SAFB1_HUMAN - dbPTM
SAFB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SAFB1_HUMAN
UniProt AC Q15424
Protein Name Scaffold attachment factor B1
Gene Name SAFB
Organism Homo sapiens (Human).
Sequence Length 915
Subcellular Localization Nucleus .
Protein Description Binds to scaffold/matrix attachment region (S/MAR) DNA and forms a molecular assembly point to allow the formation of a 'transcriptosomal' complex (consisting of SR proteins and RNA polymerase II) coupling transcription and RNA processing (By similarity). Can function as an estrogen receptor corepressor and can also bind to the HSP27 promoter and decrease its transcription. When associated with RBMX, binds to and stimulates transcription from the SREBF1 promoter (By similarity). Can inhibit cell proliferation..
Protein Sequence MAETLSGLGDSGAAGAAALSSASSETGTRRLSDLRVIDLRAELRKRNVDSSGNKSVLMERLKKAIEDEGGNPDEIEITSEGNKKTSKRSSKGRKPEEEGVEDNGLEENSGDGQEDVETSLENLQDIDIMDISVLDEAEIDNGSVADCVEDDDADNLQESLSDSRELVEGEMKELPEQLQEHAIEDKETINNLDTSSSDFTILQEIEEPSLEPENEKILDILGETCKSEPVKEESSELEQPFAQDTSSVGPDRKLAEEEDLFDSAHPEEGDLDLASESTAHAQSSKADSLLAVVKREPAEQPGDGERTDCEPVGLEPAVEQSSAASELAEASSEELAEAPTEAPSPEARDSKEDGRKFDFDACNEVPPAPKESSTSEGADQKMSSPEDDSDTKRLSKEEKGRSSCGRNFWVSGLSSTTRATDLKNLFSKYGKVVGAKVVTNARSPGARCYGFVTMSTAEEATKCINHLHKTELHGKMISVEKAKNEPVGKKTSDKRDSDGKKEKSSNSDRSTNLKRDDKCDRKDDAKKGDDGSGEKSKDQDDQKPGPSERSRATKSGSRGTERTVVMDKSKGVPVISVKTSGSKERASKSQDRKSASREKRSVVSFDKVKEPRKSRDSESHSRVRERSEREQRMQAQWEREERERLEIARERLAFQRQRLERERMERERLERERMHVEHERRREQERIHREREELRRQQELRYEQERRPAVRRPYDLDRRDDAYWPEAKRAALDERYHSDFNRQDRFHDFDHRDRGRYPDHSVDRREGSRSMMGEREGQHYPERHGGPERHGRDSRDGWGGYGSDKRMSEGRGLPPPPRRDWGDHGRREDDRSWQGTADGGMMDRDHKRWQGGERSMSGHSGPGHMMNRGGMSGRGSFAPGGASRGHPIPHGGMQGGFGGQSRGSRPSDARFTRRY
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------MAETLSGLG
------CCCCCCCCC
20.6220068231
4Phosphorylation----MAETLSGLGDS
----CCCCCCCCCCC
19.3826503892
6Phosphorylation--MAETLSGLGDSGA
--CCCCCCCCCCCHH
39.1222115753
11PhosphorylationTLSGLGDSGAAGAAA
CCCCCCCCHHHHHHH
28.6523401153
20PhosphorylationAAGAAALSSASSETG
HHHHHHHHCCCCCCC
21.0923401153
21PhosphorylationAGAAALSSASSETGT
HHHHHHHCCCCCCCC
32.7825159151
23PhosphorylationAAALSSASSETGTRR
HHHHHCCCCCCCCCC
30.5629255136
24PhosphorylationAALSSASSETGTRRL
HHHHCCCCCCCCCCH
38.6023401153
26PhosphorylationLSSASSETGTRRLSD
HHCCCCCCCCCCHHH
45.8929255136
28PhosphorylationSASSETGTRRLSDLR
CCCCCCCCCCHHHCE
21.7526503892
29MethylationASSETGTRRLSDLRV
CCCCCCCCCHHHCEE
38.60115386587
32PhosphorylationETGTRRLSDLRVIDL
CCCCCCHHHCEEEEH
32.5623927012
35MethylationTRRLSDLRVIDLRAE
CCCHHHCEEEEHHHH
28.47115493137
50PhosphorylationLRKRNVDSSGNKSVL
HHHCCCCCCCCHHHH
35.5430108239
51PhosphorylationRKRNVDSSGNKSVLM
HHCCCCCCCCHHHHH
41.7530108239
54AcetylationNVDSSGNKSVLMERL
CCCCCCCHHHHHHHH
45.5323236377
55PhosphorylationVDSSGNKSVLMERLK
CCCCCCHHHHHHHHH
25.2026055452
60MethylationNKSVLMERLKKAIED
CHHHHHHHHHHHHHC
37.53-
78PhosphorylationNPDEIEITSEGNKKT
CCCCEEECCCCCCCC
14.1330108239
79PhosphorylationPDEIEITSEGNKKTS
CCCEEECCCCCCCCC
49.5225159151
83AcetylationEITSEGNKKTSKRSS
EECCCCCCCCCCCCC
69.1826051181
83UbiquitinationEITSEGNKKTSKRSS
EECCCCCCCCCCCCC
69.1821890473
84AcetylationITSEGNKKTSKRSSK
ECCCCCCCCCCCCCC
63.1371375
85PhosphorylationTSEGNKKTSKRSSKG
CCCCCCCCCCCCCCC
40.8826074081
86PhosphorylationSEGNKKTSKRSSKGR
CCCCCCCCCCCCCCC
34.6426074081
125 (in isoform 2)Phosphorylation-43.6329116813
126 (in isoform 2)Phosphorylation-2.2029116813
127 (in isoform 2)Phosphorylation-38.1529116813
128 (in isoform 2)Phosphorylation-2.4629507054
143PhosphorylationEAEIDNGSVADCVED
HHHCCCCCHHHHCCC
22.0122468782
159PhosphorylationDADNLQESLSDSREL
CHHHHHHHHHHHHHH
21.8826074081
161PhosphorylationDNLQESLSDSRELVE
HHHHHHHHHHHHHHH
42.7026074081
163PhosphorylationLQESLSDSRELVEGE
HHHHHHHHHHHHHHH
25.0326074081
172SumoylationELVEGEMKELPEQLQ
HHHHHHHHHHHHHHH
52.36-
172SumoylationELVEGEMKELPEQLQ
HHHHHHHHHHHHHHH
52.3628112733
186SumoylationQEHAIEDKETINNLD
HHHHHCCHHHHHHCC
43.9228112733
188PhosphorylationHAIEDKETINNLDTS
HHHCCHHHHHHCCCC
34.4430278072
194PhosphorylationETINNLDTSSSDFTI
HHHHHCCCCCCCCEE
33.4030278072
195PhosphorylationTINNLDTSSSDFTIL
HHHHCCCCCCCCEEE
27.7530278072
196PhosphorylationINNLDTSSSDFTILQ
HHHCCCCCCCCEEEE
35.7026503892
197PhosphorylationNNLDTSSSDFTILQE
HHCCCCCCCCEEEEE
36.1926503892
200PhosphorylationDTSSSDFTILQEIEE
CCCCCCCEEEEECCC
26.2630278072
209PhosphorylationLQEIEEPSLEPENEK
EEECCCCCCCCCCCH
48.9528176443
224PhosphorylationILDILGETCKSEPVK
HHHHHHHHHCCCCCC
24.3628102081
225UbiquitinationLDILGETCKSEPVKE
HHHHHHHHCCCCCCC
3.8721890473
225GlutathionylationLDILGETCKSEPVKE
HHHHHHHHCCCCCCC
3.8722555962
226MethylationDILGETCKSEPVKEE
HHHHHHHCCCCCCCC
66.33-
226SumoylationDILGETCKSEPVKEE
HHHHHHHCCCCCCCC
66.33-
226SumoylationDILGETCKSEPVKEE
HHHHHHHCCCCCCCC
66.33-
226UbiquitinationDILGETCKSEPVKEE
HHHHHHHCCCCCCCC
66.33-
227PhosphorylationILGETCKSEPVKEES
HHHHHHCCCCCCCCC
49.6429255136
231SumoylationTCKSEPVKEESSELE
HHCCCCCCCCCCCCC
67.49-
231UbiquitinationTCKSEPVKEESSELE
HHCCCCCCCCCCCCC
67.4921890473
231SumoylationTCKSEPVKEESSELE
HHCCCCCCCCCCCCC
67.4921527249
234PhosphorylationSEPVKEESSELEQPF
CCCCCCCCCCCCCCC
30.1529255136
235PhosphorylationEPVKEESSELEQPFA
CCCCCCCCCCCCCCC
49.8629255136
245PhosphorylationEQPFAQDTSSVGPDR
CCCCCCCCCCCCCCH
15.7229255136
246PhosphorylationQPFAQDTSSVGPDRK
CCCCCCCCCCCCCHH
31.1729255136
247PhosphorylationPFAQDTSSVGPDRKL
CCCCCCCCCCCCHHH
32.9329255136
253SumoylationSSVGPDRKLAEEEDL
CCCCCCHHHHHHHHH
60.47-
253SumoylationSSVGPDRKLAEEEDL
CCCCCCHHHHHHHHH
60.47-
263PhosphorylationEEEDLFDSAHPEEGD
HHHHHHHCCCCCCCC
22.5730266825
275PhosphorylationEGDLDLASESTAHAQ
CCCCCCCCCCHHHHH
39.1030266825
277PhosphorylationDLDLASESTAHAQSS
CCCCCCCCHHHHHHC
28.5330266825
278PhosphorylationLDLASESTAHAQSSK
CCCCCCCHHHHHHCC
20.5730266825
283PhosphorylationESTAHAQSSKADSLL
CCHHHHHHCCHHHEE
34.2923401153
284PhosphorylationSTAHAQSSKADSLLA
CHHHHHHCCHHHEEE
21.5630108239
285UbiquitinationTAHAQSSKADSLLAV
HHHHHHCCHHHEEEE
62.55-
288PhosphorylationAQSSKADSLLAVVKR
HHHCCHHHEEEEEEC
30.0919664994
294AcetylationDSLLAVVKREPAEQP
HHEEEEEECCCCCCC
44.4371379
294SumoylationDSLLAVVKREPAEQP
HHEEEEEECCCCCCC
44.43-
294UbiquitinationDSLLAVVKREPAEQP
HHEEEEEECCCCCCC
44.4321890473
294SumoylationDSLLAVVKREPAEQP
HHEEEEEECCCCCCC
44.4321527249
294UbiquitinationDSLLAVVKREPAEQP
HHEEEEEECCCCCCC
44.4321890473
294UbiquitinationDSLLAVVKREPAEQP
HHEEEEEECCCCCCC
44.4321890473
307PhosphorylationQPGDGERTDCEPVGL
CCCCCCCCCCEECCC
40.4723927012
321PhosphorylationLEPAVEQSSAASELA
CHHHHHCCHHHHHHH
14.4025159151
322PhosphorylationEPAVEQSSAASELAE
HHHHHCCHHHHHHHH
27.7823927012
325PhosphorylationVEQSSAASELAEASS
HHCCHHHHHHHHHCH
32.6223927012
331PhosphorylationASELAEASSEELAEA
HHHHHHHCHHHHHHC
29.7726503892
332PhosphorylationSELAEASSEELAEAP
HHHHHHCHHHHHHCC
41.9830278072
340PhosphorylationEELAEAPTEAPSPEA
HHHHHCCCCCCCCCC
52.4030278072
344PhosphorylationEAPTEAPSPEARDSK
HCCCCCCCCCCCCCC
42.2829255136
350PhosphorylationPSPEARDSKEDGRKF
CCCCCCCCCCCCCCC
32.1830576142
354UbiquitinationARDSKEDGRKFDFDA
CCCCCCCCCCCCCCC
35.4521890473
356AcetylationDSKEDGRKFDFDACN
CCCCCCCCCCCCCCC
55.61-
356UbiquitinationDSKEDGRKFDFDACN
CCCCCCCCCCCCCCC
55.61-
359UbiquitinationEDGRKFDFDACNEVP
CCCCCCCCCCCCCCC
7.8421890473
362GlutathionylationRKFDFDACNEVPPAP
CCCCCCCCCCCCCCC
4.8622555962
370UbiquitinationNEVPPAPKESSTSEG
CCCCCCCCCCCCCCC
72.79-
372PhosphorylationVPPAPKESSTSEGAD
CCCCCCCCCCCCCCC
45.0723927012
373PhosphorylationPPAPKESSTSEGADQ
CCCCCCCCCCCCCCC
36.7223927012
374PhosphorylationPAPKESSTSEGADQK
CCCCCCCCCCCCCCC
39.8223927012
375PhosphorylationAPKESSTSEGADQKM
CCCCCCCCCCCCCCC
35.6622167270
381SumoylationTSEGADQKMSSPEDD
CCCCCCCCCCCCCCC
41.1028112733
381UbiquitinationTSEGADQKMSSPEDD
CCCCCCCCCCCCCCC
41.10-
383PhosphorylationEGADQKMSSPEDDSD
CCCCCCCCCCCCCHH
50.1829255136
384PhosphorylationGADQKMSSPEDDSDT
CCCCCCCCCCCCHHH
28.8929255136
389PhosphorylationMSSPEDDSDTKRLSK
CCCCCCCHHHHHCCH
60.5522167270
391PhosphorylationSPEDDSDTKRLSKEE
CCCCCHHHHHCCHHH
23.2422167270
392UbiquitinationPEDDSDTKRLSKEEK
CCCCHHHHHCCHHHH
57.22-
392AcetylationPEDDSDTKRLSKEEK
CCCCHHHHHCCHHHH
57.2226051181
392SumoylationPEDDSDTKRLSKEEK
CCCCHHHHHCCHHHH
57.2228112733
395PhosphorylationDSDTKRLSKEEKGRS
CHHHHHCCHHHHCCC
41.8920068231
402PhosphorylationSKEEKGRSSCGRNFW
CHHHHCCCCCCCCCC
38.3527174698
403PhosphorylationKEEKGRSSCGRNFWV
HHHHCCCCCCCCCCC
21.1627174698
406AcetylationKGRSSCGRNFWVSGL
HCCCCCCCCCCCCCC
39.2319608861
411PhosphorylationCGRNFWVSGLSSTTR
CCCCCCCCCCCCCCC
25.3130108239
414PhosphorylationNFWVSGLSSTTRATD
CCCCCCCCCCCCHHH
29.2130108239
415PhosphorylationFWVSGLSSTTRATDL
CCCCCCCCCCCHHHH
38.5525159151
416PhosphorylationWVSGLSSTTRATDLK
CCCCCCCCCCHHHHH
19.5425159151
417PhosphorylationVSGLSSTTRATDLKN
CCCCCCCCCHHHHHH
21.9130108239
423AcetylationTTRATDLKNLFSKYG
CCCHHHHHHHHHHHC
55.1822647301
423UbiquitinationTTRATDLKNLFSKYG
CCCHHHHHHHHHHHC
55.1821890473
423MalonylationTTRATDLKNLFSKYG
CCCHHHHHHHHHHHC
55.1826320211
423UbiquitinationTTRATDLKNLFSKYG
CCCHHHHHHHHHHHC
55.1821890473
423UbiquitinationTTRATDLKNLFSKYG
CCCHHHHHHHHHHHC
55.1821890473
427PhosphorylationTDLKNLFSKYGKVVG
HHHHHHHHHHCCCCC
28.3024719451
428AcetylationDLKNLFSKYGKVVGA
HHHHHHHHHCCCCCC
51.1722647325
428UbiquitinationDLKNLFSKYGKVVGA
HHHHHHHHHCCCCCC
51.1721890473
428UbiquitinationDLKNLFSKYGKVVGA
HHHHHHHHHCCCCCC
51.1721890473
428UbiquitinationDLKNLFSKYGKVVGA
HHHHHHHHHCCCCCC
51.1721890473
431UbiquitinationNLFSKYGKVVGAKVV
HHHHHHCCCCCCEEE
30.56-
436AcetylationYGKVVGAKVVTNARS
HCCCCCCEEEECCCC
31.1724649665
436UbiquitinationYGKVVGAKVVTNARS
HCCCCCCEEEECCCC
31.17-
436MalonylationYGKVVGAKVVTNARS
HCCCCCCEEEECCCC
31.1726320211
439PhosphorylationVVGAKVVTNARSPGA
CCCCEEEECCCCCCC
26.5825159151
443PhosphorylationKVVTNARSPGARCYG
EEEECCCCCCCEEEE
25.8528355574
448GlutathionylationARSPGARCYGFVTMS
CCCCCCEEEEEEECC
3.7522555962
449PhosphorylationRSPGARCYGFVTMST
CCCCCEEEEEEECCC
14.1920068231
453PhosphorylationARCYGFVTMSTAEEA
CEEEEEEECCCHHHH
11.8020860994
455PhosphorylationCYGFVTMSTAEEATK
EEEEEECCCHHHHHH
18.3321406692
456PhosphorylationYGFVTMSTAEEATKC
EEEEECCCHHHHHHH
27.5422210691
461PhosphorylationMSTAEEATKCINHLH
CCCHHHHHHHHHHHH
29.7222210691
469UbiquitinationKCINHLHKTELHGKM
HHHHHHHHHCCCCEE
50.48-
469AcetylationKCINHLHKTELHGKM
HHHHHHHHHCCCCEE
50.4826051181
475AcetylationHKTELHGKMISVEKA
HHHCCCCEEEEHHHH
23.4723749302
475UbiquitinationHKTELHGKMISVEKA
HHHCCCCEEEEHHHH
23.4719608861
481MalonylationGKMISVEKAKNEPVG
CEEEEHHHHCCCCCC
63.6126320211
483SumoylationMISVEKAKNEPVGKK
EEEHHHHCCCCCCCC
73.2828112733
492PhosphorylationEPVGKKTSDKRDSDG
CCCCCCCCCCCCCCC
50.44-
500AcetylationDKRDSDGKKEKSSNS
CCCCCCCCCCCCCCC
63.857926031
501AcetylationKRDSDGKKEKSSNSD
CCCCCCCCCCCCCCC
75.747926043
504PhosphorylationSDGKKEKSSNSDRST
CCCCCCCCCCCCHHH
35.5218510355
505PhosphorylationDGKKEKSSNSDRSTN
CCCCCCCCCCCHHHH
51.9630576142
507PhosphorylationKKEKSSNSDRSTNLK
CCCCCCCCCHHHHCC
36.0328102081
509MethylationEKSSNSDRSTNLKRD
CCCCCCCHHHHCCCC
45.24115386595
510PhosphorylationKSSNSDRSTNLKRDD
CCCCCCHHHHCCCCC
27.0030576142
511PhosphorylationSSNSDRSTNLKRDDK
CCCCCHHHHCCCCCC
45.5221406692
514SumoylationSDRSTNLKRDDKCDR
CCHHHHCCCCCCCCC
56.7128112733
532PhosphorylationAKKGDDGSGEKSKDQ
HCCCCCCCCCCCCCC
51.2629116813
536PhosphorylationDDGSGEKSKDQDDQK
CCCCCCCCCCCCCCC
36.8428985074
538AcetylationGSGEKSKDQDDQKPG
CCCCCCCCCCCCCCC
65.3219608861
543SumoylationSKDQDDQKPGPSERS
CCCCCCCCCCHHHHH
59.96-
543SumoylationSKDQDDQKPGPSERS
CCCCCCCCCCHHHHH
59.9628112733
543AcetylationSKDQDDQKPGPSERS
CCCCCCCCCCHHHHH
59.9626051181
547PhosphorylationDDQKPGPSERSRATK
CCCCCCHHHHHHHCC
52.1126074081
550PhosphorylationKPGPSERSRATKSGS
CCCHHHHHHHCCCCC
23.4026074081
553PhosphorylationPSERSRATKSGSRGT
HHHHHHHCCCCCCCC
25.3230576142
555PhosphorylationERSRATKSGSRGTER
HHHHHCCCCCCCCEE
37.3325159151
557PhosphorylationSRATKSGSRGTERTV
HHHCCCCCCCCEEEE
34.3325159151
560PhosphorylationTKSGSRGTERTVVMD
CCCCCCCCEEEEEEE
22.6025159151
563PhosphorylationGSRGTERTVVMDKSK
CCCCCEEEEEEECCC
15.9526074081
568AcetylationERTVVMDKSKGVPVI
EEEEEEECCCCCEEE
35.6523749302
569PhosphorylationRTVVMDKSKGVPVIS
EEEEEECCCCCEEEE
30.3126074081
570SumoylationTVVMDKSKGVPVISV
EEEEECCCCCEEEEE
70.4428112733
576PhosphorylationSKGVPVISVKTSGSK
CCCCEEEEEECCCCH
20.1430266825
578SumoylationGVPVISVKTSGSKER
CCEEEEEECCCCHHH
30.1325114211
578AcetylationGVPVISVKTSGSKER
CCEEEEEECCCCHHH
30.1325953088
579PhosphorylationVPVISVKTSGSKERA
CEEEEEECCCCHHHH
35.8425159151
580PhosphorylationPVISVKTSGSKERAS
EEEEEECCCCHHHHC
35.0425159151
582PhosphorylationISVKTSGSKERASKS
EEEECCCCHHHHCCC
30.9825159151
587PhosphorylationSGSKERASKSQDRKS
CCCHHHHCCCCCHHH
38.7830576142
589PhosphorylationSKERASKSQDRKSAS
CHHHHCCCCCHHHHH
34.5130576142
594PhosphorylationSKSQDRKSASREKRS
CCCCCHHHHHHHHHH
32.1626074081
596PhosphorylationSQDRKSASREKRSVV
CCCHHHHHHHHHHCC
48.3326074081
601PhosphorylationSASREKRSVVSFDKV
HHHHHHHHCCCHHHC
37.6323927012
604PhosphorylationREKRSVVSFDKVKEP
HHHHHCCCHHHCCCC
26.1029255136
607AcetylationRSVVSFDKVKEPRKS
HHCCCHHHCCCCCCC
53.8719608861
607UbiquitinationRSVVSFDKVKEPRKS
HHCCCHHHCCCCCCC
53.8719608861
607MalonylationRSVVSFDKVKEPRKS
HHCCCHHHCCCCCCC
53.8726320211
609AcetylationVVSFDKVKEPRKSRD
CCCHHHCCCCCCCCC
68.687307319
614PhosphorylationKVKEPRKSRDSESHS
HCCCCCCCCCCHHHH
42.4730576142
614 (in isoform 4)Phosphorylation-42.4721857030
617PhosphorylationEPRKSRDSESHSRVR
CCCCCCCCHHHHHHH
39.6329743597
617 (in isoform 4)Phosphorylation-39.6321857030
619PhosphorylationRKSRDSESHSRVRER
CCCCCCHHHHHHHHH
30.6229743597
619 (in isoform 4)Phosphorylation-30.6228102081
621PhosphorylationSRDSESHSRVRERSE
CCCCHHHHHHHHHHH
41.5720068231
627PhosphorylationHSRVRERSEREQRMQ
HHHHHHHHHHHHHHH
35.9330576142
702PhosphorylationRRQQELRYEQERRPA
HHHHHHHHHHHHCCC
34.2924043423
712MethylationERRPAVRRPYDLDRR
HHCCCCCCCCCCCCC
27.77-
723PhosphorylationLDRRDDAYWPEAKRA
CCCCCCCCCHHHHHH
28.6120090780
728MethylationDAYWPEAKRAALDER
CCCCHHHHHHHHHHH
40.69115977475
728AcetylationDAYWPEAKRAALDER
CCCCHHHHHHHHHHH
40.6925953088
738PhosphorylationALDERYHSDFNRQDR
HHHHHHHCCCCCCCC
34.6626714015
742 (in isoform 2)Methylation-39.51-
749 (in isoform 2)Dimethylation-6.82-
749 (in isoform 2)Methylation-6.82-
751 (in isoform 2)Methylation-33.27-
754MethylationHDFDHRDRGRYPDHS
CCCCCCCCCCCCCCC
31.29115368129
757PhosphorylationDHRDRGRYPDHSVDR
CCCCCCCCCCCCCCC
18.8128152594
761PhosphorylationRGRYPDHSVDRREGS
CCCCCCCCCCCCCCC
32.8528152594
764MethylationYPDHSVDRREGSRSM
CCCCCCCCCCCCCCC
36.07115493129
768PhosphorylationSVDRREGSRSMMGER
CCCCCCCCCCCCCCC
19.2127251275
770PhosphorylationDRREGSRSMMGEREG
CCCCCCCCCCCCCCC
18.1524719451
780PhosphorylationGEREGQHYPERHGGP
CCCCCCCCCCCCCCC
10.0228152594
783MethylationEGQHYPERHGGPERH
CCCCCCCCCCCCCCC
29.28115493121
794PhosphorylationPERHGRDSRDGWGGY
CCCCCCCCCCCCCCC
30.8030576142
801PhosphorylationSRDGWGGYGSDKRMS
CCCCCCCCCCCCCCC
14.9828152594
803PhosphorylationDGWGGYGSDKRMSEG
CCCCCCCCCCCCCCC
31.3225159151
805MethylationWGGYGSDKRMSEGRG
CCCCCCCCCCCCCCC
52.26130735
805AcetylationWGGYGSDKRMSEGRG
CCCCCCCCCCCCCCC
52.2626051181
808PhosphorylationYGSDKRMSEGRGLPP
CCCCCCCCCCCCCCC
40.7223401153
811MethylationDKRMSEGRGLPPPPR
CCCCCCCCCCCCCCC
39.1524129315
818MethylationRGLPPPPRRDWGDHG
CCCCCCCCCCCCCCC
55.7734666407
818DimethylationRGLPPPPRRDWGDHG
CCCCCCCCCCCCCCC
55.77-
820MethylationLPPPPRRDWGDHGRR
CCCCCCCCCCCCCCC
55.80-
832PhosphorylationGRREDDRSWQGTADG
CCCCCCCCCCCCCCC
30.6423401153
834PhosphorylationREDDRSWQGTADGGM
CCCCCCCCCCCCCCC
40.3727251275
836PhosphorylationDDRSWQGTADGGMMD
CCCCCCCCCCCCCCC
13.3828985074
847SumoylationGMMDRDHKRWQGGER
CCCCCCCCCCCCCCC
60.6728112733
855PhosphorylationRWQGGERSMSGHSGP
CCCCCCCCCCCCCCC
17.0123322592
857PhosphorylationQGGERSMSGHSGPGH
CCCCCCCCCCCCCCC
34.3023322592
860PhosphorylationERSMSGHSGPGHMMN
CCCCCCCCCCCCCCC
50.6523322592
868Asymmetric dimethylarginineGPGHMMNRGGMSGRG
CCCCCCCCCCCCCCC
25.75-
868MethylationGPGHMMNRGGMSGRG
CCCCCCCCCCCCCCC
25.7524129315
872PhosphorylationMMNRGGMSGRGSFAP
CCCCCCCCCCCCCCC
28.7222210691
874Asymmetric dimethylarginineNRGGMSGRGSFAPGG
CCCCCCCCCCCCCCC
30.21-
874MethylationNRGGMSGRGSFAPGG
CCCCCCCCCCCCCCC
30.2124129315
883PhosphorylationSFAPGGASRGHPIPH
CCCCCCCCCCCCCCC
41.9122210691
884Asymmetric dimethylarginineFAPGGASRGHPIPHG
CCCCCCCCCCCCCCC
47.08-
884MethylationFAPGGASRGHPIPHG
CCCCCCCCCCCCCCC
47.0824129315
901PhosphorylationQGGFGGQSRGSRPSD
CCCCCCCCCCCCCCC
41.7122210691
902MethylationGGFGGQSRGSRPSDA
CCCCCCCCCCCCCCC
38.9430760949
904PhosphorylationFGGQSRGSRPSDARF
CCCCCCCCCCCCCCC
39.6523186163
905MethylationGGQSRGSRPSDARFT
CCCCCCCCCCCCCCC
37.25115391805
907PhosphorylationQSRGSRPSDARFTRR
CCCCCCCCCCCCCCC
42.6721601212
910MethylationGSRPSDARFTRRY--
CCCCCCCCCCCCC--
38.1624387951

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 SAFB1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SAFB1_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 SAFB1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SAFB2_HUMANSAFB2physical
12660241
RBP56_HUMANTAF15physical
15066997
ESR1_HUMANESR1physical
15066997
CHD3_HUMANCHD3physical
16169070
ESR1_HUMANESR1physical
10707955
NCOR1_HUMANNCOR1physical
16195251
NCOR1_HUMANNCOR1physical
21527249
HDAC3_HUMANHDAC3physical
21527249
PIAS1_HUMANPIAS1physical
21527249
ESR1_HUMANESR1physical
21527249
SAP18_HUMANSAP18physical
22939629
SMU1_HUMANSMU1physical
22939629
TPBG_HUMANTPBGphysical
22939629
TRI55_HUMANTRIM55physical
22939629
U2AF1_HUMANU2AF1physical
22939629
SON_HUMANSONphysical
22939629
TR112_HUMANTRMT112physical
22939629
SEPT7_HUMANSEPT7physical
22939629
UT14A_HUMANUTP14Aphysical
22939629
VTNC_HUMANVTNphysical
22939629
ZCH18_HUMANZC3H18physical
22939629
SNUT2_HUMANUSP39physical
22939629
TMOD2_HUMANTMOD2physical
22939629
VASN_HUMANVASNphysical
22939629
SRSF7_HUMANSRSF7physical
22939629
THIL_HUMANACAT1physical
22939629
U2AF2_HUMANU2AF2physical
22939629
SURF4_HUMANSURF4physical
22939629
IL7RA_HUMANIL7Rphysical
23151878
P53_HUMANTP53physical
21130767
HNRPU_HUMANHNRNPUphysical
26344197
HNRL1_HUMANHNRNPUL1physical
26344197
MCM4_HUMANMCM4physical
26344197
PDIA1_HUMANP4HBphysical
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 SAFB1_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 THR-194; SER-288; SER-383 AND SER-384, 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-475 AND LYS-607, AND MASSSPECTROMETRY.
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-235; SER-247 ANDSER-288, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-194; SER-288; SER-383 AND SER-384, 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-55; SER-373; SER-383;SER-384; SER-601 AND SER-604, 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-555 AND SER-557, ANDMASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604, 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 SER-288; SER-601 ANDSER-604, AND MASS 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-384; SER-589; SER-604AND SER-808, AND MASS SPECTROMETRY.
Sumoylation
ReferencePubMed
"Co-repressor activity of scaffold attachment factor B1 requiressumoylation.";
Garee J.P., Meyer R., Oesterreich S.;
Biochem. Biophys. Res. Commun. 408:516-522(2011).
Cited for: SUMOYLATION AT LYS-231 AND LYS-294.

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