PUF60_HUMAN - dbPTM
PUF60_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PUF60_HUMAN
UniProt AC Q9UHX1
Protein Name Poly(U)-binding-splicing factor PUF60
Gene Name PUF60
Organism Homo sapiens (Human).
Sequence Length 559
Subcellular Localization Nucleus . Colocalizes partially with TROVE2.
Protein Description DNA- and RNA-binding protein, involved in several nuclear processes such as pre-mRNA splicing, apoptosis and transcription regulation. In association with FUBP1 regulates MYC transcription at the P2 promoter through the core-TFIIH basal transcription factor. Acts as a transcriptional repressor through the core-TFIIH basal transcription factor. Represses FUBP1-induced transcriptional activation but not basal transcription. Decreases ERCC3 helicase activity. Does not repress TFIIH-mediated transcription in xeroderma pigmentosum complementation group B (XPB) cells. Is also involved in pre-mRNA splicing. Promotes splicing of an intron with weak 3'-splice site and pyrimidine tract in a cooperative manner with U2AF2. Involved in apoptosis induction when overexpressed in HeLa cells. Isoform 6 failed to repress MYC transcription and inhibited FIR-induced apoptosis in colorectal cancer. Isoform 6 may contribute to tumor progression by enabling increased MYC expression and greater resistance to apoptosis in tumors than in normal cells. Modulates alternative splicing of several mRNAs. Binds to relaxed DNA of active promoter regions. Binds to the pyrimidine tract and 3'-splice site regions of pre-mRNA; binding is enhanced in presence of U2AF2. Binds to Y5 RNA in association with TROVE2. Binds to poly(U) RNA..
Protein Sequence MATATIALQVNGQQGGGSEPAAAAAVVAAGDKWKPPQGTDSIKMENGQSTAAKLGLPPLTPEQQEALQKAKKYAMEQSIKSVLVKQTIAHQQQQLTNLQMAAVTMGFGDPLSPLQSMAAQRQRALAIMCRVYVGSIYYELGEDTIRQAFAPFGPIKSIDMSWDSVTMKHKGFAFVEYEVPEAAQLALEQMNSVMLGGRNIKVGRPSNIGQAQPIIDQLAEEARAFNRIYVASVHQDLSDDDIKSVFEAFGKIKSCTLARDPTTGKHKGYGFIEYEKAQSSQDAVSSMNLFDLGGQYLRVGKAVTPPMPLLTPATPGGLPPAAAVAAAAATAKITAQEAVAGAAVLGTLGTPGLVSPALTLAQPLGTLPQAVMAAQAPGVITGVTPARPPIPVTIPSVGVVNPILASPPTLGLLEPKKEKEEEELFPESERPEMLSEQEHMSISGSSARHMVMQKLLRKQESTVMVLRNMVDPKDIDDDLEGEVTEECGKFGAVNRVIIYQEKQGEEEDAEIIVKIFVEFSIASETHKAIQALNGRWFAGRKVVAEVYDQERFDNSDLSA
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
3Phosphorylation-----MATATIALQV
-----CCEEEEEEEE
24.0418491316
3 (in isoform 2)Phosphorylation-24.04-
3 (in isoform 5)Phosphorylation-24.0420860994
3 (in isoform 6)Phosphorylation-24.0420860994
5Phosphorylation---MATATIALQVNG
---CCEEEEEEEECC
11.4818491316
5 (in isoform 5)Phosphorylation-11.4820860994
5 (in isoform 6)Phosphorylation-11.4820860994
10 (in isoform 5)Phosphorylation-10.1320860994
10 (in isoform 6)Phosphorylation-10.1320860994
12 (in isoform 5)Phosphorylation-23.4921406692
12 (in isoform 6)Phosphorylation-23.4921406692
14 (in isoform 5)Sumoylation-54.63-
14 (in isoform 6)Sumoylation-54.63-
18PhosphorylationNGQQGGGSEPAAAAA
CCCCCCCCCHHHHHH
43.6225867546
26UbiquitinationEPAAAAAVVAAGDKW
CHHHHHHHHHCCCCC
2.3029967540
29UbiquitinationAAAAVVAAGDKWKPP
HHHHHHHCCCCCCCC
18.3329967540
33UbiquitinationVVAAGDKWKPPQGTD
HHHCCCCCCCCCCCC
24.1129967540
34UbiquitinationVAAGDKWKPPQGTDS
HHCCCCCCCCCCCCC
53.1929967540
37UbiquitinationGDKWKPPQGTDSIKM
CCCCCCCCCCCCEEE
75.7723000965
37 (in isoform 3)Ubiquitination-75.7721890473
37 (in isoform 4)Ubiquitination-75.7721890473
40UbiquitinationWKPPQGTDSIKMENG
CCCCCCCCCEEEECC
56.0129967540
41PhosphorylationKPPQGTDSIKMENGQ
CCCCCCCCEEEECCC
24.7725627689
42UbiquitinationPPQGTDSIKMENGQS
CCCCCCCEEEECCCC
5.6923000965
43SumoylationPQGTDSIKMENGQST
CCCCCCEEEECCCCH
44.08-
43SumoylationPQGTDSIKMENGQST
CCCCCCEEEECCCCH
44.0828112733
43UbiquitinationPQGTDSIKMENGQST
CCCCCCEEEECCCCH
44.0829967540
44 (in isoform 4)Phosphorylation-4.6327251275
51UbiquitinationMENGQSTAAKLGLPP
EECCCCHHHHHCCCC
14.0823000965
51 (in isoform 5)Ubiquitination-14.0821890473
51 (in isoform 6)Ubiquitination-14.0821890473
56UbiquitinationSTAAKLGLPPLTPEQ
CHHHHHCCCCCCHHH
5.9823000965
58 (in isoform 6)Phosphorylation-54.6427251275
60PhosphorylationKLGLPPLTPEQQEAL
HHCCCCCCHHHHHHH
30.4730266825
60 (in isoform 2)Phosphorylation-30.47-
68UbiquitinationPEQQEALQKAKKYAM
HHHHHHHHHHHHHHH
51.1929967540
69AcetylationEQQEALQKAKKYAME
HHHHHHHHHHHHHHH
64.1226051181
69UbiquitinationEQQEALQKAKKYAME
HHHHHHHHHHHHHHH
64.1229967540
71UbiquitinationQEALQKAKKYAMEQS
HHHHHHHHHHHHHHH
54.0429967540
722-HydroxyisobutyrylationEALQKAKKYAMEQSI
HHHHHHHHHHHHHHH
43.00-
72AcetylationEALQKAKKYAMEQSI
HHHHHHHHHHHHHHH
43.0027452117
72MethylationEALQKAKKYAMEQSI
HHHHHHHHHHHHHHH
43.00-
72UbiquitinationEALQKAKKYAMEQSI
HHHHHHHHHHHHHHH
43.0029967540
73PhosphorylationALQKAKKYAMEQSIK
HHHHHHHHHHHHHHH
15.5228509920
78PhosphorylationKKYAMEQSIKSVLVK
HHHHHHHHHHHHHHH
20.7629978859
79UbiquitinationKYAMEQSIKSVLVKQ
HHHHHHHHHHHHHHH
3.7323000965
80SumoylationYAMEQSIKSVLVKQT
HHHHHHHHHHHHHHH
39.5028112733
80UbiquitinationYAMEQSIKSVLVKQT
HHHHHHHHHHHHHHH
39.5023000965
80 (in isoform 1)Ubiquitination-39.5021890473
80 (in isoform 2)Ubiquitination-39.5021890473
81PhosphorylationAMEQSIKSVLVKQTI
HHHHHHHHHHHHHHH
21.0020860994
84UbiquitinationQSIKSVLVKQTIAHQ
HHHHHHHHHHHHHHH
3.9623000965
85UbiquitinationSIKSVLVKQTIAHQQ
HHHHHHHHHHHHHHH
37.2523000965
87PhosphorylationKSVLVKQTIAHQQQQ
HHHHHHHHHHHHHHH
17.8924043423
87 (in isoform 2)Phosphorylation-17.8927251275
96PhosphorylationAHQQQQLTNLQMAAV
HHHHHHHHHHHHHHH
29.5524043423
104PhosphorylationNLQMAAVTMGFGDPL
HHHHHHHHCCCCCCC
13.5728102081
105UbiquitinationLQMAAVTMGFGDPLS
HHHHHHHCCCCCCCC
3.1723000965
108UbiquitinationAAVTMGFGDPLSPLQ
HHHHCCCCCCCCHHH
29.8729967540
110UbiquitinationVTMGFGDPLSPLQSM
HHCCCCCCCCHHHHH
34.8123000965
112PhosphorylationMGFGDPLSPLQSMAA
CCCCCCCCHHHHHHH
29.0220068231
116PhosphorylationDPLSPLQSMAAQRQR
CCCCHHHHHHHHHHH
20.3324043423
117UbiquitinationPLSPLQSMAAQRQRA
CCCHHHHHHHHHHHH
2.0023000965
122UbiquitinationQSMAAQRQRALAIMC
HHHHHHHHHHHHHHH
23.9523000965
125UbiquitinationAAQRQRALAIMCRVY
HHHHHHHHHHHHHHH
3.4629967540
139UbiquitinationYVGSIYYELGEDTIR
HHHHHHHHCCCCHHH
33.0729967540
150UbiquitinationDTIRQAFAPFGPIKS
CHHHHHHCCCCCCEE
11.0929967540
151UbiquitinationTIRQAFAPFGPIKSI
HHHHHHCCCCCCEEE
28.4229967540
157PhosphorylationAPFGPIKSIDMSWDS
CCCCCCEEEECCCCC
25.2521601212
167UbiquitinationMSWDSVTMKHKGFAF
CCCCCEEECCCCEEE
3.9229967540
168UbiquitinationSWDSVTMKHKGFAFV
CCCCEEECCCCEEEE
32.5729967540
172 (in isoform 5)Ubiquitination-5.94-
177PhosphorylationKGFAFVEYEVPEAAQ
CCEEEEEEECHHHHH
19.54-
183UbiquitinationEYEVPEAAQLALEQM
EEECHHHHHHHHHHH
11.8521963094
189 (in isoform 2)Phosphorylation-36.89-
191AcetylationQLALEQMNSVMLGGR
HHHHHHHHCCEECCC
31.0119608861
191UbiquitinationQLALEQMNSVMLGGR
HHHHHHHHCCEECCC
31.0133845483
191 (in isoform 4)Ubiquitination-31.0121890473
197UbiquitinationMNSVMLGGRNIKVGR
HHCCEECCCCCCCCC
18.5921963094
200UbiquitinationVMLGGRNIKVGRPSN
CEECCCCCCCCCCCC
3.5421963094
201AcetylationMLGGRNIKVGRPSNI
EECCCCCCCCCCCCC
42.0325953088
201UbiquitinationMLGGRNIKVGRPSNI
EECCCCCCCCCCCCC
42.03-
205AcetylationRNIKVGRPSNIGQAQ
CCCCCCCCCCCCCCH
26.2919608861
205UbiquitinationRNIKVGRPSNIGQAQ
CCCCCCCCCCCCCCH
26.2933845483
205 (in isoform 6)Ubiquitination-26.2921890473
206PhosphorylationNIKVGRPSNIGQAQP
CCCCCCCCCCCCCHH
39.4525159151
207UbiquitinationIKVGRPSNIGQAQPI
CCCCCCCCCCCCHHH
45.1333845483
208AcetylationKVGRPSNIGQAQPII
CCCCCCCCCCCHHHH
5.1919608861
208UbiquitinationKVGRPSNIGQAQPII
CCCCCCCCCCCHHHH
5.1933845483
208 (in isoform 3)Ubiquitination-5.1921890473
214UbiquitinationNIGQAQPIIDQLAEE
CCCCCHHHHHHHHHH
3.4521963094
214 (in isoform 5)Ubiquitination-3.45-
219UbiquitinationQPIIDQLAEEARAFN
HHHHHHHHHHHHHHC
13.6223503661
221UbiquitinationIIDQLAEEARAFNRI
HHHHHHHHHHHHCCE
37.5433845483
222AcetylationIDQLAEEARAFNRIY
HHHHHHHHHHHCCEE
10.2919608861
222UbiquitinationIDQLAEEARAFNRIY
HHHHHHHHHHHCCEE
10.2933845483
222 (in isoform 5)Ubiquitination-10.2921890473
224UbiquitinationQLAEEARAFNRIYVA
HHHHHHHHHCCEEEE
17.0833845483
224 (in isoform 5)Ubiquitination-17.08-
225UbiquitinationLAEEARAFNRIYVAS
HHHHHHHHCCEEEEE
5.4221963094
226UbiquitinationAEEARAFNRIYVASV
HHHHHHHCCEEEEEE
28.5821963094
226 (in isoform 2)Ubiquitination-28.58-
227 (in isoform 2)Phosphorylation-18.3721406692
232PhosphorylationFNRIYVASVHQDLSD
HCCEEEEEECCCCCH
15.3020873877
233AcetylationNRIYVASVHQDLSDD
CCEEEEEECCCCCHH
3.2019608861
233UbiquitinationNRIYVASVHQDLSDD
CCEEEEEECCCCCHH
3.2033845483
234AcetylationRIYVASVHQDLSDDD
CEEEEEECCCCCHHH
16.9719608861
234UbiquitinationRIYVASVHQDLSDDD
CEEEEEECCCCCHHH
16.9733845483
234 (in isoform 2)Acetylation-16.97-
234 (in isoform 2)Ubiquitination-16.9721890473
236UbiquitinationYVASVHQDLSDDDIK
EEEEECCCCCHHHHH
33.0123503661
238PhosphorylationASVHQDLSDDDIKSV
EEECCCCCHHHHHHH
47.4820873877
238UbiquitinationASVHQDLSDDDIKSV
EEECCCCCHHHHHHH
47.4833845483
238 (in isoform 5)Ubiquitination-47.48-
241UbiquitinationHQDLSDDDIKSVFEA
CCCCCHHHHHHHHHH
56.0321963094
242UbiquitinationQDLSDDDIKSVFEAF
CCCCHHHHHHHHHHH
4.6321963094
243AcetylationDLSDDDIKSVFEAFG
CCCHHHHHHHHHHHH
47.7826051181
243UbiquitinationDLSDDDIKSVFEAFG
CCCHHHHHHHHHHHH
47.7821963094
244PhosphorylationLSDDDIKSVFEAFGK
CCHHHHHHHHHHHHC
32.1630266825
247UbiquitinationDDIKSVFEAFGKIKS
HHHHHHHHHHHCCEE
40.7223503661
248UbiquitinationDIKSVFEAFGKIKSC
HHHHHHHHHHCCEEE
13.6623503661
249UbiquitinationIKSVFEAFGKIKSCT
HHHHHHHHHCCEEEE
8.9033845483
250AcetylationKSVFEAFGKIKSCTL
HHHHHHHHCCEEEEE
37.5119608861
250UbiquitinationKSVFEAFGKIKSCTL
HHHHHHHHCCEEEEE
37.5133845483
250 (in isoform 2)Ubiquitination-37.51-
251AcetylationSVFEAFGKIKSCTLA
HHHHHHHCCEEEEEE
40.2719608861
251UbiquitinationSVFEAFGKIKSCTLA
HHHHHHHCCEEEEEE
40.2733845483
251 (in isoform 1)Ubiquitination-40.2721890473
255UbiquitinationAFGKIKSCTLARDPT
HHHCCEEEEEEECCC
2.8421963094
258UbiquitinationKIKSCTLARDPTTGK
CCEEEEEEECCCCCC
8.8321963094
262PhosphorylationCTLARDPTTGKHKGY
EEEEECCCCCCCCCC
53.09-
263PhosphorylationTLARDPTTGKHKGYG
EEEECCCCCCCCCCC
50.01-
263UbiquitinationTLARDPTTGKHKGYG
EEEECCCCCCCCCCC
50.0121963094
264UbiquitinationLARDPTTGKHKGYGF
EEECCCCCCCCCCCE
32.3323503661
265UbiquitinationARDPTTGKHKGYGFI
EECCCCCCCCCCCEE
39.8023503661
266UbiquitinationRDPTTGKHKGYGFIE
ECCCCCCCCCCCEEE
30.0733845483
267AcetylationDPTTGKHKGYGFIEY
CCCCCCCCCCCEEEE
58.2626051181
267UbiquitinationDPTTGKHKGYGFIEY
CCCCCCCCCCCEEEE
58.2633845483
268UbiquitinationPTTGKHKGYGFIEYE
CCCCCCCCCCEEEEE
27.7621963094
269PhosphorylationTTGKHKGYGFIEYEK
CCCCCCCCCEEEEEE
17.4224043423
271UbiquitinationGKHKGYGFIEYEKAQ
CCCCCCCEEEEEECC
2.6321890473
272UbiquitinationKHKGYGFIEYEKAQS
CCCCCCEEEEEECCC
4.8421963094
274PhosphorylationKGYGFIEYEKAQSSQ
CCCCEEEEEECCCCC
20.2224043423
276UbiquitinationYGFIEYEKAQSSQDA
CCEEEEEECCCCCHH
51.3121890473
279PhosphorylationIEYEKAQSSQDAVSS
EEEEECCCCCHHHHH
34.5221712546
280PhosphorylationEYEKAQSSQDAVSSM
EEEECCCCCHHHHHC
21.7221712546
280UbiquitinationEYEKAQSSQDAVSSM
EEEECCCCCHHHHHC
21.7221963094
283UbiquitinationKAQSSQDAVSSMNLF
ECCCCCHHHHHCCHH
8.7521963094
284UbiquitinationAQSSQDAVSSMNLFD
CCCCCHHHHHCCHHH
6.1521963094
284 (in isoform 2)Ubiquitination-6.15-
285PhosphorylationQSSQDAVSSMNLFDL
CCCCHHHHHCCHHHC
26.1224043423
285UbiquitinationQSSQDAVSSMNLFDL
CCCCHHHHHCCHHHC
26.1223503661
286PhosphorylationSSQDAVSSMNLFDLG
CCCHHHHHCCHHHCC
12.7024043423
287UbiquitinationSQDAVSSMNLFDLGG
CCHHHHHCCHHHCCC
3.8333845483
288UbiquitinationQDAVSSMNLFDLGGQ
CHHHHHCCHHHCCCC
39.2321890473
290UbiquitinationAVSSMNLFDLGGQYL
HHHHCCHHHCCCCEE
6.5623503661
292UbiquitinationSSMNLFDLGGQYLRV
HHCCHHHCCCCEEEE
6.9523503661
294 (in isoform 2)Phosphorylation-21.91-
296PhosphorylationLFDLGGQYLRVGKAV
HHHCCCCEEEEECCC
10.3524043423
297 (in isoform 2)Phosphorylation-2.48-
300UbiquitinationGGQYLRVGKAVTPPM
CCCEEEEECCCCCCC
13.0321963094
301UbiquitinationGQYLRVGKAVTPPMP
CCEEEEECCCCCCCC
36.5121963094
302UbiquitinationQYLRVGKAVTPPMPL
CEEEEECCCCCCCCC
12.4223503661
304PhosphorylationLRVGKAVTPPMPLLT
EEEECCCCCCCCCCC
26.9120068231
304UbiquitinationLRVGKAVTPPMPLLT
EEEECCCCCCCCCCC
26.9133845483
307SulfoxidationGKAVTPPMPLLTPAT
ECCCCCCCCCCCCCC
3.7221406390
311PhosphorylationTPPMPLLTPATPGGL
CCCCCCCCCCCCCCC
20.6828674151
314PhosphorylationMPLLTPATPGGLPPA
CCCCCCCCCCCCCHH
24.5428355574
321UbiquitinationTPGGLPPAAAVAAAA
CCCCCCHHHHHHHHH
13.2021963094
326UbiquitinationPPAAAVAAAAATAKI
CHHHHHHHHHHHCCC
7.3421963094
330PhosphorylationAVAAAAATAKITAQE
HHHHHHHHCCCCHHH
24.6126552605
338UbiquitinationAKITAQEAVAGAAVL
CCCCHHHHHHHHHHH
5.6021963094
350PhosphorylationAVLGTLGTPGLVSPA
HHHHCCCCCCCCCHH
19.8026853621
355PhosphorylationLGTPGLVSPALTLAQ
CCCCCCCCHHHHHHC
14.9726074081
359PhosphorylationGLVSPALTLAQPLGT
CCCCHHHHHHCCCCC
23.3526074081
389 (in isoform 2)Phosphorylation-37.65-
394AcetylationRPPIPVTIPSVGVVN
CCCCCCCCCCCCCCC
2.1419608861
394UbiquitinationRPPIPVTIPSVGVVN
CCCCCCCCCCCCCCC
2.1423000965
398UbiquitinationPVTIPSVGVVNPILA
CCCCCCCCCCCHHHC
23.2223000965
406O-linked_GlycosylationVVNPILASPPTLGLL
CCCHHHCCCCCCCCC
28.15OGP
406PhosphorylationVVNPILASPPTLGLL
CCCHHHCCCCCCCCC
28.1520058876
408AcetylationNPILASPPTLGLLEP
CHHHCCCCCCCCCCC
37.4519608861
408UbiquitinationNPILASPPTLGLLEP
CHHHCCCCCCCCCCC
37.4523000965
411AcetylationLASPPTLGLLEPKKE
HCCCCCCCCCCCCCH
30.6019608861
411UbiquitinationLASPPTLGLLEPKKE
HCCCCCCCCCCCCCH
30.6023000965
412UbiquitinationASPPTLGLLEPKKEK
CCCCCCCCCCCCCHH
5.7223000965
415UbiquitinationPTLGLLEPKKEKEEE
CCCCCCCCCCHHHHH
53.6523000965
419SumoylationLLEPKKEKEEEELFP
CCCCCCHHHHHHHCC
78.3428112733
425AcetylationEKEEEELFPESERPE
HHHHHHHCCCCCCHH
7.7419608861
425UbiquitinationEKEEEELFPESERPE
HHHHHHHCCCCCCHH
7.7423000965
428PhosphorylationEEELFPESERPEMLS
HHHHCCCCCCHHHCC
38.8630108239
429UbiquitinationEELFPESERPEMLSE
HHHCCCCCCHHHCCC
71.2723000965
435PhosphorylationSERPEMLSEQEHMSI
CCCHHHCCCCCCCCC
35.6030108239
436AcetylationERPEMLSEQEHMSIS
CCHHHCCCCCCCCCC
56.9019608861
436UbiquitinationERPEMLSEQEHMSIS
CCHHHCCCCCCCCCC
56.9023000965
437AcetylationRPEMLSEQEHMSISG
CHHHCCCCCCCCCCH
42.3819608861
437UbiquitinationRPEMLSEQEHMSISG
CHHHCCCCCCCCCCH
42.3823000965
437 (in isoform 2)Acetylation-42.38-
440UbiquitinationMLSEQEHMSISGSSA
HCCCCCCCCCCHHHH
3.6123000965
441PhosphorylationLSEQEHMSISGSSAR
CCCCCCCCCCHHHHH
18.6030108239
441UbiquitinationLSEQEHMSISGSSAR
CCCCCCCCCCHHHHH
18.6023000965
443PhosphorylationEQEHMSISGSSARHM
CCCCCCCCHHHHHHH
25.8930108239
443UbiquitinationEQEHMSISGSSARHM
CCCCCCCCHHHHHHH
25.8924816145
445PhosphorylationEHMSISGSSARHMVM
CCCCCCHHHHHHHHH
17.6530108239
446PhosphorylationHMSISGSSARHMVMQ
CCCCCHHHHHHHHHH
32.6130108239
446UbiquitinationHMSISGSSARHMVMQ
CCCCCHHHHHHHHHH
32.6124816145
453AcetylationSARHMVMQKLLRKQE
HHHHHHHHHHHHCCH
23.1019608861
453UbiquitinationSARHMVMQKLLRKQE
HHHHHHHHHHHHCCH
23.1023000965
454AcetylationARHMVMQKLLRKQES
HHHHHHHHHHHCCHH
31.2419608861
454UbiquitinationARHMVMQKLLRKQES
HHHHHHHHHHHCCHH
31.2423000965
457UbiquitinationMVMQKLLRKQESTVM
HHHHHHHHCCHHHHE
49.3923000965
458SumoylationVMQKLLRKQESTVMV
HHHHHHHCCHHHHEE
59.39-
4582-HydroxyisobutyrylationVMQKLLRKQESTVMV
HHHHHHHCCHHHHEE
59.39-
458SumoylationVMQKLLRKQESTVMV
HHHHHHHCCHHHHEE
59.3928112733
458UbiquitinationVMQKLLRKQESTVMV
HHHHHHHCCHHHHEE
59.3923000965
460UbiquitinationQKLLRKQESTVMVLR
HHHHHCCHHHHEEEE
51.9524816145
461PhosphorylationKLLRKQESTVMVLRN
HHHHCCHHHHEEEEC
24.6530624053
462PhosphorylationLLRKQESTVMVLRNM
HHHCCHHHHEEEECC
16.3323403867
471UbiquitinationMVLRNMVDPKDIDDD
EEEECCCCHHHCCCC
33.4924816145
472UbiquitinationVLRNMVDPKDIDDDL
EEECCCCHHHCCCCC
25.4724816145
473AcetylationLRNMVDPKDIDDDLE
EECCCCHHHCCCCCC
63.9526051181
474UbiquitinationRNMVDPKDIDDDLEG
ECCCCHHHCCCCCCC
55.7423000965
478UbiquitinationDPKDIDDDLEGEVTE
CHHHCCCCCCCCCHH
42.7623000965
479UbiquitinationPKDIDDDLEGEVTEE
HHHCCCCCCCCCHHH
13.4923000965
481UbiquitinationDIDDDLEGEVTEECG
HCCCCCCCCCHHHHH
41.8124816145
483UbiquitinationDDDLEGEVTEECGKF
CCCCCCCCHHHHHCC
13.8523000965
488UbiquitinationGEVTEECGKFGAVNR
CCCHHHHHCCCCEEE
31.4424816145
489AcetylationEVTEECGKFGAVNRV
CCHHHHHCCCCEEEE
52.8926051181
489UbiquitinationEVTEECGKFGAVNRV
CCHHHHHCCCCEEEE
52.8924816145
491UbiquitinationTEECGKFGAVNRVII
HHHHHCCCCEEEEEE
31.9123000965
495UbiquitinationGKFGAVNRVIIYQEK
HCCCCEEEEEEEECC
17.8923000965
498UbiquitinationGAVNRVIIYQEKQGE
CCEEEEEEEECCCCC
2.3824816145
509UbiquitinationKQGEEEDAEIIVKIF
CCCCHHCHHHHHHHH
17.1124816145
512UbiquitinationEEEDAEIIVKIFVEF
CHHCHHHHHHHHHEE
1.6224816145
514UbiquitinationEDAEIIVKIFVEFSI
HCHHHHHHHHHEEEE
21.7324816145
523UbiquitinationFVEFSIASETHKAIQ
HHEEEECCCHHHHHH
41.1624816145
524UbiquitinationVEFSIASETHKAIQA
HEEEECCCHHHHHHH
46.0024816145
524 (in isoform 2)Malonylation-46.0032601280
526UbiquitinationFSIASETHKAIQALN
EEECCCHHHHHHHHC
17.3124816145
540UbiquitinationNGRWFAGRKVVAEVY
CCCCCCCCEEEEEEE
25.7624816145
5412-HydroxyisobutyrylationGRWFAGRKVVAEVYD
CCCCCCCEEEEEEEC
39.89-
541UbiquitinationGRWFAGRKVVAEVYD
CCCCCCCEEEEEEEC
39.8924816145
547PhosphorylationRKVVAEVYDQERFDN
CEEEEEEECHHHCCC
11.92-
555PhosphorylationDQERFDNSDLSA---
CHHHCCCCCCCC---
41.6026462736
558PhosphorylationRFDNSDLSA------
HCCCCCCCC------
36.6030108239
561UbiquitinationNSDLSA---------
CCCCCC---------
24816145
566UbiquitinationA--------------
C--------------
24816145
578Ubiquitination--------------------------
--------------------------
24816145

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 PUF60_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PUF60_HUMAN !!

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 PUF60_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BORC5_HUMANLOH12CR1physical
16189514
PUF60_HUMANPUF60physical
16189514
S30BP_HUMANSAP30BPphysical
16189514
RO60_HUMANTROVE2physical
17353931
OLA1_HUMANOLA1physical
17353931
LA_HUMANSSBphysical
17353931
RNZ2_HUMANELAC2physical
17353931
PDIA1_HUMANP4HBphysical
17353931
FUBP2_HUMANKHSRPphysical
17353931
IF2B1_HUMANIGF2BP1physical
17353931
HNRPC_HUMANHNRNPCphysical
17353931
U2AF2_HUMANU2AF2physical
17353931
HNRPQ_HUMANSYNCRIPphysical
17353931
DDX3X_HUMANDDX3Xphysical
17353931
SF3A3_HUMANSF3A3physical
17353931
IF2B3_HUMANIGF2BP3physical
17353931
IF2B2_HUMANIGF2BP2physical
17353931
SYSM_HUMANSARS2physical
17353931
UGPA_HUMANUGP2physical
17353931
HNRPL_HUMANHNRNPLphysical
17353931
SRS11_HUMANSRSF11physical
17353931
TITIN_HUMANTTNphysical
17353931
MOV10_HUMANMOV10physical
17353931
EWS_HUMANEWSR1physical
17353931
PABP1_HUMANPABPC1physical
17353931
PABP4_HUMANPABPC4physical
17353931
G3BP1_HUMANG3BP1physical
17353931
STOM_HUMANSTOMphysical
17353931
MRM3_HUMANRNMTL1physical
17353931
SF3B1_HUMANSF3B1physical
17353931
ROA3_HUMANHNRNPA3physical
17353931
CHD3_HUMANCHD3physical
16169070
VIME_HUMANVIMphysical
16169070
U2AF2_HUMANU2AF2physical
22939629
SON_HUMANSONphysical
22939629
RL6_HUMANRPL6physical
22939629
S30BP_HUMANSAP30BPphysical
18255255
ID3_HUMANID3physical
18255255
RUXF_HUMANSNRPFphysical
22365833
U2AF2_HUMANU2AF2physical
22365833
PUF60_HUMANPUF60physical
22365833
S30BP_HUMANSAP30BPphysical
22365833
PTBP2_HUMANPTBP2physical
22365833
SIAH1_HUMANSIAH1physical
21988832
NIBL1_HUMANFAM129Bphysical
22863883
H33_HUMANH3F3Aphysical
22863883
HIRP3_HUMANHIRIP3physical
22863883
NUDC_HUMANNUDCphysical
22863883
PAPOA_HUMANPAPOLAphysical
22863883
RO60_HUMANTROVE2physical
22863883
ZYX_HUMANZYXphysical
22863883
PUF60_HUMANPUF60physical
25416956
BLOM7_HUMANKIAA0907physical
25416956
RENT2_HUMANUPF2physical
25416956
S30BP_HUMANSAP30BPphysical
25416956
QRIC1_HUMANQRICH1physical
25416956
MED28_HUMANMED28physical
25416956
K1683_HUMANKIAA1683physical
25416956
BORC5_HUMANLOH12CR1physical
25416956
ARL8A_HUMANARL8Aphysical
25416956
ZG16_HUMANZG16physical
25416956
AIMP2_HUMANAIMP2physical
26344197
MY18A_HUMANMYO18Aphysical
26344197
PR40A_HUMANPRPF40Aphysical
26344197
SF3A3_HUMANSF3A3physical
26344197
SF3B1_HUMANSF3B1physical
26344197
SRRM2_HUMANSRRM2physical
26344197
PUF60_HUMANPUF60physical
21516116
S30BP_HUMANSAP30BPphysical
21516116
GDS1_HUMANRAP1GDS1physical
21516116
SIAH1_HUMANSIAH1physical
21516116
MED28_HUMANMED28physical
21516116

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615583Verheij syndrome (VRJS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PUF60_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-251 AND LYS-454, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-60 AND SER-206, AND MASSSPECTROMETRY.
"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-60, AND MASSSPECTROMETRY.
"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 THR-60, AND MASSSPECTROMETRY.

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