ARI1B_HUMAN - dbPTM
ARI1B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARI1B_HUMAN
UniProt AC Q8NFD5
Protein Name AT-rich interactive domain-containing protein 1B
Gene Name ARID1B
Organism Homo sapiens (Human).
Sequence Length 2236
Subcellular Localization Nucleus .
Protein Description Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Binds DNA non-specifically. [PubMed: 14982958]
Protein Sequence MAHNAGAAAAAGTHSAKSGGSEAALKEGGSAAALSSSSSSSAAAAAASSSSSSGPGSAMETGLLPNHKLKTVGEAPAAPPHQQHHHHHHAHHHHHHAHHLHHHHALQQQLNQFQQQQQQQQQQQQQQQQQQHPISNNNSLGGAGGGAPQPGPDMEQPQHGGAKDSAAGGQADPPGPPLLSKPGDEDDAPPKMGEPAGGRYEHPGLGALGTQQPPVAVPGGGGGPAAVPEFNNYYGSAAPASGGPGGRAGPCFDQHGGQQSPGMGMMHSASAAAAGAPGSMDPLQNSHEGYPNSQCNHYPGYSRPGAGGGGGGGGGGGGGSGGGGGGGGAGAGGAGAGAVAAAAAAAAAAAGGGGGGGYGGSSAGYGVLSSPRQQGGGMMMGPGGGGAASLSKAAAGSAAGGFQRFAGQNQHPSGATPTLNQLLTSPSPMMRSYGGSYPEYSSPSAPPPPPSQPQSQAAAAGAAAGGQQAAAGMGLGKDMGAQYAAASPAWAAAQQRSHPAMSPGTPGPTMGRSQGSPMDPMVMKRPQLYGMGSNPHSQPQQSSPYPGGSYGPPGPQRYPIGIQGRTPGAMAGMQYPQQQMPPQYGQQGVSGYCQQGQQPYYSQQPQPPHLPPQAQYLPSQSQQRYQPQQDMSQEGYGTRSQPPLAPGKPNHEDLNLIQQERPSSLPDLSGSIDDLPTGTEATLSSAVSASGSTSSQGDQSNPAQSPFSPHASPHLSSIPGGPSPSPVGSPVGSNQSRSGPISPASIPGSQMPPQPPGSQSESSSHPALSQSPMPQERGFMAGTQRNPQMAQYGPQQTGPSMSPHPSPGGQMHAGISSFQQSNSSGTYGPQMSQYGPQGNYSRPPAYSGVPSASYSGPGPGMGISANNQMHGQGPSQPCGAVPLGRMPSAGMQNRPFPGNMSSMTPSSPGMSQQGGPGMGPPMPTVNRKAQEAAAAVMQAAANSAQSRQGSFPGMNQSGLMASSSPYSQPMNNSSSLMNTQAPPYSMAPAMVNSSAASVGLADMMSPGESKLPLPLKADGKEEGTPQPESKSKKSSSSTTTGEKITKVYELGNEPERKLWVDRYLTFMEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVGTSSSAASSLKKQYIQYLFAFECKIERGEEPPPEVFSTGDTKKQPKLQPPSPANSGSLQGPQTPQSTGSNSMAEVPGDLKPPTPASTPHGQMTPMQGGRSSTISVHDPFSDVSDSSFPKRNSMTPNAPYQQGMSMPDVMGRMPYEPNKDPFGGMRKVPGSSEPFMTQGQMPNSSMQDMYNQSPSGAMSNLGMGQRQQFPYGASYDRRHEPYGQQYPGQGPPSGQPPYGGHQPGLYPQQPNYKRHMDGMYGPPAKRHEGDMYNMQYSSQQQEMYNQYGGSYSGPDRRPIQGQYPYPYSRERMQGPGQIQTHGIPPQMMGGPLQSSSSEGPQQNMWAARNDMPYPYQNRQGPGGPTQAPPYPGMNRTDDMMVPDQRINHESQWPSHVSQRQPYMSSSASMQPITRPPQPSYQTPPSLPNHISRAPSPASFQRSLENRMSPSKSPFLPSMKMQKVMPTVPTSQVTGPPPQPPPIRREITFPPGSVEASQPVLKQRRKITSKDIVTPEAWRVMMSLKSGLLAESTWALDTINILLYDDSTVATFNLSQLSGFLELLVEYFRKCLIDIFGILMEYEVGDPSQKALDHNAARKDDSQSLADDSGKEEEDAECIDDDEEDEEDEEEDSEKTESDEKSSIALTAPDAAADPKEKPKQASKFDKLPIKIVKKNNLFVVDRSDKLGRVQEFNSGLLHWQLGGGDTTEHIQTHFESKMEIPPRRRPPPPLSSAGRKKEQEGKGDSEEQQEKSIIATIDDVLSARPGALPEDANPGPQTESSKFPFGIQQAKSHRNIKLLEDEPRSRDETPLCTIAHWQDSLAKRCICVSNIVRSLSFVPGNDAEMSKHPGLVLILGKLILLHHEHPERKRAPQTYEKEEDEDKGVACSKDEWWWDCLEVLRDNTLVTLANISGQLDLSAYTESICLPILDGLLHWMVCPSAEAQDPFPTVGPNSVLSPQRLVLETLCKLSIQDNNVDLILATPPFSRQEKFYATLVRYVGDRKNPVCREMSMALLSNLAQGDALAARAIAVQKGSIGNLISFLEDGVTMAQYQQSQHNLMHMQPPPLEPPSVDMMCRAAKALLAMARVDENRSEFLLHEGRLLDISISAVLNSLVASVICDVLFQIGQL
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------MAHNAGAAA
------CCCCHHHHH
18.8819413330
15PhosphorylationAAAAGTHSAKSGGSE
HHHHCCCHHCCCCCH
36.9124719451
21PhosphorylationHSAKSGGSEAALKEG
CHHCCCCCHHHHHCC
27.8224719451
68AcetylationTGLLPNHKLKTVGEA
CCCCCCCCCCCCCCC
59.3225953088
181AcetylationPGPPLLSKPGDEDDA
CCCCCCCCCCCCCCC
53.6526051181
369PhosphorylationSAGYGVLSSPRQQGG
CCCCCCCCCCCCCCC
35.5717081983
370PhosphorylationAGYGVLSSPRQQGGG
CCCCCCCCCCCCCCC
21.6817081983
389PhosphorylationPGGGGAASLSKAAAG
CCCCHHHHHHHHHHC
32.4224425749
404MethylationSAAGGFQRFAGQNQH
CCCCCHHHHCCCCCC
22.56-
413PhosphorylationAGQNQHPSGATPTLN
CCCCCCCCCCCCCHH
38.6522199227
416PhosphorylationNQHPSGATPTLNQLL
CCCCCCCCCCHHHHH
21.9722199227
418PhosphorylationHPSGATPTLNQLLTS
CCCCCCCCHHHHHHC
33.7022199227
424PhosphorylationPTLNQLLTSPSPMMR
CCHHHHHHCCCHHHH
47.3822199227
425PhosphorylationTLNQLLTSPSPMMRS
CHHHHHHCCCHHHHH
24.2922199227
427PhosphorylationNQLLTSPSPMMRSYG
HHHHHCCCHHHHHCC
25.7922199227
483PhosphorylationGKDMGAQYAAASPAW
CHHHHHHHHHHCHHH
9.5521945579
487PhosphorylationGAQYAAASPAWAAAQ
HHHHHHHCHHHHHHH
15.4921945579
497PhosphorylationWAAAQQRSHPAMSPG
HHHHHHHCCCCCCCC
29.5023927012
502PhosphorylationQRSHPAMSPGTPGPT
HHCCCCCCCCCCCCC
23.4523401153
505PhosphorylationHPAMSPGTPGPTMGR
CCCCCCCCCCCCCCC
28.5830266825
509PhosphorylationSPGTPGPTMGRSQGS
CCCCCCCCCCCCCCC
37.8723927012
513PhosphorylationPGPTMGRSQGSPMDP
CCCCCCCCCCCCCCC
32.9128102081
516PhosphorylationTMGRSQGSPMDPMVM
CCCCCCCCCCCCCHH
14.9325159151
525DimethylationMDPMVMKRPQLYGMG
CCCCHHCCCCCCCCC
13.20-
525MethylationMDPMVMKRPQLYGMG
CCCCHHCCCCCCCCC
13.20-
529PhosphorylationVMKRPQLYGMGSNPH
HHCCCCCCCCCCCCC
10.3824043423
533PhosphorylationPQLYGMGSNPHSQPQ
CCCCCCCCCCCCCCC
37.9924043423
537PhosphorylationGMGSNPHSQPQQSSP
CCCCCCCCCCCCCCC
44.8324043423
542PhosphorylationPHSQPQQSSPYPGGS
CCCCCCCCCCCCCCC
28.2124043423
543PhosphorylationHSQPQQSSPYPGGSY
CCCCCCCCCCCCCCC
24.9024043423
545PhosphorylationQPQQSSPYPGGSYGP
CCCCCCCCCCCCCCC
19.2324043423
549PhosphorylationSSPYPGGSYGPPGPQ
CCCCCCCCCCCCCCC
32.6024043423
550PhosphorylationSPYPGGSYGPPGPQR
CCCCCCCCCCCCCCC
36.6124043423
557Asymmetric dimethylarginineYGPPGPQRYPIGIQG
CCCCCCCCCCCCCCC
42.18-
557MethylationYGPPGPQRYPIGIQG
CCCCCCCCCCCCCCC
42.1824129315
558PhosphorylationGPPGPQRYPIGIQGR
CCCCCCCCCCCCCCC
8.2424043423
565DimethylationYPIGIQGRTPGAMAG
CCCCCCCCCCCCCCC
22.75-
565MethylationYPIGIQGRTPGAMAG
CCCCCCCCCCCCCCC
22.75-
585PhosphorylationQQMPPQYGQQGVSGY
HHCCCCCCCCCCCCC
14.2132142685
588PhosphorylationPPQYGQQGVSGYCQQ
CCCCCCCCCCCCCCC
13.9932142685
632PhosphorylationYQPQQDMSQEGYGTR
CCCCCCCCCCCCCCC
33.1118077418
645PhosphorylationTRSQPPLAPGKPNHE
CCCCCCCCCCCCCHH
19.3018077418
663PhosphorylationLIQQERPSSLPDLSG
HHHHHCCCCCCCCCC
51.2126074081
664PhosphorylationIQQERPSSLPDLSGS
HHHHCCCCCCCCCCC
46.7526074081
677PhosphorylationGSIDDLPTGTEATLS
CCHHCCCCCCHHHHH
65.12-
738PhosphorylationVGSNQSRSGPISPAS
CCCCCCCCCCCCCCC
54.9223401153
742PhosphorylationQSRSGPISPASIPGS
CCCCCCCCCCCCCCC
19.9728464451
745PhosphorylationSGPISPASIPGSQMP
CCCCCCCCCCCCCCC
32.4730108239
749PhosphorylationSPASIPGSQMPPQPP
CCCCCCCCCCCCCCC
20.2526074081
758PhosphorylationMPPQPPGSQSESSSH
CCCCCCCCCCCCCCC
35.9926074081
760PhosphorylationPQPPGSQSESSSHPA
CCCCCCCCCCCCCCC
40.9426074081
762PhosphorylationPPGSQSESSSHPALS
CCCCCCCCCCCCCCC
42.2526074081
763PhosphorylationPGSQSESSSHPALSQ
CCCCCCCCCCCCCCC
28.7226074081
764PhosphorylationGSQSESSSHPALSQS
CCCCCCCCCCCCCCC
42.6526074081
769PhosphorylationSSSHPALSQSPMPQE
CCCCCCCCCCCCCCC
30.6226074081
771PhosphorylationSHPALSQSPMPQERG
CCCCCCCCCCCCCCC
21.5726074081
825PhosphorylationFQQSNSSGTYGPQMS
CCCCCCCCCCCCCHH
23.8332142685
838PhosphorylationMSQYGPQGNYSRPPA
HHHCCCCCCCCCCCC
37.8732142685
858PhosphorylationSASYSGPGPGMGISA
CCCCCCCCCCCCCCC
34.6132645325
862PhosphorylationSGPGPGMGISANNQM
CCCCCCCCCCCCCCC
19.3332142685
867PhosphorylationGMGISANNQMHGQGP
CCCCCCCCCCCCCCC
40.0233259812
888PhosphorylationVPLGRMPSAGMQNRP
CCCCCCCCCCCCCCC
28.28-
904PhosphorylationPGNMSSMTPSSPGMS
CCCCCCCCCCCCCCC
23.2022210691
906PhosphorylationNMSSMTPSSPGMSQQ
CCCCCCCCCCCCCCC
39.7427251275
907PhosphorylationMSSMTPSSPGMSQQG
CCCCCCCCCCCCCCC
27.0328348404
924PhosphorylationGMGPPMPTVNRKAQE
CCCCCCCCCCHHHHH
24.9422210691
943PhosphorylationVMQAAANSAQSRQGS
HHHHHHHHHHHHCCC
23.9828555341
946PhosphorylationAAANSAQSRQGSFPG
HHHHHHHHHCCCCCC
26.70-
1005PhosphorylationVGLADMMSPGESKLP
HCCHHCCCCCCCCCC
24.1026074081
1009PhosphorylationDMMSPGESKLPLPLK
HCCCCCCCCCCCCCC
45.4626074081
1016AcetylationSKLPLPLKADGKEEG
CCCCCCCCCCCCCCC
42.3625953088
1016SumoylationSKLPLPLKADGKEEG
CCCCCCCCCCCCCCC
42.3617000644
1020AcetylationLPLKADGKEEGTPQP
CCCCCCCCCCCCCCC
53.8126051181
1024PhosphorylationADGKEEGTPQPESKS
CCCCCCCCCCCCCCC
23.2529396449
1034PhosphorylationPESKSKKSSSSTTTG
CCCCCCCCCCCCCCH
38.9121060948
1036PhosphorylationSKSKKSSSSTTTGEK
CCCCCCCCCCCCHHH
38.50-
1037PhosphorylationKSKKSSSSTTTGEKI
CCCCCCCCCCCHHHH
31.55-
1040PhosphorylationKSSSSTTTGEKITKV
CCCCCCCCHHHHHHH
43.35-
1043AcetylationSSTTTGEKITKVYEL
CCCCCHHHHHHHEEC
57.9526051181
1048PhosphorylationGEKITKVYELGNEPE
HHHHHHHEECCCCHH
13.6430257219
1063PhosphorylationRKLWVDRYLTFMEER
HHHHHHHHHHHHHHH
12.9629691806
1065PhosphorylationLWVDRYLTFMEERGS
HHHHHHHHHHHHHCC
16.4129691806
1072PhosphorylationTFMEERGSPVSSLPA
HHHHHHCCCCHHCCC
28.4930266825
1075PhosphorylationEERGSPVSSLPAVGK
HHHCCCCHHCCCCCC
29.5527251275
1076PhosphorylationERGSPVSSLPAVGKK
HHCCCCHHCCCCCCC
38.3129449344
1081 (in isoform 3)Phosphorylation-34.0828450419
1082AcetylationSSLPAVGKKPLDLFR
HHCCCCCCCCHHHHH
44.6225953088
1083 (in isoform 3)Phosphorylation-44.9023911959
1084 (in isoform 3)Phosphorylation-34.2928450419
1085PhosphorylationPAVGKKPLDLFRLYV
CCCCCCCHHHHHHHH
14.18-
1091PhosphorylationPLDLFRLYVCVKEIG
CHHHHHHHHHHHHHC
6.37-
1091 (in isoform 3)Phosphorylation-6.37-
1114PhosphorylationKKWRELATNLNVGTS
HHHHHHHHHCCCCCC
53.5220068231
1120PhosphorylationATNLNVGTSSSAASS
HHHCCCCCCHHHHHH
22.5828787133
1121PhosphorylationTNLNVGTSSSAASSL
HHCCCCCCHHHHHHH
19.1620068231
1122PhosphorylationNLNVGTSSSAASSLK
HCCCCCCHHHHHHHH
24.6720068231
1123PhosphorylationLNVGTSSSAASSLKK
CCCCCCHHHHHHHHH
27.8520068231
1126PhosphorylationGTSSSAASSLKKQYI
CCCHHHHHHHHHHHH
35.6020068231
1127PhosphorylationTSSSAASSLKKQYIQ
CCHHHHHHHHHHHHH
39.2120068231
1169PhosphorylationQPKLQPPSPANSGSL
CCCCCCCCCCCCCCC
43.2426074081
1173PhosphorylationQPPSPANSGSLQGPQ
CCCCCCCCCCCCCCC
31.6826074081
1175PhosphorylationPSPANSGSLQGPQTP
CCCCCCCCCCCCCCC
19.8326074081
1181PhosphorylationGSLQGPQTPQSTGSN
CCCCCCCCCCCCCCC
26.8226074081
1182PhosphorylationSLQGPQTPQSTGSNS
CCCCCCCCCCCCCCC
22.37-
1184PhosphorylationQGPQTPQSTGSNSMA
CCCCCCCCCCCCCCC
35.6227251275
1185PhosphorylationGPQTPQSTGSNSMAE
CCCCCCCCCCCCCCC
39.1127251275
1189PhosphorylationPQSTGSNSMAEVPGD
CCCCCCCCCCCCCCC
22.5220068231
1197UbiquitinationMAEVPGDLKPPTPAS
CCCCCCCCCCCCCCC
12.7421890473
1201PhosphorylationPGDLKPPTPASTPHG
CCCCCCCCCCCCCCC
39.7622210691
1211PhosphorylationSTPHGQMTPMQGGRS
CCCCCCCCCCCCCCC
14.02-
1218PhosphorylationTPMQGGRSSTISVHD
CCCCCCCCCEEEECC
34.8023401153
1219PhosphorylationPMQGGRSSTISVHDP
CCCCCCCCEEEECCC
28.5320068231
1220PhosphorylationMQGGRSSTISVHDPF
CCCCCCCEEEECCCC
20.6520068231
1222PhosphorylationGGRSSTISVHDPFSD
CCCCCEEEECCCCCC
17.3120068231
1228PhosphorylationISVHDPFSDVSDSSF
EEECCCCCCCCCCCC
42.3527080861
1231PhosphorylationHDPFSDVSDSSFPKR
CCCCCCCCCCCCCCC
36.4427080861
1233PhosphorylationPFSDVSDSSFPKRNS
CCCCCCCCCCCCCCC
26.7727080861
1234PhosphorylationFSDVSDSSFPKRNSM
CCCCCCCCCCCCCCC
51.0327080861
1240PhosphorylationSSFPKRNSMTPNAPY
CCCCCCCCCCCCCCC
28.2425159151
1241PhosphorylationSFPKRNSMTPNAPYQ
CCCCCCCCCCCCCCC
9.1320068231
1242PhosphorylationFPKRNSMTPNAPYQQ
CCCCCCCCCCCCCCC
17.1425159151
1247PhosphorylationSMTPNAPYQQGMSMP
CCCCCCCCCCCCCCC
15.8528450419
1252PhosphorylationAPYQQGMSMPDVMGR
CCCCCCCCCCCCCCC
33.7127080861
1253PhosphorylationPYQQGMSMPDVMGRM
CCCCCCCCCCCCCCC
2.1420068231
1255PhosphorylationQQGMSMPDVMGRMPY
CCCCCCCCCCCCCCC
34.1020068231
1259MethylationSMPDVMGRMPYEPNK
CCCCCCCCCCCCCCC
12.57-
1272MethylationNKDPFGGMRKVPGSS
CCCCCCCCCCCCCCC
3.71-
1287UbiquitinationEPFMTQGQMPNSSMQ
CCCCCCCCCCCCHHH
34.0521890473
1340PhosphorylationYPGQGPPSGQPPYGG
CCCCCCCCCCCCCCC
53.8728555341
1360MethylationYPQQPNYKRHMDGMY
CCCCCCCCCCCCCCC
42.33-
1361MethylationPQQPNYKRHMDGMYG
CCCCCCCCCCCCCCC
21.72-
1367PhosphorylationKRHMDGMYGPPAKRH
CCCCCCCCCCCCCCC
31.82-
1373MethylationMYGPPAKRHEGDMYN
CCCCCCCCCCCCCCC
34.88-
1374MethylationYGPPAKRHEGDMYNM
CCCCCCCCCCCCCCC
42.56-
1379PhosphorylationKRHEGDMYNMQYSSQ
CCCCCCCCCCCCHHH
16.5424043423
1383PhosphorylationGDMYNMQYSSQQQEM
CCCCCCCCHHHHHHH
10.2624043423
1384PhosphorylationDMYNMQYSSQQQEMY
CCCCCCCHHHHHHHH
12.5524043423
1385PhosphorylationMYNMQYSSQQQEMYN
CCCCCCHHHHHHHHH
27.3724043423
1391PhosphorylationSSQQQEMYNQYGGSY
HHHHHHHHHHCCCCC
9.8124043423
1394PhosphorylationQQEMYNQYGGSYSGP
HHHHHHHCCCCCCCC
21.5924043423
1397PhosphorylationMYNQYGGSYSGPDRR
HHHHCCCCCCCCCCC
16.2624043423
1398PhosphorylationYNQYGGSYSGPDRRP
HHHCCCCCCCCCCCC
22.4124043423
1399PhosphorylationNQYGGSYSGPDRRPI
HHCCCCCCCCCCCCC
45.6124043423
1400UbiquitinationQYGGSYSGPDRRPIQ
HCCCCCCCCCCCCCC
21.6421890473
1415PhosphorylationGQYPYPYSRERMQGP
CCCCCCCCCCCCCCC
24.1425003641
1472PhosphorylationRQGPGGPTQAPPYPG
CCCCCCCCCCCCCCC
40.4128787133
1490UbiquitinationTDDMMVPDQRINHES
CCCCCCCCCCCCCHH
38.6921890473
1497PhosphorylationDQRINHESQWPSHVS
CCCCCCHHHCCCCHH
29.9619664995
1501PhosphorylationNHESQWPSHVSQRQP
CCHHHCCCCHHHCCC
33.3020068231
1509PhosphorylationHVSQRQPYMSSSASM
CHHHCCCCCCCCCCC
10.9924043423
1511PhosphorylationSQRQPYMSSSASMQP
HHCCCCCCCCCCCCC
18.4624043423
1512PhosphorylationQRQPYMSSSASMQPI
HCCCCCCCCCCCCCC
17.2524043423
1542PhosphorylationNHISRAPSPASFQRS
CCHHCCCCHHHHHHH
31.9223401153
1545PhosphorylationSRAPSPASFQRSLEN
HCCCCHHHHHHHHHH
25.8730266825
1549PhosphorylationSPASFQRSLENRMSP
CHHHHHHHHHHCCCC
29.2922199227
1553MethylationFQRSLENRMSPSKSP
HHHHHHHCCCCCCCC
19.99-
1555PhosphorylationRSLENRMSPSKSPFL
HHHHHCCCCCCCCCC
23.8425159151
1557PhosphorylationLENRMSPSKSPFLPS
HHHCCCCCCCCCCCC
38.1630266825
1559PhosphorylationNRMSPSKSPFLPSMK
HCCCCCCCCCCCCCC
25.8130266825
1562PhosphorylationSPSKSPFLPSMKMQK
CCCCCCCCCCCCEEE
3.31-
1564PhosphorylationSKSPFLPSMKMQKVM
CCCCCCCCCCEEECC
32.9323927012
1566AcetylationSPFLPSMKMQKVMPT
CCCCCCCCEEECCCC
42.3825953088
1566MethylationSPFLPSMKMQKVMPT
CCCCCCCCEEECCCC
42.38-
1568PhosphorylationFLPSMKMQKVMPTVP
CCCCCCEEECCCCCC
29.6732645325
1569AcetylationLPSMKMQKVMPTVPT
CCCCCEEECCCCCCH
36.6826051181
1570PhosphorylationPSMKMQKVMPTVPTS
CCCCEEECCCCCCHH
2.90-
1572PhosphorylationMKMQKVMPTVPTSQV
CCEEECCCCCCHHHC
32.9820068231
1573PhosphorylationKMQKVMPTVPTSQVT
CEEECCCCCCHHHCC
22.4823879269
1577O-linked_GlycosylationVMPTVPTSQVTGPPP
CCCCCCHHHCCCCCC
19.3120305658
1577PhosphorylationVMPTVPTSQVTGPPP
CCCCCCHHHCCCCCC
19.31-
1579AcetylationPTVPTSQVTGPPPQP
CCCCHHHCCCCCCCC
7.1819608861
1616AcetylationQRRKITSKDIVTPEA
HCCCCCCCCCCCHHH
42.7123749302
1629AcetylationEAWRVMMSLKSGLLA
HHHHHHHHHHCCHHH
17.98-
1638PhosphorylationKSGLLAESTWALDTI
HCCHHHCCCCCCCCE
24.5232645325
1651PhosphorylationTINILLYDDSTVATF
CEEEEEECCCCEEEE
43.2732645325
1655PhosphorylationLLYDDSTVATFNLSQ
EEECCCCEEEEEHHH
5.6732142685
1660PhosphorylationSTVATFNLSQLSGFL
CCEEEEEHHHHHHHH
2.7833259812
1691PhosphorylationILMEYEVGDPSQKAL
HHHHCCCCCHHHHHH
29.2232645325
1695PhosphorylationYEVGDPSQKALDHNA
CCCCCHHHHHHCCCC
40.1932142685
1700PhosphorylationPSQKALDHNAARKDD
HHHHHHCCCCCCCCC
27.0333259812
1710PhosphorylationARKDDSQSLADDSGK
CCCCCCCCCCCCCCC
29.4930576142
1715PhosphorylationSQSLADDSGKEEEDA
CCCCCCCCCCCHHHH
52.9221815630
1728PhosphorylationDAECIDDDEEDEEDE
HHHCCCCCCCCCCCH
58.3919651622
1739PhosphorylationEEDEEEDSEKTESDE
CCCHHHHHHHCCCHH
44.2530576142
1742PhosphorylationEEEDSEKTESDEKSS
HHHHHHHCCCHHHHC
36.3523312004
1744PhosphorylationEDSEKTESDEKSSIA
HHHHHCCCHHHHCEE
57.1923312004
1748PhosphorylationKTESDEKSSIALTAP
HCCCHHHHCEEEECC
25.5730266825
1749PhosphorylationTESDEKSSIALTAPD
CCCHHHHCEEEECCC
23.9730266825
1753PhosphorylationEKSSIALTAPDAAAD
HHHCEEEECCCHHCC
27.4229255136
1770AcetylationEKPKQASKFDKLPIK
CCCCCCCCCCCCCEE
61.6725953088
1773AcetylationKQASKFDKLPIKIVK
CCCCCCCCCCEEEEE
60.3326051181
1777AcetylationKFDKLPIKIVKKNNL
CCCCCCEEEEEECCE
39.2419608861
1777UbiquitinationKFDKLPIKIVKKNNL
CCCCCCEEEEEECCE
39.2429967540
1780AcetylationKLPIKIVKKNNLFVV
CCCEEEEEECCEEEE
53.947678637
1790AcetylationNLFVVDRSDKLGRVQ
CEEEEECCCCCCCCE
34.3319608861
1790UbiquitinationNLFVVDRSDKLGRVQ
CEEEEECCCCCCCCE
34.3319608861
1830UbiquitinationSKMEIPPRRRPPPPL
HCCCCCCCCCCCCCC
41.7229967540
1830 (in isoform 3)Ubiquitination-41.72-
1838PhosphorylationRRPPPPLSSAGRKKE
CCCCCCCCCCCCCHH
24.7423898821
1839PhosphorylationRPPPPLSSAGRKKEQ
CCCCCCCCCCCCHHC
42.2823898821
1858AcetylationDSEEQQEKSIIATID
CCHHHHHHHHEEHHH
42.497675419
1859O-linked_GlycosylationSEEQQEKSIIATIDD
CHHHHHHHHEEHHHH
20.6220305658
1859PhosphorylationSEEQQEKSIIATIDD
CHHHHHHHHEEHHHH
20.6227732954
1863O-linked_GlycosylationQEKSIIATIDDVLSA
HHHHHEEHHHHHHHC
17.9620305658
1863PhosphorylationQEKSIIATIDDVLSA
HHHHHEEHHHHHHHC
17.9629449344
1869PhosphorylationATIDDVLSARPGALP
EHHHHHHHCCCCCCC
23.2925022875
1887PhosphorylationNPGPQTESSKFPFGI
CCCCCCCCCCCCCCH
42.06-
1898AcetylationPFGIQQAKSHRNIKL
CCCHHHHHHHCCCCC
42.3225953088
1904AcetylationAKSHRNIKLLEDEPR
HHHHCCCCCCCCCCC
51.0425953088
1904UbiquitinationAKSHRNIKLLEDEPR
HHHHCCCCCCCCCCC
51.0429967540
1912PhosphorylationLLEDEPRSRDETPLC
CCCCCCCCCCCCCCH
55.5923898821
1917UbiquitinationPRSRDETPLCTIAHW
CCCCCCCCCHHHHHH
24.3229967540
1941PhosphorylationCVSNIVRSLSFVPGN
HHHHHHHHHCCCCCC
19.92-
1943PhosphorylationSNIVRSLSFVPGNDA
HHHHHHHCCCCCCHH
25.99-
1953PhosphorylationPGNDAEMSKHPGLVL
CCCHHHHHCCHHHEE
21.22-
1957UbiquitinationAEMSKHPGLVLILGK
HHHHCCHHHEEHHHH
28.3029967540
2011PhosphorylationLEVLRDNTLVTLANI
HHHHCCCCEEEEEEC
27.22-
2028PhosphorylationQLDLSAYTESICLPI
CCCHHHHCHHHHHHH
23.99-
2064PhosphorylationVGPNSVLSPQRLVLE
CCCCCCCCHHHHHHH
19.4824719451
2072PhosphorylationPQRLVLETLCKLSIQ
HHHHHHHHHHHCCCC
33.04-
2097UbiquitinationPPFSRQEKFYATLVR
CCCCHHHHHHHHHHH
35.0223000965
2097 (in isoform 1)Ubiquitination-35.0221890473
2110UbiquitinationVRYVGDRKNPVCREM
HHHHCCCCCHHHHHH
71.0521890473
2110 (in isoform 2)Ubiquitination-71.0521890473
2117UbiquitinationKNPVCREMSMALLSN
CCHHHHHHHHHHHHH
1.3921890473
2118PhosphorylationNPVCREMSMALLSNL
CHHHHHHHHHHHHHH
8.9923612710
2124UbiquitinationMSMALLSNLAQGDAL
HHHHHHHHHHHHHHH
39.0921890473
2150UbiquitinationIGNLISFLEDGVTMA
HHHHHHHHHCCCCHH
4.7221890473
2150 (in isoform 3)Ubiquitination-4.7221890473
2167UbiquitinationQQSQHNLMHMQPPPL
HHHHHCCCCCCCCCC
2.7621890473
2177UbiquitinationQPPPLEPPSVDMMCR
CCCCCCCCCHHHHHH
37.2921890473
2187UbiquitinationDMMCRAAKALLAMAR
HHHHHHHHHHHHHHC
38.2823000965
2187 (in isoform 1)Ubiquitination-38.2821890473
2200PhosphorylationARVDENRSEFLLHEG
HCCCCCHHHHEEECC
44.2623403867
2200UbiquitinationARVDENRSEFLLHEG
HCCCCCHHHHEEECC
44.2621890473
2200 (in isoform 2)Ubiquitination-44.2621890473
2207UbiquitinationSEFLLHEGRLLDISI
HHHEEECCCHHHHHH
18.1321890473
2214UbiquitinationGRLLDISISAVLNSL
CCHHHHHHHHHHHHH
2.9121890473
2220UbiquitinationSISAVLNSLVASVIC
HHHHHHHHHHHHHHH
21.7621890473
2240UbiquitinationIGQL-----------
HCCC-----------
21890473
2240 (in isoform 3)Ubiquitination-21890473
2257Ubiquitination----------------------------
----------------------------
21890473
2267Ubiquitination--------------------------------------
--------------------------------------
21890473
2277Ubiquitination------------------------------------------------
------------------------------------------------
21890473
2310Ubiquitination---------------------------------------------------------------------------------
---------------------------------------------------------------------------------
21890473

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
-KUbiquitinationE3 ubiquitin ligaseARID1BQ8NFD5
PMID:20086098

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARI1B_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 ARI1B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMCA4_HUMANSMARCA4physical
11988099
SMCA2_HUMANSMARCA2physical
12200431
SMCA4_HUMANSMARCA4physical
12200431
CUL2_HUMANCUL2physical
20086098
SMRC2_HUMANSMARCC2physical
20086098
SMRC1_HUMANSMARCC1physical
20086098
SMCA4_HUMANSMARCA4physical
20086098
H2B2E_HUMANHIST2H2BEphysical
20086098
ELOC_HUMANTCEB1physical
20086098
RBX1_HUMANRBX1physical
20086098
ARI1A_HUMANARID1Aphysical
15170388
SMCA4_HUMANSMARCA4physical
15170388
SMCA1_HUMANSMARCA1physical
21118156
SMCA4_HUMANSMARCA4physical
21118156
SMRC2_HUMANSMARCC2physical
21118156
SMRC1_HUMANSMARCC1physical
21118156
SMRD1_HUMANSMARCD1physical
21118156
ANM5_HUMANPRMT5physical
21118156
SMCA2_HUMANSMARCA2physical
22939629
SMCA4_HUMANSMARCA4physical
22939629
SMRC1_HUMANSMARCC1physical
22939629
SNF5_HUMANSMARCB1physical
22939629
SMRC2_HUMANSMARCC2physical
22939629
SMRD1_HUMANSMARCD1physical
22939629
SMCE1_HUMANSMARCE1physical
22939629
ARI1A_HUMANARID1Aphysical
26344197
BCL7A_HUMANBCL7Aphysical
26344197
BCL7B_HUMANBCL7Bphysical
26344197
BCL7C_HUMANBCL7Cphysical
26344197
SMCA2_HUMANSMARCA2physical
26344197
SMCA4_HUMANSMARCA4physical
26344197
SMCE1_HUMANSMARCE1physical
26344197

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614562Mental retardation, autosomal dominant 12 (MRD12)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ARI1B_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, AND MASS SPECTROMETRY.
"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-1566 AND LYS-1777, 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 SER-516; SER-1555 ANDSER-1559, AND MASS SPECTROMETRY.
"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-1555, AND MASSSPECTROMETRY.

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