SMCA4_HUMAN - dbPTM
SMCA4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMCA4_HUMAN
UniProt AC P51532
Protein Name Transcription activator BRG1
Gene Name SMARCA4
Organism Homo sapiens (Human).
Sequence Length 1647
Subcellular Localization Nucleus . Colocalizes with long non-coding RNA Evf2 in nuclear RNA clouds.
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. Component of the CREST-BRG1 complex, a multiprotein complex that regulates promoter activation by orchestrating the calcium-dependent release of a repressor complex and the recruitment of an activator complex. In resting neurons, transcription of the c-FOS promoter is inhibited by SMARCA4-dependent recruitment of a phospho-RB1-HDAC repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex. At the same time, there is increased recruitment of CREBBP to the promoter by a CREST-dependent mechanism, which leads to transcriptional activation. The CREST-BRG1 complex also binds to the NR2B promoter, and activity-dependent induction of NR2B expression involves the release of HDAC1 and recruitment of CREBBP. 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. SMARCA4/BAF190A may promote neural stem cell self-renewal/proliferation by enhancing Notch-dependent proliferative signals, while concurrently making the neural stem cell insensitive to SHH-dependent differentiating cues (By similarity). Acts as a corepressor of ZEB1 to regulate E-cadherin transcription and is required for induction of epithelial-mesenchymal transition (EMT) by ZEB1. Binds via DLX1 to enhancers located in the intergenic region between DLX5 and DLX6 and this binding is stabilized by the long non-coding RNA (lncRNA) Evf2 (By similarity). Binds to RNA in a promiscuous manner (By similarity). Binding to RNAs including lncRNA Evf2 leads to inhibition of SMARCA4 ATPase and chromatin remodeling activities (By similarity)..
Protein Sequence MSTPDPPLGGTPRPGPSPGPGPSPGAMLGPSPGPSPGSAHSMMGPSPGPPSAGHPIPTQGPGGYPQDNMHQMHKPMESMHEKGMSDDPRYNQMKGMGMRSGGHAGMGPPPSPMDQHSQGYPSPLGGSEHASSPVPASGPSSGPQMSSGPGGAPLDGADPQALGQQNRGPTPFNQNQLHQLRAQIMAYKMLARGQPLPDHLQMAVQGKRPMPGMQQQMPTLPPPSVSATGPGPGPGPGPGPGPGPAPPNYSRPHGMGGPNMPPPGPSGVPPGMPGQPPGGPPKPWPEGPMANAAAPTSTPQKLIPPQPTGRPSPAPPAVPPAASPVMPPQTQSPGQPAQPAPMVPLHQKQSRITPIQKPRGLDPVEILQEREYRLQARIAHRIQELENLPGSLAGDLRTKATIELKALRLLNFQRQLRQEVVVCMRRDTALETALNAKAYKRSKRQSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHANTEREQKKENERIEKERMRRLMAEDEEGYRKLIDQKKDKRLAYLLQQTDEYVANLTELVRQHKAAQVAKEKKKKKKKKKAENAEGQTPAIGPDGEPLDETSQMSDLPVKVIHVESGKILTGTDAPKAGQLEAWLEMNPGYEVAPRSDSEESGSEEEEEEEEEEQPQAAQPPTLPVEEKKKIPDPDSDDVSEVDARHIIENAKQDVDDEYGVSQALARGLQSYYAVAHAVTERVDKQSALMVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHKVLRPFLLRRLKKEVEAQLPEKVEYVIKCDMSALQRVLYRHMQAKGVLLTDGSEKDKKGKGGTKTLMNTIMQLRKICNHPYMFQHIEESFSEHLGFTGGIVQGLDLYRASGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRGFKYLRLDGTTKAEDRGMLLKTFNEPGSEYFIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNVDQKVIQAGMFDQKSSSHERRAFLQAILEHEEQDESRHCSTGSGSASFAHTAPPPAGVNPDLEEPPLKEEDEVPDDETVNQMIARHEEEFDLFMRMDLDRRREEARNPKRKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKMFGRGSRHRKEVDYSDSLTEKQWLKAIEEGTLEEIEEEVRQKKSSRKRKRDSDAGSSTPTTSTRSRDKDDESKKQKKRGRPPAEKLSPNPPNLTKKMKKIVDAVIKYKDSSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTSVRQKIEKEDDSEGEESEEEEEGEEEGSESESRSVKVKIKLGRKEKAQDRLKGGRRRPSRGSRAKPVVSDDDSEEEQEEDRSGSGSEED
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
2Phosphorylation------MSTPDPPLG
------CCCCCCCCC
61.0123401153
3Phosphorylation-----MSTPDPPLGG
-----CCCCCCCCCC
43.5029255136
11PhosphorylationPDPPLGGTPRPGPSP
CCCCCCCCCCCCCCC
17.8325159151
17PhosphorylationGTPRPGPSPGPGPSP
CCCCCCCCCCCCCCC
48.6926074081
23PhosphorylationPSPGPGPSPGAMLGP
CCCCCCCCCCCCCCC
41.7126074081
31PhosphorylationPGAMLGPSPGPSPGS
CCCCCCCCCCCCCCC
40.4626074081
35PhosphorylationLGPSPGPSPGSAHSM
CCCCCCCCCCCCCCC
48.0526074081
38PhosphorylationSPGPSPGSAHSMMGP
CCCCCCCCCCCCCCC
26.6226074081
41PhosphorylationPSPGSAHSMMGPSPG
CCCCCCCCCCCCCCC
15.3526074081
90PhosphorylationGMSDDPRYNQMKGMG
CCCCCCCHHHHCCCC
18.3526074081
94AcetylationDPRYNQMKGMGMRSG
CCCHHHHCCCCCCCC
35.6625953088
100PhosphorylationMKGMGMRSGGHAGMG
HCCCCCCCCCCCCCC
39.9926074081
111PhosphorylationAGMGPPPSPMDQHSQ
CCCCCCCCCCCCCCC
38.3326074081
117PhosphorylationPSPMDQHSQGYPSPL
CCCCCCCCCCCCCCC
21.4826074081
120PhosphorylationMDQHSQGYPSPLGGS
CCCCCCCCCCCCCCC
7.9026074081
122PhosphorylationQHSQGYPSPLGGSEH
CCCCCCCCCCCCCCC
25.0326074081
127PhosphorylationYPSPLGGSEHASSPV
CCCCCCCCCCCCCCC
25.1426074081
131PhosphorylationLGGSEHASSPVPASG
CCCCCCCCCCCCCCC
36.7626074081
132PhosphorylationGGSEHASSPVPASGP
CCCCCCCCCCCCCCC
30.6026074081
137PhosphorylationASSPVPASGPSSGPQ
CCCCCCCCCCCCCCC
45.2026074081
140PhosphorylationPVPASGPSSGPQMSS
CCCCCCCCCCCCCCC
51.9926074081
141PhosphorylationVPASGPSSGPQMSSG
CCCCCCCCCCCCCCC
58.5926074081
146PhosphorylationPSSGPQMSSGPGGAP
CCCCCCCCCCCCCCC
27.2226074081
147PhosphorylationSSGPQMSSGPGGAPL
CCCCCCCCCCCCCCC
43.6026074081
170PhosphorylationGQQNRGPTPFNQNQL
CCCCCCCCCCCHHHH
43.2528555341
181MethylationQNQLHQLRAQIMAYK
HHHHHHHHHHHHHHH
20.2030761079
188AcetylationRAQIMAYKMLARGQP
HHHHHHHHHHHCCCC
20.2119608861
192MethylationMAYKMLARGQPLPDH
HHHHHHHCCCCCCHH
40.08115917181
207AcetylationLQMAVQGKRPMPGMQ
HHHHHCCCCCCCCHH
35.9225953088
207UbiquitinationLQMAVQGKRPMPGMQ
HHHHHCCCCCCCCHH
35.92-
296PhosphorylationMANAAAPTSTPQKLI
CCCCCCCCCCCCCCC
40.2725627689
297PhosphorylationANAAAPTSTPQKLIP
CCCCCCCCCCCCCCC
36.7125627689
298PhosphorylationNAAAPTSTPQKLIPP
CCCCCCCCCCCCCCC
32.0125159151
308PhosphorylationKLIPPQPTGRPSPAP
CCCCCCCCCCCCCCC
40.3428348404
312PhosphorylationPQPTGRPSPAPPAVP
CCCCCCCCCCCCCCC
32.1229449344
323PhosphorylationPAVPPAASPVMPPQT
CCCCCCCCCCCCCCC
21.8225850435
330PhosphorylationSPVMPPQTQSPGQPA
CCCCCCCCCCCCCCC
36.4725850435
332PhosphorylationVMPPQTQSPGQPAQP
CCCCCCCCCCCCCCC
34.0925850435
353PhosphorylationHQKQSRITPIQKPRG
CCCCCCCCCCCCCCC
17.1525159151
357AcetylationSRITPIQKPRGLDPV
CCCCCCCCCCCCCHH
37.0825953088
357UbiquitinationSRITPIQKPRGLDPV
CCCCCCCCCCCCCHH
37.08-
391PhosphorylationELENLPGSLAGDLRT
HHHCCCCCCCCCCCC
17.0720068231
399UbiquitinationLAGDLRTKATIELKA
CCCCCCCCHHHHHHH
36.7821890473
399UbiquitinationLAGDLRTKATIELKA
CCCCCCCCHHHHHHH
36.7821890473
399UbiquitinationLAGDLRTKATIELKA
CCCCCCCCHHHHHHH
36.7821890473
399UbiquitinationLAGDLRTKATIELKA
CCCCCCCCHHHHHHH
36.7821890473
3992-HydroxyisobutyrylationLAGDLRTKATIELKA
CCCCCCCCHHHHHHH
36.78-
399UbiquitinationLAGDLRTKATIELKA
CCCCCCCCHHHHHHH
36.7821890473
405UbiquitinationTKATIELKALRLLNF
CCHHHHHHHHHHHHH
32.3621890473
405UbiquitinationTKATIELKALRLLNF
CCHHHHHHHHHHHHH
32.3621890473
405UbiquitinationTKATIELKALRLLNF
CCHHHHHHHHHHHHH
32.3621890473
405UbiquitinationTKATIELKALRLLNF
CCHHHHHHHHHHHHH
32.3621890473
405UbiquitinationTKATIELKALRLLNF
CCHHHHHHHHHHHHH
32.3621890473
428PhosphorylationVVCMRRDTALETALN
HHHCCCHHHHHHHHH
31.1928555341
437UbiquitinationLETALNAKAYKRSKR
HHHHHHHHHHHHHHH
51.6921890473
437UbiquitinationLETALNAKAYKRSKR
HHHHHHHHHHHHHHH
51.6921890473
437UbiquitinationLETALNAKAYKRSKR
HHHHHHHHHHHHHHH
51.6921890473
437UbiquitinationLETALNAKAYKRSKR
HHHHHHHHHHHHHHH
51.6921890473
437MethylationLETALNAKAYKRSKR
HHHHHHHHHHHHHHH
51.6930795557
437UbiquitinationLETALNAKAYKRSKR
HHHHHHHHHHHHHHH
51.6921890473
446PhosphorylationYKRSKRQSLREARIT
HHHHHHHHHHHHHHH
33.1726074081
453PhosphorylationSLREARITEKLEKQQ
HHHHHHHHHHHHHHH
22.8624702127
455AcetylationREARITEKLEKQQKI
HHHHHHHHHHHHHHH
53.9823749302
455UbiquitinationREARITEKLEKQQKI
HHHHHHHHHHHHHHH
53.98-
458UbiquitinationRITEKLEKQQKIEQE
HHHHHHHHHHHHHHH
69.35-
461AcetylationEKLEKQQKIEQERKR
HHHHHHHHHHHHHHH
45.8030592461
471UbiquitinationQERKRRQKHQEYLNS
HHHHHHHHHHHHHHH
45.5021890473
471UbiquitinationQERKRRQKHQEYLNS
HHHHHHHHHHHHHHH
45.5021890473
471UbiquitinationQERKRRQKHQEYLNS
HHHHHHHHHHHHHHH
45.5021890473
471UbiquitinationQERKRRQKHQEYLNS
HHHHHHHHHHHHHHH
45.5021890473
471UbiquitinationQERKRRQKHQEYLNS
HHHHHHHHHHHHHHH
45.5021890473
487UbiquitinationLQHAKDFKEYHRSVT
HHHHHHHHHHHHHHH
68.45-
4962-HydroxyisobutyrylationYHRSVTGKIQKLTKA
HHHHHHHHHHHHHHH
32.38-
496AcetylationYHRSVTGKIQKLTKA
HHHHHHHHHHHHHHH
32.3825953088
496UbiquitinationYHRSVTGKIQKLTKA
HHHHHHHHHHHHHHH
32.38-
502AcetylationGKIQKLTKAVATYHA
HHHHHHHHHHHHHHH
51.8326051181
502UbiquitinationGKIQKLTKAVATYHA
HHHHHHHHHHHHHHH
51.83-
529MethylationIEKERMRRLMAEDEE
HHHHHHHHHHHHCHH
21.33-
538PhosphorylationMAEDEEGYRKLIDQK
HHHCHHHHHHHHHHH
14.0921406692
588AcetylationKKKKKKKKAENAEGQ
HHHHHHHHHHCCCCC
70.5726051181
596PhosphorylationAENAEGQTPAIGPDG
HHCCCCCCCCCCCCC
26.0823927012
609PhosphorylationDGEPLDETSQMSDLP
CCCCCCCCCCCCCCC
24.7529255136
610PhosphorylationGEPLDETSQMSDLPV
CCCCCCCCCCCCCCE
23.1029255136
613PhosphorylationLDETSQMSDLPVKVI
CCCCCCCCCCCEEEE
28.4929255136
618AcetylationQMSDLPVKVIHVESG
CCCCCCEEEEEEECC
33.2726051181
624PhosphorylationVKVIHVESGKILTGT
EEEEEEECCCEEECC
44.2723312004
626UbiquitinationVIHVESGKILTGTDA
EEEEECCCEEECCCC
43.7721890473
626UbiquitinationVIHVESGKILTGTDA
EEEEECCCEEECCCC
43.7721890473
626UbiquitinationVIHVESGKILTGTDA
EEEEECCCEEECCCC
43.7721890473
626UbiquitinationVIHVESGKILTGTDA
EEEEECCCEEECCCC
43.7721890473
626AcetylationVIHVESGKILTGTDA
EEEEECCCEEECCCC
43.7723954790
626UbiquitinationVIHVESGKILTGTDA
EEEEECCCEEECCCC
43.7721890473
649PhosphorylationWLEMNPGYEVAPRSD
HHHCCCCCCCCCCCC
14.4217081983
655PhosphorylationGYEVAPRSDSEESGS
CCCCCCCCCCCCCCC
44.4228985074
657PhosphorylationEVAPRSDSEESGSEE
CCCCCCCCCCCCCHH
44.5022817900
660PhosphorylationPRSDSEESGSEEEEE
CCCCCCCCCCHHHHH
43.5028985074
662PhosphorylationSDSEESGSEEEEEEE
CCCCCCCCHHHHHHH
51.6328985074
681PhosphorylationPQAAQPPTLPVEEKK
CCCCCCCCCCHHHHC
50.8324144214
689AcetylationLPVEEKKKIPDPDSD
CCHHHHCCCCCCCCC
71.2226051181
689UbiquitinationLPVEEKKKIPDPDSD
CCHHHHCCCCCCCCC
71.22-
695PhosphorylationKKIPDPDSDDVSEVD
CCCCCCCCCCCCHHH
40.8929255136
699PhosphorylationDPDSDDVSEVDARHI
CCCCCCCCHHHHHHH
38.6129255136
711AcetylationRHIIENAKQDVDDEY
HHHHHHHHHCCCCCC
59.6226051181
711UbiquitinationRHIIENAKQDVDDEY
HHHHHHHHHCCCCCC
59.6221890473
718PhosphorylationKQDVDDEYGVSQALA
HHCCCCCCHHHHHHH
29.80-
721PhosphorylationVDDEYGVSQALARGL
CCCCCHHHHHHHHHH
12.8417525332
730PhosphorylationALARGLQSYYAVAHA
HHHHHHHHHHHHHHH
25.7528796482
731PhosphorylationLARGLQSYYAVAHAV
HHHHHHHHHHHHHHH
5.1828796482
732PhosphorylationARGLQSYYAVAHAVT
HHHHHHHHHHHHHHH
10.3928796482
746PhosphorylationTERVDKQSALMVNGV
HHCCCHHHHHHHCCE
29.1622210691
767PhosphorylationKGLEWLVSLYNNNLN
CCHHHHHHHHHCCCC
23.9824248375
769PhosphorylationLEWLVSLYNNNLNGI
HHHHHHHHHCCCCCH
14.3424248375
786PhosphorylationDEMGLGKTIQTIALI
HHCCCCHHHHHHHHH
19.2721406692
789PhosphorylationGLGKTIQTIALITYL
CCCHHHHHHHHHHHH
12.3621406692
794PhosphorylationIQTIALITYLMEHKR
HHHHHHHHHHHHCCC
16.0821406692
795PhosphorylationQTIALITYLMEHKRI
HHHHHHHHHHHCCCC
9.3221406692
831UbiquitinationKWAPSVVKVSYKGSP
CCCCCEEEEEECCCH
24.25-
833PhosphorylationAPSVVKVSYKGSPAA
CCCEEEEEECCCHHH
18.5320860994
834PhosphorylationPSVVKVSYKGSPAAR
CCEEEEEECCCHHHH
23.5020860994
835UbiquitinationSVVKVSYKGSPAARR
CEEEEEECCCHHHHH
45.46-
837PhosphorylationVKVSYKGSPAARRAF
EEEEECCCHHHHHHH
13.7630624053
850PhosphorylationAFVPQLRSGKFNVLL
HHHHHHHCCCCCEEE
55.7329083192
858PhosphorylationGKFNVLLTTYEYIIK
CCCCEEEEEHHHHHC
24.1525954137
859PhosphorylationKFNVLLTTYEYIIKD
CCCEEEEEHHHHHCC
17.8324719451
860PhosphorylationFNVLLTTYEYIIKDK
CCEEEEEHHHHHCCC
11.0824719451
862PhosphorylationVLLTTYEYIIKDKHI
EEEEEHHHHHCCCHH
9.4925954137
872UbiquitinationKDKHILAKIRWKYMI
CCCHHHHEEEEEEEE
29.38-
991AcetylationVEAQLPEKVEYVIKC
HHHHCCCCCEEEHHC
38.1326051181
991UbiquitinationVEAQLPEKVEYVIKC
HHHHCCCCCEEEHHC
38.13-
997AcetylationEKVEYVIKCDMSALQ
CCCEEEHHCCHHHHH
17.7125953088
997UbiquitinationEKVEYVIKCDMSALQ
CCCEEEHHCCHHHHH
17.71-
1008PhosphorylationSALQRVLYRHMQAKG
HHHHHHHHHHHHHCC
8.8023403867
10142-HydroxyisobutyrylationLYRHMQAKGVLLTDG
HHHHHHHCCEEECCC
32.43-
1014UbiquitinationLYRHMQAKGVLLTDG
HHHHHHHCCEEECCC
32.43-
1024AcetylationLLTDGSEKDKKGKGG
EECCCCCCCCCCCCC
76.2525953088
1024UbiquitinationLLTDGSEKDKKGKGG
EECCCCCCCCCCCCC
76.25-
1033AcetylationKKGKGGTKTLMNTIM
CCCCCCHHHHHHHHH
42.8319608861
1050PhosphorylationRKICNHPYMFQHIEE
HHHCCCHHHHHHHHH
11.74-
1081UbiquitinationDLYRASGKFELLDRI
HHHHHCCCHHHHHHH
32.9221890473
1081UbiquitinationDLYRASGKFELLDRI
HHHHHCCCHHHHHHH
32.9221890473
1081UbiquitinationDLYRASGKFELLDRI
HHHHHCCCHHHHHHH
32.9221890473
1081UbiquitinationDLYRASGKFELLDRI
HHHHHCCCHHHHHHH
32.9221890473
1081UbiquitinationDLYRASGKFELLDRI
HHHHHCCCHHHHHHH
32.9221890473
1087MethylationGKFELLDRILPKLRA
CCHHHHHHHHHHHHH
32.11-
1122AcetylationYFAYRGFKYLRLDGT
HHHHCCCCEEEECCC
46.3126051181
1123PhosphorylationFAYRGFKYLRLDGTT
HHHCCCCEEEECCCC
8.5218083107
1131UbiquitinationLRLDGTTKAEDRGML
EEECCCCCHHHHCEE
50.0121890473
1213UbiquitinationTVNSVEEKILAAAKY
ECCCHHHHHHHHHHH
29.52-
1219AcetylationEKILAAAKYKLNVDQ
HHHHHHHHHCCCCCH
37.8919822091
1219UbiquitinationEKILAAAKYKLNVDQ
HHHHHHHHHCCCCCH
37.89-
1220PhosphorylationKILAAAKYKLNVDQK
HHHHHHHHCCCCCHH
18.91-
1221UbiquitinationILAAAKYKLNVDQKV
HHHHHHHCCCCCHHH
32.64-
1227SumoylationYKLNVDQKVIQAGMF
HCCCCCHHHHHHCCC
36.52-
1227SumoylationYKLNVDQKVIQAGMF
HCCCCCHHHHHHCCC
36.52-
1227UbiquitinationYKLNVDQKVIQAGMF
HCCCCCHHHHHHCCC
36.52-
1237UbiquitinationQAGMFDQKSSSHERR
HHCCCCCCCCHHHHH
54.90-
1238PhosphorylationAGMFDQKSSSHERRA
HCCCCCCCCHHHHHH
31.2921406692
1239PhosphorylationGMFDQKSSSHERRAF
CCCCCCCCHHHHHHH
42.6321406692
1240PhosphorylationMFDQKSSSHERRAFL
CCCCCCCHHHHHHHH
36.1421406692
1291SumoylationDLEEPPLKEEDEVPD
CCCCCCCCCCCCCCC
65.90-
1345PhosphorylationMEEDELPSWIIKDDA
CCCCCCCCEEECCCH
43.4622199227
1349SumoylationELPSWIIKDDAEVER
CCCCEEECCCHHCEE
40.18-
1349UbiquitinationELPSWIIKDDAEVER
CCCCEEECCCHHCEE
40.1821890473
1353 (in isoform 3)Ubiquitination-52.48-
1358PhosphorylationDAEVERLTCEEEEEK
CHHCEECCCHHHHHH
24.8821130716
1365SumoylationTCEEEEEKMFGRGSR
CCHHHHHHHHCCCCC
42.6928112733
1365UbiquitinationTCEEEEEKMFGRGSR
CCHHHHHHHHCCCCC
42.69-
1366SulfoxidationCEEEEEKMFGRGSRH
CHHHHHHHHCCCCCC
4.9421406390
1371PhosphorylationEKMFGRGSRHRKEVD
HHHHCCCCCCCCCCC
24.4521406692
1375UbiquitinationGRGSRHRKEVDYSDS
CCCCCCCCCCCCCCC
56.83-
1379PhosphorylationRHRKEVDYSDSLTEK
CCCCCCCCCCCCCHH
21.3923927012
1380PhosphorylationHRKEVDYSDSLTEKQ
CCCCCCCCCCCCHHH
19.0923401153
1382PhosphorylationKEVDYSDSLTEKQWL
CCCCCCCCCCHHHHH
31.1129255136
1384PhosphorylationVDYSDSLTEKQWLKA
CCCCCCCCHHHHHHH
45.1229255136
1386UbiquitinationYSDSLTEKQWLKAIE
CCCCCCHHHHHHHHH
41.35-
1396PhosphorylationLKAIEEGTLEEIEEE
HHHHHHCCHHHHHHH
33.9921712546
1410PhosphorylationEVRQKKSSRKRKRDS
HHHHHHHHCCCCCCC
51.1829457462
1417PhosphorylationSRKRKRDSDAGSSTP
HCCCCCCCCCCCCCC
33.1323401153
1421PhosphorylationKRDSDAGSSTPTTST
CCCCCCCCCCCCCCC
32.5325159151
1422PhosphorylationRDSDAGSSTPTTSTR
CCCCCCCCCCCCCCC
37.1729255136
1423PhosphorylationDSDAGSSTPTTSTRS
CCCCCCCCCCCCCCC
26.7629255136
1425PhosphorylationDAGSSTPTTSTRSRD
CCCCCCCCCCCCCCC
33.2028176443
1426PhosphorylationAGSSTPTTSTRSRDK
CCCCCCCCCCCCCCC
29.3328176443
1427PhosphorylationGSSTPTTSTRSRDKD
CCCCCCCCCCCCCCC
25.0528176443
1428PhosphorylationSSTPTTSTRSRDKDD
CCCCCCCCCCCCCCC
30.4828176443
1430PhosphorylationTPTTSTRSRDKDDES
CCCCCCCCCCCCCHH
44.9426074081
1448 (in isoform 5)Phosphorylation-29.28-
1450AcetylationRGRPPAEKLSPNPPN
CCCCCHHHCCCCCCC
57.2723236377
1451 (in isoform 3)Phosphorylation-8.50-
1452PhosphorylationRPPAEKLSPNPPNLT
CCCHHHCCCCCCCHH
33.4329255136
1459PhosphorylationSPNPPNLTKKMKKIV
CCCCCCHHHHHHHHH
34.9523927012
1464AcetylationNLTKKMKKIVDAVIK
CHHHHHHHHHHHHHH
44.4526051181
1490PhosphorylationEVFIQLPSRKELPEY
EEEEECCCCCCCHHH
65.66-
1492UbiquitinationFIQLPSRKELPEYYE
EEECCCCCCCHHHHH
68.86-
1497PhosphorylationSRKELPEYYELIRKP
CCCCCHHHHHHHHCC
10.57-
1519PhosphorylationERIRNHKYRSLNDLE
HHHHHCCCCCHHHHH
9.6220873877
1521PhosphorylationIRNHKYRSLNDLEKD
HHHCCCCCHHHHHHH
28.5620873877
1570PhosphorylationKIEKEDDSEGEESEE
HHHHCCCCCCCCCHH
60.8820164059
1575PhosphorylationDDSEGEESEEEEEGE
CCCCCCCCHHHHHCC
46.1120164059
1586PhosphorylationEEGEEEGSESESRSV
HHCCCCCCCCCCCCE
41.0323927012
1588PhosphorylationGEEEGSESESRSVKV
CCCCCCCCCCCCEEE
42.4423927012
1590PhosphorylationEEGSESESRSVKVKI
CCCCCCCCCCEEEEE
38.8523927012
1592PhosphorylationGSESESRSVKVKIKL
CCCCCCCCEEEEEEE
35.25-
1617PhosphorylationKGGRRRPSRGSRAKP
CCCCCCCCCCCCCCC
47.6824144214
1620PhosphorylationRRRPSRGSRAKPVVS
CCCCCCCCCCCCCCC
28.1424144214
1627PhosphorylationSRAKPVVSDDDSEEE
CCCCCCCCCCCCHHH
35.2429255136
1631PhosphorylationPVVSDDDSEEEQEED
CCCCCCCCHHHHHHH
54.6329255136
1640PhosphorylationEEQEEDRSGSGSEED
HHHHHHCCCCCCCCC
50.0228355574
1642PhosphorylationQEEDRSGSGSEED--
HHHHCCCCCCCCC--
40.1521955146
1644PhosphorylationEDRSGSGSEED----
HHCCCCCCCCC----
39.2421955146

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
31SPhosphorylationKinaseCK1DP48730
PSP
35SPhosphorylationKinaseCK1DP48730
PSP
721SPhosphorylationKinaseATMQ13315
PSP
-KUbiquitinationE3 ubiquitin ligaseCHFRQ96EP1
PMID:22285184

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMCA4_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 SMCA4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ESR1_HUMANESR1physical
9099865
BRCA1_HUMANBRCA1physical
10943845
CTNB1_HUMANCTNNB1physical
11532957
FANCA_HUMANFANCAphysical
11726552
RPB1_HUMANPOLR2Aphysical
11238380
SMRC1_HUMANSMARCC1physical
11238380
SIN3A_HUMANSIN3Aphysical
11238380
HDAC2_HUMANHDAC2physical
11238380
RBBP4_HUMANRBBP4physical
11238380
PHB_HUMANPHBphysical
12065415
STAT2_HUMANSTAT2physical
12244326
ARI1A_HUMANARID1Aphysical
8895581
SMRC2_HUMANSMARCC2physical
8895581
SMRC1_HUMANSMARCC1physical
8895581
SMCE1_HUMANSMARCE1physical
8895581
SNF5_HUMANSMARCB1physical
8895581
RPB1_HUMANPOLR2Aphysical
8895581
ACL6A_HUMANACTL6Aphysical
8895581
SMRC2_HUMANSMARCC2physical
11726552
SMRC1_HUMANSMARCC1physical
11726552
SNF5_HUMANSMARCB1physical
11726552
ENPL_HUMANHSP90B1physical
11726552
ARI1B_HUMANARID1Bphysical
12200431
ARI1A_HUMANARID1Aphysical
9845365
SMRC2_HUMANSMARCC2physical
9845365
SMRC1_HUMANSMARCC1physical
9845365
SMCE1_HUMANSMARCE1physical
9845365
ACTB_HUMANACTBphysical
9845365
SNF5_HUMANSMARCB1physical
9845365
RPB1_HUMANPOLR2Aphysical
9845365
ACL6A_HUMANACTL6Aphysical
9845365
CBP_HUMANCREBBPgenetic
11003650
NCOA1_HUMANNCOA1genetic
11003650
ING1_HUMANING1physical
11784859
SIN3A_HUMANSIN3Aphysical
11784859
SMCA2_HUMANSMARCA2physical
9128241
SNF5_HUMANSMARCB1physical
9128241
RB_HUMANRB1physical
9128241
GCR_HUMANNR3C1physical
9128241
JUNB_HUMANJUNBphysical
9128241
RPB1_HUMANPOLR2Aphysical
9128241
LMNB1_HUMANLMNB1physical
9128241
SRF_HUMANSRFphysical
19342595
MYCD_HUMANMYOCDphysical
19342595
CREST_HUMANSS18L1physical
19081374
DDX5_HUMANDDX5physical
17011493
NF2L2_HUMANNFE2L2physical
16923960
SNF5_HUMANSMARCB1physical
18809673
SMCE1_HUMANSMARCE1physical
18809673
SMRC1_HUMANSMARCC1physical
18809673
SIN3A_HUMANSIN3Aphysical
16800816
HDAC2_HUMANHDAC2physical
16800816
PAX6_HUMANPAX6physical
16675956
SMRC1_HUMANSMARCC1physical
16452305
MYOG_HUMANMYOGphysical
16424906
MYEF2_HUMANMYEF2physical
16424906
ARI1A_HUMANARID1Aphysical
14559996
SMRC2_HUMANSMARCC2physical
14559996
SMRC1_HUMANSMARCC1physical
14559996
ANM5_HUMANPRMT5physical
14559996
SMRD1_HUMANSMARCD1physical
14559996
SMRD2_HUMANSMARCD2physical
14559996
SMCE1_HUMANSMARCE1physical
14559996
ACL6A_HUMANACTL6Aphysical
14559996
SNF5_HUMANSMARCB1physical
14559996
SIN3A_HUMANSIN3Aphysical
14559996
HDAC2_HUMANHDAC2physical
14559996
CHD4_HUMANCHD4physical
14530259
ARI1A_HUMANARID1Aphysical
16287714
SMRC1_HUMANSMARCC1physical
16287714
SMCE1_HUMANSMARCE1physical
16287714
SNF5_HUMANSMARCB1physical
16287714
CHD4_HUMANCHD4physical
16217013
SMRC1_HUMANSMARCC1physical
16217013
HNRPC_HUMANHNRNPCphysical
16217013
STAT1_HUMANSTAT1physical
16195385
USF1_HUMANUSF1physical
16195385
IRF1_HUMANIRF1physical
16195385
RPB1_HUMANPOLR2Aphysical
16195385
SP1_HUMANSP1physical
12192045
REST_HUMANRESTphysical
12192000
RCOR1_HUMANRCOR1physical
12192000
HDAC1_HUMANHDAC1physical
12192000
HDAC2_HUMANHDAC2physical
12192000
C2TA_HUMANCIITAphysical
12077331
GEMI_HUMANGMNNphysical
16024661
NGN2_HUMANNEUROG2physical
16024661
NDF1_HUMANNEUROD1physical
16024661
NF1_HUMANNF1physical
15999204
RPB1_HUMANPOLR2Aphysical
15999204
PBX1_HUMANPBX1physical
15870273
MYOD1_HUMANMYOD1physical
15870273
MYEF2_HUMANMYEF2physical
15870273
RB_HUMANRB1physical
15485920
SP1_HUMANSP1physical
15317818
STAT3_HUMANSTAT3physical
15286705
RB_HUMANRB1physical
10778858
PHB_HUMANPHBphysical
15141164
ARI1A_HUMANARID1Aphysical
18086889
SMRC1_HUMANSMARCC1physical
18086889
SMRC2_HUMANSMARCC2physical
18086889
NONO_HUMANNONOphysical
18042045
SMCA2_HUMANSMARCA2physical
18042045
SNF5_HUMANSMARCB1physical
18042045
SNF5_HUMANSMARCB1physical
9584200
SMAD2_HUMANSMAD2physical
18003620
SMAD3_HUMANSMAD3physical
18003620
CARM1_HUMANCARM1physical
14729568
ADNP_HUMANADNPphysical
17878164
STA5A_HUMANSTAT5Aphysical
17387179
CEBPB_HUMANCEBPBphysical
17387179
GCR_HUMANNR3C1physical
17387179
P53_HUMANTP53physical
17666433
RB_HUMANRB1physical
17666433
PML_HUMANPMLphysical
21360626
REQU_HUMANDPF2physical
20460684
SMRC1_HUMANSMARCC1physical
20460684
ARI1A_HUMANARID1Aphysical
20460684
SMRC2_HUMANSMARCC2physical
20460684
SNF5_HUMANSMARCB1physical
20460684
SMRD1_HUMANSMARCD1physical
20460684
ACL6A_HUMANACTL6Aphysical
20460684
SMCE1_HUMANSMARCE1physical
20460684
HDAC2_HUMANHDAC2physical
20460684
NPM_HUMANNPM1physical
20460684
NONO_HUMANNONOphysical
20460684
IMA1_HUMANKPNA2physical
20460684
BCL7A_HUMANBCL7Aphysical
20460684
ZEB1_HUMANZEB1physical
20418909
TOPB1_HUMANTOPBP1physical
20571081
SNF5_HUMANSMARCB1physical
20506188
RUNX1_HUMANRUNX1physical
20506188
H31_HUMANHIST1H3Aphysical
20011120
CBX5_HUMANCBX5physical
20011120
ARID2_HUMANARID2physical
15985610
HSF1_HUMANHSF1physical
21079652
SNF5_HUMANSMARCB1physical
16687403
TAT_HV1H2tatphysical
16687403
SNF5_HUMANSMARCB1physical
21520050
SMRC1_HUMANSMARCC1physical
21520050
ATF3_HUMANATF3physical
21300803
ACTB_HUMANACTBphysical
21300803
CDK8_HUMANCDK8physical
22668559
CDK19_HUMANCDK19physical
22668559
MED6_HUMANMED6physical
22668559
MED17_HUMANMED17physical
22668559
ANGL4_HUMANANGPTL4physical
22573825
SMRC2_HUMANSMARCC2physical
22573825
SNF5_HUMANSMARCB1physical
22573825
ACTC_HUMANACTC1physical
22573825
ACTB_HUMANACTBphysical
22573825
SMRC1_HUMANSMARCC1physical
18303029
P53_MOUSETrp53physical
18303029
CHFR_HUMANCHFRphysical
22285184
KDM6A_HUMANKDM6Aphysical
22192413
SMRD3_HUMANSMARCD3physical
22068056
H32_HUMANHIST2H3Cphysical
17274598
H2B2E_HUMANHIST2H2BEphysical
17274598
SMRC1_HUMANSMARCC1physical
22939629
SNF5_HUMANSMARCB1physical
22939629
SMCE1_HUMANSMARCE1physical
22939629
SMRC2_HUMANSMARCC2physical
22939629
SMRD1_HUMANSMARCD1physical
22939629
SMRD2_HUMANSMARCD2physical
22939629
SMRD3_HUMANSMARCD3physical
22939629
TOP2B_HUMANTOP2Bphysical
22939629
SUH_HUMANRBPJphysical
23022380
NOTC1_HUMANNOTCH1physical
23022380
BRCA1_HUMANBRCA1physical
23438604
RB_HUMANRB1physical
23438604
HDAC1_HUMANHDAC1genetic
11003650
ACL6A_HUMANACTL6Aphysical
26344197
BYST_HUMANBYSLphysical
26344197
REQU_HUMANDPF2physical
26344197
DPF3_HUMANDPF3physical
26344197
EP400_HUMANEP400physical
26344197
HMGB1_HUMANHMGB1physical
26344197
MDC1_HUMANMDC1physical
26344197
MY18A_HUMANMYO18Aphysical
26344197
PELO_HUMANPELOphysical
26344197
SNF5_HUMANSMARCB1physical
26344197
SMRC1_HUMANSMARCC1physical
26344197
SMRC2_HUMANSMARCC2physical
26344197
SSXT_HUMANSS18physical
26344197
SMRC2_HUMANSMARCC2physical
9584200
ARI1A_HUMANARID1Aphysical
9584200
SNF5_HUMANSMARCB1genetic
28319113
SPTA1_HUMANSPTA1physical
16889989

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613325Rhabdoid tumor predisposition syndrome 2 (RTPS2)
614609Mental retardation, autosomal dominant 16 (MRD16)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SMCA4_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-188 AND LYS-455, 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 THR-609; SER-610; SER-613;SER-695; SER-699; SER-1382; SER-1452; SER-1570; SER-1575; SER-1627 ANDSER-1631, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-609; SER-610; SER-613;SER-1382 AND SER-1452, AND MASS SPECTROMETRY.
"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-613; SER-1382; SER-1452;SER-1570; SER-1575; SER-1586; SER-1627; SER-1631; SER-1640; SER-1642AND SER-1644, AND MASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-610 AND SER-721, ANDMASS 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 THR-11; SER-655; SER-657;SER-660; SER-662 AND SER-1452, AND MASS 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-695 AND SER-1382, ANDMASS SPECTROMETRY.

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