SF3B2_HUMAN - dbPTM
SF3B2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SF3B2_HUMAN
UniProt AC Q13435
Protein Name Splicing factor 3B subunit 2
Gene Name SF3B2
Organism Homo sapiens (Human).
Sequence Length 895
Subcellular Localization Nucleus . Nucleus speckle .
Protein Description Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex. [PubMed: 27720643 SF3B complex is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA]
Protein Sequence MATEHPEPPKAELQLPPPPPPGHYGAWAAQELQAKLAEIGAPIQGNREELVERLQSYTRQTGIVLNRPVLRGEDGDKAAPPPMSAQLPGIPMPPPPLGLPPLQPPPPPPPPPPGLGLGFPMAHPPNLGPPPPLRVGEPVALSEEERLKLAQQQAALLMQQEERAKQQGDHSLKEHELLEQQKRAAVLLEQERQQEIAKMGTPVPRPPQDMGQIGVRTPLGPRVAAPVGPVGPTPTVLPMGAPVPRPRGPPPPPGDENREMDDPSVGPKIPQALEKILQLKESRQEEMNSQQEEEEMETDARSSLGQSASETEEDTVSVSKKEKNRKRRNRKKKKKPQRVRGVSSESSGDREKDSTRSRGSDSPAADVEIEYVTEEPEIYEPNFIFFKRIFEAFKLTDDVKKEKEKEPEKLDKLENSAAPKKKGFEEEHKDSDDDSSDDEQEKKPEAPKLSKKKLRRMNRFTVAELKQLVARPDVVEMHDVTAQDPKLLVHLKATRNSVPVPRHWCFKRKYLQGKRGIEKPPFELPDFIKRTGIQEMREALQEKEEQKTMKSKMREKVRPKMGKIDIDYQKLHDAFFKWQTKPKLTIHGDLYYEGKEFETRLKEKKPGDLSDELRISLGMPVGPNAHKVPPPWLIAMQRYGPPPSYPNLKIPGLNSPIPESCSFGYHAGGWGKPPVDETGKPLYGDVFGTNAAEFQTKTEEEEIDRTPWGELEPSDEESSEEEEEEESDEDKPDETGFITPADSGLITPGGFSSVPAGMETPELIELRKKKIEEAMDGSETPQLFTVLPEKRTATVGGAMMGSTHIYDMSTVMSRKGPAPELQGVEVALAPEELELDPMAMTQKYEEHVREQQAQVEKEDFSDMVAEHAAKQKQKKRKAQPQDSRGGSKKYKEFKF
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
10SumoylationTEHPEPPKAELQLPP
CCCCCCCCCCCCCCC
66.2728112733
71MethylationVLNRPVLRGEDGDKA
EECCCEECCCCCCCC
46.84115916649
142PhosphorylationVGEPVALSEEERLKL
CCCCCCCCHHHHHHH
32.9721815630
148AcetylationLSEEERLKLAQQQAA
CCHHHHHHHHHHHHH
48.2625953088
148UbiquitinationLSEEERLKLAQQQAA
CCHHHHHHHHHHHHH
48.2632015554
158SulfoxidationQQQAALLMQQEERAK
HHHHHHHHHHHHHHH
3.9321406390
171PhosphorylationAKQQGDHSLKEHELL
HHHHCCCCHHHHHHH
45.9728555341
173UbiquitinationQQGDHSLKEHELLEQ
HHCCCCHHHHHHHHH
61.1032015554
178PhosphorylationSLKEHELLEQQKRAA
CHHHHHHHHHHHHHH
5.2018669648
182UbiquitinationHELLEQQKRAAVLLE
HHHHHHHHHHHHHHH
43.6432015554
192MethylationAVLLEQERQQEIAKM
HHHHHHHHHHHHHHC
43.08115916629
194PhosphorylationLLEQERQQEIAKMGT
HHHHHHHHHHHHCCC
50.7318669648
197UbiquitinationQERQQEIAKMGTPVP
HHHHHHHHHCCCCCC
8.6024816145
198UbiquitinationERQQEIAKMGTPVPR
HHHHHHHHCCCCCCC
43.4524816145
201PhosphorylationQEIAKMGTPVPRPPQ
HHHHHCCCCCCCCCC
20.0221712546
205DimethylationKMGTPVPRPPQDMGQ
HCCCCCCCCCCCCCC
56.62-
205MethylationKMGTPVPRPPQDMGQ
HCCCCCCCCCCCCCC
56.6254559177
216DimethylationDMGQIGVRTPLGPRV
CCCCCCCCCCCCCCC
25.97-
216MethylationDMGQIGVRTPLGPRV
CCCCCCCCCCCCCCC
25.9730761005
217PhosphorylationMGQIGVRTPLGPRVA
CCCCCCCCCCCCCCC
22.0625159151
222DimethylationVRTPLGPRVAAPVGP
CCCCCCCCCCCCCCC
28.98-
222MethylationVRTPLGPRVAAPVGP
CCCCCCCCCCCCCCC
28.9824129315
233PhosphorylationPVGPVGPTPTVLPMG
CCCCCCCCCCEECCC
26.1828555341
239SulfoxidationPTPTVLPMGAPVPRP
CCCCEECCCCCCCCC
6.6421406390
245DimethylationPMGAPVPRPRGPPPP
CCCCCCCCCCCCCCC
33.51-
245MethylationPMGAPVPRPRGPPPP
CCCCCCCCCCCCCCC
33.5124129315
247DimethylationGAPVPRPRGPPPPPG
CCCCCCCCCCCCCCC
72.09-
247MethylationGAPVPRPRGPPPPPG
CCCCCCCCCCCCCCC
72.0924129315
258MethylationPPPGDENREMDDPSV
CCCCCCCCCCCCCCC
38.27115916633
260SulfoxidationPGDENREMDDPSVGP
CCCCCCCCCCCCCCC
6.8121406390
264PhosphorylationNREMDDPSVGPKIPQ
CCCCCCCCCCCCHHH
46.8528555341
266PhosphorylationEMDDPSVGPKIPQAL
CCCCCCCCCCHHHHH
23.3218669648
266UbiquitinationEMDDPSVGPKIPQAL
CCCCCCCCCCHHHHH
23.3224816145
267UbiquitinationMDDPSVGPKIPQALE
CCCCCCCCCHHHHHH
29.2824816145
268AcetylationDDPSVGPKIPQALEK
CCCCCCCCHHHHHHH
62.1826051181
268MethylationDDPSVGPKIPQALEK
CCCCCCCCHHHHHHH
62.18115916621
268UbiquitinationDDPSVGPKIPQALEK
CCCCCCCCHHHHHHH
62.1824816145
273UbiquitinationGPKIPQALEKILQLK
CCCHHHHHHHHHHHH
6.0821890473
274UbiquitinationPKIPQALEKILQLKE
CCHHHHHHHHHHHHH
40.8621890473
275UbiquitinationKIPQALEKILQLKES
CHHHHHHHHHHHHHH
49.9521890473
275UbiquitinationKIPQALEKILQLKES
CHHHHHHHHHHHHHH
49.9521890473
275AcetylationKIPQALEKILQLKES
CHHHHHHHHHHHHHH
49.9519608861
275UbiquitinationKIPQALEKILQLKES
CHHHHHHHHHHHHHH
49.9523000965
275UbiquitinationKIPQALEKILQLKES
CHHHHHHHHHHHHHH
49.9521890473
275UbiquitinationKIPQALEKILQLKES
CHHHHHHHHHHHHHH
49.9521890473
275UbiquitinationKIPQALEKILQLKES
CHHHHHHHHHHHHHH
49.9521890473
278UbiquitinationQALEKILQLKESRQE
HHHHHHHHHHHHHHH
54.7023000965
279PhosphorylationALEKILQLKESRQEE
HHHHHHHHHHHHHHH
6.2718669648
279UbiquitinationALEKILQLKESRQEE
HHHHHHHHHHHHHHH
6.2723000965
280UbiquitinationLEKILQLKESRQEEM
HHHHHHHHHHHHHHH
40.4621890473
280UbiquitinationLEKILQLKESRQEEM
HHHHHHHHHHHHHHH
40.4621890473
280AcetylationLEKILQLKESRQEEM
HHHHHHHHHHHHHHH
40.4625953088
280PhosphorylationLEKILQLKESRQEEM
HHHHHHHHHHHHHHH
40.4618669648
280SumoylationLEKILQLKESRQEEM
HHHHHHHHHHHHHHH
40.4628112733
280UbiquitinationLEKILQLKESRQEEM
HHHHHHHHHHHHHHH
40.4623000965
280UbiquitinationLEKILQLKESRQEEM
HHHHHHHHHHHHHHH
40.4621890473
280UbiquitinationLEKILQLKESRQEEM
HHHHHHHHHHHHHHH
40.4621890473
280UbiquitinationLEKILQLKESRQEEM
HHHHHHHHHHHHHHH
40.4621890473
282PhosphorylationKILQLKESRQEEMNS
HHHHHHHHHHHHHHH
37.3622199227
284PhosphorylationLQLKESRQEEMNSQQ
HHHHHHHHHHHHHHH
61.3518669648
286PhosphorylationLKESRQEEMNSQQEE
HHHHHHHHHHHHHHH
35.0118669648
287SulfoxidationKESRQEEMNSQQEEE
HHHHHHHHHHHHHHH
6.0228465586
288PhosphorylationESRQEEMNSQQEEEE
HHHHHHHHHHHHHHH
39.6918669648
289PhosphorylationSRQEEMNSQQEEEEM
HHHHHHHHHHHHHHH
31.7517525332
296SulfoxidationSQQEEEEMETDARSS
HHHHHHHHHHHHHHH
8.3228465586
298PhosphorylationQEEEEMETDARSSLG
HHHHHHHHHHHHHHC
33.3821815630
302PhosphorylationEMETDARSSLGQSAS
HHHHHHHHHHCCCCC
31.4725159151
303PhosphorylationMETDARSSLGQSASE
HHHHHHHHHCCCCCC
30.8523927012
307PhosphorylationARSSLGQSASETEED
HHHHHCCCCCCCCCC
31.7819664994
309PhosphorylationSSLGQSASETEEDTV
HHHCCCCCCCCCCCC
50.7419664994
311PhosphorylationLGQSASETEEDTVSV
HCCCCCCCCCCCCCC
42.0329255136
315PhosphorylationASETEEDTVSVSKKE
CCCCCCCCCCCCHHH
20.2625463755
317PhosphorylationETEEDTVSVSKKEKN
CCCCCCCCCCHHHHH
23.8325159151
319PhosphorylationEEDTVSVSKKEKNRK
CCCCCCCCHHHHHHH
30.4223927012
319UbiquitinationEEDTVSVSKKEKNRK
CCCCCCCCHHHHHHH
30.4224816145
320PhosphorylationEDTVSVSKKEKNRKR
CCCCCCCHHHHHHHH
63.9017287340
320UbiquitinationEDTVSVSKKEKNRKR
CCCCCCCHHHHHHHH
63.9024816145
321UbiquitinationDTVSVSKKEKNRKRR
CCCCCCHHHHHHHHH
67.4324816145
332UbiquitinationRKRRNRKKKKKPQRV
HHHHHHHHCCCCHHH
67.5924816145
333UbiquitinationKRRNRKKKKKPQRVR
HHHHHHHCCCCHHHC
69.8924816145
334UbiquitinationRRNRKKKKKPQRVRG
HHHHHHCCCCHHHCC
77.7924816145
337PhosphorylationRKKKKKPQRVRGVSS
HHHCCCCHHHCCCCC
66.4417287340
340MethylationKKKPQRVRGVSSESS
CCCCHHHCCCCCCCC
41.82115916637
343PhosphorylationPQRVRGVSSESSGDR
CHHHCCCCCCCCCCC
31.0823401153
344PhosphorylationQRVRGVSSESSGDRE
HHHCCCCCCCCCCCC
38.8127273156
346PhosphorylationVRGVSSESSGDREKD
HCCCCCCCCCCCCCC
41.3823401153
347PhosphorylationRGVSSESSGDREKDS
CCCCCCCCCCCCCCC
40.4326055452
350UbiquitinationSSESSGDREKDSTRS
CCCCCCCCCCCCCCC
57.2922817900
351UbiquitinationSESSGDREKDSTRSR
CCCCCCCCCCCCCCC
66.9922817900
352AcetylationESSGDREKDSTRSRG
CCCCCCCCCCCCCCC
58.8525953088
352UbiquitinationESSGDREKDSTRSRG
CCCCCCCCCCCCCCC
58.8522817900
357PhosphorylationREKDSTRSRGSDSPA
CCCCCCCCCCCCCCC
40.8725159151
360PhosphorylationDSTRSRGSDSPAADV
CCCCCCCCCCCCCCE
33.5325159151
362PhosphorylationTRSRGSDSPAADVEI
CCCCCCCCCCCCEEE
20.3825159151
370UbiquitinationPAADVEIEYVTEEPE
CCCCEEEEEECCCCC
22.0521890473
371PhosphorylationAADVEIEYVTEEPEI
CCCEEEEEECCCCCC
20.5224043423
373PhosphorylationDVEIEYVTEEPEIYE
CEEEEEECCCCCCCC
33.4624043423
379PhosphorylationVTEEPEIYEPNFIFF
ECCCCCCCCCCCCHH
24.5420873877
385UbiquitinationIYEPNFIFFKRIFEA
CCCCCCCHHHHHHHH
5.3021963094
386UbiquitinationYEPNFIFFKRIFEAF
CCCCCCHHHHHHHHH
4.4321963094
387UbiquitinationEPNFIFFKRIFEAFK
CCCCCHHHHHHHHHH
33.5621963094
390UbiquitinationFIFFKRIFEAFKLTD
CCHHHHHHHHHHCCH
6.8621890473
392UbiquitinationFFKRIFEAFKLTDDV
HHHHHHHHHHCCHHH
8.9823000965
393UbiquitinationFKRIFEAFKLTDDVK
HHHHHHHHHCCHHHH
5.4023000965
394AcetylationKRIFEAFKLTDDVKK
HHHHHHHHCCHHHHH
58.4825953088
394UbiquitinationKRIFEAFKLTDDVKK
HHHHHHHHCCHHHHH
58.4823000965
396PhosphorylationIFEAFKLTDDVKKEK
HHHHHHCCHHHHHHH
30.6428555341
396UbiquitinationIFEAFKLTDDVKKEK
HHHHHHCCHHHHHHH
30.6421890473
398UbiquitinationEAFKLTDDVKKEKEK
HHHHCCHHHHHHHHH
49.2323000965
399UbiquitinationAFKLTDDVKKEKEKE
HHHCCHHHHHHHHHC
12.1223000965
400SumoylationFKLTDDVKKEKEKEP
HHCCHHHHHHHHHCH
63.31-
4002-HydroxyisobutyrylationFKLTDDVKKEKEKEP
HHCCHHHHHHHHHCH
63.31-
400AcetylationFKLTDDVKKEKEKEP
HHCCHHHHHHHHHCH
63.3125953088
400SumoylationFKLTDDVKKEKEKEP
HHCCHHHHHHHHHCH
63.3128112733
400UbiquitinationFKLTDDVKKEKEKEP
HHCCHHHHHHHHHCH
63.3123000965
401UbiquitinationKLTDDVKKEKEKEPE
HCCHHHHHHHHHCHH
74.0822817900
402UbiquitinationLTDDVKKEKEKEPEK
CCHHHHHHHHHCHHH
61.8122817900
403UbiquitinationTDDVKKEKEKEPEKL
CHHHHHHHHHCHHHH
80.9122817900
404UbiquitinationDDVKKEKEKEPEKLD
HHHHHHHHHCHHHHH
64.8422817900
405UbiquitinationDVKKEKEKEPEKLDK
HHHHHHHHCHHHHHH
84.9822817900
407UbiquitinationKKEKEKEPEKLDKLE
HHHHHHCHHHHHHHC
55.9023000965
408PhosphorylationKEKEKEPEKLDKLEN
HHHHHCHHHHHHHCC
68.3018669648
408UbiquitinationKEKEKEPEKLDKLEN
HHHHHCHHHHHHHCC
68.3023000965
409UbiquitinationEKEKEPEKLDKLENS
HHHHCHHHHHHHCCC
73.1023000965
410UbiquitinationKEKEPEKLDKLENSA
HHHCHHHHHHHCCCC
7.1923000965
411UbiquitinationEKEPEKLDKLENSAA
HHCHHHHHHHCCCCC
65.6423000965
412SumoylationKEPEKLDKLENSAAP
HCHHHHHHHCCCCCC
69.04-
412AcetylationKEPEKLDKLENSAAP
HCHHHHHHHCCCCCC
69.0423236377
412PhosphorylationKEPEKLDKLENSAAP
HCHHHHHHHCCCCCC
69.0418669648
412SumoylationKEPEKLDKLENSAAP
HCHHHHHHHCCCCCC
69.0428112733
412UbiquitinationKEPEKLDKLENSAAP
HCHHHHHHHCCCCCC
69.0423000965
413PhosphorylationEPEKLDKLENSAAPK
CHHHHHHHCCCCCCC
8.2218669648
416PhosphorylationKLDKLENSAAPKKKG
HHHHHCCCCCCCCCC
19.2129255136
4202-HydroxyisobutyrylationLENSAAPKKKGFEEE
HCCCCCCCCCCCHHH
63.49-
420UbiquitinationLENSAAPKKKGFEEE
HCCCCCCCCCCCHHH
63.4933845483
431PhosphorylationFEEEHKDSDDDSSDD
CHHHCCCCCCCCCHH
47.9826846344
433UbiquitinationEEHKDSDDDSSDDEQ
HHCCCCCCCCCHHHH
62.7421890473
435PhosphorylationHKDSDDDSSDDEQEK
CCCCCCCCCHHHHHH
42.5326846344
436PhosphorylationKDSDDDSSDDEQEKK
CCCCCCCCHHHHHHC
56.9526846344
441UbiquitinationDSSDDEQEKKPEAPK
CCCHHHHHHCCCCCC
62.0827667366
442UbiquitinationSSDDEQEKKPEAPKL
CCHHHHHHCCCCCCC
73.6327667366
443UbiquitinationSDDEQEKKPEAPKLS
CHHHHHHCCCCCCCC
47.5427667366
450PhosphorylationKPEAPKLSKKKLRRM
CCCCCCCCHHHHHHC
48.8625159151
461PhosphorylationLRRMNRFTVAELKQL
HHHCCCCCHHHHHHH
18.6428555341
464UbiquitinationMNRFTVAELKQLVAR
CCCCCHHHHHHHHHC
52.7621890473
465UbiquitinationNRFTVAELKQLVARP
CCCCHHHHHHHHHCC
2.8621890473
466UbiquitinationRFTVAELKQLVARPD
CCCHHHHHHHHHCCC
32.8421890473
466UbiquitinationRFTVAELKQLVARPD
CCCHHHHHHHHHCCC
32.8421890473
466UbiquitinationRFTVAELKQLVARPD
CCCHHHHHHHHHCCC
32.8422817900
466UbiquitinationRFTVAELKQLVARPD
CCCHHHHHHHHHCCC
32.8421890473
466UbiquitinationRFTVAELKQLVARPD
CCCHHHHHHHHHCCC
32.8421890473
466UbiquitinationRFTVAELKQLVARPD
CCCHHHHHHHHHCCC
32.8421890473
474UbiquitinationQLVARPDVVEMHDVT
HHHHCCCEEEEECCC
4.3221890473
481UbiquitinationVVEMHDVTAQDPKLL
EEEEECCCCCCCCEE
25.3421890473
484UbiquitinationMHDVTAQDPKLLVHL
EECCCCCCCCEEEEE
39.5821890473
485UbiquitinationHDVTAQDPKLLVHLK
ECCCCCCCCEEEEEE
19.6721890473
486UbiquitinationDVTAQDPKLLVHLKA
CCCCCCCCEEEEEEE
63.8421890473
486UbiquitinationDVTAQDPKLLVHLKA
CCCCCCCCEEEEEEE
63.8421890473
4862-HydroxyisobutyrylationDVTAQDPKLLVHLKA
CCCCCCCCEEEEEEE
63.84-
486AcetylationDVTAQDPKLLVHLKA
CCCCCCCCEEEEEEE
63.8426051181
486UbiquitinationDVTAQDPKLLVHLKA
CCCCCCCCEEEEEEE
63.8423000965
486UbiquitinationDVTAQDPKLLVHLKA
CCCCCCCCEEEEEEE
63.8421890473
486UbiquitinationDVTAQDPKLLVHLKA
CCCCCCCCEEEEEEE
63.8421890473
486UbiquitinationDVTAQDPKLLVHLKA
CCCCCCCCEEEEEEE
63.8421890473
490UbiquitinationQDPKLLVHLKATRNS
CCCCEEEEEEECCCC
22.9121890473
491UbiquitinationDPKLLVHLKATRNSV
CCCEEEEEEECCCCC
2.9221890473
492UbiquitinationPKLLVHLKATRNSVP
CCEEEEEEECCCCCC
32.6021890473
492UbiquitinationPKLLVHLKATRNSVP
CCEEEEEEECCCCCC
32.6021890473
492MethylationPKLLVHLKATRNSVP
CCEEEEEEECCCCCC
32.6021685013
492SumoylationPKLLVHLKATRNSVP
CCEEEEEEECCCCCC
32.6028112733
492UbiquitinationPKLLVHLKATRNSVP
CCEEEEEEECCCCCC
32.6023000965
492UbiquitinationPKLLVHLKATRNSVP
CCEEEEEEECCCCCC
32.6021890473
492UbiquitinationPKLLVHLKATRNSVP
CCEEEEEEECCCCCC
32.6021890473
492UbiquitinationPKLLVHLKATRNSVP
CCEEEEEEECCCCCC
32.6021890473
502DimethylationRNSVPVPRHWCFKRK
CCCCCCCCHHHHHHH
35.85-
502MethylationRNSVPVPRHWCFKRK
CCCCCCCCHHHHHHH
35.8524383531
507MethylationVPRHWCFKRKYLQGK
CCCHHHHHHHHHCCC
44.8623748837
508DimethylationPRHWCFKRKYLQGKR
CCHHHHHHHHHCCCC
16.76-
508MethylationPRHWCFKRKYLQGKR
CCHHHHHHHHHCCCC
16.7625737013
512UbiquitinationCFKRKYLQGKRGIEK
HHHHHHHCCCCCCCC
52.8822817900
513UbiquitinationFKRKYLQGKRGIEKP
HHHHHHCCCCCCCCC
21.0222817900
514UbiquitinationKRKYLQGKRGIEKPP
HHHHHCCCCCCCCCC
34.1922817900
515MethylationRKYLQGKRGIEKPPF
HHHHCCCCCCCCCCC
59.1424129315
517UbiquitinationYLQGKRGIEKPPFEL
HHCCCCCCCCCCCCC
7.7522817900
518UbiquitinationLQGKRGIEKPPFELP
HCCCCCCCCCCCCCC
63.4322817900
519AcetylationQGKRGIEKPPFELPD
CCCCCCCCCCCCCCH
56.9526051181
519UbiquitinationQGKRGIEKPPFELPD
CCCCCCCCCCCCCCH
56.9521906983
527UbiquitinationPPFELPDFIKRTGIQ
CCCCCCHHHHHHCHH
7.1923000965
528UbiquitinationPFELPDFIKRTGIQE
CCCCCHHHHHHCHHH
3.7323000965
529UbiquitinationFELPDFIKRTGIQEM
CCCCHHHHHHCHHHH
43.8521890473
529UbiquitinationFELPDFIKRTGIQEM
CCCCHHHHHHCHHHH
43.8521890473
5292-HydroxyisobutyrylationFELPDFIKRTGIQEM
CCCCHHHHHHCHHHH
43.85-
529AcetylationFELPDFIKRTGIQEM
CCCCHHHHHHCHHHH
43.8526051181
529UbiquitinationFELPDFIKRTGIQEM
CCCCHHHHHHCHHHH
43.8523000965
529UbiquitinationFELPDFIKRTGIQEM
CCCCHHHHHHCHHHH
43.8521890473
529UbiquitinationFELPDFIKRTGIQEM
CCCCHHHHHHCHHHH
43.8521890473
529UbiquitinationFELPDFIKRTGIQEM
CCCCHHHHHHCHHHH
43.8521890473
531PhosphorylationLPDFIKRTGIQEMRE
CCHHHHHHCHHHHHH
33.3726074081
537MethylationRTGIQEMREALQEKE
HHCHHHHHHHHHHHH
25.86115916641
541UbiquitinationQEMREALQEKEEQKT
HHHHHHHHHHHHHHH
67.7622817900
542UbiquitinationEMREALQEKEEQKTM
HHHHHHHHHHHHHHH
64.3822817900
543AcetylationMREALQEKEEQKTMK
HHHHHHHHHHHHHHH
54.3023749302
543SumoylationMREALQEKEEQKTMK
HHHHHHHHHHHHHHH
54.3028112733
543UbiquitinationMREALQEKEEQKTMK
HHHHHHHHHHHHHHH
54.3021906983
545UbiquitinationEALQEKEEQKTMKSK
HHHHHHHHHHHHHHH
69.3322817900
546UbiquitinationALQEKEEQKTMKSKM
HHHHHHHHHHHHHHH
47.8422817900
547AcetylationLQEKEEQKTMKSKMR
HHHHHHHHHHHHHHH
54.5926051181
547UbiquitinationLQEKEEQKTMKSKMR
HHHHHHHHHHHHHHH
54.5922817900
548PhosphorylationQEKEEQKTMKSKMRE
HHHHHHHHHHHHHHH
29.53-
558UbiquitinationSKMREKVRPKMGKID
HHHHHHHHHCCCCCC
35.8722817900
559UbiquitinationKMREKVRPKMGKIDI
HHHHHHHHCCCCCCC
33.6922817900
560UbiquitinationMREKVRPKMGKIDID
HHHHHHHCCCCCCCC
50.1222817900
561UbiquitinationREKVRPKMGKIDIDY
HHHHHHCCCCCCCCH
7.9722817900
562UbiquitinationEKVRPKMGKIDIDYQ
HHHHHCCCCCCCCHH
29.8722817900
563AcetylationKVRPKMGKIDIDYQK
HHHHCCCCCCCCHHH
33.4425953088
563UbiquitinationKVRPKMGKIDIDYQK
HHHHCCCCCCCCHHH
33.4421906983
568PhosphorylationMGKIDIDYQKLHDAF
CCCCCCCHHHHHHHH
14.10-
568UbiquitinationMGKIDIDYQKLHDAF
CCCCCCCHHHHHHHH
14.1021890473
569UbiquitinationGKIDIDYQKLHDAFF
CCCCCCHHHHHHHHH
37.7821890473
570UbiquitinationKIDIDYQKLHDAFFK
CCCCCHHHHHHHHHH
41.3721890473
570UbiquitinationKIDIDYQKLHDAFFK
CCCCCHHHHHHHHHH
41.3721890473
5702-HydroxyisobutyrylationKIDIDYQKLHDAFFK
CCCCCHHHHHHHHHH
41.37-
570AcetylationKIDIDYQKLHDAFFK
CCCCCHHHHHHHHHH
41.3726051181
570UbiquitinationKIDIDYQKLHDAFFK
CCCCCHHHHHHHHHH
41.3723000965
570UbiquitinationKIDIDYQKLHDAFFK
CCCCCHHHHHHHHHH
41.3721890473
570UbiquitinationKIDIDYQKLHDAFFK
CCCCCHHHHHHHHHH
41.3721890473
570UbiquitinationKIDIDYQKLHDAFFK
CCCCCHHHHHHHHHH
41.3721890473
575UbiquitinationYQKLHDAFFKWQTKP
HHHHHHHHHHCCCCC
8.9021890473
576UbiquitinationQKLHDAFFKWQTKPK
HHHHHHHHHCCCCCC
9.3621890473
577UbiquitinationKLHDAFFKWQTKPKL
HHHHHHHHCCCCCCE
31.7521890473
577UbiquitinationKLHDAFFKWQTKPKL
HHHHHHHHCCCCCCE
31.7521890473
577AcetylationKLHDAFFKWQTKPKL
HHHHHHHHCCCCCCE
31.7525825284
577UbiquitinationKLHDAFFKWQTKPKL
HHHHHHHHCCCCCCE
31.7523000965
577UbiquitinationKLHDAFFKWQTKPKL
HHHHHHHHCCCCCCE
31.7521890473
577UbiquitinationKLHDAFFKWQTKPKL
HHHHHHHHCCCCCCE
31.7521890473
577UbiquitinationKLHDAFFKWQTKPKL
HHHHHHHHCCCCCCE
31.7521890473
579UbiquitinationHDAFFKWQTKPKLTI
HHHHHHCCCCCCEEE
39.9923000965
580UbiquitinationDAFFKWQTKPKLTIH
HHHHHCCCCCCEEEE
48.4723000965
581UbiquitinationAFFKWQTKPKLTIHG
HHHHCCCCCCEEEEE
25.6723000965
582UbiquitinationFFKWQTKPKLTIHGD
HHHCCCCCCEEEEEE
40.0323000965
583UbiquitinationFKWQTKPKLTIHGDL
HHCCCCCCEEEEEEE
60.8723000965
591PhosphorylationLTIHGDLYYEGKEFE
EEEEEEEEECCCHHH
12.2925884760
592PhosphorylationTIHGDLYYEGKEFET
EEEEEEEECCCHHHH
26.0425159151
595AcetylationGDLYYEGKEFETRLK
EEEEECCCHHHHHHC
47.4926051181
595UbiquitinationGDLYYEGKEFETRLK
EEEEECCCHHHHHHC
47.4933845483
602UbiquitinationKEFETRLKEKKPGDL
CHHHHHHCCCCCCCC
65.2824816145
603UbiquitinationEFETRLKEKKPGDLS
HHHHHHCCCCCCCCC
71.5424816145
604UbiquitinationFETRLKEKKPGDLSD
HHHHHCCCCCCCCCC
63.7824816145
605SumoylationETRLKEKKPGDLSDE
HHHHCCCCCCCCCCC
56.15-
605SumoylationETRLKEKKPGDLSDE
HHHHCCCCCCCCCCC
56.15-
605UbiquitinationETRLKEKKPGDLSDE
HHHHCCCCCCCCCCC
56.1533845483
610PhosphorylationEKKPGDLSDELRISL
CCCCCCCCCCHHHHC
33.5029507054
614MethylationGDLSDELRISLGMPV
CCCCCCHHHHCCCCC
17.88115916645
625UbiquitinationGMPVGPNAHKVPPPW
CCCCCCCCCCCCCCC
13.6523000965
626UbiquitinationMPVGPNAHKVPPPWL
CCCCCCCCCCCCCCE
37.9823000965
627UbiquitinationPVGPNAHKVPPPWLI
CCCCCCCCCCCCCEE
54.7723000965
639PhosphorylationWLIAMQRYGPPPSYP
CEEEEHHHCCCCCCC
19.6628152594
644PhosphorylationQRYGPPPSYPNLKIP
HHHCCCCCCCCCCCC
60.0228152594
645PhosphorylationRYGPPPSYPNLKIPG
HHCCCCCCCCCCCCC
11.2528152594
655PhosphorylationLKIPGLNSPIPESCS
CCCCCCCCCCCCCCC
29.2825159151
672AcetylationYHAGGWGKPPVDETG
CCCCCCCCCCCCCCC
39.3726051181
672UbiquitinationYHAGGWGKPPVDETG
CCCCCCCCCCCCCCC
39.3729967540
680AcetylationPPVDETGKPLYGDVF
CCCCCCCCCCCCCHH
38.9926051181
680SumoylationPPVDETGKPLYGDVF
CCCCCCCCCCCCCHH
38.99-
680UbiquitinationPPVDETGKPLYGDVF
CCCCCCCCCCCCCHH
38.9929967540
697SumoylationNAAEFQTKTEEEEID
CHHHHCCCCCHHHCC
43.06-
698PhosphorylationAAEFQTKTEEEEIDR
HHHHCCCCCHHHCCC
52.6021815630
706PhosphorylationEEEEIDRTPWGELEP
CHHHCCCCCCCCCCC
21.4621406692
714PhosphorylationPWGELEPSDEESSEE
CCCCCCCCCCCCCHH
48.5621406692
718PhosphorylationLEPSDEESSEEEEEE
CCCCCCCCCHHHHHH
40.7921406692
719PhosphorylationEPSDEESSEEEEEEE
CCCCCCCCHHHHHHH
52.9221406692
727PhosphorylationEEEEEEESDEDKPDE
HHHHHHHCCCCCCCC
49.9721406692
735PhosphorylationDEDKPDETGFITPAD
CCCCCCCCCCCCCCC
44.7821406692
739PhosphorylationPDETGFITPADSGLI
CCCCCCCCCCCCCCC
15.3420068231
743PhosphorylationGFITPADSGLITPGG
CCCCCCCCCCCCCCC
37.2921406692
747PhosphorylationPADSGLITPGGFSSV
CCCCCCCCCCCCCCC
22.4121406692
752PhosphorylationLITPGGFSSVPAGME
CCCCCCCCCCCCCCC
33.4321406692
753PhosphorylationITPGGFSSVPAGMET
CCCCCCCCCCCCCCC
29.8321406692
755PhosphorylationPGGFSSVPAGMETPE
CCCCCCCCCCCCCHH
25.6618669648
757PhosphorylationGFSSVPAGMETPELI
CCCCCCCCCCCHHHH
14.3718669648
760PhosphorylationSVPAGMETPELIELR
CCCCCCCCHHHHHHH
17.1126657352
770SumoylationLIELRKKKIEEAMDG
HHHHHHHHHHHHHCC
59.39-
770SumoylationLIELRKKKIEEAMDG
HHHHHHHHHHHHHCC
59.3928112733
778PhosphorylationIEEAMDGSETPQLFT
HHHHHCCCCCCCCEE
33.7529255136
780PhosphorylationEAMDGSETPQLFTVL
HHHCCCCCCCCEECC
20.3129255136
783PhosphorylationDGSETPQLFTVLPEK
CCCCCCCCEECCCCC
4.0118669648
785PhosphorylationSETPQLFTVLPEKRT
CCCCCCEECCCCCCC
29.7127794612
786PhosphorylationETPQLFTVLPEKRTA
CCCCCEECCCCCCCC
7.0418669648
787PhosphorylationTPQLFTVLPEKRTAT
CCCCEECCCCCCCCE
4.0518669648
788UbiquitinationPQLFTVLPEKRTATV
CCCEECCCCCCCCEE
40.5022817900
789UbiquitinationQLFTVLPEKRTATVG
CCEECCCCCCCCEEC
51.5122817900
790SumoylationLFTVLPEKRTATVGG
CEECCCCCCCCEECC
53.7828112733
790UbiquitinationLFTVLPEKRTATVGG
CEECCCCCCCCEECC
53.7822817900
792PhosphorylationTVLPEKRTATVGGAM
ECCCCCCCCEECCCC
37.4330576142
794PhosphorylationLPEKRTATVGGAMMG
CCCCCCCEECCCCCC
21.0420068231
802PhosphorylationVGGAMMGSTHIYDMS
ECCCCCCCEEEEEHH
10.0220068231
803PhosphorylationGGAMMGSTHIYDMST
CCCCCCCEEEEEHHH
13.4320068231
806PhosphorylationMMGSTHIYDMSTVMS
CCCCEEEEEHHHHHH
9.6627259358
809PhosphorylationSTHIYDMSTVMSRKG
CEEEEEHHHHHHCCC
18.2318669648
810PhosphorylationTHIYDMSTVMSRKGP
EEEEEHHHHHHCCCC
17.3730576142
813PhosphorylationYDMSTVMSRKGPAPE
EEHHHHHHCCCCCCC
26.8920068231
815UbiquitinationMSTVMSRKGPAPELQ
HHHHHHCCCCCCCCC
63.04-
841PhosphorylationELDPMAMTQKYEEHV
CCCHHHHHHHHHHHH
16.6330576142
841UbiquitinationELDPMAMTQKYEEHV
CCCHHHHHHHHHHHH
16.6324816145
842UbiquitinationLDPMAMTQKYEEHVR
CCHHHHHHHHHHHHH
33.0024816145
843MethylationDPMAMTQKYEEHVRE
CHHHHHHHHHHHHHH
45.52116252643
843SumoylationDPMAMTQKYEEHVRE
CHHHHHHHHHHHHHH
45.5228112733
843UbiquitinationDPMAMTQKYEEHVRE
CHHHHHHHHHHHHHH
45.5232015554
844PhosphorylationPMAMTQKYEEHVREQ
HHHHHHHHHHHHHHH
19.4127642862
855UbiquitinationVREQQAQVEKEDFSD
HHHHHHHHHHHHHHH
14.7424816145
856UbiquitinationREQQAQVEKEDFSDM
HHHHHHHHHHHHHHH
38.3524816145
8572-HydroxyisobutyrylationEQQAQVEKEDFSDMV
HHHHHHHHHHHHHHH
64.82-
857AcetylationEQQAQVEKEDFSDMV
HHHHHHHHHHHHHHH
64.8226051181
857SumoylationEQQAQVEKEDFSDMV
HHHHHHHHHHHHHHH
64.8228112733
857UbiquitinationEQQAQVEKEDFSDMV
HHHHHHHHHHHHHHH
64.8224816145
861PhosphorylationQVEKEDFSDMVAEHA
HHHHHHHHHHHHHHH
36.8029255136
863SulfoxidationEKEDFSDMVAEHAAK
HHHHHHHHHHHHHHH
2.7421406390
870AcetylationMVAEHAAKQKQKKRK
HHHHHHHHHHHHHHH
59.8325953088
870UbiquitinationMVAEHAAKQKQKKRK
HHHHHHHHHHHHHHH
59.8332015554
883PhosphorylationRKAQPQDSRGGSKKY
HHCCCCCCCCCCHHC
27.8122496350
884MethylationKAQPQDSRGGSKKYK
HCCCCCCCCCCHHCC
62.8854559183
887PhosphorylationPQDSRGGSKKYKEFK
CCCCCCCCHHCCCCC
28.8826074081
890PhosphorylationSRGGSKKYKEFKF--
CCCCCHHCCCCCC--
21.3426074081
891AcetylationRGGSKKYKEFKF---
CCCCHHCCCCCC---
66.607296823

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
379YPhosphorylationKinaseSRCP12931
PSP
592YPhosphorylationKinaseSRCP12931
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
508RMethylation

25737013

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 SF3B2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SF3B1_HUMANSF3B1physical
10490618
SF3B3_HUMANSF3B3physical
10490618
ECM29_HUMANKIAA0368physical
20682791
A4_HUMANAPPphysical
21832049
SF3B4_HUMANSF3B4physical
22939629
SF3B3_HUMANSF3B3physical
22939629
SMD1_HUMANSNRPD1physical
22939629
SF3B5_HUMANSF3B5physical
22939629
SMD3_HUMANSNRPD3physical
22939629
SRSF9_HUMANSRSF9physical
22939629
YBOX1_HUMANYBX1physical
22939629
TCEA1_HUMANTCEA1physical
22939629
THOC1_HUMANTHOC1physical
22939629
TR150_HUMANTHRAP3physical
22939629
TMED9_HUMANTMED9physical
22939629
TMOD2_HUMANTMOD2physical
22939629
TPM1_HUMANTPM1physical
22939629
SIM20_HUMANSMIM20physical
22939629
TPM2_HUMANTPM2physical
22939629
VASP_HUMANVASPphysical
22939629
TIF1A_HUMANTRIM24physical
22939629
TOX4_HUMANTOX4physical
22939629
PR40A_HUMANPRPF40Aphysical
22365833
SF3B4_HUMANSF3B4physical
22365833
U2AF1_HUMANU2AF1physical
22365833
HNRPC_HUMANHNRNPCphysical
22365833
PRP8_HUMANPRPF8physical
22365833
U520_HUMANSNRNP200physical
22365833
LSM2_HUMANLSM2physical
22365833
LSM3_HUMANLSM3physical
22365833
PRPF3_HUMANPRPF3physical
22365833
SYF1_HUMANXAB2physical
22365833
DHX16_HUMANDHX16physical
22365833
SLU7_HUMANSLU7physical
22365833
RBM8A_HUMANRBM8Aphysical
22365833
THOC1_HUMANTHOC1physical
22365833
F10C1_HUMANFRA10AC1physical
22365833
ZN830_HUMANZNF830physical
22365833
RBM7_HUMANRBM7physical
22365833
PCBP2_HUMANPCBP2physical
22365833
TOE1_HUMANTOE1physical
22365833
TTC14_HUMANTTC14physical
22365833
ZCH10_HUMANZCCHC10physical
22365833
R113A_HUMANRNF113Aphysical
22365833
KDM1A_HUMANKDM1Aphysical
23455924
COPB_HUMANCOPB1physical
26344197
COPE_HUMANCOPEphysical
26344197
COPG1_HUMANCOPG1physical
26344197
PSME3_HUMANPSME3physical
26344197
SF3B3_HUMANSF3B3physical
26344197
SF3B5_HUMANSF3B5physical
26344197
SF3B6_HUMANSF3B6physical
26344197

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 SF3B2_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-275, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-307; SER-309; SER-360;SER-362 AND THR-780, 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 SER-307; SER-309 ANDTHR-780, AND MASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431; SER-435 ANDSER-436, 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-201; THR-217; SER-289;SER-307; SER-309; THR-311; SER-431; SER-435; SER-436 AND THR-780, ANDMASS 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-307 AND SER-309, ANDMASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309 AND THR-311, ANDMASS SPECTROMETRY.
"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-289, AND MASSSPECTROMETRY.
"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 SER-343; SER-360; SER-431;SER-435; SER-436; SER-778 AND THR-780, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307 AND SER-309, ANDMASS SPECTROMETRY.
"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-362; SER-416; SER-431;SER-435 AND SER-436, AND MASS SPECTROMETRY.

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