ARI1A_HUMAN - dbPTM
ARI1A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARI1A_HUMAN
UniProt AC O14497
Protein Name AT-rich interactive domain-containing protein 1A
Gene Name ARID1A
Organism Homo sapiens (Human).
Sequence Length 2285
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. Binds DNA non-specifically. 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)..
Protein Sequence MAAQVAPAAASSLGNPPPPPPSELKKAEQQQREEAGGEAAAAAAAERGEMKAAAGQESEGPAVGPPQPLGKELQDGAESNGGGGGGGAGSGGGPGAEPDLKNSNGNAGPRPALNNNLTEPPGGGGGGSSDGVGAPPHSAAAALPPPAYGFGQPYGRSPSAVAAAAAAVFHQQHGGQQSPGLAALQSGGGGGLEPYAGPQQNSHDHGFPNHQYNSYYPNRSAYPPPAPAYALSSPRGGTPGSGAAAAAGSKPPPSSSASASSSSSSFAQQRFGAMGGGGPSAAGGGTPQPTATPTLNQLLTSPSSARGYQGYPGGDYSGGPQDGGAGKGPADMASQCWGAAAAAAAAAAASGGAQQRSHHAPMSPGSSGGGGQPLARTPQPSSPMDQMGKMRPQPYGGTNPYSQQQGPPSGPQQGHGYPGQPYGSQTPQRYPMTMQGRAQSAMGGLSYTQQIPPYGQQGPSGYGQQGQTPYYNQQSPHPQQQQPPYSQQPPSQTPHAQPSYQQQPQSQPPQLQSSQPPYSQQPSQPPHQQSPAPYPSQQSTTQQHPQSQPPYSQPQAQSPYQQQQPQQPAPSTLSQQAAYPQPQSQQSQQTAYSQQRFPPPQELSQDSFGSQASSAPSMTSSKGGQEDMNLSLQSRPSSLPDLSGSIDDLPMGTEGALSPGVSTSGISSSQGEQSNPAQSPFSPHTSPHLPGIRGPSPSPVGSPASVAQSRSGPLSPAAVPGNQMPPRPPSGQSDSIMHPSMNQSSIAQDRGYMQRNPQMPQYSSPQPGSALSPRQPSGGQIHTGMGSYQQNSMGSYGPQGGQYGPQGGYPRQPNYNALPNANYPSAGMAGGINPMGAGGQMHGQPGIPPYGTLPPGRMSHASMGNRPYGPNMANMPPQVGSGMCPPPGGMNRKTQETAVAMHVAANSIQNRPPGYPNMNQGGMMGTGPPYGQGINSMAGMINPQGPPYSMGGTMANNSAGMAASPEMMGLGDVKLTPATKMNNKADGTPKTESKSKKSSSSTTTNEKITKLYELGGEPERKMWVDRYLAFTEEKAMGMTNLPAVGRKPLDLYRLYVSVKEIGGLTQVNKNKKWRELATNLNVGTSSSAASSLKKQYIQCLYAFECKIERGEDPPPDIFAAADSKKSQPKIQPPSPAGSGSMQGPQTPQSTSSSMAEGGDLKPPTPASTPHSQIPPLPGMSRSNSVGIQDAFNDGSDSTFQKRNSMTPNPGYQPSMNTSDMMGRMSYEPNKDPYGSMRKAPGSDPFMSSGQGPNGGMGDPYSRAAGPGLGNVAMGPRQHYPYGGPYDRVRTEPGIGPEGNMSTGAPQPNLMPSNPDSGMYSPSRYPPQQQQQQQQRHDSYGNQFSTQGTPSGSPFPSQQTTMYQQQQQNYKRPMDGTYGPPAKRHEGEMYSVPYSTGQGQPQQQQLPPAQPQPASQQQAAQPSPQQDVYNQYGNAYPATATAATERRPAGGPQNQFPFQFGRDRVSAPPGTNAQQNMPPQMMGGPIQASAEVAQQGTMWQGRNDMTYNYANRQSTGSAPQGPAYHGVNRTDEMLHTDQRANHEGSWPSHGTRQPPYGPSAPVPPMTRPPPSNYQPPPSMQNHIPQVSSPAPLPRPMENRTSPSKSPFLHSGMKMQKAGPPVPASHIAPAPVQPPMIRRDITFPPGSVEATQPVLKQRRRLTMKDIGTPEAWRVMMSLKSGLLAESTWALDTINILLYDDNSIMTFNLSQLPGLLELLVEYFRRCLIEIFGILKEYEVGDPGQRTLLDPGRFSKVSSPAPMEGGEEEEELLGPKLEEEEEEEVVENDEEIAFSGKDKPASENSEEKLISKFDKLPVKIVQKNDPFVVDCSDKLGRVQEFDSGLLHWRIGGGDTTEHIQTHFESKTELLPSRPHAPCPPAPRKHVTTAEGTPGTTDQEGPPPDGPPEKRITATMDDMLSTRSSTLTEDGAKSSEAIKESSKFPFGISPAQSHRNIKILEDEPHSKDETPLCTLLDWQDSLAKRCVCVSNTIRSLSFVPGNDFEMSKHPGLLLILGKLILLHHKHPERKQAPLTYEKEEEQDQGVSCNKVEWWWDCLEMLRENTLVTLANISGQLDLSPYPESICLPVLDGLLHWAVCPSAEAQDPFSTLGPNAVLSPQRLVLETLSKLSIQDNNVDLILATPPFSRLEKLYSTMVRFLSDRKNPVCREMAVVLLANLAQGDSLAARAIAVQKGSIGNLLGFLEDSLAATQFQQSQASLLHMQNPPFEPTSVDMMRRAARALLALAKVDENHSEFTLYESRLLDISVSPLMNSLVSQVICDVLFLIGQS
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------MAAQVAPAA
------CCCCCCHHH
20.2222814378
11PhosphorylationQVAPAAASSLGNPPP
CCCHHHHHHHCCCCC
22.75-
25AcetylationPPPPSELKKAEQQQR
CCCHHHHHHHHHHHH
45.9825953088
26UbiquitinationPPPSELKKAEQQQRE
CCHHHHHHHHHHHHH
70.5424816145
51AcetylationAAERGEMKAAAGQES
HHHHCHHHHHCCCCC
30.4825953088
58O-linked_GlycosylationKAAAGQESEGPAVGP
HHHCCCCCCCCCCCC
39.7130059200
58PhosphorylationKAAAGQESEGPAVGP
HHHCCCCCCCCCCCC
39.7130624053
71AcetylationGPPQPLGKELQDGAE
CCCCCCCHHHCCCCC
64.0323749302
79PhosphorylationELQDGAESNGGGGGG
HHCCCCCCCCCCCCC
39.9925159151
90PhosphorylationGGGGGAGSGGGPGAE
CCCCCCCCCCCCCCC
33.4625262027
128O-linked_GlycosylationPGGGGGGSSDGVGAP
CCCCCCCCCCCCCCC
28.6530059200
157PhosphorylationFGQPYGRSPSAVAAA
CCCCCCCCHHHHHHH
20.8826074081
159PhosphorylationQPYGRSPSAVAAAAA
CCCCCCHHHHHHHHH
36.3026074081
220PhosphorylationNSYYPNRSAYPPPAP
CCCCCCCCCCCCCCC
38.5023403867
222PhosphorylationYYPNRSAYPPPAPAY
CCCCCCCCCCCCCCC
19.9523403867
229PhosphorylationYPPPAPAYALSSPRG
CCCCCCCCCCCCCCC
13.6623898821
232PhosphorylationPAPAYALSSPRGGTP
CCCCCCCCCCCCCCC
30.0823898821
233PhosphorylationAPAYALSSPRGGTPG
CCCCCCCCCCCCCCC
21.3321712546
233 (in isoform 2)Phosphorylation-21.33-
235MethylationAYALSSPRGGTPGSG
CCCCCCCCCCCCCCC
59.11-
238O-linked_GlycosylationLSSPRGGTPGSGAAA
CCCCCCCCCCCCHHH
27.5730059200
238PhosphorylationLSSPRGGTPGSGAAA
CCCCCCCCCCCCHHH
27.5726074081
241PhosphorylationPRGGTPGSGAAAAAG
CCCCCCCCCHHHHCC
26.8526074081
249O-linked_GlycosylationGAAAAAGSKPPPSSS
CHHHHCCCCCCCCCC
36.9430059200
249PhosphorylationGAAAAAGSKPPPSSS
CHHHHCCCCCCCCCC
36.9421082442
250AcetylationAAAAAGSKPPPSSSA
HHHHCCCCCCCCCCC
61.7025953088
254O-linked_GlycosylationAGSKPPPSSSASASS
CCCCCCCCCCCCCCC
42.5730059200
255O-linked_GlycosylationGSKPPPSSSASASSS
CCCCCCCCCCCCCCC
35.3830059200
256O-linked_GlycosylationSKPPPSSSASASSSS
CCCCCCCCCCCCCCC
30.4930059200
258O-linked_GlycosylationPPPSSSASASSSSSS
CCCCCCCCCCCCCCH
30.5430059200
260O-linked_GlycosylationPSSSASASSSSSSFA
CCCCCCCCCCCCHHH
28.4030059200
261O-linked_GlycosylationSSSASASSSSSSFAQ
CCCCCCCCCCCHHHH
33.6830059200
264O-linked_GlycosylationASASSSSSSFAQQRF
CCCCCCCCHHHHHHH
31.2730059200
265O-linked_GlycosylationSASSSSSSFAQQRFG
CCCCCCCHHHHHHHC
26.9230059200
280PhosphorylationAMGGGGPSAAGGGTP
CCCCCCCCCCCCCCC
33.7429496963
286PhosphorylationPSAAGGGTPQPTATP
CCCCCCCCCCCCCCC
23.2521712546
286 (in isoform 2)Phosphorylation-23.25-
290PhosphorylationGGGTPQPTATPTLNQ
CCCCCCCCCCCCHHH
37.6119690332
292PhosphorylationGTPQPTATPTLNQLL
CCCCCCCCCCHHHHH
21.2022199227
294PhosphorylationPQPTATPTLNQLLTS
CCCCCCCCHHHHHCC
33.7022199227
300PhosphorylationPTLNQLLTSPSSARG
CCHHHHHCCCCCCCC
47.3825850435
301PhosphorylationTLNQLLTSPSSARGY
CHHHHHCCCCCCCCC
23.8221712546
301 (in isoform 2)Phosphorylation-23.82-
303PhosphorylationNQLLTSPSSARGYQG
HHHHCCCCCCCCCCC
36.0822199227
304PhosphorylationQLLTSPSSARGYQGY
HHHCCCCCCCCCCCC
25.9329496963
316PhosphorylationQGYPGGDYSGGPQDG
CCCCCCCCCCCCCCC
16.70-
317PhosphorylationGYPGGDYSGGPQDGG
CCCCCCCCCCCCCCC
41.8521815630
350PhosphorylationAAAAAAASGGAQQRS
HHHHHHHCCCCCCCC
32.7926074081
357PhosphorylationSGGAQQRSHHAPMSP
CCCCCCCCCCCCCCC
18.4523927012
363PhosphorylationRSHHAPMSPGSSGGG
CCCCCCCCCCCCCCC
25.6729255136
363 (in isoform 2)Phosphorylation-25.67-
366PhosphorylationHAPMSPGSSGGGGQP
CCCCCCCCCCCCCCC
29.2430266825
367PhosphorylationAPMSPGSSGGGGQPL
CCCCCCCCCCCCCCC
47.5823927012
367 (in isoform 2)Phosphorylation-47.58-
376MethylationGGGQPLARTPQPSSP
CCCCCCCCCCCCCCC
55.40-
377PhosphorylationGGQPLARTPQPSSPM
CCCCCCCCCCCCCCH
22.2223401153
381PhosphorylationLARTPQPSSPMDQMG
CCCCCCCCCCHHHCC
41.6530266825
382PhosphorylationARTPQPSSPMDQMGK
CCCCCCCCCHHHCCC
30.8123927012
382 (in isoform 2)Phosphorylation-30.81-
384SulfoxidationTPQPSSPMDQMGKMR
CCCCCCCHHHCCCCC
6.3721406390
389MethylationSPMDQMGKMRPQPYG
CCHHHCCCCCCCCCC
26.79-
391DimethylationMDQMGKMRPQPYGGT
HHHCCCCCCCCCCCC
30.13-
391MethylationMDQMGKMRPQPYGGT
HHHCCCCCCCCCCCC
30.13-
429Asymmetric dimethylarginineYGSQTPQRYPMTMQG
CCCCCCCCCCCCCCC
38.43-
429MethylationYGSQTPQRYPMTMQG
CCCCCCCCCCCCCCC
38.4324129315
592PhosphorylationQQSQQTAYSQQRFPP
HHHHHHHHHHHCCCC
15.48-
604PhosphorylationFPPPQELSQDSFGSQ
CCCCHHHCCCCCCCC
31.0517525332
604 (in isoform 2)Phosphorylation-31.05-
607PhosphorylationPQELSQDSFGSQASS
CHHHCCCCCCCCCCC
24.7030266825
610PhosphorylationLSQDSFGSQASSAPS
HCCCCCCCCCCCCCC
22.1430266825
613PhosphorylationDSFGSQASSAPSMTS
CCCCCCCCCCCCCCC
21.2830266825
614PhosphorylationSFGSQASSAPSMTSS
CCCCCCCCCCCCCCC
47.4130266825
628SulfoxidationSKGGQEDMNLSLQSR
CCCCCCCCCEEHHCC
5.5221406390
631PhosphorylationGQEDMNLSLQSRPSS
CCCCCCEEHHCCCCC
21.2529255136
634PhosphorylationDMNLSLQSRPSSLPD
CCCEEHHCCCCCCCC
51.9929255136
637PhosphorylationLSLQSRPSSLPDLSG
EEHHCCCCCCCCCCC
43.3126074081
638PhosphorylationSLQSRPSSLPDLSGS
EHHCCCCCCCCCCCC
46.7526074081
653PhosphorylationIDDLPMGTEGALSPG
CCCCCCCCCCCCCCC
25.6228348404
658PhosphorylationMGTEGALSPGVSTSG
CCCCCCCCCCCCCCC
21.0528348404
662PhosphorylationGALSPGVSTSGISSS
CCCCCCCCCCCCCCC
23.8328348404
663PhosphorylationALSPGVSTSGISSSQ
CCCCCCCCCCCCCCC
28.6829496963
682PhosphorylationNPAQSPFSPHTSPHL
CCCCCCCCCCCCCCC
21.1125921289
685PhosphorylationQSPFSPHTSPHLPGI
CCCCCCCCCCCCCCC
47.5425921289
696PhosphorylationLPGIRGPSPSPVGSP
CCCCCCCCCCCCCCH
40.6129255136
696 (in isoform 2)Phosphorylation-40.61-
698PhosphorylationGIRGPSPSPVGSPAS
CCCCCCCCCCCCHHH
36.2329255136
698 (in isoform 2)Phosphorylation-36.23-
702PhosphorylationPSPSPVGSPASVAQS
CCCCCCCCHHHHHCC
19.9529255136
702 (in isoform 2)Phosphorylation-19.95-
705PhosphorylationSPVGSPASVAQSRSG
CCCCCHHHHHCCCCC
22.7530266825
709PhosphorylationSPASVAQSRSGPLSP
CHHHHHCCCCCCCCC
20.7622167270
711O-linked_GlycosylationASVAQSRSGPLSPAA
HHHHCCCCCCCCCCC
50.4330059200
711PhosphorylationASVAQSRSGPLSPAA
HHHHCCCCCCCCCCC
50.4330108239
715PhosphorylationQSRSGPLSPAAVPGN
CCCCCCCCCCCCCCC
18.6723401153
727MethylationPGNQMPPRPPSGQSD
CCCCCCCCCCCCCCC
50.30-
730PhosphorylationQMPPRPPSGQSDSIM
CCCCCCCCCCCCCCC
52.7423401153
733PhosphorylationPRPPSGQSDSIMHPS
CCCCCCCCCCCCCCC
36.5330108239
735PhosphorylationPPSGQSDSIMHPSMN
CCCCCCCCCCCCCCC
27.3628464451
740PhosphorylationSDSIMHPSMNQSSIA
CCCCCCCCCCHHHHH
18.7130108239
744PhosphorylationMHPSMNQSSIAQDRG
CCCCCCHHHHHHHCC
20.7830108239
745PhosphorylationHPSMNQSSIAQDRGY
CCCCCHHHHHHHCCH
16.5130108239
750MethylationQSSIAQDRGYMQRNP
HHHHHHHCCHHHCCC
26.51-
755DimethylationQDRGYMQRNPQMPQY
HHCCHHHCCCCCCCC
40.02-
755MethylationQDRGYMQRNPQMPQY
HHCCHHHCCCCCCCC
40.02-
762PhosphorylationRNPQMPQYSSPQPGS
CCCCCCCCCCCCCCC
12.7823927012
763PhosphorylationNPQMPQYSSPQPGSA
CCCCCCCCCCCCCCC
30.2330266825
764PhosphorylationPQMPQYSSPQPGSAL
CCCCCCCCCCCCCCC
23.7130266825
764 (in isoform 2)Phosphorylation-23.71-
769PhosphorylationYSSPQPGSALSPRQP
CCCCCCCCCCCCCCC
32.4929255136
772PhosphorylationPQPGSALSPRQPSGG
CCCCCCCCCCCCCCC
20.1129255136
772 (in isoform 2)Phosphorylation-20.11-
774MethylationPGSALSPRQPSGGQI
CCCCCCCCCCCCCCC
58.63-
777PhosphorylationALSPRQPSGGQIHTG
CCCCCCCCCCCCCCC
47.4126074081
783PhosphorylationPSGGQIHTGMGSYQQ
CCCCCCCCCCCCCCC
30.4126074081
787PhosphorylationQIHTGMGSYQQNSMG
CCCCCCCCCCCCCCC
15.7526074081
788PhosphorylationIHTGMGSYQQNSMGS
CCCCCCCCCCCCCCC
14.3726074081
811MethylationGPQGGYPRQPNYNAL
CCCCCCCCCCCCCCC
56.98-
958PhosphorylationGGTMANNSAGMAASP
CCCCCCCCCCCCCCH
26.4626074081
964PhosphorylationNSAGMAASPEMMGLG
CCCCCCCCHHHHCCC
16.3226074081
976PhosphorylationGLGDVKLTPATKMNN
CCCCCCCCCCCCCCC
12.7426074081
979PhosphorylationDVKLTPATKMNNKAD
CCCCCCCCCCCCCCC
31.8426074081
980AcetylationVKLTPATKMNNKADG
CCCCCCCCCCCCCCC
41.5625953088
988PhosphorylationMNNKADGTPKTESKS
CCCCCCCCCCCCCCC
23.3526074081
991PhosphorylationKADGTPKTESKSKKS
CCCCCCCCCCCCCCC
46.8526074081
997AcetylationKTESKSKKSSSSTTT
CCCCCCCCCCCCCCC
63.76129971
1007AcetylationSSTTTNEKITKLYEL
CCCCCHHHHHHHHHC
58.7225953088
1010UbiquitinationTTNEKITKLYELGGE
CCHHHHHHHHHCCCC
53.1729967540
1012PhosphorylationNEKITKLYELGGEPE
HHHHHHHHHCCCCHH
15.6327642862
1055PhosphorylationPLDLYRLYVSVKEIG
CCHHHEEEEEHHHHC
5.0225367160
1057PhosphorylationDLYRLYVSVKEIGGL
HHHEEEEEHHHHCCC
17.5725367160
1065PhosphorylationVKEIGGLTQVNKNKK
HHHHCCCEECCCCHH
33.4721406692
1069AcetylationGGLTQVNKNKKWREL
CCCEECCCCHHHHHH
71.8825953088
1069UbiquitinationGGLTQVNKNKKWREL
CCCEECCCCHHHHHH
71.8832142685
1078PhosphorylationKKWRELATNLNVGTS
HHHHHHHHHCCCCCC
53.5220068231
1084PhosphorylationATNLNVGTSSSAASS
HHHCCCCCCHHHHHH
22.5828787133
1085PhosphorylationTNLNVGTSSSAASSL
HHCCCCCCHHHHHHH
19.1620068231
1086PhosphorylationNLNVGTSSSAASSLK
HCCCCCCHHHHHHHH
24.6720068231
1087PhosphorylationLNVGTSSSAASSLKK
CCCCCCHHHHHHHHH
27.8520068231
1087 (in isoform 2)Phosphorylation-27.85-
1090O-linked_GlycosylationGTSSSAASSLKKQYI
CCCHHHHHHHHHHHH
35.6030059200
1090PhosphorylationGTSSSAASSLKKQYI
CCCHHHHHHHHHHHH
35.6020068231
1091O-linked_GlycosylationTSSSAASSLKKQYIQ
CCHHHHHHHHHHHHH
39.2130059200
1091PhosphorylationTSSSAASSLKKQYIQ
CCHHHHHHHHHHHHH
39.2120068231
1123PhosphorylationDIFAAADSKKSQPKI
CCEEECCCCCCCCCC
36.9426074081
1126PhosphorylationAAADSKKSQPKIQPP
EECCCCCCCCCCCCC
56.2926074081
1134PhosphorylationQPKIQPPSPAGSGSM
CCCCCCCCCCCCCCC
33.7826074081
1138PhosphorylationQPPSPAGSGSMQGPQ
CCCCCCCCCCCCCCC
29.7826074081
1140PhosphorylationPSPAGSGSMQGPQTP
CCCCCCCCCCCCCCC
15.0526074081
1146PhosphorylationGSMQGPQTPQSTSSS
CCCCCCCCCCCCCCC
26.8226074081
1149PhosphorylationQGPQTPQSTSSSMAE
CCCCCCCCCCCCCCC
31.3126074081
1150PhosphorylationGPQTPQSTSSSMAEG
CCCCCCCCCCCCCCC
27.6426074081
1151PhosphorylationPQTPQSTSSSMAEGG
CCCCCCCCCCCCCCC
26.1826074081
1152PhosphorylationQTPQSTSSSMAEGGD
CCCCCCCCCCCCCCC
24.9926074081
1153PhosphorylationTPQSTSSSMAEGGDL
CCCCCCCCCCCCCCC
23.0626074081
1164PhosphorylationGGDLKPPTPASTPHS
CCCCCCCCCCCCCHH
39.7626074081
1167PhosphorylationLKPPTPASTPHSQIP
CCCCCCCCCCHHCCC
43.6126074081
1168PhosphorylationKPPTPASTPHSQIPP
CCCCCCCCCHHCCCC
27.4226074081
1171PhosphorylationTPASTPHSQIPPLPG
CCCCCCHHCCCCCCC
30.8926074081
1180PhosphorylationIPPLPGMSRSNSVGI
CCCCCCCCCCCCCCC
38.1726074081
1182PhosphorylationPLPGMSRSNSVGIQD
CCCCCCCCCCCCCHH
26.5929255136
1182 (in isoform 2)Phosphorylation-26.59-
1184PhosphorylationPGMSRSNSVGIQDAF
CCCCCCCCCCCHHHC
23.9829255136
1184 (in isoform 2)Phosphorylation-23.98-
1195PhosphorylationQDAFNDGSDSTFQKR
HHHCCCCCCCCCCCC
31.1130266825
1197PhosphorylationAFNDGSDSTFQKRNS
HCCCCCCCCCCCCCC
32.5830266825
1198PhosphorylationFNDGSDSTFQKRNSM
CCCCCCCCCCCCCCC
34.7730266825
1201UbiquitinationGSDSTFQKRNSMTPN
CCCCCCCCCCCCCCC
49.7232015554
1204PhosphorylationSTFQKRNSMTPNPGY
CCCCCCCCCCCCCCC
28.2423401153
1206PhosphorylationFQKRNSMTPNPGYQP
CCCCCCCCCCCCCCC
21.5323401153
1211PhosphorylationSMTPNPGYQPSMNTS
CCCCCCCCCCCCCHH
20.6428450419
1214PhosphorylationPNPGYQPSMNTSDMM
CCCCCCCCCCHHHHC
14.7828450419
1217PhosphorylationGYQPSMNTSDMMGRM
CCCCCCCHHHHCCCC
19.9129978859
1218PhosphorylationYQPSMNTSDMMGRMS
CCCCCCHHHHCCCCC
20.6426074081
1223MethylationNTSDMMGRMSYEPNK
CHHHHCCCCCCCCCC
7.93-
1225PhosphorylationSDMMGRMSYEPNKDP
HHHCCCCCCCCCCCC
25.6129396449
1226PhosphorylationDMMGRMSYEPNKDPY
HHCCCCCCCCCCCCC
26.5129214152
1230AcetylationRMSYEPNKDPYGSMR
CCCCCCCCCCCCCCC
71.4523236377
1230UbiquitinationRMSYEPNKDPYGSMR
CCCCCCCCCCCCCCC
71.4524816145
1233PhosphorylationYEPNKDPYGSMRKAP
CCCCCCCCCCCCCCC
31.7823322592
1235O-linked_GlycosylationPNKDPYGSMRKAPGS
CCCCCCCCCCCCCCC
15.0130059200
1235PhosphorylationPNKDPYGSMRKAPGS
CCCCCCCCCCCCCCC
15.0123401153
1237MethylationKDPYGSMRKAPGSDP
CCCCCCCCCCCCCCC
33.41-
1242O-linked_GlycosylationSMRKAPGSDPFMSSG
CCCCCCCCCCCCCCC
40.8430059200
1273SulfoxidationPGLGNVAMGPRQHYP
CCCCCCCCCCCCCCC
7.0821406390
1276DimethylationGNVAMGPRQHYPYGG
CCCCCCCCCCCCCCC
30.13-
1276MethylationGNVAMGPRQHYPYGG
CCCCCCCCCCCCCCC
30.1324129315
1279 (in isoform 3)Ubiquitination-6.9821890473
1287MethylationPYGGPYDRVRTEPGI
CCCCCCCCCCCCCCC
17.61-
1301PhosphorylationIGPEGNMSTGAPQPN
CCCCCCCCCCCCCCC
27.9128111955
1302PhosphorylationGPEGNMSTGAPQPNL
CCCCCCCCCCCCCCC
26.9628111955
1312PhosphorylationPQPNLMPSNPDSGMY
CCCCCCCCCCCCCCC
47.2126074081
1316PhosphorylationLMPSNPDSGMYSPSR
CCCCCCCCCCCCCCC
27.0730108239
1319PhosphorylationSNPDSGMYSPSRYPP
CCCCCCCCCCCCCCH
22.4330108239
1320PhosphorylationNPDSGMYSPSRYPPQ
CCCCCCCCCCCCCHH
13.9130108239
1322PhosphorylationDSGMYSPSRYPPQQQ
CCCCCCCCCCCHHHH
38.2130108239
1324PhosphorylationGMYSPSRYPPQQQQQ
CCCCCCCCCHHHHHH
24.4926074081
1338PhosphorylationQQQQRHDSYGNQFST
HHHHHHHHCCCCCCC
28.9026074081
1339PhosphorylationQQQRHDSYGNQFSTQ
HHHHHHHCCCCCCCC
26.5926074081
1344PhosphorylationDSYGNQFSTQGTPSG
HHCCCCCCCCCCCCC
15.2826074081
1345PhosphorylationSYGNQFSTQGTPSGS
HCCCCCCCCCCCCCC
32.1026074081
1348PhosphorylationNQFSTQGTPSGSPFP
CCCCCCCCCCCCCCC
12.4026074081
1350PhosphorylationFSTQGTPSGSPFPSQ
CCCCCCCCCCCCCCH
52.3030576142
1352PhosphorylationTQGTPSGSPFPSQQT
CCCCCCCCCCCCHHH
27.9230576142
1356PhosphorylationPSGSPFPSQQTTMYQ
CCCCCCCCHHHHHHH
34.9926074081
1359PhosphorylationSPFPSQQTTMYQQQQ
CCCCCHHHHHHHHHH
13.0926074081
1360PhosphorylationPFPSQQTTMYQQQQQ
CCCCHHHHHHHHHHH
15.0026074081
1362PhosphorylationPSQQTTMYQQQQQNY
CCHHHHHHHHHHHHC
10.9027080861
1369PhosphorylationYQQQQQNYKRPMDGT
HHHHHHHCCCCCCCC
12.2026074081
1376PhosphorylationYKRPMDGTYGPPAKR
CCCCCCCCCCCCCCC
22.50-
1377PhosphorylationKRPMDGTYGPPAKRH
CCCCCCCCCCCCCCC
32.91-
1382AcetylationGTYGPPAKRHEGEMY
CCCCCCCCCCCCEEE
61.1225953088
1387PhosphorylationPAKRHEGEMYSVPYS
CCCCCCCEEEECCCC
31.7832142685
1395AcetylationMYSVPYSTGQGQPQQ
EEECCCCCCCCCCCC
27.9019608861
1395 (in isoform 2)Acetylation-27.90-
1445UbiquitinationTATAATERRPAGGPQ
CCCCCCCCCCCCCCC
45.5921890473
1445 (in isoform 2)Ubiquitination-45.5921890473
1465PhosphorylationQFGRDRVSAPPGTNA
CCCCCCCCCCCCCCC
35.6323532336
1505PhosphorylationWQGRNDMTYNYANRQ
CCCCCCCCCEECCCC
16.1024732914
1506PhosphorylationQGRNDMTYNYANRQS
CCCCCCCCEECCCCC
10.2724732914
1508PhosphorylationRNDMTYNYANRQSTG
CCCCCCEECCCCCCC
8.5424732914
1511MethylationMTYNYANRQSTGSAP
CCCEECCCCCCCCCC
24.53-
1513PhosphorylationYNYANRQSTGSAPQG
CEECCCCCCCCCCCC
31.3424732914
1514PhosphorylationNYANRQSTGSAPQGP
EECCCCCCCCCCCCC
27.1524732914
1516PhosphorylationANRQSTGSAPQGPAY
CCCCCCCCCCCCCCC
36.5429496963
1523PhosphorylationSAPQGPAYHGVNRTD
CCCCCCCCCCCCCHH
11.4022461510
1534 (in isoform 2)Phosphorylation-26.53-
1537 (in isoform 2)Phosphorylation-47.76-
1538PhosphorylationEMLHTDQRANHEGSW
HCCCCCCCCCCCCCC
39.9232142685
1538 (in isoform 2)Phosphorylation-39.92-
1544PhosphorylationQRANHEGSWPSHGTR
CCCCCCCCCCCCCCC
32.5926714015
1586PhosphorylationQNHIPQVSSPAPLPR
HCCCCCCCCCCCCCC
25.9222210691
1587PhosphorylationNHIPQVSSPAPLPRP
CCCCCCCCCCCCCCC
26.6526074081
1598UbiquitinationLPRPMENRTSPSKSP
CCCCCCCCCCCCCCC
24.2329967540
1599PhosphorylationPRPMENRTSPSKSPF
CCCCCCCCCCCCCCC
57.4823401153
1600PhosphorylationRPMENRTSPSKSPFL
CCCCCCCCCCCCCCH
24.7623401153
1602PhosphorylationMENRTSPSKSPFLHS
CCCCCCCCCCCCHHC
45.6023401153
1603AcetylationENRTSPSKSPFLHSG
CCCCCCCCCCCHHCC
66.5825953088
1604PhosphorylationNRTSPSKSPFLHSGM
CCCCCCCCCCHHCCC
25.8123401153
1609PhosphorylationSKSPFLHSGMKMQKA
CCCCCHHCCCCCCCC
42.6125159151
1612AcetylationPFLHSGMKMQKAGPP
CCHHCCCCCCCCCCC
41.5319608861
1613UbiquitinationFLHSGMKMQKAGPPV
CHHCCCCCCCCCCCC
3.5229967540
1640PhosphorylationPMIRRDITFPPGSVE
CCEECCCCCCCCCCC
34.0920068231
1660PhosphorylationLKQRRRLTMKDIGTP
HHHCCCCCHHHCCCH
21.9924719451
1662AcetylationQRRRLTMKDIGTPEA
HCCCCCHHHCCCHHH
40.7423749302
1662UbiquitinationQRRRLTMKDIGTPEA
HCCCCCHHHCCCHHH
40.7421890473
1662 (in isoform 1)Ubiquitination-40.7421890473
1663UbiquitinationRRRLTMKDIGTPEAW
CCCCCHHHCCCHHHH
33.4529967540
1666PhosphorylationLTMKDIGTPEAWRVM
CCHHHCCCHHHHHHH
20.4926714015
1688AcetylationLAESTWALDTINILL
HHCCCEECCCEEEEE
4.5019608861
1688 (in isoform 2)Acetylation-4.50-
1717UbiquitinationPGLLELLVEYFRRCL
CCHHHHHHHHHHHHH
9.7833845483
1721UbiquitinationELLVEYFRRCLIEIF
HHHHHHHHHHHHHHH
27.7429967540
1727PhosphorylationFRRCLIEIFGILKEY
HHHHHHHHHHHHHHC
2.8032142685
1727 (in isoform 2)Phosphorylation-2.80-
1736UbiquitinationGILKEYEVGDPGQRT
HHHHHCCCCCCCCCC
11.7429967540
1743PhosphorylationVGDPGQRTLLDPGRF
CCCCCCCCCCCCCCC
24.6428122231
1745UbiquitinationDPGQRTLLDPGRFSK
CCCCCCCCCCCCCCC
8.0529967540
1751PhosphorylationLLDPGRFSKVSSPAP
CCCCCCCCCCCCCCC
30.6825159151
1754PhosphorylationPGRFSKVSSPAPMEG
CCCCCCCCCCCCCCC
34.0529255136
1755PhosphorylationGRFSKVSSPAPMEGG
CCCCCCCCCCCCCCC
28.2429255136
1762UbiquitinationSPAPMEGGEEEEELL
CCCCCCCCHHHHHHH
26.3229967540
1763 (in isoform 3)Ubiquitination-73.4321890473
1803UbiquitinationPASENSEEKLISKFD
CCCCCCHHHHHHHHH
53.6429967540
1808AcetylationSEEKLISKFDKLPVK
CHHHHHHHHHCCCEE
51.0623749302
1808UbiquitinationSEEKLISKFDKLPVK
CHHHHHHHHHCCCEE
51.0629967540
1811AcetylationKLISKFDKLPVKIVQ
HHHHHHHCCCEEEEE
58.8025953088
1815AcetylationKFDKLPVKIVQKNDP
HHHCCCEEEEECCCC
34.9125953088
1815UbiquitinationKFDKLPVKIVQKNDP
HHHCCCEEEEECCCC
34.9129967540
1819AcetylationLPVKIVQKNDPFVVD
CCEEEEECCCCEEEE
53.0425953088
1830AcetylationFVVDCSDKLGRVQEF
EEEECCCCCCCEEEE
36.2323749302
1830UbiquitinationFVVDCSDKLGRVQEF
EEEECCCCCCCEEEE
36.2329967540
1868PhosphorylationSKTELLPSRPHAPCP
CCCCCCCCCCCCCCC
59.4125278378
1880AcetylationPCPPAPRKHVTTAEG
CCCCCCCCCCCCCCC
41.1726210075
1880UbiquitinationPCPPAPRKHVTTAEG
CCCCCCCCCCCCCCC
41.1729967540
1883PhosphorylationPAPRKHVTTAEGTPG
CCCCCCCCCCCCCCC
21.7328122231
1884PhosphorylationAPRKHVTTAEGTPGT
CCCCCCCCCCCCCCC
22.9429255136
1888O-linked_GlycosylationHVTTAEGTPGTTDQE
CCCCCCCCCCCCCCC
15.2830059200
1888PhosphorylationHVTTAEGTPGTTDQE
CCCCCCCCCCCCCCC
15.2823401153
1891PhosphorylationTAEGTPGTTDQEGPP
CCCCCCCCCCCCCCC
28.5329255136
1892PhosphorylationAEGTPGTTDQEGPPP
CCCCCCCCCCCCCCC
41.4228348404
1905AcetylationPPDGPPEKRITATMD
CCCCCCHHHEEEEHH
55.6719608861
1911SulfoxidationEKRITATMDDMLSTR
HHHEEEEHHHHHHCC
3.6921406390
1916PhosphorylationATMDDMLSTRSSTLT
EEHHHHHHCCCCCCC
18.3524719451
1917PhosphorylationTMDDMLSTRSSTLTE
EHHHHHHCCCCCCCC
30.5222817900
1920PhosphorylationDMLSTRSSTLTEDGA
HHHHCCCCCCCCCCC
24.93-
1921PhosphorylationMLSTRSSTLTEDGAK
HHHCCCCCCCCCCCC
38.6624719451
1923PhosphorylationSTRSSTLTEDGAKSS
HCCCCCCCCCCCCCH
31.92-
1928AcetylationTLTEDGAKSSEAIKE
CCCCCCCCCHHHHHH
61.1126051181
1929PhosphorylationLTEDGAKSSEAIKES
CCCCCCCCHHHHHHH
32.6428450419
1929UbiquitinationLTEDGAKSSEAIKES
CCCCCCCCHHHHHHH
32.6421890473
1929 (in isoform 2)Ubiquitination-32.6421890473
1930PhosphorylationTEDGAKSSEAIKESS
CCCCCCCHHHHHHHC
30.2723186163
1934UbiquitinationAKSSEAIKESSKFPF
CCCHHHHHHHCCCCC
59.6033845483
1936PhosphorylationSSEAIKESSKFPFGI
CHHHHHHHCCCCCCC
33.5523403867
1937PhosphorylationSEAIKESSKFPFGIS
HHHHHHHCCCCCCCC
39.1323403867
1938AcetylationEAIKESSKFPFGISP
HHHHHHCCCCCCCCH
67.3525953088
1938UbiquitinationEAIKESSKFPFGISP
HHHHHHCCCCCCCCH
67.3529967540
1944PhosphorylationSKFPFGISPAQSHRN
CCCCCCCCHHHHHCC
17.9825159151
1948PhosphorylationFGISPAQSHRNIKIL
CCCCHHHHHCCEEEE
26.9030266825
1953AcetylationAQSHRNIKILEDEPH
HHHHCCEEEECCCCC
44.8025953088
1953UbiquitinationAQSHRNIKILEDEPH
HHHHCCEEEECCCCC
44.8029967540
1962UbiquitinationLEDEPHSKDETPLCT
ECCCCCCCCCCCCHH
57.4629967540
1979UbiquitinationDWQDSLAKRCVCVSN
HHHHHHHHHHEEECC
52.1829967540
1990PhosphorylationCVSNTIRSLSFVPGN
EECCCHHHHCCCCCC
25.2329083192
1992PhosphorylationSNTIRSLSFVPGNDF
CCCHHHHCCCCCCCC
25.9929083192
2001SulfoxidationVPGNDFEMSKHPGLL
CCCCCCCCCCCHHHH
6.9821406390
2002PhosphorylationPGNDFEMSKHPGLLL
CCCCCCCCCCHHHHH
22.1829083192
2020AcetylationKLILLHHKHPERKQA
HHHHHHCCCCCCCCC
50.5425953088
2020UbiquitinationKLILLHHKHPERKQA
HHHHHHCCCCCCCCC
50.5429967540
2025UbiquitinationHHKHPERKQAPLTYE
HCCCCCCCCCCCCCC
49.5029967540
2030PhosphorylationERKQAPLTYEKEEEQ
CCCCCCCCCCCHHHH
28.6828978645
2113PhosphorylationLGPNAVLSPQRLVLE
CCCCCCCCHHHHHHH
16.6424719451
2146AcetylationPPFSRLEKLYSTMVR
CCHHHHHHHHHHHHH
58.2725953088
2146UbiquitinationPPFSRLEKLYSTMVR
CCHHHHHHHHHHHHH
58.2722817900
2146 (in isoform 1)Ubiquitination-58.2721890473
2262O-linked_GlycosylationESRLLDISVSPLMNS
EHHHHCCCHHHHHHH
19.0630059200

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
363SPhosphorylationKinaseCDK2P24941
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARI1A_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 ARI1A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PB1_HUMANPBRM1physical
19650111
SMRC2_HUMANSMARCC2physical
19650111
SMRC1_HUMANSMARCC1physical
19650111
CUL2_HUMANCUL2physical
20086098
SMCA4_HUMANSMARCA4physical
15170388
RARA_HUMANRARAphysical
17363140
SMCA4_HUMANSMARCA4physical
22939629
SMCA2_HUMANSMARCA2physical
22939629
SMRC2_HUMANSMARCC2physical
22939629
SMCE1_HUMANSMARCE1physical
22939629
SMRC1_HUMANSMARCC1physical
22939629
SNF5_HUMANSMARCB1physical
22939629
SMRD1_HUMANSMARCD1physical
22939629
ARI1B_HUMANARID1Bphysical
22939629
SMRD2_HUMANSMARCD2physical
22939629
SMRD3_HUMANSMARCD3physical
22939629
PHF10_HUMANPHF10physical
22939629
SMCA2_HUMANSMARCA2physical
26344197
SMCA4_HUMANSMARCA4physical
26344197
ESR1_HUMANESR1physical
17363140
NCOA1_HUMANNCOA1physical
17363140
RARB_HUMANRARBphysical
17363140
RARG_HUMANRARGphysical
17363140
CUL1_HUMANCUL1physical
26400522
SKP1_HUMANSKP1physical
26400522
TOP1_HUMANTOP1genetic
28319113
CHK1_HUMANCHEK1genetic
28319113
VHL_HUMANVHLgenetic
28319113

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614607Mental retardation, autosomal dominant 14 (MRD14)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ARI1A_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-363; SER-696; SER-702; SER-764; SER-772 ANDSER-1755, 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-1612 AND LYS-1905, 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 THR-286; SER-696; SER-698;SER-764; SER-772 AND SER-1944, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-696 AND SER-772, ANDMASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-696, AND MASSSPECTROMETRY.
"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-604, 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-363 AND SER-1755, ANDMASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-696; SER-772 ANDSER-1755, 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-79; SER-233; THR-286;SER-363; SER-382; SER-604; SER-696; SER-698; SER-702; SER-764; SER-772AND SER-1184, 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 SER-363; SER-696; SER-702; SER-764; SER-772 ANDSER-1755, AND MASS SPECTROMETRY.

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