ATX3_HUMAN - dbPTM
ATX3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATX3_HUMAN
UniProt AC P54252
Protein Name Ataxin-3
Gene Name ATXN3
Organism Homo sapiens (Human).
Sequence Length 361
Subcellular Localization Nucleus matrix . Predominantly nuclear, but not exclusively, inner nuclear matrix.
Protein Description Deubiquitinating enzyme involved in protein homeostasis maintenance, transcription, cytoskeleton regulation, myogenesis and degradation of misfolded chaperone substrates. [PubMed: 12297501]
Protein Sequence MESIFHEKQEGSLCAQHCLNNLLQGEYFSPVELSSIAHQLDEEERMRMAEGGVTSEDYRTFLQQPSGNMDDSGFFSIQVISNALKVWGLELILFNSPEYQRLRIDPINERSFICNYKEHWFTVRKLGKQWFNLNSLLTGPELISDTYLALFLAQLQQEGYSIFVVKGDLPDCEADQLLQMIRVQQMHRPKLIGEELAQLKEQRVHKTDLERVLEANDGSGMLDEDEEDLQRALALSRQEIDMEDEEADLRRAIQLSMQGSSRNISQDMTQTSGTNLTSEELRKRREAYFEKQQQKQQQQQQQQQQGDLSGQSSHPCERPATSSGALGSDLGDAMSEEDMLQAAVTMSLETVRNDLKTEGKK
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
12PhosphorylationFHEKQEGSLCAQHCL
CCCCCCCCHHHHHHH
21.37-
27PhosphorylationNNLLQGEYFSPVELS
HHHHCCCCCCHHHHH
19.0428796482
29PhosphorylationLLQGEYFSPVELSSI
HHCCCCCCHHHHHHH
27.4328796482
54PhosphorylationRMAEGGVTSEDYRTF
HHHHCCCCHHHHHHH
29.6729978859
55PhosphorylationMAEGGVTSEDYRTFL
HHHCCCCHHHHHHHH
26.5129978859
58PhosphorylationGGVTSEDYRTFLQQP
CCCCHHHHHHHHCCC
13.9129978859
60PhosphorylationVTSEDYRTFLQQPSG
CCHHHHHHHHCCCCC
23.59-
62 (in isoform 3)Ubiquitination-4.5821890473
117UbiquitinationRSFICNYKEHWFTVR
CCCCCCCHHHEEEHH
29.1621890473
117 (in isoform 1)Ubiquitination-29.1621890473
117 (in isoform 2)Ubiquitination-29.1621890473
135 (in isoform 3)Ubiquitination-28.1121890473
145 (in isoform 3)Ubiquitination-32.1721890473
151 (in isoform 3)Ubiquitination-4.4021890473
166SumoylationGYSIFVVKGDLPDCE
CCEEEEEECCCCCCC
41.21-
180SulfoxidationEADQLLQMIRVQQMH
CHHHHHHHHHHHHHC
1.8221406390
190 (in isoform 2)Ubiquitination-53.3321890473
190 (in isoform 1)Ubiquitination-53.3321890473
190UbiquitinationVQQMHRPKLIGEELA
HHHHCCCCHHHHHHH
53.3321890473
200UbiquitinationGEELAQLKEQRVHKT
HHHHHHHHHHHCCCC
39.4621890473
200AcetylationGEELAQLKEQRVHKT
HHHHHHHHHHHCCCC
39.4625953088
200 (in isoform 1)Ubiquitination-39.4621890473
200 (in isoform 2)Ubiquitination-39.4621890473
206UbiquitinationLKEQRVHKTDLERVL
HHHHHCCCCHHHHHH
40.6621890473
206 (in isoform 1)Ubiquitination-40.6621890473
206 (in isoform 2)Ubiquitination-40.6621890473
219PhosphorylationVLEANDGSGMLDEDE
HHHHCCCCCCCCCCH
24.7221815630
236 (in isoform 3)Ubiquitination-26.7221890473
236PhosphorylationLQRALALSRQEIDME
HHHHHHHHHHHCCCC
26.7227251275
242SulfoxidationLSRQEIDMEDEEADL
HHHHHCCCCCHHHHH
9.5621406390
256PhosphorylationLRRAIQLSMQGSSRN
HHHHHHHHHCCCCCC
7.8417434145
257SulfoxidationRRAIQLSMQGSSRNI
HHHHHHHHCCCCCCC
7.7121406390
260PhosphorylationIQLSMQGSSRNISQD
HHHHHCCCCCCCCCC
14.8328857561
261PhosphorylationQLSMQGSSRNISQDM
HHHHCCCCCCCCCCC
35.8528857561
265PhosphorylationQGSSRNISQDMTQTS
CCCCCCCCCCCHHCC
24.5525159151
268SulfoxidationSRNISQDMTQTSGTN
CCCCCCCCHHCCCCC
2.0121406390
269PhosphorylationRNISQDMTQTSGTNL
CCCCCCCHHCCCCCC
36.6628857561
271PhosphorylationISQDMTQTSGTNLTS
CCCCCHHCCCCCCCH
21.6929888752
272PhosphorylationSQDMTQTSGTNLTSE
CCCCHHCCCCCCCHH
33.5321815630
274PhosphorylationDMTQTSGTNLTSEEL
CCHHCCCCCCCHHHH
27.1627486199
278PhosphorylationTSGTNLTSEELRKRR
CCCCCCCHHHHHHHH
32.04-
291 (in isoform 2)Ubiquitination-43.4321890473
291 (in isoform 1)Ubiquitination-43.4321890473
291UbiquitinationRREAYFEKQQQKQQQ
HHHHHHHHHHHHHHH
43.4321890473
328PhosphorylationTSSGALGSDLGDAMS
CCCCCCCCCHHHCCC
30.43-
335PhosphorylationSDLGDAMSEEDMLQA
CCHHHCCCHHHHHHH
27.92-
347PhosphorylationLQAAVTMSLETVRND
HHHHHHHCHHHHHHH
4.65-
360AcetylationNDLKTEGKK------
HHHHHCCCC------
18.1136760807

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
236SPhosphorylationKinaseCSNK2A1P68400
GPS
236SPhosphorylationKinaseCK2-FAMILY-GPS
256SPhosphorylationKinaseGSK3BP49841
PSP
335SPhosphorylationKinaseCSNK2A1P68400
GPS
335SPhosphorylationKinaseCK2-FAMILY-GPS
347SPhosphorylationKinaseCSNK2A1P68400
GPS
347SPhosphorylationKinaseCK2-FAMILY-GPS
-KUbiquitinationE3 ubiquitin ligaseSTUB1Q9UNE7
PMID:24106274
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20804422
-KUbiquitinationE3 ubiquitin ligaseUBE4BO95155
PMID:14749733
-KUbiquitinationE3 ubiquitin ligaseMARCHF8Q5T0T0
PMID:22199232
-KUbiquitinationE3 ubiquitin ligasePRKNO60260
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseMARCHF5Q9NX47
PMID:20851218

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATX3_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 ATX3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TERA_HUMANVCPphysical
12944474
RD23A_HUMANRAD23Aphysical
10915768
RD23B_HUMANRAD23Bphysical
10915768
UBC_HUMANUBCphysical
18599482
UBP13_HUMANUSP13physical
19615732
OTUB2_HUMANOTUB2physical
19615732
BACD3_HUMANKCTD10physical
19615732
UBC_HUMANUBCphysical
16118278
UBC_HUMANUBCphysical
16040601
HDAC3_HUMANHDAC3physical
17079677
NCOR1_HUMANNCOR1physical
17079677
CBP_HUMANCREBBPphysical
12297501
EP300_HUMANEP300physical
12297501
KAT2B_HUMANKAT2Bphysical
12297501
TERA_HUMANVCPphysical
14749733
UBE4B_HUMANUBE4Bphysical
14749733
XRCC6_HUMANXRCC6physical
17885668
CBP_HUMANCREBBPphysical
17885668
CHIP_HUMANSTUB1physical
21855799
PRKN_HUMANPARK2physical
20940148
RD23B_HUMANRAD23Bphysical
19843543
TERA_HUMANVCPphysical
19843543
CHIP_HUMANSTUB1physical
20943656
PRKN_HUMANPARK2physical
22081612
FOXO4_HUMANFOXO4physical
21536589
UBC_HUMANUBCphysical
20622874
UBE2S_HUMANUBE2Sphysical
20622874
TRAF6_HUMANTRAF6physical
20622874
TERA_HUMANVCPphysical
16822850
PRS8_HUMANPSMC5physical
17302910
TERA_HUMANVCPphysical
19175675
UBC_HUMANUBCphysical
20865150
CSK2B_HUMANCSNK2Bphysical
18839019
ATX3_HUMANATXN3physical
16194547
UBC_HUMANUBCphysical
12857950
CREB1_HUMANCREB1physical
11572863
PML_HUMANPMLphysical
11572863
UBC_HUMANUBCphysical
14602712
TBB2B_RATTubb2bphysical
19666135
TBA1A_RATTuba1aphysical
19666135
TBB4B_RATTubb4bphysical
19666135
CNTFR_RATCntfrphysical
19666135
HAP1_HUMANHAP1physical
21386698
GSK3B_HUMANGSK3Bphysical
17434145
RHG19_HUMANARHGAP19physical
16713569
EWS_HUMANEWSR1physical
16713569
CP070_HUMANC16orf70physical
16713569
RD23A_HUMANRAD23Aphysical
16713569
RD23B_HUMANRAD23Bphysical
16713569
TEX11_HUMANTEX11physical
16713569
PICK1_HUMANPICK1physical
16713569
RD23A_HUMANRAD23Aphysical
22970133
TERA_HUMANVCPphysical
22970133
ATX3_HUMANATXN3physical
21780213
NEDD8_HUMANNEDD8physical
17935801
GDIR1_HUMANARHGDIAphysical
15952105
ASIC1_HUMANASIC1physical
15952105
SUMO1_HUMANSUMO1physical
15952105
A4_HUMANAPPphysical
21832049
ATX3_HUMANATXN3physical
22129356
B2CL1_HUMANBCL2L1physical
23562578
ELOA1_YEASTELA1physical
23993092
ELOC_YEASTELC1physical
23993092
PRKN_HUMANPARK2physical
24063750
SYVN1_HUMANSYVN1physical
24068323
UBC_HUMANUBCphysical
23625928
MGRN1_HUMANMGRN1physical
24769000
ITCH_HUMANITCHphysical
24865853
TERA_HUMANVCPphysical
25231079
UBC_HUMANUBCphysical
25231079
UBC_HUMANUBCphysical
25144244
SQSTM_HUMANSQSTM1physical
25158237
UBC_HUMANUBCphysical
21118805
UBC_HUMANUBCphysical
25988170
UBC_HUMANUBCphysical
25527291
UBC_HUMANUBCphysical
25448680
CALX_HUMANCANXphysical
26496610
SDC2_HUMANSDC2physical
26496610
4F2_HUMANSLC3A2physical
26496610
SORCN_HUMANSRIphysical
26496610
BCL7C_HUMANBCL7Cphysical
26496610
RSF1_HUMANRSF1physical
26496610
TMCO1_HUMANTMCO1physical
26496610
CNOT6_HUMANCNOT6physical
26496610
CAMP3_HUMANCAMSAP3physical
26496610
PSRC1_HUMANPSRC1physical
26496610
NDUF2_HUMANNDUFAF2physical
26496610
TIM23_HUMANTIMM23physical
26496610
1A02_HUMANHLA-Aphysical
26496610
1A03_HUMANHLA-Aphysical
26496610
1A01_HUMANHLA-Aphysical
26496610
1A26_HUMANHLA-Aphysical
26496610
TERA_HUMANVCPphysical
27851749
HS90A_HUMANHSP90AA1physical
27851749
P53_HUMANTP53physical
27851749
TERA_HUMANVCPphysical
28275011
MDC1_HUMANMDC1physical
28275011
UBC_HUMANUBCphysical
28918024
SDHB_HUMANSDHBphysical
29111377
COA7_HUMANCOA7physical
29111377
SERPH_HUMANSERPINH1physical
29111377
NDUA4_HUMANNDUFA4physical
29111377
ACLY_HUMANACLYphysical
29111377
UBB_HUMANUBBphysical
29111377
HS105_HUMANHSPH1physical
29111377
F184B_HUMANFAM184Bphysical
29111377
GNPAT_HUMANGNPATphysical
29111377
CDK4_HUMANCDK4physical
29111377
HSDL2_HUMANHSDL2physical
29111377
HSP7C_HUMANHSPA8physical
29111377
RDH13_HUMANRDH13physical
29111377
GHC1_HUMANSLC25A22physical
29111377
SDHA_HUMANSDHAphysical
29111377
ADT2_HUMANSLC25A5physical
29111377
RHOG_HUMANRHOGphysical
29111377
SFXN4_HUMANSFXN4physical
29111377
MALT1_HUMANMALT1physical
29111377
HS74L_HUMANHSPA4Lphysical
29111377
ACOT9_HUMANACOT9physical
29111377
S27A4_HUMANSLC27A4physical
29111377
TXTP_HUMANSLC25A1physical
29111377
ADT3_HUMANSLC25A6physical
29111377
SEH1_HUMANSEH1Lphysical
29111377
DIC_HUMANSLC25A10physical
29111377
DNM1L_HUMANDNM1Lphysical
29111377
CAF17_HUMANIBA57physical
29111377
MTDC_HUMANMTHFD2physical
29111377
MPCP_HUMANSLC25A3physical
29111377
UBAC2_HUMANUBAC2physical
29111377
MGME1_HUMANMGME1physical
29111377
TECR_HUMANTECRphysical
29111377
ARFP2_HUMANARFIP2physical
29111377
RMD1_HUMANRMDN1physical
29111377
CH082_HUMANC8orf82physical
29111377
PCAT1_HUMANLPCAT1physical
29111377
IDH3B_HUMANIDH3Bphysical
29111377
DX39A_HUMANDDX39Aphysical
29111377
ALG1_HUMANALG1physical
29111377
RLA0_HUMANRPLP0physical
29111377
MARH5_HUMANMARCH5physical
29111377
PRPS1_HUMANPRPS1physical
29111377
RAB21_HUMANRAB21physical
29111377
MOT1_HUMANSLC16A1physical
29111377
KBL_HUMANGCATphysical
29111377
DNJA1_HUMANDNAJA1physical
29111377
NDUA8_HUMANNDUFA8physical
29111377
CISD2_HUMANCISD2physical
29111377
DHB11_HUMANHSD17B11physical
29111377
MCU_HUMANMCUphysical
29111377
CHIP_HUMANSTUB1physical
29111377

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
109150Spinocerebellar ataxia 3 (SCA3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ATX3_HUMAN

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Related Literatures of Post-Translational Modification

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