UBE3A_HUMAN - dbPTM
UBE3A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBE3A_HUMAN
UniProt AC Q05086
Protein Name Ubiquitin-protein ligase E3A
Gene Name UBE3A {ECO:0000312|HGNC:HGNC:12496}
Organism Homo sapiens (Human).
Sequence Length 875
Subcellular Localization Cytoplasm . Nucleus .
Protein Description E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and transfers it to its substrates. [PubMed: 10373495]
Protein Sequence MEKLHQCYWKSGEPQSDDIEASRMKRAAAKHLIERYYHQLTEGCGNEACTNEFCASCPTFLRMDNNAAAIKALELYKINAKLCDPHPSKKGASSAYLENSKGAPNNSCSEIKMNKKGARIDFKDVTYLTEEKVYEILELCREREDYSPLIRVIGRVFSSAEALVQSFRKVKQHTKEELKSLQAKDEDKDEDEKEKAACSAAAMEEDSEASSSRIGDSSQGDNNLQKLGPDDVSVDIDAIRRVYTRLLSNEKIETAFLNALVYLSPNVECDLTYHNVYSRDPNYLNLFIIVMENRNLHSPEYLEMALPLFCKAMSKLPLAAQGKLIRLWSKYNADQIRRMMETFQQLITYKVISNEFNSRNLVNDDDAIVAASKCLKMVYYANVVGGEVDTNHNEEDDEEPIPESSELTLQELLGEERRNKKGPRVDPLETELGVKTLDCRKPLIPFEEFINEPLNEVLEMDKDYTFFKVETENKFSFMTCPFILNAVTKNLGLYYDNRIRMYSERRITVLYSLVQGQQLNPYLRLKVRRDHIIDDALVRLEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDESTKLFWFNPSSFETEGQFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDLLEYEGNVEDDMMITFQISQTDLFGNPMMYDLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKYLFRPEEIELLICGSRNLDFQALEETTEYDGGYTRDSVLIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLGKLKMIIAKNGPDTERLPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGFGML
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
7Ubiquitination-MEKLHQCYWKSGEP
-CCCCCCCCCCCCCC
2.8122053931
19 (in isoform 3)Phosphorylation-5.98-
22PhosphorylationQSDDIEASRMKRAAA
CCCHHHHHHHHHHHH
21.81-
27 (in isoform 3)Ubiquitination-13.2721890473
30AcetylationRMKRAAAKHLIERYY
HHHHHHHHHHHHHHH
33.9325953088
30UbiquitinationRMKRAAAKHLIERYY
HHHHHHHHHHHHHHH
33.9321890473
30 (in isoform 1)Ubiquitination-33.9321890473
48UbiquitinationTEGCGNEACTNEFCA
HCCCCCHHHCCHHHH
14.9422053931
48 (in isoform 2)Ubiquitination-14.9421890473
54 (in isoform 2)Ubiquitination-1.9121890473
67 (in isoform 2)Ubiquitination-12.4321890473
68 (in isoform 3)Ubiquitination-16.3121890473
71UbiquitinationDNNAAAIKALELYKI
CCCHHHHHHHHHHHH
42.0421890473
71 (in isoform 1)Ubiquitination-42.0421890473
74 (in isoform 3)Ubiquitination-55.7121890473
77UbiquitinationIKALELYKINAKLCD
HHHHHHHHHCCCCCC
41.9521890473
77 (in isoform 1)Ubiquitination-41.9521890473
81UbiquitinationELYKINAKLCDPHPS
HHHHHCCCCCCCCCC
45.20-
87 (in isoform 3)Ubiquitination-53.9121890473
89UbiquitinationLCDPHPSKKGASSAY
CCCCCCCCCCCCHHH
60.73-
90UbiquitinationCDPHPSKKGASSAYL
CCCCCCCCCCCHHHH
65.1490473
90 (in isoform 1)Ubiquitination-65.1421890473
93PhosphorylationHPSKKGASSAYLENS
CCCCCCCCHHHHHCC
24.9523312004
94PhosphorylationPSKKGASSAYLENSK
CCCCCCCHHHHHCCC
22.0228348404
96PhosphorylationKKGASSAYLENSKGA
CCCCCHHHHHCCCCC
19.2527642862
100PhosphorylationSSAYLENSKGAPNNS
CHHHHHCCCCCCCCC
24.0825159151
100 (in isoform 2)Ubiquitination-24.0821890473
101UbiquitinationSAYLENSKGAPNNSC
HHHHHCCCCCCCCCC
71.34-
107PhosphorylationSKGAPNNSCSEIKMN
CCCCCCCCCHHCCCC
26.1728348404
109PhosphorylationGAPNNSCSEIKMNKK
CCCCCCCHHCCCCCC
42.0225627689
109UbiquitinationGAPNNSCSEIKMNKK
CCCCCCCHHCCCCCC
42.0222053931
112UbiquitinationNNSCSEIKMNKKGAR
CCCCHHCCCCCCCCC
32.16-
120 (in isoform 3)Ubiquitination-7.8721890473
123AcetylationKGARIDFKDVTYLTE
CCCCCCCCCCEEECH
47.7625953088
123UbiquitinationKGARIDFKDVTYLTE
CCCCCCCCCCEEECH
47.7621890473
123 (in isoform 1)Ubiquitination-47.7621890473
126PhosphorylationRIDFKDVTYLTEEKV
CCCCCCCEEECHHHH
23.9728152594
127PhosphorylationIDFKDVTYLTEEKVY
CCCCCCEEECHHHHH
16.1025884760
129PhosphorylationFKDVTYLTEEKVYEI
CCCCEEECHHHHHHH
31.5228152594
132UbiquitinationVTYLTEEKVYEILEL
CEEECHHHHHHHHHH
43.83-
132 (in isoform 1)Ubiquitination-43.8321890473
147PhosphorylationCREREDYSPLIRVIG
HHCCCCCHHHHHHHH
26.0824719451
158PhosphorylationRVIGRVFSSAEALVQ
HHHHHHHCCHHHHHH
26.28-
159PhosphorylationVIGRVFSSAEALVQS
HHHHHHCCHHHHHHH
20.75-
161 (in isoform 2)Ubiquitination-44.4721890473
179UbiquitinationQHTKEELKSLQAKDE
HHCHHHHHHCCCCCC
53.02-
181 (in isoform 3)Ubiquitination-5.6921890473
184UbiquitinationELKSLQAKDEDKDED
HHHHCCCCCCCCCHH
49.0021906983
184 (in isoform 1)Ubiquitination-49.0021890473
195 (in isoform 2)Phosphorylation-52.96-
199PhosphorylationEKEKAACSAAAMEED
HHHHHHHHHHHHHHC
19.06-
203SulfoxidationAACSAAAMEEDSEAS
HHHHHHHHHHCCHHH
5.0621406390
203 (in isoform 2)Ubiquitination-5.0621890473
207PhosphorylationAAAMEEDSEASSSRI
HHHHHHCCHHHHCCC
38.0430108239
210PhosphorylationMEEDSEASSSRIGDS
HHHCCHHHHCCCCCC
25.4624719451
211PhosphorylationEEDSEASSSRIGDSS
HHCCHHHHCCCCCCC
30.5930108239
212PhosphorylationEDSEASSSRIGDSSQ
HCCHHHHCCCCCCCC
25.9730108239
215 (in isoform 3)Phosphorylation-27.86-
217PhosphorylationSSSRIGDSSQGDNNL
HHCCCCCCCCCCCCH
21.2429255136
218PhosphorylationSSRIGDSSQGDNNLQ
HCCCCCCCCCCCCHH
42.8117525332
223 (in isoform 3)Ubiquitination-48.8921890473
226UbiquitinationQGDNNLQKLGPDDVS
CCCCCHHHHCCCCCE
59.592266
226 (in isoform 1)Ubiquitination-59.5921890473
288 (in isoform 2)Ubiquitination-2.3321890473
294MethylationFIIVMENRNLHSPEY
EEEEEECCCCCCHHH
33.515169925
300 (in isoform 2)Ubiquitination-66.8121890473
307 (in isoform 2)Ubiquitination-17.5321890473
308 (in isoform 3)Ubiquitination-9.0621890473
311UbiquitinationMALPLFCKAMSKLPL
HHHHHHHHHHHCCCH
39.5321890473
311 (in isoform 1)Ubiquitination-39.5321890473
315UbiquitinationLFCKAMSKLPLAAQG
HHHHHHHCCCHHHHC
40.83-
320 (in isoform 3)Ubiquitination-26.7521890473
323UbiquitinationLPLAAQGKLIRLWSK
CCHHHHCHHHHHHHH
28.7621890473
323 (in isoform 1)Ubiquitination-28.7621890473
327 (in isoform 2)Ubiquitination-4.8621890473
327 (in isoform 3)Ubiquitination-4.8621890473
330UbiquitinationKLIRLWSKYNADQIR
HHHHHHHHCCHHHHH
30.8321890473
330 (in isoform 1)Ubiquitination-30.8321890473
342PhosphorylationQIRRMMETFQQLITY
HHHHHHHHHHHHHHH
14.62-
347 (in isoform 3)Ubiquitination-3.2521890473
349PhosphorylationTFQQLITYKVISNEF
HHHHHHHHHHHCCCC
9.03-
350UbiquitinationFQQLITYKVISNEFN
HHHHHHHHHHCCCCC
25.1721890473
350 (in isoform 1)Ubiquitination-25.1721890473
350 (in isoform 2)Ubiquitination-25.1721890473
370 (in isoform 3)Ubiquitination-10.4121890473
372O-linked_GlycosylationDDAIVAASKCLKMVY
HHHHHHHHHHHHHHH
17.7330379171
372PhosphorylationDDAIVAASKCLKMVY
HHHHHHHHHHHHHHH
17.7327732954
373UbiquitinationDAIVAASKCLKMVYY
HHHHHHHHHHHHHHH
38.5721890473
373 (in isoform 1)Ubiquitination-38.5721890473
418 (in isoform 2)Ubiquitination-63.70-
420UbiquitinationLGEERRNKKGPRVDP
HCHHHHCCCCCCCCH
58.24-
421UbiquitinationGEERRNKKGPRVDPL
CHHHHCCCCCCCCHH
77.14-
435UbiquitinationLETELGVKTLDCRKP
HHHHCCCCCCCCCCC
41.39-
441UbiquitinationVKTLDCRKPLIPFEE
CCCCCCCCCCCCHHH
50.97-
445 (in isoform 2)Ubiquitination-37.9821890473
465PhosphorylationLEMDKDYTFFKVETE
HHCCCCCCEEEEEEC
32.50-
465 (in isoform 3)Ubiquitination-32.5021890473
468UbiquitinationDKDYTFFKVETENKF
CCCCCEEEEEECCCE
34.6621890473
468 (in isoform 1)Ubiquitination-34.6621890473
471PhosphorylationYTFFKVETENKFSFM
CCEEEEEECCCEEHH
48.09-
474UbiquitinationFKVETENKFSFMTCP
EEEEECCCEEHHHHH
35.83-
479PhosphorylationENKFSFMTCPFILNA
CCCEEHHHHHHHHHH
18.28-
485 (in isoform 2)Phosphorylation-27.78-
489 (in isoform 2)Phosphorylation-43.51-
494PhosphorylationVTKNLGLYYDNRIRM
HHHHCCCCCCCCCCC
13.6325147952
503O-linked_GlycosylationDNRIRMYSERRITVL
CCCCCCCCHHHHHHH
18.4530379171
508PhosphorylationMYSERRITVLYSLVQ
CCCHHHHHHHHHHHC
11.57-
511PhosphorylationERRITVLYSLVQGQQ
HHHHHHHHHHHCCCC
8.81-
512PhosphorylationRRITVLYSLVQGQQL
HHHHHHHHHHCCCCC
20.22-
529 (in isoform 2)Ubiquitination-42.7321890473
530 (in isoform 2)Ubiquitination-27.1221890473
542SulfoxidationDALVRLEMIAMENPA
HHHHHHHHHHHCCHH
2.5421406390
549 (in isoform 3)Ubiquitination-46.4821890473
550 (in isoform 3)Ubiquitination-61.3521890473
552UbiquitinationMENPADLKKQLYVEF
HCCHHHHHHHEEEEE
38.7321906983
552 (in isoform 1)Ubiquitination-38.7321890473
553UbiquitinationENPADLKKQLYVEFE
CCHHHHHHHEEEEEE
53.4821906983
553 (in isoform 1)Ubiquitination-53.4821890473
636 (in isoform 2)Phosphorylation-3.31-
645UbiquitinationYRKLMGKKGTFRDLG
HHHHCCCCCCCCCCC
58.41-
659PhosphorylationGDSHPVLYQSLKDLL
CCCCHHHHHHHHHHH
9.049143503
688 (in isoform 2)Ubiquitination-11.2021890473
697AcetylationNPMMYDLKENGDKIP
CCCEEEHHHCCCCCC
46.3525953088
701 (in isoform 2)Ubiquitination-58.2421890473
702UbiquitinationDLKENGDKIPITNEN
EHHHCCCCCCCCCCC
52.35-
705 (in isoform 2)Ubiquitination-8.0121890473
708 (in isoform 3)Ubiquitination-50.1621890473
711UbiquitinationPITNENRKEFVNLYS
CCCCCCHHHHHHHHH
68.0621890473
711 (in isoform 1)Ubiquitination-68.0621890473
720PhosphorylationFVNLYSDYILNKSVE
HHHHHHHHHCCHHHH
11.0218083107
721 (in isoform 3)Ubiquitination-4.0321890473
724UbiquitinationYSDYILNKSVEKQFK
HHHHHCCHHHHHHHH
53.0521890473
724 (in isoform 1)Ubiquitination-53.0521890473
725 (in isoform 3)Ubiquitination-34.1421890473
728UbiquitinationILNKSVEKQFKAFRR
HCCHHHHHHHHHHHH
59.9021890473
728 (in isoform 1)Ubiquitination-59.9021890473
731UbiquitinationKSVEKQFKAFRRGFH
HHHHHHHHHHHHCCE
44.09-
741PhosphorylationRRGFHMVTNESPLKY
HHCCEECCCCCCCHH
26.2028122231
744PhosphorylationFHMVTNESPLKYLFR
CEECCCCCCCHHCCC
37.2924719451
776PhosphorylationALEETTEYDGGYTRD
HHHHCCCCCCCCCHH
20.1427642862
779 (in isoform 2)Ubiquitination-20.1021890473
799 (in isoform 3)Ubiquitination-55.0821890473
802UbiquitinationHSFTDEQKRLFLQFT
HHCCHHHHHEEEEEC
49.3621906983
802 (in isoform 1)Ubiquitination-49.3621890473
806 (in isoform 2)Ubiquitination-4.9121890473
822AcetylationAPVGGLGKLKMIIAK
CCCCCHHHEEEEEEC
50.4025953088
822UbiquitinationAPVGGLGKLKMIIAK
CCCCCHHHEEEEEEC
50.40-
824UbiquitinationVGGLGKLKMIIAKNG
CCCHHHEEEEEECCC
31.38-
826 (in isoform 3)Ubiquitination-2.3721890473
829UbiquitinationKLKMIIAKNGPDTER
HEEEEEECCCCCCCC
52.622190698
829 (in isoform 1)Ubiquitination-52.6221890473
847 (in isoform 2)Ubiquitination-4.22-
855UbiquitinationLLPEYSSKEKLKERL
CCCCCCCHHHHHHHH
53.58-
857UbiquitinationPEYSSKEKLKERLLK
CCCCCHHHHHHHHHH
69.47-
864UbiquitinationKLKERLLKAITYAKG
HHHHHHHHHHHHHHC
42.19-
870UbiquitinationLKAITYAKGFGML--
HHHHHHHHCCCCC--
44.34-

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
485TPhosphorylationKinasePRKACAP17612
GPS
636YPhosphorylationKinaseABL1P00520
GPS
659YPhosphorylationKinaseABL1P00519
Uniprot
-KUbiquitinationE3 ubiquitin ligaseUBE3AQ05086
PMID:10864652

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBE3A_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 UBE3A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBQL2_HUMANUBQLN2physical
10983987
LCK_HUMANLCKphysical
10449731
BLK_HUMANBLKphysical
10449731
TSC2_HUMANTSC2physical
15175323
UB2D2_HUMANUBE2D2physical
9182527
UB2L3_HUMANUBE2L3physical
10558980
UBQL1_HUMANUBQLN1physical
10983987
TSC2_HUMANTSC2physical
18298802
UB2L3_HUMANUBE2L3physical
11431533
RING2_HUMANRNF2physical
20351251
RD23A_HUMANRAD23Aphysical
10373495
RD23B_HUMANRAD23Bphysical
10373495
UBE3A_HUMANUBE3Aphysical
9688277
DLG1_HUMANDLG1physical
16482544
SCRIB_HUMANSCRIBphysical
16482544
CDN1B_HUMANCDKN1Bphysical
19591933
NELFD_HUMANNELFCDphysical
17131388
UBE3A_HUMANUBE3Aphysical
21033666
ANXA1_HUMANANXA1physical
19204938
MYH9_HUMANMYH9physical
16051665
XRCC6_HUMANXRCC6physical
16051665
ACTS_HUMANACTA1physical
16051665
ANXA2_HUMANANXA2physical
16051665
MYCB2_HUMANMYCBP2physical
16051665
GOGA3_HUMANGOLGA3physical
16051665
KPB2_HUMANPHKA2physical
16051665
KPBB_HUMANPHKBphysical
16051665
WDCP_HUMANC2orf44physical
16051665
PSMD3_HUMANPSMD3physical
16051665
PHKG2_HUMANPHKG2physical
16051665
PHKG1_HUMANPHKG1physical
16051665
PSMD4_HUMANPSMD4physical
19240029
HSP74_HUMANHSPA4physical
19233847
HSP7C_HUMANHSPA8physical
19233847
CFTR_HUMANCFTRphysical
19233847
PRDX1_HUMANPRDX1physical
20589759
PML_HUMANPMLphysical
19325566
ARHGF_HUMANARHGEF15physical
21029865
NOMO2_HUMANNOMO2physical
21900206
PDE1B_HUMANPDE1Bphysical
21900206
EID1_HUMANEID1physical
21900206
SUMO3_HUMANSUMO3physical
21900206
CK049_HUMANC11orf49physical
21900206
PARVA_HUMANPARVAphysical
21900206
1433E_HUMANYWHAEphysical
21900206
PRAG1_HUMANSGK223physical
21900206
TCF19_HUMANTCF19physical
21900206
HPCL4_HUMANHPCAL4physical
21900206
RMI1_HUMANRMI1physical
21900206
TRI65_HUMANTRIM65physical
21900206
DPOE4_HUMANPOLE4physical
21900206
JADE1_HUMANJADE1physical
21900206
HBA_HUMANHBA1physical
21900206
IF4G1_HUMANEIF4G1physical
21900206
AFTIN_HUMANAFTPHphysical
21900206
TBC14_HUMANTBC1D14physical
21900206
CEBPZ_HUMANCEBPZphysical
21900206
1433Z_HUMANYWHAZphysical
21900206
TTC3_HUMANTTC3physical
21900206
SAP_HUMANPSAPphysical
21900206
P53_HUMANTP53physical
19364824
NCOA3_HUMANNCOA3physical
16951183
MK06_HUMANMAPK6physical
22645313
HIF1N_HUMANHIF1ANphysical
22645313
NEUL4_HUMANNEURL4physical
22645313
HERC2_HUMANHERC2physical
22645313
PSMD4_HUMANPSMD4physical
22645313
ESR1_HUMANESR1physical
22865929
UB2L3_HUMANUBE2L3physical
17603074
HERC2_HUMANHERC2physical
21493713
UBE3A_HUMANUBE3Aphysical
15331633
UB2L3_HUMANUBE2L3physical
17433363
UB2L6_HUMANUBE2L6physical
17433363
P53_HUMANTP53physical
8090726
PSMD4_HUMANPSMD4physical
22350919
UBC_HUMANUBCphysical
9575161
UBE3A_HUMANUBE3Aphysical
9575161
ASPM_HUMANASPMphysical
21633703
UBE3A_HUMANUBE3Aphysical
22496338
EAPP_HUMANEAPPphysical
16713569
JADE1_HUMANJADE1physical
16713569
RARA_HUMANRARAphysical
16713569
SCAM1_HUMANSCAMP1physical
16713569
SODC_HUMANSOD1physical
23040663
HSP74_HUMANHSPA4physical
23040663
P53_HUMANTP53physical
23040663
UB2L3_HUMANUBE2L3physical
10373495
UB2L3_HUMANUBE2L3physical
19204938
UB2L3_HUMANUBE2L3physical
19364824
UB2D3_HUMANUBE2D3physical
11486026
MDM2_HUMANMDM2physical
11486026
UB2D1_HUMANUBE2D1physical
15001357
P53_HUMANTP53physical
15001357
UB2L3_HUMANUBE2L3physical
20351251
UB2L3_HUMANUBE2L3physical
9688277
UB2L3_HUMANUBE2L3physical
19591933
UB2D1_HUMANUBE2D1physical
8090726
UB2D1_HUMANUBE2D1physical
9575161
UB2L3_HUMANUBE2L3physical
9575161
UB2L3_HUMANUBE2L3physical
20589759
UB2D2_HUMANUBE2D2physical
19325566
A4_HUMANAPPphysical
21832049
UBP14_HUMANUSP14physical
22939629
UN45A_HUMANUNC45Aphysical
22939629
UFD1_HUMANUFD1Lphysical
22939629
ANDR_HUMANARphysical
16254014
P53_HUMANTP53physical
16493710
UBC_HUMANUBCphysical
23439649
P53_HUMANTP53physical
11027293
SCRIB_HUMANSCRIBphysical
11027293
CEBPA_HUMANCEBPAphysical
23598402
PTN3_HUMANPTPN3physical
17166906
NC2B_HUMANDR1physical
22863883
HSF1_HUMANHSF1physical
22863883
IPO11_HUMANIPO11physical
22863883
LSM1_HUMANLSM1physical
22863883
UBE3A_HUMANUBE3Aphysical
24273172
UB2L3_HUMANUBE2L3physical
11027293
BMAL1_HUMANARNTLphysical
24728990
JADE1_HUMANJADE1physical
24722188
MAGA8_HUMANMAGEA8physical
24722188
MEOX2_HUMANMEOX2physical
24722188
ATTY_HUMANTATphysical
24722188
UB2D1_HUMANUBE2D1physical
19240029
AHSP_HUMANAHSPphysical
25416956
ASAP3_HUMANASAP3physical
25416956
ATG9A_HUMANATG9Aphysical
25416956
KLH38_HUMANKLHL38physical
25416956
UB2D1_HUMANUBE2D1physical
8576257
UB2L3_HUMANUBE2L3physical
8576257
UB2E1_HUMANUBE2E1physical
8576257
PSMD4_HUMANPSMD4physical
24743594
ADRM1_HUMANADRM1physical
24743594
UCHL5_HUMANUCHL5physical
24743594
PRS6A_HUMANPSMC3physical
24743594
UB2D1_HUMANUBE2D1physical
24743594
UB2D2_HUMANUBE2D2physical
24743594
UB2D3_HUMANUBE2D3physical
24743594
P53_HUMANTP53physical
9450543
UB2D1_HUMANUBE2D1physical
9450543
P53_HUMANTP53physical
7708685
UB2E1_HUMANUBE2E1physical
9153201
UB2L3_HUMANUBE2L3physical
9153201
RD23A_HUMANRAD23Aphysical
9153201
UB2L3_HUMANUBE2L3physical
17131388
K2C1_HUMANKRT1physical
26506232
K2C6B_HUMANKRT6Bphysical
26506232
PDIA3_HUMANPDIA3physical
26506232
ARP3_HUMANACTR3physical
26506232
GFAP_HUMANGFAPphysical
26506232
MNT_HUMANMNTphysical
26506232
UBE3A_HUMANUBE3Aphysical
26506232
PDIA6_HUMANPDIA6physical
26506232
K2C7_HUMANKRT7physical
26506232
CALR_HUMANCALRphysical
26506232
K1C9_HUMANKRT9physical
26506232
TF3C1_HUMANGTF3C1physical
26506232
K2C5_HUMANKRT5physical
26506232
GRP78_HUMANHSPA5physical
26506232
MDM1_HUMANMDM1physical
26506232
ACTB_HUMANACTBphysical
26506232
ACTBL_HUMANACTBL2physical
26506232
TALDO_HUMANTALDO1physical
26506232
ACTA_HUMANACTA2physical
26506232
HS90B_HUMANHSP90AB1physical
26506232
RS15A_HUMANRPS15Aphysical
26506232
ISK1_HUMANSPINK1physical
26506232
GDIR2_HUMANARHGDIBphysical
26506232
UBE3A_HUMANUBE3Aphysical
26216987
RING2_HUMANRNF2physical
26216987
UB2D2_HUMANUBE2D2physical
26216987
UB2L3_HUMANUBE2L3physical
26216987
RD23A_HUMANRAD23Aphysical
26216987
P53_HUMANTP53physical
26789255
UBE3A_HUMANUBE3Aphysical
17426036
UB2D1_HUMANUBE2D1physical
17426036
RD23A_HUMANRAD23Aphysical
17426036
UB2D2_HUMANUBE2D2physical
7724550
P53_HUMANTP53physical
7724550
ANDR_HUMANARphysical
27903893
UB2D1_HUMANUBE2D1physical
27903893
CTNB1_HUMANCTNNB1physical
27902311
UB2D2_HUMANUBE2D2physical
27902311
E2F1_HUMANE2F1physical
28074012
RD23A_HUMANRAD23Aphysical
15263005
UB2L3_HUMANUBE2L3physical
15263005
UBE3A_HUMANUBE3Aphysical
15263005
CSN6_HUMANCOPS6physical
26318036
WBP2_HUMANWBP2physical
16772533
UB2L3_HUMANUBE2L3physical
28244869
MAP1B_MOUSEMap1bphysical
28957379
UB2L3_HUMANUBE2L3physical
28957379

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
105830Angelman syndrome (AS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBE3A_HUMAN

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Related Literatures of Post-Translational Modification
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-218, 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-218, AND MASSSPECTROMETRY.

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