RBP56_HUMAN - dbPTM
RBP56_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBP56_HUMAN
UniProt AC Q92804
Protein Name TATA-binding protein-associated factor 2N
Gene Name TAF15
Organism Homo sapiens (Human).
Sequence Length 592
Subcellular Localization Nucleus . Cytoplasm . Shuttles from the nucleus to the cytoplasm.
Protein Description RNA and ssDNA-binding protein that may play specific roles during transcription initiation at distinct promoters. Can enter the preinitiation complex together with the RNA polymerase II (Pol II)..
Protein Sequence MSDSGSYGQSGGEQQSYSTYGNPGSQGYGQASQSYSGYGQTTDSSYGQNYSGYSSYGQSQSGYSQSYGGYENQKQSSYSQQPYNNQGQQQNMESSGSQGGRAPSYDQPDYGQQDSYDQQSGYDQHQGSYDEQSNYDQQHDSYSQNQQSYHSQRENYSHHTQDDRRDVSRYGEDNRGYGGSQGGGRGRGGYDKDGRGPMTGSSGGDRGGFKNFGGHRDYGPRTDADSESDNSDNNTIFVQGLGEGVSTDQVGEFFKQIGIIKTNKKTGKPMINLYTDKDTGKPKGEATVSFDDPPSAKAAIDWFDGKEFHGNIIKVSFATRRPEFMRGGGSGGGRRGRGGYRGRGGFQGRGGDPKSGDWVCPNPSCGNMNFARRNSCNQCNEPRPEDSRPSGGDFRGRGYGGERGYRGRGGRGGDRGGYGGDRSGGGYGGDRSSGGGYSGDRSGGGYGGDRSGGGYGGDRGGGYGGDRGGGYGGDRGGGYGGDRGGYGGDRGGGYGGDRGGYGGDRGGYGGDRGGYGGDRGGYGGDRSRGGYGGDRGGGSGYGGDRSGGYGGDRSGGGYGGDRGGGYGGDRGGYGGKMGGRNDYRNDQRNRPY
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
4Phosphorylation----MSDSGSYGQSG
----CCCCCCCCCCC
23.4925137130
28UbiquitinationGNPGSQGYGQASQSY
CCCCCCCCCCCCCCC
9.8322053931
37UbiquitinationQASQSYSGYGQTTDS
CCCCCCCCCCCCCCC
23.5121890473
50PhosphorylationDSSYGQNYSGYSSYG
CCCCCCCCCCCCCCC
8.79-
70PhosphorylationYSQSYGGYENQKQSS
CCCCCCCCCCCCCCC
13.82-
76PhosphorylationGYENQKQSSYSQQPY
CCCCCCCCCCCCCCC
37.9721945579
76 (in isoform 2)Phosphorylation-37.97-
77PhosphorylationYENQKQSSYSQQPYN
CCCCCCCCCCCCCCC
26.7221945579
78PhosphorylationENQKQSSYSQQPYNN
CCCCCCCCCCCCCCC
18.7521945579
79PhosphorylationNQKQSSYSQQPYNNQ
CCCCCCCCCCCCCCH
25.0421945579
83PhosphorylationSSYSQQPYNNQGQQQ
CCCCCCCCCCHHHHH
23.5421945579
94PhosphorylationGQQQNMESSGSQGGR
HHHHHHHCCCCCCCC
29.2721945579
94 (in isoform 2)Phosphorylation-29.27-
95PhosphorylationQQQNMESSGSQGGRA
HHHHHHCCCCCCCCC
29.2021945579
97PhosphorylationQNMESSGSQGGRAPS
HHHHCCCCCCCCCCC
27.8321945579
104PhosphorylationSQGGRAPSYDQPDYG
CCCCCCCCCCCCCCC
40.1224275569
110PhosphorylationPSYDQPDYGQQDSYD
CCCCCCCCCCCCCCC
24.4220736484
115PhosphorylationPDYGQQDSYDQQSGY
CCCCCCCCCCCCCCC
26.6930576142
116PhosphorylationDYGQQDSYDQQSGYD
CCCCCCCCCCCCCCC
26.5130576142
120PhosphorylationQDSYDQQSGYDQHQG
CCCCCCCCCCCCCCC
33.4222817901
122PhosphorylationSYDQQSGYDQHQGSY
CCCCCCCCCCCCCCC
20.0630576142
128PhosphorylationGYDQHQGSYDEQSNY
CCCCCCCCCCCCCCC
23.8830576142
133PhosphorylationQGSYDEQSNYDQQHD
CCCCCCCCCCHHHCC
35.0030576142
135PhosphorylationSYDEQSNYDQQHDSY
CCCCCCCCHHHCCHH
22.00-
142PhosphorylationYDQQHDSYSQNQQSY
CHHHCCHHHHHHHHH
21.97-
149PhosphorylationYSQNQQSYHSQRENY
HHHHHHHHHHCHHHC
10.93-
156PhosphorylationYHSQRENYSHHTQDD
HHHCHHHCCCCCCCH
12.4828796482
157PhosphorylationHSQRENYSHHTQDDR
HHCHHHCCCCCCCHH
22.0028796482
160PhosphorylationRENYSHHTQDDRRDV
HHHCCCCCCCHHHCH
28.4129978859
164MethylationSHHTQDDRRDVSRYG
CCCCCCHHHCHHHHC
45.0182955195
170PhosphorylationDRRDVSRYGEDNRGY
HHHCHHHHCCCCCCC
19.84-
175MethylationSRYGEDNRGYGGSQG
HHHCCCCCCCCCCCC
52.6254559741
177PhosphorylationYGEDNRGYGGSQGGG
HCCCCCCCCCCCCCC
18.3125839225
180PhosphorylationDNRGYGGSQGGGRGR
CCCCCCCCCCCCCCC
22.6825627689
185DimethylationGGSQGGGRGRGGYDK
CCCCCCCCCCCCCCC
34.60-
185MethylationGGSQGGGRGRGGYDK
CCCCCCCCCCCCCCC
34.6016288479
187DimethylationSQGGGRGRGGYDKDG
CCCCCCCCCCCCCCC
33.72-
187MethylationSQGGGRGRGGYDKDG
CCCCCCCCCCCCCCC
33.7216288487
190PhosphorylationGGRGRGGYDKDGRGP
CCCCCCCCCCCCCCC
23.73-
192TrimethylationRGRGGYDKDGRGPMT
CCCCCCCCCCCCCCC
54.31-
192MethylationRGRGGYDKDGRGPMT
CCCCCCCCCCCCCCC
54.3123748837
195MethylationGGYDKDGRGPMTGSS
CCCCCCCCCCCCCCC
57.0654559787
199PhosphorylationKDGRGPMTGSSGGDR
CCCCCCCCCCCCCCC
36.73-
201PhosphorylationGRGPMTGSSGGDRGG
CCCCCCCCCCCCCCC
19.35-
202PhosphorylationRGPMTGSSGGDRGGF
CCCCCCCCCCCCCCC
48.41-
203MethylationGPMTGSSGGDRGGFK
CCCCCCCCCCCCCCC
43.6615782174
203 (in isoform 2)Methylation-43.66-
206Asymmetric dimethylarginineTGSSGGDRGGFKNFG
CCCCCCCCCCCCCCC
50.86-
206MethylationTGSSGGDRGGFKNFG
CCCCCCCCCCCCCCC
50.8624129315
206UbiquitinationTGSSGGDRGGFKNFG
CCCCCCCCCCCCCCC
50.8622053931
210"N6,N6-dimethyllysine"GGDRGGFKNFGGHRD
CCCCCCCCCCCCCCC
55.42-
210MethylationGGDRGGFKNFGGHRD
CCCCCCCCCCCCCCC
55.4223748837
215UbiquitinationGFKNFGGHRDYGPRT
CCCCCCCCCCCCCCC
21.5921890473
218PhosphorylationNFGGHRDYGPRTDAD
CCCCCCCCCCCCCCC
29.0525394399
219 (in isoform 2)Phosphorylation-14.98-
222PhosphorylationHRDYGPRTDADSESD
CCCCCCCCCCCCCCC
38.3826503892
223PhosphorylationRDYGPRTDADSESDN
CCCCCCCCCCCCCCC
50.0532142685
223 (in isoform 2)Phosphorylation-50.05-
225 (in isoform 2)Phosphorylation-56.60-
226PhosphorylationGPRTDADSESDNSDN
CCCCCCCCCCCCCCC
40.4930278072
228PhosphorylationRTDADSESDNSDNNT
CCCCCCCCCCCCCCE
46.1530278072
228 (in isoform 2)Phosphorylation-46.15-
231PhosphorylationADSESDNSDNNTIFV
CCCCCCCCCCCEEEE
46.8630278072
235PhosphorylationSDNSDNNTIFVQGLG
CCCCCCCEEEEECCC
23.2628176443
246PhosphorylationQGLGEGVSTDQVGEF
ECCCCCCCHHHHHHH
36.8020873877
247PhosphorylationGLGEGVSTDQVGEFF
CCCCCCCHHHHHHHH
28.2220873877
258UbiquitinationGEFFKQIGIIKTNKK
HHHHHHHCCEEECCC
17.0529967540
261UbiquitinationFKQIGIIKTNKKTGK
HHHHCCEEECCCCCC
44.0929967540
262UbiquitinationKQIGIIKTNKKTGKP
HHHCCEEECCCCCCC
41.6929967540
265AcetylationGIIKTNKKTGKPMIN
CCEEECCCCCCCCEE
65.6619608861
265SumoylationGIIKTNKKTGKPMIN
CCEEECCCCCCCCEE
65.6628112733
265UbiquitinationGIIKTNKKTGKPMIN
CCEEECCCCCCCCEE
65.6633845483
265 (in isoform 2)Acetylation-65.66-
268AcetylationKTNKKTGKPMINLYT
EECCCCCCCCEEEEE
36.3219608861
268SumoylationKTNKKTGKPMINLYT
EECCCCCCCCEEEEE
36.3228112733
268UbiquitinationKTNKKTGKPMINLYT
EECCCCCCCCEEEEE
36.3233845483
277"N6,N6-dimethyllysine"MINLYTDKDTGKPKG
CEEEEECCCCCCCCC
49.76-
2772-HydroxyisobutyrylationMINLYTDKDTGKPKG
CEEEEECCCCCCCCC
49.76-
277AcetylationMINLYTDKDTGKPKG
CEEEEECCCCCCCCC
49.7626051181
277MethylationMINLYTDKDTGKPKG
CEEEEECCCCCCCCC
49.76-
277UbiquitinationMINLYTDKDTGKPKG
CEEEEECCCCCCCCC
49.76-
280UbiquitinationLYTDKDTGKPKGEAT
EEECCCCCCCCCEEE
55.1733845483
281AcetylationYTDKDTGKPKGEATV
EECCCCCCCCCEEEE
45.7226051181
283SumoylationDKDTGKPKGEATVSF
CCCCCCCCCEEEEEE
73.24-
283UbiquitinationDKDTGKPKGEATVSF
CCCCCCCCCEEEEEE
73.2433845483
287PhosphorylationGKPKGEATVSFDDPP
CCCCCEEEEEECCCC
16.6325850435
289PhosphorylationPKGEATVSFDDPPSA
CCCEEEEEECCCCCC
20.7125159151
294UbiquitinationTVSFDDPPSAKAAID
EEEECCCCCCCEEEE
54.6422053931
294 (in isoform 2)Ubiquitination-54.6421890473
295PhosphorylationVSFDDPPSAKAAIDW
EEECCCCCCCEEEEC
48.0325159151
297UbiquitinationFDDPPSAKAAIDWFD
ECCCCCCCEEEECCC
42.5621890473
297SumoylationFDDPPSAKAAIDWFD
ECCCCCCCEEEECCC
42.56-
297UbiquitinationFDDPPSAKAAIDWFD
ECCCCCCCEEEECCC
42.5622053931
297 (in isoform 1)Ubiquitination-42.5621890473
303UbiquitinationAKAAIDWFDGKEFHG
CCEEEECCCCCEECC
8.6621890473
303 (in isoform 2)Ubiquitination-8.6621890473
306UbiquitinationAIDWFDGKEFHGNII
EEECCCCCEECCCEE
60.0821890473
3062-HydroxyisobutyrylationAIDWFDGKEFHGNII
EEECCCCCEECCCEE
60.08-
306AcetylationAIDWFDGKEFHGNII
EEECCCCCEECCCEE
60.0826051181
306UbiquitinationAIDWFDGKEFHGNII
EEECCCCCEECCCEE
60.0829967540
306 (in isoform 1)Ubiquitination-60.0821890473
311UbiquitinationDGKEFHGNIIKVSFA
CCCEECCCEEEEEEE
25.0033845483
314UbiquitinationEFHGNIIKVSFATRR
EECCCEEEEEEECCC
28.2033845483
320MethylationIKVSFATRRPEFMRG
EEEEEECCCCHHHCC
49.04-
321MethylationKVSFATRRPEFMRGG
EEEEECCCCHHHCCC
30.6497816469
326DimethylationTRRPEFMRGGGSGGG
CCCCHHHCCCCCCCC
46.02-
326MethylationTRRPEFMRGGGSGGG
CCCCHHHCCCCCCCC
46.0218583751
330PhosphorylationEFMRGGGSGGGRRGR
HHHCCCCCCCCCCCC
37.22-
334MethylationGGGSGGGRRGRGGYR
CCCCCCCCCCCCCCC
40.9597816459
335MethylationGGSGGGRRGRGGYRG
CCCCCCCCCCCCCCC
42.3024411387
349MethylationGRGGFQGRGGDPKSG
CCCCCCCCCCCCCCC
34.83115387919
354AcetylationQGRGGDPKSGDWVCP
CCCCCCCCCCCEECC
72.3426051181
354UbiquitinationQGRGGDPKSGDWVCP
CCCCCCCCCCCEECC
72.34-
355PhosphorylationGRGGDPKSGDWVCPN
CCCCCCCCCCEECCC
47.5826714015
375PhosphorylationMNFARRNSCNQCNEP
CCHHHHCCCCCCCCC
16.7829255136
383MethylationCNQCNEPRPEDSRPS
CCCCCCCCCCCCCCC
40.8581121021
387PhosphorylationNEPRPEDSRPSGGDF
CCCCCCCCCCCCCCC
44.4120873877
388MethylationEPRPEDSRPSGGDFR
CCCCCCCCCCCCCCC
41.5554559763
395MethylationRPSGGDFRGRGYGGE
CCCCCCCCCCCCCCC
38.3412019843
397DimethylationSGGDFRGRGYGGERG
CCCCCCCCCCCCCCC
30.79-
397MethylationSGGDFRGRGYGGERG
CCCCCCCCCCCCCCC
30.7930761291
403MethylationGRGYGGERGYRGRGG
CCCCCCCCCCCCCCC
51.2030761297
412MethylationYRGRGGRGGDRGGYG
CCCCCCCCCCCCCCC
45.7015782174
412 (in isoform 2)Methylation-45.70-
415MethylationRGGRGGDRGGYGGDR
CCCCCCCCCCCCCCC
43.6524395775
418PhosphorylationRGGDRGGYGGDRSGG
CCCCCCCCCCCCCCC
22.28-
422MethylationRGGYGGDRSGGGYGG
CCCCCCCCCCCCCCC
40.2497770775
423PhosphorylationGGYGGDRSGGGYGGD
CCCCCCCCCCCCCCC
46.6723403867
427PhosphorylationGDRSGGGYGGDRSSG
CCCCCCCCCCCCCCC
22.6224732914
429 (in isoform 2)Phosphorylation-20.76-
430 (in isoform 2)Phosphorylation-42.81-
431MethylationGGGYGGDRSSGGGYS
CCCCCCCCCCCCCCC
35.6824129315
432PhosphorylationGGYGGDRSSGGGYSG
CCCCCCCCCCCCCCC
37.7721955146
433PhosphorylationGYGGDRSSGGGYSGD
CCCCCCCCCCCCCCC
42.2122617229
434 (in isoform 2)Phosphorylation-34.49-
435PhosphorylationGGDRSSGGGYSGDRS
CCCCCCCCCCCCCCC
33.5433259812
437PhosphorylationDRSSGGGYSGDRSGG
CCCCCCCCCCCCCCC
16.8622115753
438PhosphorylationRSSGGGYSGDRSGGG
CCCCCCCCCCCCCCC
37.1822115753
441MethylationGGGYSGDRSGGGYGG
CCCCCCCCCCCCCCC
40.5080700905
442PhosphorylationGGYSGDRSGGGYGGD
CCCCCCCCCCCCCCC
46.6723403867
446PhosphorylationGDRSGGGYGGDRSGG
CCCCCCCCCCCCCCC
22.6223403867
450MethylationGGGYGGDRSGGGYGG
CCCCCCCCCCCCCCC
40.2431118111
451PhosphorylationGGYGGDRSGGGYGGD
CCCCCCCCCCCCCCC
46.6721406692
455PhosphorylationGDRSGGGYGGDRGGG
CCCCCCCCCCCCCCC
22.6218083107
456MethylationDRSGGGYGGDRGGGY
CCCCCCCCCCCCCCC
34.5015782174
456 (in isoform 2)Methylation-34.50-
459DimethylationGGGYGGDRGGGYGGD
CCCCCCCCCCCCCCC
49.26-
459MethylationGGGYGGDRGGGYGGD
CCCCCCCCCCCCCCC
49.2624129315
463PhosphorylationGGDRGGGYGGDRGGG
CCCCCCCCCCCCCCC
22.6225839225
464 (in isoform 2)Methylation-34.50-
467DimethylationGGGYGGDRGGGYGGD
CCCCCCCCCCCCCCC
49.26-
467MethylationGGGYGGDRGGGYGGD
CCCCCCCCCCCCCCC
49.2612019863
471PhosphorylationGGDRGGGYGGDRGGG
CCCCCCCCCCCCCCC
22.6218083107
472MethylationGDRGGGYGGDRGGGY
CCCCCCCCCCCCCCC
34.5015782174
472 (in isoform 2)Methylation-34.50-
475DimethylationGGGYGGDRGGGYGGD
CCCCCCCCCCCCCCC
49.26-
475MethylationGGGYGGDRGGGYGGD
CCCCCCCCCCCCCCC
49.2624129315
479PhosphorylationGGDRGGGYGGDRGGY
CCCCCCCCCCCCCCC
22.6218083107
480MethylationGDRGGGYGGDRGGYG
CCCCCCCCCCCCCCC
34.5015782174
480 (in isoform 2)Methylation-34.50-
483DimethylationGGGYGGDRGGYGGDR
CCCCCCCCCCCCCCC
43.65-
483MethylationGGGYGGDRGGYGGDR
CCCCCCCCCCCCCCC
43.6512019883
486PhosphorylationYGGDRGGYGGDRGGG
CCCCCCCCCCCCCCC
22.2818083107
487MethylationGGDRGGYGGDRGGGY
CCCCCCCCCCCCCCC
34.5015782174
487 (in isoform 2)Methylation-34.50-
490DimethylationRGGYGGDRGGGYGGD
CCCCCCCCCCCCCCC
49.26-
490MethylationRGGYGGDRGGGYGGD
CCCCCCCCCCCCCCC
49.2612019893
494PhosphorylationGGDRGGGYGGDRGGY
CCCCCCCCCCCCCCC
22.6218083107
495MethylationGDRGGGYGGDRGGYG
CCCCCCCCCCCCCCC
34.5015782174
495 (in isoform 2)Methylation-34.50-
498DimethylationGGGYGGDRGGYGGDR
CCCCCCCCCCCCCCC
43.65-
498MethylationGGGYGGDRGGYGGDR
CCCCCCCCCCCCCCC
43.6512019901
501PhosphorylationYGGDRGGYGGDRGGY
CCCCCCCCCCCCCCC
22.2818083107
502MethylationGGDRGGYGGDRGGYG
CCCCCCCCCCCCCCC
34.5015782174
502 (in isoform 2)Methylation-34.50-
505DimethylationRGGYGGDRGGYGGDR
CCCCCCCCCCCCCCC
43.65-
505MethylationRGGYGGDRGGYGGDR
CCCCCCCCCCCCCCC
43.6524383667
508PhosphorylationYGGDRGGYGGDRGGY
CCCCCCCCCCCCCCC
22.2818083107
509 (in isoform 2)Methylation-34.50-
512DimethylationRGGYGGDRGGYGGDR
CCCCCCCCCCCCCCC
43.65-
512MethylationRGGYGGDRGGYGGDR
CCCCCCCCCCCCCCC
43.6524383673
515PhosphorylationYGGDRGGYGGDRGGY
CCCCCCCCCCCCCCC
22.2818083107
516 (in isoform 2)Methylation-34.50-
519DimethylationRGGYGGDRGGYGGDR
CCCCCCCCCCCCCCC
43.65-
519MethylationRGGYGGDRGGYGGDR
CCCCCCCCCCCCCCC
43.6524383679
522PhosphorylationYGGDRGGYGGDRSRG
CCCCCCCCCCCCCCC
22.2822210691
527PhosphorylationGGYGGDRSRGGYGGD
CCCCCCCCCCCCCCC
39.7622210691
528Asymmetric dimethylarginineGYGGDRSRGGYGGDR
CCCCCCCCCCCCCCC
43.37-
528MethylationGYGGDRSRGGYGGDR
CCCCCCCCCCCCCCC
43.3719124016
531PhosphorylationGDRSRGGYGGDRGGG
CCCCCCCCCCCCCCC
22.28-
532MethylationDRSRGGYGGDRGGGS
CCCCCCCCCCCCCCC
34.5015782174
532 (in isoform 2)Methylation-34.50-
535Asymmetric dimethylarginineRGGYGGDRGGGSGYG
CCCCCCCCCCCCCCC
49.26-
535MethylationRGGYGGDRGGGSGYG
CCCCCCCCCCCCCCC
49.2619124016
545MethylationGSGYGGDRSGGYGGD
CCCCCCCCCCCCCCC
40.24115368493
553MethylationSGGYGGDRSGGGYGG
CCCCCCCCCCCCCCC
40.2454559757
554PhosphorylationGGYGGDRSGGGYGGD
CCCCCCCCCCCCCCC
46.6721406692
558PhosphorylationGDRSGGGYGGDRGGG
CCCCCCCCCCCCCCC
22.6218083107
559MethylationDRSGGGYGGDRGGGY
CCCCCCCCCCCCCCC
34.5015782174
559 (in isoform 2)Methylation-34.50-
562DimethylationGGGYGGDRGGGYGGD
CCCCCCCCCCCCCCC
49.26-
562MethylationGGGYGGDRGGGYGGD
CCCCCCCCCCCCCCC
49.2624129315
566PhosphorylationGGDRGGGYGGDRGGY
CCCCCCCCCCCCCCC
22.6225839225
567MethylationGDRGGGYGGDRGGYG
CCCCCCCCCCCCCCC
34.5015782174
567 (in isoform 2)Methylation-34.50-
570Asymmetric dimethylarginineGGGYGGDRGGYGGKM
CCCCCCCCCCCCCCC
43.65-
570MethylationGGGYGGDRGGYGGKM
CCCCCCCCCCCCCCC
43.6519124016
576TrimethylationDRGGYGGKMGGRNDY
CCCCCCCCCCCCCCC
29.97-
576MethylationDRGGYGGKMGGRNDY
CCCCCCCCCCCCCCC
29.9723748837
580MethylationYGGKMGGRNDYRNDQ
CCCCCCCCCCCCCCC
27.4154559779
583PhosphorylationKMGGRNDYRNDQRNR
CCCCCCCCCCCCCCC
18.18-
588MethylationNDYRNDQRNRPY---
CCCCCCCCCCCC---
43.94115387927
590MethylationYRNDQRNRPY-----
CCCCCCCCCC-----
33.80115387935

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 RBP56_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
206RMethylation



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 RBP56_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SAFB1_HUMANSAFBphysical
15066997
TAF7_HUMANTAF7physical
9488465
TAF5_HUMANTAF5physical
9488465
TAF13_HUMANTAF13physical
9488465
TAF11_HUMANTAF11physical
9488465
RPB3_HUMANPOLR2Cphysical
9488465
RPB7_HUMANPOLR2Gphysical
9488465
RPAB1_HUMANPOLR2Ephysical
9488465
SF01_HUMANSF1physical
9660765
RPB1_HUMANPOLR2Aphysical
8890175
TPR_HUMANTPRphysical
22939629
S30BP_HUMANSAP30BPphysical
22939629
RN168_HUMANRNF168physical
22939629
SCRB2_HUMANSCARB2physical
22939629
TPM2_HUMANTPM2physical
22939629
TMED9_HUMANTMED9physical
22939629
HS104_YEASTHSP104genetic
25062688
THIM_HUMANACAA2physical
26344197
DNPEP_HUMANDNPEPphysical
28514442
KLHL8_HUMANKLHL8physical
28514442
ANM1_HUMANPRMT1physical
28514442

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 RBP56_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-268, AND MASS SPECTROMETRY.
Methylation
ReferencePubMed
"PRMT1 mediated methylation of TAF15 is required for its positive generegulatory function.";
Jobert L., Argentini M., Tora L.;
Exp. Cell Res. 315:1273-1286(2009).
Cited for: FUNCTION, METHYLATION AT ARG-206 BY PRMT1, MASS SPECTROMETRY, ANDSUBCELLULAR LOCATION.
"Identifying and quantifying in vivo methylation sites by heavy methylSILAC.";
Ong S.E., Mittler G., Mann M.;
Nat. Methods 1:119-126(2004).
Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-206, 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-226 AND SER-231, 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-97, AND MASSSPECTROMETRY.

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