FUBP2_MOUSE - dbPTM
FUBP2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FUBP2_MOUSE
UniProt AC Q3U0V1
Protein Name Far upstream element-binding protein 2
Gene Name Khsrp
Organism Mus musculus (Mouse).
Sequence Length 748
Subcellular Localization Nucleus. Cytoplasm. A small proportion is also found in the cytoplasm of neuronal cell bodies and dendrites..
Protein Description Binds to the dendritic targeting element and may play a role in mRNA trafficking. Part of a ternary complex that binds to the downstream control sequence (DCS) of the pre-mRNA. Mediates exon inclusion in transcripts that are subject to tissue-specific alternative splicing. May interact with single-stranded DNA from the far-upstream element (FUSE). May activate gene expression. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly by recruiting degradation machinery to ARE-containing mRNAs (By similarity)..
Protein Sequence MSDYNTGGPPPGPPPPAGGGGGAAGAGGGPPPGPPGAGDRGGGGPGGGGPGGGGASGGPSQPPGGGGPGIRKDAFADAVQRARQIAAKIGGDAATTVNNNTPDFGFGGQKRQLEDGDQPDSKKLASQGDSIGSQLGPIHPPPRTSMTEEYRVPDGMVGLIIGRGGEQINKIQQDSGCKVQISPDSGGLPERSVSLTGAPESVQKAKMMLDDIVSRGRGGPPGQFHDNANGGQNGTVQEIMIPAGKAGLVIGKGGETIKQLQERAGVKMILIQDGSQNTNVDKPLRIIGDPYKVQQACEMVMDILRERDQGGFGDRNEYGSRVGGGIDVPVPRHSVGVVIGRSGEMIKKIQNDAGVRIQFKQDDGTGPEKIAHIMGPPDRCEHAARIINDLLQSLRSGPPGPPGAPGMPPGGRGRGRGQGNWGPPGGEMTFSIPTHKCGLVIGRGGENVKAINQQTGAFVEISRQLPPNGDPNFKLFVIRGSPQQIDHAKQLIEEKIEGPLCPVGPGPGGPGPAGPMGPFNPGPFNQGPPGAPPHAGGPPPHQYPPQGWGNTYPQWQPPAPHDPNKAAAAATDPNAAWAAYYSHYYQQPPGPVPGPAPAPAAPPAQGEPPQPPPTGQSDYTKAWEEYYKKIGQQPQQPGAPPQQDYTKAWEEYYKKQAQVATGGGPGAPPGSQPDYSAAWAEYYRQQAAYYGQTPGPGGPQPPPTQQGQQQASGNCHPPPPPFSFQPPATVHPALVGSAGNPFPCGVCP
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------MSDYNTGGP
------CCCCCCCCC		49.13-
2Phosphorylation------MSDYNTGGP
------CCCCCCCCC		49.1329514104
40MethylationGPPGAGDRGGGGPGG
CCCCCCCCCCCCCCC		44.7524129315
56PhosphorylationGPGGGGASGGPSQPP
CCCCCCCCCCCCCCC		47.7828576409
72UbiquitinationGGGPGIRKDAFADAV
CCCCCHHHHHHHHHH		52.03-
72MalonylationGGGPGIRKDAFADAV
CCCCCHHHHHHHHHH		52.0326320211
72AcetylationGGGPGIRKDAFADAV
CCCCCHHHHHHHHHH		52.0323806337
88AcetylationRARQIAAKIGGDAAT
HHHHHHHHHCCCHHH		32.6323806337
88UbiquitinationRARQIAAKIGGDAAT
HHHHHHHHHCCCHHH		32.6322790023
95PhosphorylationKIGGDAATTVNNNTP
HHCCCHHHCCCCCCC		32.7527087446
96PhosphorylationIGGDAATTVNNNTPD
HCCCHHHCCCCCCCC		19.2625266776
101PhosphorylationATTVNNNTPDFGFGG
HHCCCCCCCCCCCCC		26.7625521595
110AcetylationDFGFGGQKRQLEDGD
CCCCCCCCCCCCCCC		45.44109321
110UbiquitinationDFGFGGQKRQLEDGD
CCCCCCCCCCCCCCC		45.4422790023
122UbiquitinationDGDQPDSKKLASQGD
CCCCCCHHHHHHCCC		60.2227667366
123UbiquitinationGDQPDSKKLASQGDS
CCCCCHHHHHHCCCC		53.9222790023
126PhosphorylationPDSKKLASQGDSIGS
CCHHHHHHCCCCCHH		45.1725521595
130PhosphorylationKLASQGDSIGSQLGP
HHHHCCCCCHHHCCC		35.3625521595
133PhosphorylationSQGDSIGSQLGPIHP
HCCCCCHHHCCCCCC		22.1429514104
144PhosphorylationPIHPPPRTSMTEEYR
CCCCCCCCCCCCEEE		28.7328833060
145PhosphorylationIHPPPRTSMTEEYRV
CCCCCCCCCCCEEEC		25.6128833060
147PhosphorylationPPPRTSMTEEYRVPD
CCCCCCCCCEEECCC		25.9826060331
150PhosphorylationRTSMTEEYRVPDGMV
CCCCCCEEECCCCCE		15.6426060331
170UbiquitinationRGGEQINKIQQDSGC
CCHHHHHHHHHHCCC		43.4522790023
170AcetylationRGGEQINKIQQDSGC
CCHHHHHHHHHHCCC		43.4522826441
177GlutathionylationKIQQDSGCKVQISPD
HHHHHCCCEEEECCC		4.5224333276
182PhosphorylationSGCKVQISPDSGGLP
CCCEEEECCCCCCCC		12.9324925903
185PhosphorylationKVQISPDSGGLPERS
EEEECCCCCCCCCCC		37.8425521595
192PhosphorylationSGGLPERSVSLTGAP
CCCCCCCCEECCCCC		17.8825521595
194PhosphorylationGLPERSVSLTGAPES
CCCCCCEECCCCCHH		22.8126824392
196PhosphorylationPERSVSLTGAPESVQ
CCCCEECCCCCHHHH		24.6428833060
201PhosphorylationSLTGAPESVQKAKMM
ECCCCCHHHHHHHHH		28.8725777480
204UbiquitinationGAPESVQKAKMMLDD
CCCHHHHHHHHHHHH		48.0622790023
235PhosphorylationANGGQNGTVQEIMIP
CCCCCCCEEEEEEEC		26.9422705319
252AcetylationKAGLVIGKGGETIKQ
CCEEEECCCCHHHHH		53.2524494767
252UbiquitinationKAGLVIGKGGETIKQ
CCEEEECCCCHHHHH		53.25-
258UbiquitinationGKGGETIKQLQERAG
CCCCHHHHHHHHHHC		52.9922790023
267UbiquitinationLQERAGVKMILIQDG
HHHHHCCEEEEEECC		21.2122790023
275PhosphorylationMILIQDGSQNTNVDK
EEEEECCCCCCCCCC		28.6617525332
278PhosphorylationIQDGSQNTNVDKPLR
EECCCCCCCCCCCEE		29.05-
282UbiquitinationSQNTNVDKPLRIIGD
CCCCCCCCCEEECCC		41.4922790023
297S-nitrosylationPYKVQQACEMVMDIL
HHHHHHHHHHHHHHH		2.7722178444
297S-nitrosocysteinePYKVQQACEMVMDIL
HHHHHHHHHHHHHHH		2.77-
360AcetylationAGVRIQFKQDDGTGP
CCCEEEEECCCCCCH		36.1222826441
412DimethylationPGMPPGGRGRGRGQG
CCCCCCCCCCCCCCC		37.23-
412MethylationPGMPPGGRGRGRGQG
CCCCCCCCCCCCCCC		37.2324129315
414MethylationMPPGGRGRGRGQGNW
CCCCCCCCCCCCCCC		30.2124129315
414DimethylationMPPGGRGRGRGQGNW
CCCCCCCCCCCCCCC		30.21-
416MethylationPGGRGRGRGQGNWGP
CCCCCCCCCCCCCCC		32.6624129315
416DimethylationPGGRGRGRGQGNWGP
CCCCCCCCCCCCCCC		32.66-
437GlutathionylationFSIPTHKCGLVIGRG
EECCCCCCCEEECCC		3.8524333276
443MethylationKCGLVIGRGGENVKA
CCCEEECCCCCCHHH		38.5324129315
443DimethylationKCGLVIGRGGENVKA
CCCEEECCCCCCHHH		38.53-
449UbiquitinationGRGGENVKAINQQTG
CCCCCCHHHHHHCCC		55.9522790023
481PhosphorylationKLFVIRGSPQQIDHA
EEEEEECCHHHHHHH		15.0825521595
489AcetylationPQQIDHAKQLIEEKI
HHHHHHHHHHHHHHC		42.0722826441
629UbiquitinationAWEEYYKKIGQQPQQ
HHHHHHHHHCCCCCC		35.63-
647UbiquitinationPPQQDYTKAWEEYYK
CCCCHHHHHHHHHHH		45.32-
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 FUBP2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FUBP2_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 FUBP2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of FUBP2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FUBP2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-275, AND MASSSPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND MASSSPECTROMETRY.

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