SP16H_HUMAN - dbPTM
SP16H_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SP16H_HUMAN
UniProt AC Q9Y5B9
Protein Name FACT complex subunit SPT16
Gene Name SUPT16H
Organism Homo sapiens (Human).
Sequence Length 1047
Subcellular Localization Nucleus . Chromosome . Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci.
Protein Description Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II)..
Protein Sequence MAVTLDKDAYYRRVKRLYSNWRKGEDEYANVDAIVVSVGVDEEIVYAKSTALQTWLFGYELTDTIMVFCDDKIIFMASKKKVEFLKQIANTKGNENANGAPAITLLIREKNESNKSSFDKMIEAIKESKNGKKIGVFSKDKFPGEFMKSWNDCLNKEGFDKIDISAVVAYTIAVKEDGELNLMKKAASITSEVFNKFFKERVMEIVDADEKVRHSKLAESVEKAIEEKKYLAGADPSTVEMCYPPIIQSGGNYNLKFSVVSDKNHMHFGAITCAMGIRFKSYCSNLVRTLMVDPSQEVQENYNFLLQLQEELLKELRHGVKICDVYNAVMDVVKKQKPELLNKITKNLGFGMGIEFREGSLVINSKNQYKLKKGMVFSINLGFSDLTNKEGKKPEEKTYALFIGDTVLVDEDGPATVLTSVKKKVKNVGIFLKNEDEEEEEEEKDEAEDLLGRGSRAALLTERTRNEMTAEEKRRAHQKELAAQLNEEAKRRLTEQKGEQQIQKARKSNVSYKNPSLMPKEPHIREMKIYIDKKYETVIMPVFGIATPFHIATIKNISMSVEGDYTYLRINFYCPGSALGRNEGNIFPNPEATFVKEITYRASNIKAPGEQTVPALNLQNAFRIIKEVQKRYKTREAEEKEKEGIVKQDSLVINLNRSNPKLKDLYIRPNIAQKRMQGSLEAHVNGFRFTSVRGDKVDILYNNIKHALFQPCDGEMIIVLHFHLKNAIMFGKKRHTDVQFYTEVGEITTDLGKHQHMHDRDDLYAEQMEREMRHKLKTAFKNFIEKVEALTKEELEFEVPFRDLGFNGAPYRSTCLLQPTSSALVNATEWPPFVVTLDEVELIHFERVQFHLKNFDMVIVYKDYSKKVTMINAIPVASLDPIKEWLNSCDLKYTEGVQSLNWTKIMKTIVDDPEGFFEQGGWSFLEPEGEGSDAEEGDSESEIEDETFNPSEDDYEEEEEDSDEDYSSEAEESDYSKESLGSEEESGKDWDELEEEARKADRESRYEEEEEQSRSMSRKRKASVHSSGRGSNRGSRHSSAPPKKKRK
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------MAVTLDKDA
------CCCCCCHHH
17.8222223895
72-Hydroxyisobutyrylation-MAVTLDKDAYYRRV
-CCCCCCHHHHHHHH
47.58-
7Acetylation-MAVTLDKDAYYRRV
-CCCCCCHHHHHHHH
47.5823749302
7Ubiquitination-MAVTLDKDAYYRRV
-CCCCCCHHHHHHHH
47.5824816145
10PhosphorylationVTLDKDAYYRRVKRL
CCCCHHHHHHHHHHH
13.9820068231
11PhosphorylationTLDKDAYYRRVKRLY
CCCHHHHHHHHHHHH
8.1520068231
12MethylationLDKDAYYRRVKRLYS
CCHHHHHHHHHHHHH
25.0030761167
13MethylationDKDAYYRRVKRLYSN
CHHHHHHHHHHHHHC
23.3730761173
16UbiquitinationAYYRRVKRLYSNWRK
HHHHHHHHHHHCCCC
35.6822817900
18PhosphorylationYRRVKRLYSNWRKGE
HHHHHHHHHCCCCCC
12.1823186163
19PhosphorylationRRVKRLYSNWRKGED
HHHHHHHHCCCCCCC
34.2123312004
21UbiquitinationVKRLYSNWRKGEDEY
HHHHHHCCCCCCCCC
9.4521890473
50UbiquitinationEIVYAKSTALQTWLF
HHHCEEHHHHHHHHH
30.5822817900
55UbiquitinationKSTALQTWLFGYELT
EHHHHHHHHHCCCCC
4.0921890473
78PhosphorylationDKIIFMASKKKVEFL
CEEEEECCHHHHHHH
32.97-
80UbiquitinationIIFMASKKKVEFLKQ
EEEECCHHHHHHHHH
60.60-
81UbiquitinationIFMASKKKVEFLKQI
EEECCHHHHHHHHHH
51.2222817900
86UbiquitinationKKKVEFLKQIANTKG
HHHHHHHHHHHCCCC
45.0021890473
91UbiquitinationFLKQIANTKGNENAN
HHHHHHCCCCCCCCC
31.1623000965
92UbiquitinationLKQIANTKGNENANG
HHHHHCCCCCCCCCC
60.5932015554
96UbiquitinationANTKGNENANGAPAI
HCCCCCCCCCCCCEE
42.5823000965
113PhosphorylationLIREKNESNKSSFDK
EEECCCCCCCHHHHH
59.9830622161
115UbiquitinationREKNESNKSSFDKMI
ECCCCCCCHHHHHHH
57.6733845483
116PhosphorylationEKNESNKSSFDKMIE
CCCCCCCHHHHHHHH
40.2530622161
117PhosphorylationKNESNKSSFDKMIEA
CCCCCCHHHHHHHHH
38.7930622161
1202-HydroxyisobutyrylationSNKSSFDKMIEAIKE
CCCHHHHHHHHHHHH
39.50-
120AcetylationSNKSSFDKMIEAIKE
CCCHHHHHHHHHHHH
39.5023749302
120UbiquitinationSNKSSFDKMIEAIKE
CCCHHHHHHHHHHHH
39.5022817900
126AcetylationDKMIEAIKESKNGKK
HHHHHHHHHCCCCCE
64.0825953088
126UbiquitinationDKMIEAIKESKNGKK
HHHHHHHHHCCCCCE
64.08-
128PhosphorylationMIEAIKESKNGKKIG
HHHHHHHCCCCCEEE
26.8128258704
131UbiquitinationAIKESKNGKKIGVFS
HHHHCCCCCEEEEEE
36.0521890473
134UbiquitinationESKNGKKIGVFSKDK
HCCCCCEEEEEECCC
6.9223000965
138PhosphorylationGKKIGVFSKDKFPGE
CCEEEEEECCCCCHH
37.2228258704
139AcetylationKKIGVFSKDKFPGEF
CEEEEEECCCCCHHH
54.1719608861
139UbiquitinationKKIGVFSKDKFPGEF
CEEEEEECCCCCHHH
54.1719608861
141AcetylationIGVFSKDKFPGEFMK
EEEEECCCCCHHHHH
58.1423749302
146UbiquitinationKDKFPGEFMKSWNDC
CCCCCHHHHHHHHHH
10.4122817900
151UbiquitinationGEFMKSWNDCLNKEG
HHHHHHHHHHCCCCC
36.8922817900
156AcetylationSWNDCLNKEGFDKID
HHHHHCCCCCCCCCC
46.3925825284
156MethylationSWNDCLNKEGFDKID
HHHHHCCCCCCCCCC
46.3924818181
156UbiquitinationSWNDCLNKEGFDKID
HHHHHCCCCCCCCCC
46.3923000965
161UbiquitinationLNKEGFDKIDISAVV
CCCCCCCCCCHHHEE
39.7623000965
165PhosphorylationGFDKIDISAVVAYTI
CCCCCCHHHEEEEEE
15.9721601212
171PhosphorylationISAVVAYTIAVKEDG
HHHEEEEEEEECCCC
7.8521601212
1842-HydroxyisobutyrylationDGELNLMKKAASITS
CCCCCHHHHHHHCHH
42.29-
184AcetylationDGELNLMKKAASITS
CCCCCHHHHHHHCHH
42.2925953088
184UbiquitinationDGELNLMKKAASITS
CCCCCHHHHHHHCHH
42.2932015554
185MalonylationGELNLMKKAASITSE
CCCCHHHHHHHCHHH
34.9126320211
185UbiquitinationGELNLMKKAASITSE
CCCCHHHHHHHCHHH
34.9129967540
188PhosphorylationNLMKKAASITSEVFN
CHHHHHHHCHHHHHH
31.1230266825
190PhosphorylationMKKAASITSEVFNKF
HHHHHHCHHHHHHHH
19.1530266825
191PhosphorylationKKAASITSEVFNKFF
HHHHHCHHHHHHHHH
30.0530266825
196AcetylationITSEVFNKFFKERVM
CHHHHHHHHHHHHHH
40.4919608861
196UbiquitinationITSEVFNKFFKERVM
CHHHHHHHHHHHHHH
40.4923000965
199UbiquitinationEVFNKFFKERVMEIV
HHHHHHHHHHHHHHC
47.9823000965
203SulfoxidationKFFKERVMEIVDADE
HHHHHHHHHHCCCCH
3.4921406390
211AcetylationEIVDADEKVRHSKLA
HHCCCCHHHCHHHHH
45.1523749302
211UbiquitinationEIVDADEKVRHSKLA
HHCCCCHHHCHHHHH
45.1521906983
2162-HydroxyisobutyrylationDEKVRHSKLAESVEK
CHHHCHHHHHHHHHH
45.66-
216AcetylationDEKVRHSKLAESVEK
CHHHCHHHHHHHHHH
45.6623749302
216UbiquitinationDEKVRHSKLAESVEK
CHHHCHHHHHHHHHH
45.6622817900
220O-linked_GlycosylationRHSKLAESVEKAIEE
CHHHHHHHHHHHHHH
29.9323301498
2232-HydroxyisobutyrylationKLAESVEKAIEEKKY
HHHHHHHHHHHHHHH
53.13-
223AcetylationKLAESVEKAIEEKKY
HHHHHHHHHHHHHHH
53.1319608861
223UbiquitinationKLAESVEKAIEEKKY
HHHHHHHHHHHHHHH
53.1319608861
263AcetylationKFSVVSDKNHMHFGA
EEEEEECCCCCEECC
41.0425953088
263UbiquitinationKFSVVSDKNHMHFGA
EEEEEECCCCCEECC
41.04-
280AcetylationCAMGIRFKSYCSNLV
HHHCCHHHHHHHCHH
30.5725825284
280MalonylationCAMGIRFKSYCSNLV
HHHCCHHHHHHHCHH
30.5726320211
280MethylationCAMGIRFKSYCSNLV
HHHCCHHHHHHHCHH
30.57109063049
280UbiquitinationCAMGIRFKSYCSNLV
HHHCCHHHHHHHCHH
30.57-
301UbiquitinationPSQEVQENYNFLLQL
CCHHHHHHHHHHHHH
21.6923000965
305UbiquitinationVQENYNFLLQLQEEL
HHHHHHHHHHHHHHH
2.3723000965
307UbiquitinationENYNFLLQLQEELLK
HHHHHHHHHHHHHHH
43.1623000965
321AcetylationKELRHGVKICDVYNA
HHHHHCCCHHHHHHH
42.0626051181
326PhosphorylationGVKICDVYNAVMDVV
CCCHHHHHHHHHHHH
5.55-
334AcetylationNAVMDVVKKQKPELL
HHHHHHHHHHCHHHH
49.7025953088
334NeddylationNAVMDVVKKQKPELL
HHHHHHHHHHCHHHH
49.7032015554
334UbiquitinationNAVMDVVKKQKPELL
HHHHHHHHHHCHHHH
49.7032015554
335AcetylationAVMDVVKKQKPELLN
HHHHHHHHHCHHHHH
52.5219608861
335UbiquitinationAVMDVVKKQKPELLN
HHHHHHHHHCHHHHH
52.5232015554
337AcetylationMDVVKKQKPELLNKI
HHHHHHHCHHHHHHH
49.7119608861
337UbiquitinationMDVVKKQKPELLNKI
HHHHHHHCHHHHHHH
49.7129967540
357UbiquitinationFGMGIEFREGSLVIN
CCCCEEECCCEEEEE
34.2822817900
358UbiquitinationGMGIEFREGSLVINS
CCCEEECCCEEEEEC
59.4622817900
359UbiquitinationMGIEFREGSLVINSK
CCEEECCCEEEEECC
23.2522817900
360PhosphorylationGIEFREGSLVINSKN
CEEECCCEEEEECCC
18.0823312004
361UbiquitinationIEFREGSLVINSKNQ
EEECCCEEEEECCCC
7.0621890473
366AcetylationGSLVINSKNQYKLKK
CEEEEECCCCEEECC
43.5125953088
366MalonylationGSLVINSKNQYKLKK
CEEEEECCCCEEECC
43.5126320211
366UbiquitinationGSLVINSKNQYKLKK
CEEEEECCCCEEECC
43.5123000965
370UbiquitinationINSKNQYKLKKGMVF
EECCCCEEECCCEEE
44.0323000965
372UbiquitinationSKNQYKLKKGMVFSI
CCCCEEECCCEEEEE
43.0323000965
392AcetylationDLTNKEGKKPEEKTY
HCCCCCCCCHHHCEE
67.2712431835
408UbiquitinationLFIGDTVLVDEDGPA
EEECCEEEECCCCCC
4.3323000965
414UbiquitinationVLVDEDGPATVLTSV
EEECCCCCCEEECCH
36.7623000965
422SumoylationATVLTSVKKKVKNVG
CEEECCHHHHHCEEE
46.79-
422UbiquitinationATVLTSVKKKVKNVG
CEEECCHHHHHCEEE
46.7922817900
423UbiquitinationTVLTSVKKKVKNVGI
EEECCHHHHHCEEEE
61.7222817900
424UbiquitinationVLTSVKKKVKNVGIF
EECCHHHHHCEEEEE
53.3622817900
426UbiquitinationTSVKKKVKNVGIFLK
CCHHHHHCEEEEEEE
55.5922817900
432UbiquitinationVKNVGIFLKNEDEEE
HCEEEEEEECCCHHH
5.7122817900
433AcetylationKNVGIFLKNEDEEEE
CEEEEEEECCCHHHH
47.7626051181
433SumoylationKNVGIFLKNEDEEEE
CEEEEEEECCCHHHH
47.76-
433UbiquitinationKNVGIFLKNEDEEEE
CEEEEEEECCCHHHH
47.7632015554
439UbiquitinationLKNEDEEEEEEEKDE
EECCCHHHHHHHHHH
69.5324816145
442UbiquitinationEDEEEEEEEKDEAED
CCHHHHHHHHHHHHH
73.8823000965
444AcetylationEEEEEEEKDEAEDLL
HHHHHHHHHHHHHHH
65.2426051181
444UbiquitinationEEEEEEEKDEAEDLL
HHHHHHHHHHHHHHH
65.2429967540
448UbiquitinationEEEKDEAEDLLGRGS
HHHHHHHHHHHCHHH
47.3323000965
455PhosphorylationEDLLGRGSRAALLTE
HHHHCHHHHHHHHHH
19.8625159151
461PhosphorylationGSRAALLTERTRNEM
HHHHHHHHHHHHHCC
25.0328555341
464PhosphorylationAALLTERTRNEMTAE
HHHHHHHHHHCCCHH
31.4528555341
469PhosphorylationERTRNEMTAEEKRRA
HHHHHCCCHHHHHHH
25.4127470641
473AcetylationNEMTAEEKRRAHQKE
HCCCHHHHHHHHHHH
38.3925953088
473UbiquitinationNEMTAEEKRRAHQKE
HCCCHHHHHHHHHHH
38.3923000965
479SumoylationEKRRAHQKELAAQLN
HHHHHHHHHHHHHHC
44.84-
479SumoylationEKRRAHQKELAAQLN
HHHHHHHHHHHHHHC
44.84-
479UbiquitinationEKRRAHQKELAAQLN
HHHHHHHHHHHHHHC
44.8423000965
490AcetylationAQLNEEAKRRLTEQK
HHHCHHHHHHHHHHH
41.1325953088
490UbiquitinationAQLNEEAKRRLTEQK
HHHCHHHHHHHHHHH
41.1332015554
494PhosphorylationEEAKRRLTEQKGEQQ
HHHHHHHHHHHHHHH
34.2621601212
497SumoylationKRRLTEQKGEQQIQK
HHHHHHHHHHHHHHH
59.17-
497SumoylationKRRLTEQKGEQQIQK
HHHHHHHHHHHHHHH
59.1728112733
497UbiquitinationKRRLTEQKGEQQIQK
HHHHHHHHHHHHHHH
59.1721906983
504AcetylationKGEQQIQKARKSNVS
HHHHHHHHHHHCCCC
52.3625953088
504UbiquitinationKGEQQIQKARKSNVS
HHHHHHHHHHHCCCC
52.3624816145
507UbiquitinationQQIQKARKSNVSYKN
HHHHHHHHCCCCCCC
51.7723000965
508PhosphorylationQIQKARKSNVSYKNP
HHHHHHHCCCCCCCC
36.5926055452
511PhosphorylationKARKSNVSYKNPSLM
HHHHCCCCCCCCCCC
34.3424732914
512PhosphorylationARKSNVSYKNPSLMP
HHHCCCCCCCCCCCC
15.5324732914
513AcetylationRKSNVSYKNPSLMPK
HHCCCCCCCCCCCCC
55.6719608861
513SumoylationRKSNVSYKNPSLMPK
HHCCCCCCCCCCCCC
55.6728112733
513UbiquitinationRKSNVSYKNPSLMPK
HHCCCCCCCCCCCCC
55.6723000965
516PhosphorylationNVSYKNPSLMPKEPH
CCCCCCCCCCCCCCC
46.8527251275
520UbiquitinationKNPSLMPKEPHIREM
CCCCCCCCCCCCCEE
70.6629967540
528AcetylationEPHIREMKIYIDKKY
CCCCCEEEEEECCCC
27.8325825284
531UbiquitinationIREMKIYIDKKYETV
CCEEEEEECCCCCEE
7.7321890473
533AcetylationEMKIYIDKKYETVIM
EEEEEECCCCCEEEE
47.9326051181
533NeddylationEMKIYIDKKYETVIM
EEEEEECCCCCEEEE
47.9332015554
534AcetylationMKIYIDKKYETVIMP
EEEEECCCCCEEEEE
44.5726051181
535PhosphorylationKIYIDKKYETVIMPV
EEEECCCCCEEEEEC
23.6728064214
540SulfoxidationKKYETVIMPVFGIAT
CCCCEEEEECCCCCC
1.6928183972
541UbiquitinationKYETVIMPVFGIATP
CCCEEEEECCCCCCC
13.7324816145
547PhosphorylationMPVFGIATPFHIATI
EECCCCCCCCEEEEE
25.27-
558PhosphorylationIATIKNISMSVEGDY
EEEEEEEEEEEECCE
17.8820068231
560PhosphorylationTIKNISMSVEGDYTY
EEEEEEEEEECCEEE
15.3825072903
565PhosphorylationSMSVEGDYTYLRINF
EEEEECCEEEEEEEE
14.2427273156
566PhosphorylationMSVEGDYTYLRINFY
EEEECCEEEEEEEEE
22.3328152594
567PhosphorylationSVEGDYTYLRINFYC
EEECCEEEEEEEEEE
6.4328152594
573PhosphorylationTYLRINFYCPGSALG
EEEEEEEEECCCCCC
8.0128152594
577PhosphorylationINFYCPGSALGRNEG
EEEEECCCCCCCCCC
12.8828152594
577UbiquitinationINFYCPGSALGRNEG
EEEEECCCCCCCCCC
12.8822817900
582UbiquitinationPGSALGRNEGNIFPN
CCCCCCCCCCCCCCC
60.7821890473
593PhosphorylationIFPNPEATFVKEITY
CCCCCCCEEEEEEEE
27.57-
596AcetylationNPEATFVKEITYRAS
CCCCEEEEEEEEECC
38.9325825284
596UbiquitinationNPEATFVKEITYRAS
CCCCEEEEEEEEECC
38.9321963094
598UbiquitinationEATFVKEITYRASNI
CCEEEEEEEEECCCC
3.2121890473
599PhosphorylationATFVKEITYRASNIK
CEEEEEEEEECCCCC
14.19-
600PhosphorylationTFVKEITYRASNIKA
EEEEEEEEECCCCCC
15.16-
603PhosphorylationKEITYRASNIKAPGE
EEEEEECCCCCCCCC
30.04-
606UbiquitinationTYRASNIKAPGEQTV
EEECCCCCCCCCCCC
53.4227667366
609UbiquitinationASNIKAPGEQTVPAL
CCCCCCCCCCCCCCC
44.5021890473
626AcetylationQNAFRIIKEVQKRYK
HHHHHHHHHHHHHHH
49.8426051181
626UbiquitinationQNAFRIIKEVQKRYK
HHHHHHHHHHHHHHH
49.8429967540
631UbiquitinationIIKEVQKRYKTREAE
HHHHHHHHHHCHHHH
22.5321890473
632PhosphorylationIKEVQKRYKTREAEE
HHHHHHHHHCHHHHH
24.6019369195
634PhosphorylationEVQKRYKTREAEEKE
HHHHHHHCHHHHHHH
25.47-
640AcetylationKTREAEEKEKEGIVK
HCHHHHHHHHCCCCC
66.6425953088
640UbiquitinationKTREAEEKEKEGIVK
HCHHHHHHHHCCCCC
66.64-
6422-HydroxyisobutyrylationREAEEKEKEGIVKQD
HHHHHHHHCCCCCCC
72.77-
642UbiquitinationREAEEKEKEGIVKQD
HHHHHHHHCCCCCCC
72.7722817900
647SumoylationKEKEGIVKQDSLVIN
HHHCCCCCCCEEEEE
46.60-
647SumoylationKEKEGIVKQDSLVIN
HHHCCCCCCCEEEEE
46.6028112733
647UbiquitinationKEKEGIVKQDSLVIN
HHHCCCCCCCEEEEE
46.6021906983
650PhosphorylationEGIVKQDSLVINLNR
CCCCCCCEEEEECCC
23.2628355574
658PhosphorylationLVINLNRSNPKLKDL
EEEECCCCCCCHHHE
57.3125159151
661UbiquitinationNLNRSNPKLKDLYIR
ECCCCCCCHHHEEEC
72.8622817900
663SumoylationNRSNPKLKDLYIRPN
CCCCCCHHHEEECCH
52.38-
663AcetylationNRSNPKLKDLYIRPN
CCCCCCHHHEEECCH
52.3823749302
663MalonylationNRSNPKLKDLYIRPN
CCCCCCHHHEEECCH
52.3826320211
663SumoylationNRSNPKLKDLYIRPN
CCCCCCHHHEEECCH
52.38-
663UbiquitinationNRSNPKLKDLYIRPN
CCCCCCHHHEEECCH
52.3821890473
666PhosphorylationNPKLKDLYIRPNIAQ
CCCHHHEEECCHHHH
12.6728152594
674AcetylationIRPNIAQKRMQGSLE
ECCHHHHHHHHCCEE
40.5923749302
674UbiquitinationIRPNIAQKRMQGSLE
ECCHHHHHHHHCCEE
40.5922817900
690PhosphorylationHVNGFRFTSVRGDKV
EECCEEEEEECCCCE
23.2723186163
691PhosphorylationVNGFRFTSVRGDKVD
ECCEEEEEECCCCEE
13.7023186163
6962-HydroxyisobutyrylationFTSVRGDKVDILYNN
EEEECCCCEEEEECC
44.63-
696AcetylationFTSVRGDKVDILYNN
EEEECCCCEEEEECC
44.6325953088
696UbiquitinationFTSVRGDKVDILYNN
EEEECCCCEEEEECC
44.6323000965
701PhosphorylationGDKVDILYNNIKHAL
CCCEEEEECCHHHHE
13.3928152594
712UbiquitinationKHALFQPCDGEMIIV
HHHEECCCCCCEEEE
7.9422817900
716UbiquitinationFQPCDGEMIIVLHFH
ECCCCCCEEEEEEEE
2.8721890473
721UbiquitinationGEMIIVLHFHLKNAI
CCEEEEEEEEHHCHH
9.3721890473
727UbiquitinationLHFHLKNAIMFGKKR
EEEEHHCHHHHCCCC
7.9522817900
732AcetylationKNAIMFGKKRHTDVQ
HCHHHHCCCCCCCCC
35.0619608861
732UbiquitinationKNAIMFGKKRHTDVQ
HCHHHHCCCCCCCCC
35.0632015554
733UbiquitinationNAIMFGKKRHTDVQF
CHHHHCCCCCCCCCE
50.20-
741PhosphorylationRHTDVQFYTEVGEIT
CCCCCCEEEEEEEEE
5.7222817900
753UbiquitinationEITTDLGKHQHMHDR
EEECCCCCCCCCCCH
47.6029967540
760MethylationKHQHMHDRDDLYAEQ
CCCCCCCHHHHHHHH
25.35115917601
764PhosphorylationMHDRDDLYAEQMERE
CCCHHHHHHHHHHHH
18.32-
777UbiquitinationREMRHKLKTAFKNFI
HHHHHHHHHHHHHHH
42.4822817900
781AcetylationHKLKTAFKNFIEKVE
HHHHHHHHHHHHHHH
48.7823749302
781UbiquitinationHKLKTAFKNFIEKVE
HHHHHHHHHHHHHHH
48.7822817900
7862-HydroxyisobutyrylationAFKNFIEKVEALTKE
HHHHHHHHHHHHCHH
40.33-
786AcetylationAFKNFIEKVEALTKE
HHHHHHHHHHHHCHH
40.3319608861
786UbiquitinationAFKNFIEKVEALTKE
HHHHHHHHHHHHCHH
40.3322817900
792UbiquitinationEKVEALTKEELEFEV
HHHHHHCHHHCEEEC
50.4721906983
839UbiquitinationPFVVTLDEVELIHFE
CEEEEECCEEEEEEE
40.7921890473
842UbiquitinationVTLDEVELIHFERVQ
EEECCEEEEEEEEEE
4.4422817900
861PhosphorylationNFDMVIVYKDYSKKV
CCCEEEEECCCCCCE
6.24-
864PhosphorylationMVIVYKDYSKKVTMI
EEEEECCCCCCEEEE
20.4521214269
865PhosphorylationVIVYKDYSKKVTMIN
EEEECCCCCCEEEEE
35.8121214269
867UbiquitinationVYKDYSKKVTMINAI
EECCCCCCEEEEEEE
36.6829967540
883UbiquitinationVASLDPIKEWLNSCD
CCCCCHHHHHHHHCC
48.5029967540
892UbiquitinationWLNSCDLKYTEGVQS
HHHHCCCCCCCCCCC
36.5532015554
893PhosphorylationLNSCDLKYTEGVQSL
HHHCCCCCCCCCCCC
19.8123186163
894PhosphorylationNSCDLKYTEGVQSLN
HHCCCCCCCCCCCCC
25.3628152594
899PhosphorylationKYTEGVQSLNWTKIM
CCCCCCCCCCHHHHH
22.6729978859
903PhosphorylationGVQSLNWTKIMKTIV
CCCCCCHHHHHHHHC
15.0419664994
904AcetylationVQSLNWTKIMKTIVD
CCCCCHHHHHHHHCC
32.2019608861
904UbiquitinationVQSLNWTKIMKTIVD
CCCCCHHHHHHHHCC
32.2022817900
907UbiquitinationLNWTKIMKTIVDDPE
CCHHHHHHHHCCCCC
38.2822817900
932PhosphorylationLEPEGEGSDAEEGDS
CCCCCCCCCCCCCCC
29.3719007248
979PhosphorylationESDYSKESLGSEEES
HCCCCHHHHCCCCHH
41.5920164059
979UbiquitinationESDYSKESLGSEEES
HCCCCHHHHCCCCHH
41.5924816145
982PhosphorylationYSKESLGSEEESGKD
CCHHHHCCCCHHCCC
47.3222167270
986PhosphorylationSLGSEEESGKDWDEL
HHCCCCHHCCCHHHH
55.1922167270
1004PhosphorylationARKADRESRYEEEEE
HHHHHHHHHHHHHHH
40.8525159151
1006PhosphorylationKADRESRYEEEEEQS
HHHHHHHHHHHHHHH
36.6528796482
1013PhosphorylationYEEEEEQSRSMSRKR
HHHHHHHHHHHCHHH
29.6025159151
1014MethylationEEEEEQSRSMSRKRK
HHHHHHHHHHCHHHH
35.75115917597
1015PhosphorylationEEEEQSRSMSRKRKA
HHHHHHHHHCHHHHH
26.7625159151
1017PhosphorylationEEQSRSMSRKRKASV
HHHHHHHCHHHHHHH
35.5825159151
1023PhosphorylationMSRKRKASVHSSGRG
HCHHHHHHHCCCCCC
24.3326055452
1026PhosphorylationKRKASVHSSGRGSNR
HHHHHHCCCCCCCCC
32.1223403867
1027PhosphorylationRKASVHSSGRGSNRG
HHHHHCCCCCCCCCC
20.0323403867
1029DimethylationASVHSSGRGSNRGSR
HHHCCCCCCCCCCCC
47.52-
1029MethylationASVHSSGRGSNRGSR
HHHCCCCCCCCCCCC
47.5254559583
1031PhosphorylationVHSSGRGSNRGSRHS
HCCCCCCCCCCCCCC
23.2223911959
1033DimethylationSSGRGSNRGSRHSSA
CCCCCCCCCCCCCCC
46.27-
1033MethylationSSGRGSNRGSRHSSA
CCCCCCCCCCCCCCC
46.2754559591
1036MethylationRGSNRGSRHSSAPPK
CCCCCCCCCCCCCCC
36.2154559599
1038PhosphorylationSNRGSRHSSAPPKKK
CCCCCCCCCCCCCCC
27.3818510355
1039PhosphorylationNRGSRHSSAPPKKKR
CCCCCCCCCCCCCCC
38.3718510355
1044UbiquitinationHSSAPPKKKRK----
CCCCCCCCCCC----
64.6824816145

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
494TPhosphorylationKinaseAURKBQ96GD4
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SP16H_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 SP16H_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPA49_HUMANPOLR1Ephysical
19214185
SSRP1_HUMANSSRP1physical
16902406
SSRP1_HUMANSSRP1physical
16682447
TRI33_HUMANTRIM33physical
20603019
TAL1_HUMANTAL1physical
20603019
SP16H_HUMANSUPT16Hphysical
20603019
CDK9_HUMANCDK9physical
20603019
SSRP1_HUMANSSRP1physical
22939629
TOP1_HUMANTOP1physical
22939629
FRIH_HUMANFTH1physical
22863883
BRE1A_HUMANRNF20physical
24357716
PAF1_HUMANPAF1physical
24357716
TONSL_HUMANTONSLphysical
25184681
BRD3_HUMANBRD3physical
26344197
CDK12_HUMANCDK12physical
26344197
CSK2B_HUMANCSNK2Bphysical
26344197
CTR9_HUMANCTR9physical
26344197
H2B1A_HUMANHIST1H2BAphysical
26344197
HMGB1_HUMANHMGB1physical
26344197
IWS1_HUMANIWS1physical
26344197
NP1L1_HUMANNAP1L1physical
26344197
PESC_HUMANPES1physical
26344197
SMRCD_HUMANSMARCAD1physical
26344197
SRRM1_HUMANSRRM1physical
26344197
SSRP1_HUMANSSRP1physical
26344197
TOP1_HUMANTOP1physical
26344197
ZCH18_HUMANZC3H18physical
26344197
UBR5_HUMANUBR5physical
27647897
RFA3_HUMANRPA3physical
27173435
WRN_HUMANWRNphysical
27173435
SSRP1_HUMANSSRP1physical
27173435

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 SP16H_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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-979; SER-982 AND SER-986, AND MASSSPECTROMETRY.
"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-139; LYS-196; LYS-223;LYS-513; LYS-732; LYS-786 AND LYS-904, 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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-979; SER-982 AND SER-986, AND MASSSPECTROMETRY.
"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 SER-508; SER-650 ANDSER-1015, 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 SER-932, 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-979; SER-982 ANDSER-986, AND MASS 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 TYR-632, AND MASSSPECTROMETRY.

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