FUBP2_HUMAN - dbPTM
FUBP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FUBP2_HUMAN
UniProt AC Q92945
Protein Name Far upstream element-binding protein 2
Gene Name KHSRP
Organism Homo sapiens (Human).
Sequence Length 711
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 (By similarity). 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..
Protein Sequence MSDYSTGGPPPGPPPPAGGGGGAGGAGGGPPPGPPGAGDRGGGGPGGGGPGGGSAGGPSQPPGGGGPGIRKDAFADAVQRARQIAAKIGGDAATTVNNSTPDFGFGGQKRQLEDGDQPESKKLASQGDSISSQLGPIHPPPRTSMTEEYRVPDGMVGLIIGRGGEQINKIQQDSGCKVQISPDSGGLPERSVSLTGAPESVQKAKMMLDDIVSRGRGGPPGQFHDNANGGQNGTVQEIMIPAGKAGLVIGKGGETIKQLQERAGVKMILIQDGSQNTNVDKPLRIIGDPYKVQQACEMVMDILRERDQGGFGDRNEYGSRIGGGIDVPVPRHSVGVVIGRSGEMIKKIQNDAGVRIQFKQDDGTGPEKIAHIMGPPDRCEHAARIINDLLQSLRSGPPGPPGGPGMPPGGRGRGRGQGNWGPPGGEMTFSIPTHKCGLVIGRGGENVKAINQQTGAFVEISRQLPPNGDPNFKLFIIRGSPQQIDHAKQLIEEKIEGPLCPVGPGPGGPGPAGPMGPFNPGPFNQGPPGAPPHAGGPPPHQYPPQGWGNTYPQWQPPAPHDPSKAAAAAADPNAAWAAYYSHYYQQPPGPVPGPAPAPAAPPAQGEPPQPPPTGQSDYTKAWEEYYKKIGQQPQQPGAPPQQDYTKAWEEYYKKQAQVATGGGPGAPPGSQPDYSAAWAEYYRQQAAYYGQTPGPGGPQPPPTQQGQQQAQ
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------MSDYSTGGP
------CCCCCCCCC
45.3019413330
2Phosphorylation------MSDYSTGGP
------CCCCCCCCC
45.3028188228
4Phosphorylation----MSDYSTGGPPP
----CCCCCCCCCCC
10.7921406692
5Phosphorylation---MSDYSTGGPPPG
---CCCCCCCCCCCC
26.1018491316
6Phosphorylation--MSDYSTGGPPPGP
--CCCCCCCCCCCCC
39.6718491316
25UbiquitinationGGGGGAGGAGGGPPP
CCCCCCCCCCCCCCC
22.1024816145
27UbiquitinationGGGAGGAGGGPPPGP
CCCCCCCCCCCCCCC
44.8822053931
33UbiquitinationAGGGPPPGPPGAGDR
CCCCCCCCCCCCCCC
46.9723000965
40MethylationGPPGAGDRGGGGPGG
CCCCCCCCCCCCCCC
44.75-
43UbiquitinationGAGDRGGGGPGGGGP
CCCCCCCCCCCCCCC
41.7823000965
54PhosphorylationGGGPGGGSAGGPSQP
CCCCCCCCCCCCCCC
27.3228985074
59PhosphorylationGGSAGGPSQPPGGGG
CCCCCCCCCCCCCCC
59.6027251275
59UbiquitinationGGSAGGPSQPPGGGG
CCCCCCCCCCCCCCC
59.6023000965
61UbiquitinationSAGGPSQPPGGGGPG
CCCCCCCCCCCCCCC
33.5621890473
65UbiquitinationPSQPPGGGGPGIRKD
CCCCCCCCCCCHHHH
45.0723000965
71MalonylationGGGPGIRKDAFADAV
CCCCCHHHHHHHHHH
52.0326320211
71MethylationGGGPGIRKDAFADAV
CCCCCHHHHHHHHHH
52.0354390711
71UbiquitinationGGGPGIRKDAFADAV
CCCCCHHHHHHHHHH
52.0322053931
77UbiquitinationRKDAFADAVQRARQI
HHHHHHHHHHHHHHH
8.9123000965
78UbiquitinationKDAFADAVQRARQIA
HHHHHHHHHHHHHHH
3.9923000965
87AcetylationRARQIAAKIGGDAAT
HHHHHHHHHCCCHHH
32.6323954790
87UbiquitinationRARQIAAKIGGDAAT
HHHHHHHHHCCCHHH
32.6323000965
94O-linked_GlycosylationKIGGDAATTVNNSTP
HHCCCHHHCCCCCCC
32.7530059200
94PhosphorylationKIGGDAATTVNNSTP
HHCCCHHHCCCCCCC
32.7523401153
95O-linked_GlycosylationIGGDAATTVNNSTPD
HCCCHHHCCCCCCCC
19.2630059200
95PhosphorylationIGGDAATTVNNSTPD
HCCCHHHCCCCCCCC
19.2629255136
99O-linked_GlycosylationAATTVNNSTPDFGFG
HHHCCCCCCCCCCCC
35.7930059200
99PhosphorylationAATTVNNSTPDFGFG
HHHCCCCCCCCCCCC
35.7929255136
100PhosphorylationATTVNNSTPDFGFGG
HHCCCCCCCCCCCCC
29.0629255136
107UbiquitinationTPDFGFGGQKRQLED
CCCCCCCCCCCCCCC
27.8123000965
109AcetylationDFGFGGQKRQLEDGD
CCCCCCCCCCCCCCC
45.4423749302
109MethylationDFGFGGQKRQLEDGD
CCCCCCCCCCCCCCC
45.4491365
109UbiquitinationDFGFGGQKRQLEDGD
CCCCCCCCCCCCCCC
45.4423000965
109 (in isoform 1)Ubiquitination-45.4421890473
113UbiquitinationGGQKRQLEDGDQPES
CCCCCCCCCCCCHHH
52.1623000965
120PhosphorylationEDGDQPESKKLASQG
CCCCCHHHHHHHHCC
41.6025159151
121AcetylationDGDQPESKKLASQGD
CCCCHHHHHHHHCCC
50.5825953088
121SumoylationDGDQPESKKLASQGD
CCCCHHHHHHHHCCC
50.5825114211
121UbiquitinationDGDQPESKKLASQGD
CCCCHHHHHHHHCCC
50.5823000965
122AcetylationGDQPESKKLASQGDS
CCCHHHHHHHHCCCC
59.5730584043
122UbiquitinationGDQPESKKLASQGDS
CCCHHHHHHHHCCCC
59.5723000965
125PhosphorylationPESKKLASQGDSISS
HHHHHHHHCCCCHHH
45.1725159151
125UbiquitinationPESKKLASQGDSISS
HHHHHHHHCCCCHHH
45.1724816145
129PhosphorylationKLASQGDSISSQLGP
HHHHCCCCHHHHCCC
31.0625159151
131PhosphorylationASQGDSISSQLGPIH
HHCCCCHHHHCCCCC
18.9125159151
132PhosphorylationSQGDSISSQLGPIHP
HCCCCHHHHCCCCCC
27.9617525332
133UbiquitinationQGDSISSQLGPIHPP
CCCCHHHHCCCCCCC
43.5823000965
137UbiquitinationISSQLGPIHPPPRTS
HHHHCCCCCCCCCCC
7.8523000965
143PhosphorylationPIHPPPRTSMTEEYR
CCCCCCCCCCCCEEE
28.7330108239
144O-linked_GlycosylationIHPPPRTSMTEEYRV
CCCCCCCCCCCEEEC
25.6130059200
144PhosphorylationIHPPPRTSMTEEYRV
CCCCCCCCCCCEEEC
25.6121815630
146PhosphorylationPPPRTSMTEEYRVPD
CCCCCCCCCEEECCC
25.9828857561
149PhosphorylationRTSMTEEYRVPDGMV
CCCCCCEEECCCCCE
15.6428985074
159UbiquitinationPDGMVGLIIGRGGEQ
CCCCEEEEECCCHHH
2.3023000965
161UbiquitinationGMVGLIIGRGGEQIN
CCEEEEECCCHHHHH
18.3921890473
162MethylationMVGLIIGRGGEQINK
CEEEEECCCHHHHHH
39.26115480997
169AcetylationRGGEQINKIQQDSGC
CCHHHHHHHHHHCCC
43.4525953088
169UbiquitinationRGGEQINKIQQDSGC
CCHHHHHHHHHHCCC
43.4533845483
174PhosphorylationINKIQQDSGCKVQIS
HHHHHHHCCCEEEEC
41.5820068231
176S-nitrosocysteineKIQQDSGCKVQISPD
HHHHHCCCEEEECCC
4.52-
176GlutathionylationKIQQDSGCKVQISPD
HHHHHCCCEEEECCC
4.5222555962
176S-nitrosylationKIQQDSGCKVQISPD
HHHHHCCCEEEECCC
4.5220140087
1772-HydroxyisobutyrylationIQQDSGCKVQISPDS
HHHHCCCEEEECCCC
40.47-
177AcetylationIQQDSGCKVQISPDS
HHHHCCCEEEECCCC
40.4725953088
177UbiquitinationIQQDSGCKVQISPDS
HHHHCCCEEEECCCC
40.4723000965
181PhosphorylationSGCKVQISPDSGGLP
CCCEEEECCCCCCCC
12.9319664994
184PhosphorylationKVQISPDSGGLPERS
EEEECCCCCCCCCCC
37.8429255136
191O-linked_GlycosylationSGGLPERSVSLTGAP
CCCCCCCCEECCCCC
17.8830059200
191PhosphorylationSGGLPERSVSLTGAP
CCCCCCCCEECCCCC
17.8830266825
193PhosphorylationGLPERSVSLTGAPES
CCCCCCEECCCCCHH
22.8130266825
195PhosphorylationPERSVSLTGAPESVQ
CCCCEECCCCCHHHH
24.6430266825
200PhosphorylationSLTGAPESVQKAKMM
ECCCCCHHHHHHHHH
28.8730266825
203AcetylationGAPESVQKAKMMLDD
CCCHHHHHHHHHHHH
48.0625953088
203UbiquitinationGAPESVQKAKMMLDD
CCCHHHHHHHHHHHH
48.0623000965
205UbiquitinationPESVQKAKMMLDDIV
CHHHHHHHHHHHHHH
31.7023000965
205 (in isoform 1)Ubiquitination-31.7021890473
206SulfoxidationESVQKAKMMLDDIVS
HHHHHHHHHHHHHHH
3.7321406390
207SulfoxidationSVQKAKMMLDDIVSR
HHHHHHHHHHHHHHC
3.5128183972
207UbiquitinationSVQKAKMMLDDIVSR
HHHHHHHHHHHHHHC
3.5123000965
213UbiquitinationMMLDDIVSRGRGGPP
HHHHHHHHCCCCCCC
29.3823000965
215UbiquitinationLDDIVSRGRGGPPGQ
HHHHHHCCCCCCCCC
25.6924816145
234PhosphorylationANGGQNGTVQEIMIP
CCCCCCCEEEEEEEC
26.94-
237UbiquitinationGQNGTVQEIMIPAGK
CCCCEEEEEEECCCC
30.1323000965
251AcetylationKAGLVIGKGGETIKQ
CCEEEECCCCHHHHH
53.2525953088
251UbiquitinationKAGLVIGKGGETIKQ
CCEEEECCCCHHHHH
53.2523000965
251 (in isoform 1)Ubiquitination-53.2521890473
255PhosphorylationVIGKGGETIKQLQER
EECCCCHHHHHHHHH
36.4322817900
2572-HydroxyisobutyrylationGKGGETIKQLQERAG
CCCCHHHHHHHHHHC
52.99-
257AcetylationGKGGETIKQLQERAG
CCCCHHHHHHHHHHC
52.9925953088
257UbiquitinationGKGGETIKQLQERAG
CCCCHHHHHHHHHHC
52.9923000965
257 (in isoform 1)Ubiquitination-52.9921890473
266AcetylationLQERAGVKMILIQDG
HHHHHCCEEEEEECC
21.2125953088
267SulfoxidationQERAGVKMILIQDGS
HHHHCCEEEEEECCC
2.5428183972
274PhosphorylationMILIQDGSQNTNVDK
EEEEECCCCCCCCCC
28.6623401153
277PhosphorylationIQDGSQNTNVDKPLR
EECCCCCCCCCCCEE
29.0530183078
2812-HydroxyisobutyrylationSQNTNVDKPLRIIGD
CCCCCCCCCEEECCC
41.49-
281AcetylationSQNTNVDKPLRIIGD
CCCCCCCCCEEECCC
41.4925953088
281UbiquitinationSQNTNVDKPLRIIGD
CCCCCCCCCEEECCC
41.4923000965
296GlutathionylationPYKVQQACEMVMDIL
HHHHHHHHHHHHHHH
2.7722555962
298SulfoxidationKVQQACEMVMDILRE
HHHHHHHHHHHHHHH
2.8121406390
303UbiquitinationCEMVMDILRERDQGG
HHHHHHHHHHHHCCC
3.9724816145
304UbiquitinationEMVMDILRERDQGGF
HHHHHHHHHHHCCCC
36.9223000965
314MethylationDQGGFGDRNEYGSRI
HCCCCCCCCCCCCCC
37.95115480949
315UbiquitinationQGGFGDRNEYGSRIG
CCCCCCCCCCCCCCC
52.1324816145
317PhosphorylationGFGDRNEYGSRIGGG
CCCCCCCCCCCCCCC
24.7728152594
319PhosphorylationGDRNEYGSRIGGGID
CCCCCCCCCCCCCCC
21.5928152594
333PhosphorylationDVPVPRHSVGVVIGR
CCCCCHHHEEEEECC
23.1124719451
340MethylationSVGVVIGRSGEMIKK
HEEEEECCCHHHHHH
30.29115480957
341PhosphorylationVGVVIGRSGEMIKKI
EEEEECCCHHHHHHH
33.6124719451
344UbiquitinationVIGRSGEMIKKIQND
EECCCHHHHHHHHHC
6.5821890473
3462-HydroxyisobutyrylationGRSGEMIKKIQNDAG
CCCHHHHHHHHHCCC
42.38-
346AcetylationGRSGEMIKKIQNDAG
CCCHHHHHHHHHCCC
42.3825953088
3472-HydroxyisobutyrylationRSGEMIKKIQNDAGV
CCHHHHHHHHHCCCC
38.30-
347UbiquitinationRSGEMIKKIQNDAGV
CCHHHHHHHHHCCCC
38.3024816145
355MethylationIQNDAGVRIQFKQDD
HHHCCCCEEEEECCC
18.97-
359SumoylationAGVRIQFKQDDGTGP
CCCEEEEECCCCCCH
36.12-
3592-HydroxyisobutyrylationAGVRIQFKQDDGTGP
CCCEEEEECCCCCCH
36.12-
359AcetylationAGVRIQFKQDDGTGP
CCCEEEEECCCCCCH
36.1225953088
359SumoylationAGVRIQFKQDDGTGP
CCCEEEEECCCCCCH
36.12-
359UbiquitinationAGVRIQFKQDDGTGP
CCCEEEEECCCCCCH
36.1233845483
368AcetylationDDGTGPEKIAHIMGP
CCCCCHHHHHHHHCC
48.6125953088
373SulfoxidationPEKIAHIMGPPDRCE
HHHHHHHHCCHHHHH
4.7821406390
378MethylationHIMGPPDRCEHAARI
HHHCCHHHHHHHHHH
33.23115480965
379GlutathionylationIMGPPDRCEHAARII
HHCCHHHHHHHHHHH
6.1522555962
394MethylationNDLLQSLRSGPPGPP
HHHHHHHHCCCCCCC
44.83115480973
395PhosphorylationDLLQSLRSGPPGPPG
HHHHHHHCCCCCCCC
62.0328961369
404UbiquitinationPPGPPGGPGMPPGGR
CCCCCCCCCCCCCCC
41.6523000965
406SulfoxidationGPPGGPGMPPGGRGR
CCCCCCCCCCCCCCC
3.9921406390
411DimethylationPGMPPGGRGRGRGQG
CCCCCCCCCCCCCCC
37.23-
411MethylationPGMPPGGRGRGRGQG
CCCCCCCCCCCCCCC
37.2324129315
413DimethylationMPPGGRGRGRGQGNW
CCCCCCCCCCCCCCC
30.21-
413MethylationMPPGGRGRGRGQGNW
CCCCCCCCCCCCCCC
30.2124129315
415DimethylationPGGRGRGRGQGNWGP
CCCCCCCCCCCCCCC
32.66-
415MethylationPGGRGRGRGQGNWGP
CCCCCCCCCCCCCCC
32.6624129315
428PhosphorylationGPPGGEMTFSIPTHK
CCCCCEEEEECCCCC
15.2130257219
430PhosphorylationPGGEMTFSIPTHKCG
CCCEEEEECCCCCCC
20.6330257219
433PhosphorylationEMTFSIPTHKCGLVI
EEEEECCCCCCCEEE
32.0930257219
436S-nitrosocysteineFSIPTHKCGLVIGRG
EECCCCCCCEEECCC
3.85-
436GlutathionylationFSIPTHKCGLVIGRG
EECCCCCCCEEECCC
3.8522555962
436S-nitrosylationFSIPTHKCGLVIGRG
EECCCCCCCEEECCC
3.8520140087
442DimethylationKCGLVIGRGGENVKA
CCCEEECCCCCCHHH
38.53-
442MethylationKCGLVIGRGGENVKA
CCCEEECCCCCCHHH
38.5324129315
444UbiquitinationGLVIGRGGENVKAIN
CEEECCCCCCHHHHH
23.1921890473
448AcetylationGRGGENVKAINQQTG
CCCCCCHHHHHHCCC
55.9526051181
448MethylationGRGGENVKAINQQTG
CCCCCCHHHHHHCCC
55.9554390695
448UbiquitinationGRGGENVKAINQQTG
CCCCCCHHHHHHCCC
55.9523000965
461PhosphorylationTGAFVEISRQLPPNG
CCCEEEEECCCCCCC
10.64-
478MethylationNFKLFIIRGSPQQID
CCEEEEEECCHHHHH
34.42115480989
480PhosphorylationKLFIIRGSPQQIDHA
EEEEEECCHHHHHHH
15.0826846344
483UbiquitinationIIRGSPQQIDHAKQL
EEECCHHHHHHHHHH
46.6022817900
484UbiquitinationIRGSPQQIDHAKQLI
EECCHHHHHHHHHHH
3.3622817900
4882-HydroxyisobutyrylationPQQIDHAKQLIEEKI
HHHHHHHHHHHHHHC
42.07-
488AcetylationPQQIDHAKQLIEEKI
HHHHHHHHHHHHHHC
42.0726051181
488UbiquitinationPQQIDHAKQLIEEKI
HHHHHHHHHHHHHHC
42.0722817900
488 (in isoform 1)Ubiquitination-42.0721890473
502UbiquitinationIEGPLCPVGPGPGGP
CCCCCCCCCCCCCCC
16.4322817900
509UbiquitinationVGPGPGGPGPAGPMG
CCCCCCCCCCCCCCC
52.0522817900
510UbiquitinationGPGPGGPGPAGPMGP
CCCCCCCCCCCCCCC
28.1522817900
577UbiquitinationADPNAAWAAYYSHYY
CCCCHHHHHHHHHHC
4.8522817900
583PhosphorylationWAAYYSHYYQQPPGP
HHHHHHHHCCCCCCC
9.3122817900
583UbiquitinationWAAYYSHYYQQPPGP
HHHHHHHHCCCCCCC
9.3122817900
584UbiquitinationAAYYSHYYQQPPGPV
HHHHHHHCCCCCCCC
8.6822817900
585UbiquitinationAYYSHYYQQPPGPVP
HHHHHHCCCCCCCCC
41.9822817900
602UbiquitinationAPAPAAPPAQGEPPQ
CCCCCCCCCCCCCCC
32.2722817900
609UbiquitinationPAQGEPPQPPPTGQS
CCCCCCCCCCCCCCC
74.0722817900
610UbiquitinationAQGEPPQPPPTGQSD
CCCCCCCCCCCCCCH
42.4822817900
625PhosphorylationYTKAWEEYYKKIGQQ
HHHHHHHHHHHHCCC
14.7428152594
626PhosphorylationTKAWEEYYKKIGQQP
HHHHHHHHHHHCCCC
14.7528152594
627AcetylationKAWEEYYKKIGQQPQ
HHHHHHHHHHCCCCC
36.6919608861
627MalonylationKAWEEYYKKIGQQPQ
HHHHHHHHHHCCCCC
36.6926320211
627UbiquitinationKAWEEYYKKIGQQPQ
HHHHHHHHHHCCCCC
36.6927667366
628UbiquitinationAWEEYYKKIGQQPQQ
HHHHHHHHHCCCCCC
35.6321906983
628 (in isoform 1)Ubiquitination-35.6321890473
644PhosphorylationGAPPQQDYTKAWEEY
CCCCCCHHHHHHHHH
13.0522817900
646AcetylationPPQQDYTKAWEEYYK
CCCCHHHHHHHHHHH
45.3226051181
646UbiquitinationPPQQDYTKAWEEYYK
CCCCHHHHHHHHHHH
45.3221906983
646 (in isoform 1)Ubiquitination-45.3221890473
651PhosphorylationYTKAWEEYYKKQAQV
HHHHHHHHHHHHHCH
14.7428152594
652PhosphorylationTKAWEEYYKKQAQVA
HHHHHHHHHHHHCHH
18.2628152594
653AcetylationKAWEEYYKKQAQVAT
HHHHHHHHHHHCHHC
37.1927452117
653MalonylationKAWEEYYKKQAQVAT
HHHHHHHHHHHCHHC
37.1926320211
653UbiquitinationKAWEEYYKKQAQVAT
HHHHHHHHHHHCHHC
37.1922817900
654UbiquitinationAWEEYYKKQAQVATG
HHHHHHHHHHCHHCC
34.4422817900
654 (in isoform 1)Ubiquitination-34.4421890473
670O-linked_GlycosylationGPGAPPGSQPDYSAA
CCCCCCCCCCCHHHH
44.2930059200
670PhosphorylationGPGAPPGSQPDYSAA
CCCCCCCCCCCHHHH
44.2917525332
674PhosphorylationPPGSQPDYSAAWAEY
CCCCCCCHHHHHHHH
13.5917360941
681PhosphorylationYSAAWAEYYRQQAAY
HHHHHHHHHHHHHHH
9.01-
682PhosphorylationSAAWAEYYRQQAAYY
HHHHHHHHHHHHHHH
8.08-
688PhosphorylationYYRQQAAYYGQTPGP
HHHHHHHHHCCCCCC
15.9020090780
689PhosphorylationYRQQAAYYGQTPGPG
HHHHHHHHCCCCCCC
9.6828555341
692PhosphorylationQAAYYGQTPGPGGPQ
HHHHHCCCCCCCCCC
26.3328555341

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
193SPhosphorylationKinaseAKT1P31749
PSP
193SPhosphorylationKinaseAKT2P31751
PSP
274SPhosphorylationKinaseATMQ13315
PSP
317YPhosphorylationKinaseSRCP12931
PSP
583YPhosphorylationKinaseSRCP12931
PSP
670SPhosphorylationKinaseATMQ13315
PSP
688YPhosphorylationKinaseSRCP12931
PSP
692TPhosphorylationKinaseMAPK14Q16539
GPS
-KUbiquitinationE3 ubiquitin ligaseKLHL12Q53G59
PMID:27899653:32032490

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
193SPhosphorylation

23186163

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_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EXOS2_HUMANEXOSC2physical
15175153
PARN_HUMANPARNphysical
15175153
PTBP2_HUMANPTBP2physical
11003644
ROA1_HUMANHNRNPA1physical
11003644
HNRH1_HUMANHNRNPH1physical
11003644
GARS_HUMANGARSphysical
22863883
GFPT1_HUMANGFPT1physical
22863883
HNRPD_HUMANHNRNPDphysical
22863883
NP1L4_HUMANNAP1L4physical
22863883
CHCH2_HUMANCHCHD2physical
26344197
CPSF6_HUMANCPSF6physical
26344197
CPSF7_HUMANCPSF7physical
26344197
FUBP3_HUMANFUBP3physical
26344197
HTRA2_HUMANHTRA2physical
26344197
KYNU_HUMANKYNUphysical
26344197
NUP50_HUMANNUP50physical
26344197
PRDX2_HUMANPRDX2physical
26344197
PRDX5_HUMANPRDX5physical
26344197
SIN3A_HUMANSIN3Aphysical
26344197
SMRC1_HUMANSMARCC1physical
26344197
SMRC2_HUMANSMARCC2physical
26344197
SYMPK_HUMANSYMPKphysical
26344197
KLH12_HUMANKLHL12physical
27899653
CUL3_HUMANCUL3physical
27899653
RNC_HUMANDROSHAphysical
29020972
DGCR8_HUMANDGCR8physical
29020972

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FUBP2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-87, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Phosphorylation-mediated unfolding of a KH domain regulates KSRPlocalization via 14-3-3 binding.";
Diaz-Moreno I., Hollingworth D., Frenkiel T.A., Kelly G., Martin S.,Howell S., Garcia-Mayoral M., Gherzi R., Briata P., Ramos A.;
Nat. Struct. Mol. Biol. 16:238-246(2009).
Cited for: STRUCTURE BY NMR OF 130-218 AND 221-305, PHOSPHORYLATION AT SER-193,AND SUBCELLULAR LOCATION.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-184, ANDMASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-181; SER-274 ANDSER-480, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6; THR-100; SER-181 ANDSER-184, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-100; SER-181; SER-274AND SER-480, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND MASSSPECTROMETRY.
"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-132; SER-274 ANDSER-670, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-480, ANDMASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-100, AND MASSSPECTROMETRY.

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