
450PhosphorylationQESEGETYEDIDSSK
HHHCCCCHHHCCCHH
25159016
455PhosphorylationETYEDIDSSKERDKK
CCHHHCCCHHHHHHH
25777480
456PhosphorylationTYEDIDSSKERDKKR
CHHHCCCHHHHHHHH
25777480
495PhosphorylationLKKKFKLTGPIQVIH
HHHHHCCCCCCEEEE
27600695
511AcetylationAKACCDVKGGKNELS
CEEHHCCCCCCCEEE
15605871
542PhosphorylationEGKWLGRTARGSYGY
CCCEECCCCCCCCCE
25266776
546PhosphorylationLGRTARGSYGYIKTT
ECCCCCCCCCEEEEE
28833060
547PhosphorylationGRTARGSYGYIKTTA
CCCCCCCCCEEEEEE
28833060
559PhosphorylationTTAVEIDYDSLKRKK
EEEEEECHHHHHHHH
21082442
561PhosphorylationAVEIDYDSLKRKKNS
EEEECHHHHHHHHCC
26824392
568PhosphorylationSLKRKKNSLNAVPPR
HHHHHHCCCCCCCCC
22942356
647AcetylationWGILKMLKGKDDRKK
HHHHHHHCCCCHHHH
15611585
655PhosphorylationGKDDRKKSIREKPKV
CCCHHHHHHHHCCCC
24719451
663PhosphorylationIREKPKVSESDNNEG
HHHCCCCCCCCCCCC
26824392
665PhosphorylationEKPKVSESDNNEGSS
HCCCCCCCCCCCCCC
29472430
671PhosphorylationESDNNEGSSLPSQHK
CCCCCCCCCCCHHHC
30635358
672PhosphorylationSDNNEGSSLPSQHKQ
CCCCCCCCCCHHHCC
25367039
675PhosphorylationNEGSSLPSQHKQLDV
CCCCCCCHHHCCCCC
30635358
687PhosphorylationLDVGEEVYDDVDASD
CCCCCHHHCCCCHHH
22817900
770PhosphorylationLQIKPGESLEVIQST
CEECCCCCEEEEEEC
25266776
791PhosphorylationCRNEEGKYGYVLRSY
EECCCCCCEEEEEEE
22817900
793PhosphorylationNEEGKYGYVLRSYLV
CCCCCCEEEEEEEEE
28725479
807PhosphorylationVDNDGEIYDDIADGC
ECCCCCEEECCCCCC
22817900
816PhosphorylationDIADGCIYDND----
CCCCCCCCCCC----
30635358

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 FYB1_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FYB1_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 FYB1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC9_MOUSEUbe2iphysical
29127148

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FYB1_MOUSE

loading...

Related Literatures of Post-Translational Modification

TOP