UBF1_HUMAN - dbPTM
UBF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBF1_HUMAN
UniProt AC P17480
Protein Name Nucleolar transcription factor 1
Gene Name UBTF
Organism Homo sapiens (Human).
Sequence Length 764
Subcellular Localization Nucleus, nucleolus .
Protein Description Recognizes the ribosomal RNA gene promoter and activates transcription mediated by RNA polymerase I through cooperative interactions with the transcription factor SL1/TIF-IB complex. It binds specifically to the upstream control element..
Protein Sequence MNGEADCPTDLEMAAPKGQDRWSQEDMLTLLECMKNNLPSNDSSKFKTTESHMDWEKVAFKDFSGDMCKLKWVEISNEVRKFRTLTELILDAQEHVKNPYKGKKLKKHPDFPKKPLTPYFRFFMEKRAKYAKLHPEMSNLDLTKILSKKYKELPEKKKMKYIQDFQREKQEFERNLARFREDHPDLIQNAKKSDIPEKPKTPQQLWYTHEKKVYLKVRPDATTKEVKDSLGKQWSQLSDKKRLKWIHKALEQRKEYEEIMRDYIQKHPELNISEEGITKSTLTKAERQLKDKFDGRPTKPPPNSYSLYCAELMANMKDVPSTERMVLCSQQWKLLSQKEKDAYHKKCDQKKKDYEVELLRFLESLPEEEQQRVLGEEKMLNINKKQATSPASKKPAQEGGKGGSEKPKRPVSAMFIFSEEKRRQLQEERPELSESELTRLLARMWNDLSEKKKAKYKAREAALKAQSERKPGGEREERGKLPESPKRAEEIWQQSVIGDYLARFKNDRVKALKAMEMTWNNMEKKEKLMWIKKAAEDQKRYERELSEMRAPPAATNSSKKMKFQGEPKKPPMNGYQKFSQELLSNGELNHLPLKERMVEIGSRWQRISQSQKEHYKKLAEEQQKQYKVHLDLWVKSLSPQDRAAYKEYISNKRKSMTKLRGPNPKSSRTTLQSKSESEEDDEEDEDDEDEDEEEEDDENGDSSEDGGDSSESSSEDESEDGDENEEDDEDEDDDEDDDEDEDNESEGSSSSSSSSGDSSDSDSN
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
1Acetylation-------MNGEADCP
-------CCCCCCCC
15.2319413330
9PhosphorylationNGEADCPTDLEMAAP
CCCCCCCCCHHHHCC
60.5923401153
17UbiquitinationDLEMAAPKGQDRWSQ
CHHHHCCCCCCCCCH
65.5629967540
23PhosphorylationPKGQDRWSQEDMLTL
CCCCCCCCHHHHHHH
25.2823401153
29PhosphorylationWSQEDMLTLLECMKN
CCHHHHHHHHHHHHH
23.7423532336
33GlutathionylationDMLTLLECMKNNLPS
HHHHHHHHHHHCCCC
4.7922555962
35UbiquitinationLTLLECMKNNLPSND
HHHHHHHHHCCCCCC
55.1029967540
44PhosphorylationNLPSNDSSKFKTTES
CCCCCCCHHCCCCCC
45.00-
45AcetylationLPSNDSSKFKTTESH
CCCCCCHHCCCCCCC
55.6325953088
45UbiquitinationLPSNDSSKFKTTESH
CCCCCCHHCCCCCCC
55.6329967540
47UbiquitinationSNDSSKFKTTESHMD
CCCCHHCCCCCCCCC
59.2729967540
48PhosphorylationNDSSKFKTTESHMDW
CCCHHCCCCCCCCCH
38.6429116813
57UbiquitinationESHMDWEKVAFKDFS
CCCCCHHHHHCCCCC
34.3129967540
61AcetylationDWEKVAFKDFSGDMC
CHHHHHCCCCCCCCC
48.3925953088
61UbiquitinationDWEKVAFKDFSGDMC
CHHHHHCCCCCCCCC
48.3929967540
64PhosphorylationKVAFKDFSGDMCKLK
HHHCCCCCCCCCEEE
43.9729496963
69UbiquitinationDFSGDMCKLKWVEIS
CCCCCCCEEEEEEEC
46.6029967540
71AcetylationSGDMCKLKWVEISNE
CCCCCEEEEEEECHH
34.3926051181
71UbiquitinationSGDMCKLKWVEISNE
CCCCCEEEEEEECHH
34.3933845483
71 (in isoform 1)Ubiquitination-34.3921890473
71 (in isoform 2)Ubiquitination-34.3921890473
97UbiquitinationLDAQEHVKNPYKGKK
HHHHHHCCCCCCCCC
54.8629967540
107UbiquitinationYKGKKLKKHPDFPKK
CCCCCCCCCCCCCCC
71.4629967540
114SumoylationKHPDFPKKPLTPYFR
CCCCCCCCCCCHHHH
45.56-
114AcetylationKHPDFPKKPLTPYFR
CCCCCCCCCCCHHHH
45.5623749302
114SumoylationKHPDFPKKPLTPYFR
CCCCCCCCCCCHHHH
45.56-
114UbiquitinationKHPDFPKKPLTPYFR
CCCCCCCCCCCHHHH
45.56-
117PhosphorylationDFPKKPLTPYFRFFM
CCCCCCCCHHHHHHH
25.1911741541
119PhosphorylationPKKPLTPYFRFFMEK
CCCCCCHHHHHHHHH
11.3623312004
126UbiquitinationYFRFFMEKRAKYAKL
HHHHHHHHHHHHHHH
45.9623000965
129UbiquitinationFFMEKRAKYAKLHPE
HHHHHHHHHHHHCHH
50.1823000965
132AcetylationEKRAKYAKLHPEMSN
HHHHHHHHHCHHHCC
44.2125953088
132UbiquitinationEKRAKYAKLHPEMSN
HHHHHHHHHCHHHCC
44.2123000965
132 (in isoform 1)Ubiquitination-44.2121890473
132 (in isoform 2)Ubiquitination-44.2121890473
144UbiquitinationMSNLDLTKILSKKYK
HCCCCHHHHHHHHHH
49.2829967540
147PhosphorylationLDLTKILSKKYKELP
CCHHHHHHHHHHHCC
30.4920068231
150PhosphorylationTKILSKKYKELPEKK
HHHHHHHHHHCCHHH
17.27-
151UbiquitinationKILSKKYKELPEKKK
HHHHHHHHHCCHHHH
62.75-
156UbiquitinationKYKELPEKKKMKYIQ
HHHHCCHHHHCHHHH
56.6122817900
157UbiquitinationYKELPEKKKMKYIQD
HHHCCHHHHCHHHHH
57.3422817900
158UbiquitinationKELPEKKKMKYIQDF
HHCCHHHHCHHHHHH
52.2522817900
160SumoylationLPEKKKMKYIQDFQR
CCHHHHCHHHHHHHH
48.35-
160SumoylationLPEKKKMKYIQDFQR
CCHHHHCHHHHHHHH
48.35-
160UbiquitinationLPEKKKMKYIQDFQR
CCHHHHCHHHHHHHH
48.3521890473
160 (in isoform 1)Ubiquitination-48.3521890473
160 (in isoform 2)Ubiquitination-48.3521890473
169UbiquitinationIQDFQREKQEFERNL
HHHHHHHHHHHHHHH
58.2629967540
191UbiquitinationPDLIQNAKKSDIPEK
HHHHHHHHHCCCCCC
61.4329967540
193PhosphorylationLIQNAKKSDIPEKPK
HHHHHHHCCCCCCCC
39.8127251275
198UbiquitinationKKSDIPEKPKTPQQL
HHCCCCCCCCCHHHH
46.5929967540
200UbiquitinationSDIPEKPKTPQQLWY
CCCCCCCCCHHHHEE
81.5329967540
201O-linked_GlycosylationDIPEKPKTPQQLWYT
CCCCCCCCHHHHEEE
34.5523301498
201PhosphorylationDIPEKPKTPQQLWYT
CCCCCCCCHHHHEEE
34.5525159151
207PhosphorylationKTPQQLWYTHEKKVY
CCHHHHEEEECCEEE
13.5523312004
208PhosphorylationTPQQLWYTHEKKVYL
CHHHHEEEECCEEEE
16.3925159151
208 (in isoform 2)Phosphorylation-16.3925159151
211UbiquitinationQLWYTHEKKVYLKVR
HHEEEECCEEEEEEC
39.6832015554
212UbiquitinationLWYTHEKKVYLKVRP
HEEEECCEEEEEECC
32.8829967540
216UbiquitinationHEKKVYLKVRPDATT
ECCEEEEEECCCCCH
20.6421890473
216 (in isoform 2)Ubiquitination-20.6421890473
224UbiquitinationVRPDATTKEVKDSLG
ECCCCCHHHHHHHHH
57.0429967540
229UbiquitinationTTKEVKDSLGKQWSQ
CHHHHHHHHHHHHHH
33.0521890473
229 (in isoform 2)Ubiquitination-33.0521890473
232TrimethylationEVKDSLGKQWSQLSD
HHHHHHHHHHHHHCH
54.62-
232MethylationEVKDSLGKQWSQLSD
HHHHHHHHHHHHHCH
54.62-
232UbiquitinationEVKDSLGKQWSQLSD
HHHHHHHHHHHHHCH
54.6229967540
238PhosphorylationGKQWSQLSDKKRLKW
HHHHHHHCHHHHHHH
39.4825159151
240UbiquitinationQWSQLSDKKRLKWIH
HHHHHCHHHHHHHHH
36.1029967540
242UbiquitinationSQLSDKKRLKWIHKA
HHHCHHHHHHHHHHH
47.4421963094
242 (in isoform 2)Ubiquitination-47.4421890473
244UbiquitinationLSDKKRLKWIHKALE
HCHHHHHHHHHHHHH
48.40-
247UbiquitinationKKRLKWIHKALEQRK
HHHHHHHHHHHHHHH
14.2822817900
248UbiquitinationKRLKWIHKALEQRKE
HHHHHHHHHHHHHHH
45.6029967540
254TrimethylationHKALEQRKEYEEIMR
HHHHHHHHHHHHHHH
65.43-
254MethylationHKALEQRKEYEEIMR
HHHHHHHHHHHHHHH
65.43-
254UbiquitinationHKALEQRKEYEEIMR
HHHHHHHHHHHHHHH
65.4329967540
262UbiquitinationEYEEIMRDYIQKHPE
HHHHHHHHHHHHCCC
27.7529967540
263PhosphorylationYEEIMRDYIQKHPEL
HHHHHHHHHHHCCCC
8.5528152594
266AcetylationIMRDYIQKHPELNIS
HHHHHHHHCCCCCCC
52.1226051181
266UbiquitinationIMRDYIQKHPELNIS
HHHHHHHHCCCCCCC
52.1223000965
266 (in isoform 1)Ubiquitination-52.1221890473
273PhosphorylationKHPELNISEEGITKS
HCCCCCCCCCCCCHH
28.6425159151
278PhosphorylationNISEEGITKSTLTKA
CCCCCCCCHHHHHHH
29.7830576142
279AcetylationISEEGITKSTLTKAE
CCCCCCCHHHHHHHH
39.2525953088
279SumoylationISEEGITKSTLTKAE
CCCCCCCHHHHHHHH
39.25-
279UbiquitinationISEEGITKSTLTKAE
CCCCCCCHHHHHHHH
39.2521906983
279 (in isoform 1)Ubiquitination-39.2521890473
284SumoylationITKSTLTKAERQLKD
CCHHHHHHHHHHHHH
51.90-
284AcetylationITKSTLTKAERQLKD
CCHHHHHHHHHHHHH
51.9023749302
284SumoylationITKSTLTKAERQLKD
CCHHHHHHHHHHHHH
51.90-
284UbiquitinationITKSTLTKAERQLKD
CCHHHHHHHHHHHHH
51.9022817900
296UbiquitinationLKDKFDGRPTKPPPN
HHHCCCCCCCCCCCC
37.2432015554
299AcetylationKFDGRPTKPPPNSYS
CCCCCCCCCCCCCHH
59.2025953088
299UbiquitinationKFDGRPTKPPPNSYS
CCCCCCCCCCCCCHH
59.2029967540
301UbiquitinationDGRPTKPPPNSYSLY
CCCCCCCCCCCHHHH
42.1129967540
306PhosphorylationKPPPNSYSLYCAELM
CCCCCCHHHHHHHHH
16.81-
308PhosphorylationPPNSYSLYCAELMAN
CCCCHHHHHHHHHHC
5.44-
314UbiquitinationLYCAELMANMKDVPS
HHHHHHHHCCCCCCC
26.1129967540
315UbiquitinationYCAELMANMKDVPST
HHHHHHHCCCCCCCC
24.8729967540
321PhosphorylationANMKDVPSTERMVLC
HCCCCCCCCHHHHHH
42.6329978859
322PhosphorylationNMKDVPSTERMVLCS
CCCCCCCCHHHHHHH
22.8829978859
329PhosphorylationTERMVLCSQQWKLLS
CHHHHHHHHHHHHHH
22.6529978859
333AcetylationVLCSQQWKLLSQKEK
HHHHHHHHHHHHHHH
34.9025953088
333UbiquitinationVLCSQQWKLLSQKEK
HHHHHHHHHHHHHHH
34.9032015554
336PhosphorylationSQQWKLLSQKEKDAY
HHHHHHHHHHHHHHH
50.03-
338UbiquitinationQWKLLSQKEKDAYHK
HHHHHHHHHHHHHHH
64.4529967540
341UbiquitinationLLSQKEKDAYHKKCD
HHHHHHHHHHHHHHH
54.1529967540
347UbiquitinationKDAYHKKCDQKKKDY
HHHHHHHHHHHCCHH
8.8129967540
351UbiquitinationHKKCDQKKKDYEVEL
HHHHHHHCCHHHHHH
45.2929967540
3522-HydroxyisobutyrylationKKCDQKKKDYEVELL
HHHHHHCCHHHHHHH
73.00-
352AcetylationKKCDQKKKDYEVELL
HHHHHHCCHHHHHHH
73.0021546905
352PhosphorylationKKCDQKKKDYEVELL
HHHHHHCCHHHHHHH
73.0033259812
352UbiquitinationKKCDQKKKDYEVELL
HHHHHHCCHHHHHHH
73.0029967540
364PhosphorylationELLRFLESLPEEEQQ
HHHHHHHHCCHHHHH
51.9125849741
378UbiquitinationQRVLGEEKMLNINKK
HHHHCHHHHHCCCHH
44.3729967540
3842-HydroxyisobutyrylationEKMLNINKKQATSPA
HHHHCCCHHHCCCCC
42.33-
384AcetylationEKMLNINKKQATSPA
HHHHCCCHHHCCCCC
42.3325953088
384UbiquitinationEKMLNINKKQATSPA
HHHHCCCHHHCCCCC
42.3329967540
385AcetylationKMLNINKKQATSPAS
HHHCCCHHHCCCCCC
40.4519813169
385UbiquitinationKMLNINKKQATSPAS
HHHCCCHHHCCCCCC
40.45-
388PhosphorylationNINKKQATSPASKKP
CCCHHHCCCCCCCCC
32.5228176443
389PhosphorylationINKKQATSPASKKPA
CCHHHCCCCCCCCCC
22.8323401153
392PhosphorylationKQATSPASKKPAQEG
HHCCCCCCCCCCCCC
44.5923403867
393AcetylationQATSPASKKPAQEGG
HCCCCCCCCCCCCCC
65.9525953088
394AcetylationATSPASKKPAQEGGK
CCCCCCCCCCCCCCC
42.9912435135
401AcetylationKPAQEGGKGGSEKPK
CCCCCCCCCCCCCCC
71.5926051181
406AcetylationGGKGGSEKPKRPVSA
CCCCCCCCCCCCCEE
58.5012435143
412PhosphorylationEKPKRPVSAMFIFSE
CCCCCCCEEEEECCH
19.3925159151
418PhosphorylationVSAMFIFSEEKRRQL
CEEEEECCHHHHHHH
39.7824732914
421UbiquitinationMFIFSEEKRRQLQEE
EEECCHHHHHHHHHH
49.1529967540
427UbiquitinationEKRRQLQEERPELSE
HHHHHHHHHCCCCCH
65.6524816145
429MethylationRRQLQEERPELSESE
HHHHHHHCCCCCHHH
29.2812018527
433PhosphorylationQEERPELSESELTRL
HHHCCCCCHHHHHHH
37.1023401153
435PhosphorylationERPELSESELTRLLA
HCCCCCHHHHHHHHH
34.2330266825
438PhosphorylationELSESELTRLLARMW
CCCHHHHHHHHHHHH
18.4129255136
443MethylationELTRLLARMWNDLSE
HHHHHHHHHHHHHCH
30.5312018535
443UbiquitinationELTRLLARMWNDLSE
HHHHHHHHHHHHHCH
30.5332142685
449O-linked_GlycosylationARMWNDLSEKKKAKY
HHHHHHHCHHHHHHH
50.6723301498
449PhosphorylationARMWNDLSEKKKAKY
HHHHHHHCHHHHHHH
50.6725159151
4512-HydroxyisobutyrylationMWNDLSEKKKAKYKA
HHHHHCHHHHHHHHH
57.08-
452UbiquitinationWNDLSEKKKAKYKAR
HHHHCHHHHHHHHHH
54.64-
456PhosphorylationSEKKKAKYKAREAAL
CHHHHHHHHHHHHHH
18.1025884760
464SumoylationKAREAALKAQSERKP
HHHHHHHHHHHHCCC
39.39-
464AcetylationKAREAALKAQSERKP
HHHHHHHHHHHHCCC
39.3925953088
464SumoylationKAREAALKAQSERKP
HHHHHHHHHHHHCCC
39.39-
464UbiquitinationKAREAALKAQSERKP
HHHHHHHHHHHHCCC
39.3924816145
480UbiquitinationGEREERGKLPESPKR
CCHHHCCCCCCCHHH
68.0732142685
484PhosphorylationERGKLPESPKRAEEI
HCCCCCCCHHHHHHH
33.5129255136
4862-HydroxyisobutyrylationGKLPESPKRAEEIWQ
CCCCCCHHHHHHHHH
73.79-
495PhosphorylationAEEIWQQSVIGDYLA
HHHHHHHHHHHHHHH
10.7023312004
500PhosphorylationQQSVIGDYLARFKND
HHHHHHHHHHHHCHH
9.3124732914
524AcetylationMTWNNMEKKEKLMWI
HHHCCHHHHHHHHHH
56.3025953088
5272-HydroxyisobutyrylationNNMEKKEKLMWIKKA
CCHHHHHHHHHHHHH
53.15-
546PhosphorylationKRYERELSEMRAPPA
HHHHHHHHHCCCCCC
25.2921815630
555PhosphorylationMRAPPAATNSSKKMK
CCCCCCCCCCCCCCC
37.4327251275
557PhosphorylationAPPAATNSSKKMKFQ
CCCCCCCCCCCCCCC
38.9025849741
557UbiquitinationAPPAATNSSKKMKFQ
CCCCCCCCCCCCCCC
38.9032015554
558PhosphorylationPPAATNSSKKMKFQG
CCCCCCCCCCCCCCC
38.0627251275
5592-HydroxyisobutyrylationPAATNSSKKMKFQGE
CCCCCCCCCCCCCCC
57.62-
559AcetylationPAATNSSKKMKFQGE
CCCCCCCCCCCCCCC
57.6225953088
575PhosphorylationKKPPMNGYQKFSQEL
CCCCCCHHHHHHHHH
11.9729759185
584PhosphorylationKFSQELLSNGELNHL
HHHHHHHHCCCCCCC
56.2525159151
587UbiquitinationQELLSNGELNHLPLK
HHHHHCCCCCCCCHH
51.1229967540
5942-HydroxyisobutyrylationELNHLPLKERMVEIG
CCCCCCHHHHHHHHH
41.14-
594AcetylationELNHLPLKERMVEIG
CCCCCCHHHHHHHHH
41.1426051181
594UbiquitinationELNHLPLKERMVEIG
CCCCCCHHHHHHHHH
41.1432015554
601PhosphorylationKERMVEIGSRWQRIS
HHHHHHHHHHHHHHH
9.5432645325
602PhosphorylationERMVEIGSRWQRISQ
HHHHHHHHHHHHHHH
35.6919664994
608PhosphorylationGSRWQRISQSQKEHY
HHHHHHHHHHHHHHH
26.4323312004
609UbiquitinationSRWQRISQSQKEHYK
HHHHHHHHHHHHHHH
47.7329967540
610PhosphorylationRWQRISQSQKEHYKK
HHHHHHHHHHHHHHH
36.1123312004
615UbiquitinationSQSQKEHYKKLAEEQ
HHHHHHHHHHHHHHH
15.7724816145
621UbiquitinationHYKKLAEEQQKQYKV
HHHHHHHHHHHHHHH
53.3424816145
624AcetylationKLAEEQQKQYKVHLD
HHHHHHHHHHHHHHH
56.1226051181
624UbiquitinationKLAEEQQKQYKVHLD
HHHHHHHHHHHHHHH
56.1229967540
627UbiquitinationEEQQKQYKVHLDLWV
HHHHHHHHHHHHHHH
22.23-
632UbiquitinationQYKVHLDLWVKSLSP
HHHHHHHHHHHCCCH
7.7324816145
635AcetylationVHLDLWVKSLSPQDR
HHHHHHHHCCCHHHH
33.8126051181
636PhosphorylationHLDLWVKSLSPQDRA
HHHHHHHCCCHHHHH
25.1824732914
638PhosphorylationDLWVKSLSPQDRAAY
HHHHHCCCHHHHHHH
27.8325159151
638UbiquitinationDLWVKSLSPQDRAAY
HHHHHCCCHHHHHHH
27.8324816145
642MethylationKSLSPQDRAAYKEYI
HCCCHHHHHHHHHHH
18.83115919405
646AcetylationPQDRAAYKEYISNKR
HHHHHHHHHHHHHHH
39.0426051181
646UbiquitinationPQDRAAYKEYISNKR
HHHHHHHHHHHHHHH
39.0429967540
648PhosphorylationDRAAYKEYISNKRKS
HHHHHHHHHHHHHHH
12.90-
6522-HydroxyisobutyrylationYKEYISNKRKSMTKL
HHHHHHHHHHHCHHC
55.18-
652AcetylationYKEYISNKRKSMTKL
HHHHHHHHHHHCHHC
55.1825953088
652UbiquitinationYKEYISNKRKSMTKL
HHHHHHHHHHHCHHC
55.1824816145
655PhosphorylationYISNKRKSMTKLRGP
HHHHHHHHCHHCCCC
35.4029449344
657PhosphorylationSNKRKSMTKLRGPNP
HHHHHHCHHCCCCCC
33.7429449344
658UbiquitinationNKRKSMTKLRGPNPK
HHHHHCHHCCCCCCC
27.7824816145
666PhosphorylationLRGPNPKSSRTTLQS
CCCCCCCCCCCCCCC
26.7219651622
669UbiquitinationPNPKSSRTTLQSKSE
CCCCCCCCCCCCCCC
33.5324816145
675UbiquitinationRTTLQSKSESEEDDE
CCCCCCCCCCCCCCC
52.1524816145

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
117TPhosphorylationKinaseMAPK1P28482
GPS
117TPhosphorylationKinaseMAPK3P27361
GPS
201TPhosphorylationKinaseMAPK1P28482
GPS
201TPhosphorylationKinaseMAPK3P27361
GPS
389SPhosphorylationKinaseCDK2P24941
PhosphoELM
412SPhosphorylationKinasePKCIP41743
PSP
484SPhosphorylationKinaseCDK4P11802
PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBF1_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 UBF1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TBP_HUMANTBPphysical
8552083
TAF1C_HUMANTAF1Cphysical
11698641
RPA34_HUMANCD3EAPphysical
9426281
RB_HUMANRB1physical
11042686
ACTN4_HUMANACTN4physical
20197409
TLE1_HUMANTLE1physical
20160071
IRS1_HUMANIRS1physical
17332342
PK3CA_HUMANPIK3CAphysical
17332342
SIR7_HUMANSIRT7physical
22147730
RPA1_HUMANPOLR1Aphysical
22147730
MBB1A_HUMANMYBBP1Aphysical
22147730
SMCA5_HUMANSMARCA5physical
22147730
SIR7_HUMANSIRT7physical
22586326
HDAC1_HUMANHDAC1physical
22393235
RUNX2_HUMANRUNX2physical
22393235
RB_HUMANRB1physical
7877691
WDR70_HUMANWDR70physical
22939629
YETS4_HUMANYEATS4physical
22939629
KAT2B_HUMANKAT2Bphysical
23667505
AP3M1_HUMANAP3M1physical
26344197
RTF1_HUMANRTF1physical
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 UBF1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-484, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-484, 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; SER-412; SER-484AND SER-638, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-201; SER-484 ANDSER-638, AND MASS 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 SER-484, AND MASSSPECTROMETRY.

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