ATX7_HUMAN - dbPTM
ATX7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATX7_HUMAN
UniProt AC O15265
Protein Name Ataxin-7
Gene Name ATXN7
Organism Homo sapiens (Human).
Sequence Length 892
Subcellular Localization Isoform a: Nucleus. Nucleus, nucleolus. Nucleus matrix. Cytoplasm, cytoskeleton. In addition to a diffuse distribution throughout the nucleus, it is associated with the nuclear matrix and the nucleolus. It is able to shuttle between the nucleus and c
Protein Description Acts as component of the STAGA transcription coactivator-HAT complex. Mediates the interaction of STAGA complex with the CRX and is involved in CRX-dependent gene activation. Necessary for microtubule cytoskeleton stabilization..
Protein Sequence MSERAADDVRGEPRRAAAAAGGAAAAAARQQQQQQQQQQPPPPQPQRQQHPPPPPRRTRPEDGGPGAASTSAAAMATVGERRPLPSPEVMLGQSWNLWVEASKLPGKDGTELDESFKEFGKNREVMGLCREDMPIFGFCPAHDDFYLVVCNDCNQVVKPQAFQSHYERRHSSSSKPPLAVPPTSVFSFFPSLSKSKGGSASGSNRSSSGGVLSASSSSSKLLKSPKEKLQLRGNTRPMHPIQQSRVPHGRIMTPSVKVEKIHPKMDGTLLKSAVGPTCPATVSSLVKPGLNCPSIPKPTLPSPGQILNGKGLPAPPTLEKKPEDNSNNRKFLNKRLSEREFDPDIHCGVIDLDTKKPCTRSLTCKTHSLTQRRAVQGRRKRFDVLLAEHKNKTREKELIRHPDSQQPPQPLRDPHPAPPRTSQEPHQNPHGVIPSESKPFVASKPKPHTPSLPRPPGCPAQQGGSAPIDPPPVHESPHPPLPATEPASRLSSEEGEGDDKEESVEKLDCHYSGHHPQPASFCTFGSRQIGRGYYVFDSRWNRLRCALNLMVEKHLNAQLWKKIPPVPSTTSPISTRIPHRTNSVPTSQCGVSYLAAATVSTSPVLLSSTCISPNSKSVPAHGTTLNAQPAASGAMDPVCSMQSRQVSSSSSSPSTPSGLSSVPSSPMSRKPQKLKSSKSLRPKESSGNSTNCQNASSSTSGGSGKKRKNSSPLLVHSSSSSSSSSSSSHSMESFRKNCVAHSGPPYPSTVTSSHSIGLNCVTNKANAVNVRHDQSGRGPPTGSPAESIKRMSVMVNSSDSTLSLGPFIHQSNELPVNSHGSFSHSHTPLDKLIGKKRKCSPSSSSINNSSSKPTKVAKVPAVNNVHMKHTGTIPGAQGLMNSSLLHQPKARP
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
6 (in isoform 3)Phosphorylation-21.5426657352
69PhosphorylationDGGPGAASTSAAAMA
CCCCCHHHHHHHHHH		23.51-
70PhosphorylationGGPGAASTSAAAMAT
CCCCHHHHHHHHHHC		20.05-
71PhosphorylationGPGAASTSAAAMATV
CCCHHHHHHHHHHCC		17.2628464451
77PhosphorylationTSAAAMATVGERRPL
HHHHHHHCCCCCCCC		18.8928464451
86PhosphorylationGERRPLPSPEVMLGQ
CCCCCCCCHHHHCCC		41.1823898821
107AcetylationEASKLPGKDGTELDE
HHHCCCCCCCCCCCH		51.5526051181
115PhosphorylationDGTELDESFKEFGKN
CCCCCCHHHHHHCCC		41.0821815630
117AcetylationTELDESFKEFGKNRE
CCCCHHHHHHCCCHH		62.5026051181
206PhosphorylationSASGSNRSSSGGVLS
CCCCCCCCCCCCCEE		32.8625954137
207PhosphorylationASGSNRSSSGGVLSA
CCCCCCCCCCCCEEC		29.7525627689
213PhosphorylationSSSGGVLSASSSSSK
CCCCCCEECCCCCCH		24.5725954137
215PhosphorylationSGGVLSASSSSSKLL
CCCCEECCCCCCHHH		27.6425627689
216PhosphorylationGGVLSASSSSSKLLK
CCCEECCCCCCHHHC		33.6825159151
217PhosphorylationGVLSASSSSSKLLKS
CCEECCCCCCHHHCC		35.8125627689
218PhosphorylationVLSASSSSSKLLKSP
CEECCCCCCHHHCCH		33.1825627689
219PhosphorylationLSASSSSSKLLKSPK
EECCCCCCHHHCCHH		29.3025159151
220AcetylationSASSSSSKLLKSPKE
ECCCCCCHHHCCHHH		60.8425953088
224PhosphorylationSSSKLLKSPKEKLQL
CCCHHHCCHHHHHHH		40.9724719451
235PhosphorylationKLQLRGNTRPMHPIQ
HHHHCCCCCCCCCCC		38.6930266825
244PhosphorylationPMHPIQQSRVPHGRI
CCCCCCCCCCCCCCC		20.9030266825
253PhosphorylationVPHGRIMTPSVKVEK
CCCCCCCCCCEEEEE		15.2729449344
255PhosphorylationHGRIMTPSVKVEKIH
CCCCCCCCEEEEECC		25.9629449344
257SumoylationRIMTPSVKVEKIHPK
CCCCCCEEEEECCCC		49.35-
257AcetylationRIMTPSVKVEKIHPK
CCCCCCEEEEECCCC		49.3525953088
257SumoylationRIMTPSVKVEKIHPK
CCCCCCEEEEECCCC		49.3528112733
302PhosphorylationIPKPTLPSPGQILNG
CCCCCCCCCCCCCCC		44.7925159151
317PhosphorylationKGLPAPPTLEKKPED
CCCCCCCCCCCCCCC		46.6328555341
337PhosphorylationKFLNKRLSEREFDPD
HHHHHHHHHCCCCCC		38.3424247654
361PhosphorylationTKKPCTRSLTCKTHS
CCCCCCCCCCCCCCC		15.18-
438AcetylationGVIPSESKPFVASKP
CCCCCCCCCCCCCCC		38.1223236377
443O-linked_GlycosylationESKPFVASKPKPHTP
CCCCCCCCCCCCCCC		44.1629351928
476PhosphorylationDPPPVHESPHPPLPA
CCCCCCCCCCCCCCC		17.4026657352
484PhosphorylationPHPPLPATEPASRLS
CCCCCCCCCCHHHCC		40.3326657352
491PhosphorylationTEPASRLSSEEGEGD
CCCHHHCCCCCCCCC		34.2929255136
492PhosphorylationEPASRLSSEEGEGDD
CCHHHCCCCCCCCCC		44.2329255136
503PhosphorylationEGDDKEESVEKLDCH
CCCCHHHHHHHHHCC		36.3520873877
531MethylationFGSRQIGRGYYVFDS
ECCCEECCCEEEECH		31.41-
533PhosphorylationSRQIGRGYYVFDSRW
CCEECCCEEEECHHH		8.6222210691
534PhosphorylationRQIGRGYYVFDSRWN
CEECCCEEEECHHHH		9.4722210691
561UbiquitinationHLNAQLWKKIPPVPS
HHHHHHHHHCCCCCC		49.79-
568PhosphorylationKKIPPVPSTTSPIST
HHCCCCCCCCCCCCC		44.5530624053
569PhosphorylationKIPPVPSTTSPISTR
HCCCCCCCCCCCCCC		25.8127732954
570PhosphorylationIPPVPSTTSPISTRI
CCCCCCCCCCCCCCC		36.5225159151
571PhosphorylationPPVPSTTSPISTRIP
CCCCCCCCCCCCCCC		21.9625159151
574PhosphorylationPSTTSPISTRIPHRT
CCCCCCCCCCCCCCC		18.2827050516
575PhosphorylationSTTSPISTRIPHRTN
CCCCCCCCCCCCCCC		33.0827732954
598PhosphorylationVSYLAAATVSTSPVL
HHHHHCCEECCCCEE		15.4028348404
600PhosphorylationYLAAATVSTSPVLLS
HHHCCEECCCCEEEE		20.8628348404
601PhosphorylationLAAATVSTSPVLLSS
HHCCEECCCCEEEEC		32.4828348404
602PhosphorylationAAATVSTSPVLLSST
HCCEECCCCEEEECE		12.9028348404
607PhosphorylationSTSPVLLSSTCISPN
CCCCEEEECEEECCC		21.3126074081
608PhosphorylationTSPVLLSSTCISPNS
CCCEEEECEEECCCC		27.5426074081
609PhosphorylationSPVLLSSTCISPNSK
CCEEEECEEECCCCC		15.5226074081
612PhosphorylationLLSSTCISPNSKSVP
EEECEEECCCCCCCC		21.8526074081
615PhosphorylationSTCISPNSKSVPAHG
CEEECCCCCCCCCCC		29.6826074081
617PhosphorylationCISPNSKSVPAHGTT
EECCCCCCCCCCCCE		32.9026074081
647PhosphorylationSMQSRQVSSSSSSPS
HCCCEECCCCCCCCC		19.0328348404
648PhosphorylationMQSRQVSSSSSSPST
CCCEECCCCCCCCCC		35.0728348404
649PhosphorylationQSRQVSSSSSSPSTP
CCEECCCCCCCCCCC		27.0821712546
650PhosphorylationSRQVSSSSSSPSTPS
CEECCCCCCCCCCCC		36.4628674151
651PhosphorylationRQVSSSSSSPSTPSG
EECCCCCCCCCCCCC		48.4921712546
652PhosphorylationQVSSSSSSPSTPSGL
ECCCCCCCCCCCCCC		25.4721712546
654PhosphorylationSSSSSSPSTPSGLSS
CCCCCCCCCCCCCCC		55.7028348404
655PhosphorylationSSSSSPSTPSGLSSV
CCCCCCCCCCCCCCC		25.5128348404
660PhosphorylationPSTPSGLSSVPSSPM
CCCCCCCCCCCCCCC		32.5821712546
664PhosphorylationSGLSSVPSSPMSRKP
CCCCCCCCCCCCCCC		44.9425159151
665PhosphorylationGLSSVPSSPMSRKPQ
CCCCCCCCCCCCCCC		20.6728985074
678AcetylationPQKLKSSKSLRPKES
CCCCCCCCCCCCCCC		61.6826210075
697PhosphorylationTNCQNASSSTSGGSG
CCCCCCCCCCCCCCC		34.9129449344
698PhosphorylationNCQNASSSTSGGSGK
CCCCCCCCCCCCCCC		24.8929449344
699PhosphorylationCQNASSSTSGGSGKK
CCCCCCCCCCCCCCC		33.0829449344
700PhosphorylationQNASSSTSGGSGKKR
CCCCCCCCCCCCCCC		43.0029449344
703PhosphorylationSSSTSGGSGKKRKNS
CCCCCCCCCCCCCCC		51.4725159151
710PhosphorylationSGKKRKNSSPLLVHS
CCCCCCCCCCEEEEC		36.0527080861
711PhosphorylationGKKRKNSSPLLVHSS
CCCCCCCCCEEEECC		29.0327470641
717PhosphorylationSSPLLVHSSSSSSSS
CCCEEEECCCCCCCC		25.1627080861
718PhosphorylationSPLLVHSSSSSSSSS
CCEEEECCCCCCCCC		21.2527080861
719PhosphorylationPLLVHSSSSSSSSSS
CEEEECCCCCCCCCC		36.9423312004
720PhosphorylationLLVHSSSSSSSSSSS
EEEECCCCCCCCCCC		35.8723312004
721PhosphorylationLVHSSSSSSSSSSSS
EEECCCCCCCCCCCC		35.8723312004
722PhosphorylationVHSSSSSSSSSSSSH
EECCCCCCCCCCCCC		35.8723312004
723PhosphorylationHSSSSSSSSSSSSHS
ECCCCCCCCCCCCCC		35.8727080861
724PhosphorylationSSSSSSSSSSSSHSM
CCCCCCCCCCCCCCH		35.8727080861
725PhosphorylationSSSSSSSSSSSHSME
CCCCCCCCCCCCCHH		35.8727080861
726PhosphorylationSSSSSSSSSSHSMES
CCCCCCCCCCCCHHH		37.5027080861
727PhosphorylationSSSSSSSSSHSMESF
CCCCCCCCCCCHHHH		33.7427080861
728PhosphorylationSSSSSSSSHSMESFR
CCCCCCCCCCHHHHH		22.8727080861
730PhosphorylationSSSSSSHSMESFRKN
CCCCCCCCHHHHHHH		26.6227080861
733PhosphorylationSSSHSMESFRKNCVA
CCCCCHHHHHHHHHH		23.0127080861
781PhosphorylationQSGRGPPTGSPAESI
CCCCCCCCCCHHHHH		54.1230266825
783PhosphorylationGRGPPTGSPAESIKR
CCCCCCCCHHHHHHE		24.3425849741
787PhosphorylationPTGSPAESIKRMSVM
CCCCHHHHHHEEEEE		35.20-
789AcetylationGSPAESIKRMSVMVN
CCHHHHHHEEEEEEC		51.8625953088
840PhosphorylationIGKKRKCSPSSSSIN
CCCCCCCCCCCCCCC		30.7423401153
842PhosphorylationKKRKCSPSSSSINNS
CCCCCCCCCCCCCCC		26.9328450419
843PhosphorylationKRKCSPSSSSINNSS
CCCCCCCCCCCCCCC		31.3328450419
844PhosphorylationRKCSPSSSSINNSSS
CCCCCCCCCCCCCCC		39.3128450419
845PhosphorylationKCSPSSSSINNSSSK
CCCCCCCCCCCCCCC		31.1423927012
849PhosphorylationSSSSINNSSSKPTKV
CCCCCCCCCCCCCEE		31.3430576142
850PhosphorylationSSSINNSSSKPTKVA
CCCCCCCCCCCCEEE		44.5030576142
851PhosphorylationSSINNSSSKPTKVAK
CCCCCCCCCCCEEEE		42.3427794612
854PhosphorylationNNSSSKPTKVAKVPA
CCCCCCCCEEEECCC		41.7223927012
872PhosphorylationVHMKHTGTIPGAQGL
EECCCCCCCCCCCHH		25.7524719451
882PhosphorylationGAQGLMNSSLLHQPK
CCCHHCCCHHHCCCC		14.3824719451
883PhosphorylationAQGLMNSSLLHQPKA
CCHHCCCHHHCCCCC		29.9124719451
899 (in isoform 2)Phosphorylation-27251275
901 (in isoform 2)Phosphorylation-30266825
902 (in isoform 2)Phosphorylation-30266825
905 (in isoform 2)Phosphorylation-30266825
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

Oops, there are no upstream regulatory protein records of ATX7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATX7_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 ATX7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CRX_HUMANCRXphysical
11580893
PRS4_HUMANPSMC1physical
11734547
PSMD2_HUMANPSMD2physical
11734547
PSMD7_HUMANPSMD7physical
11734547
PRS8_HUMANPSMC5physical
11734547
PRS7_HUMANPSMC2physical
11734547
PRS10_HUMANPSMC6physical
11734547
TRRAP_HUMANTRRAPphysical
18206972
UBP22_HUMANUSP22physical
18206972
KAT2A_HUMANKAT2Aphysical
18206972
AT7L3_HUMANATXN7L3physical
18206972
SUPT3_HUMANSUPT3Hphysical
18206972
TAF10_HUMANTAF10physical
18206972
TRRAP_HUMANTRRAPphysical
16494529
KAT2A_HUMANKAT2Aphysical
16494529
TAF12_HUMANTAF12physical
16494529
TRRAP_HUMANTRRAPphysical
15932940
EP300_HUMANEP300physical
15932940
KAT2A_HUMANKAT2Aphysical
15932940
TAF5L_HUMANTAF5Lphysical
15932940
TAD2A_HUMANTADA2Aphysical
15932940
TADA3_HUMANTADA3physical
15932940
TBP_HUMANTBPphysical
15932940
SUPT3_HUMANSUPT3Hphysical
15932940
SGF29_HUMANCCDC101physical
15932940
TAF9_HUMANTAF9physical
15932940
TAF12_HUMANTAF12physical
15932940
CRX_HUMANCRXphysical
15932940
TRRAP_HUMANTRRAPphysical
17375202
KAT2A_HUMANKAT2Aphysical
17375202
TAF10_HUMANTAF10physical
17375202
H3_YEASTHHT1physical
20634802
H2B1_YEASTHTB1physical
20634802
ACTN1_HUMANACTN1physical
21078624
ACTN2_HUMANACTN2physical
21078624
ACTN4_HUMANACTN4physical
21078624
ADA33_HUMANADAM33physical
21078624
AGRIN_HUMANAGRNphysical
21078624
CAR10_HUMANCARD10physical
21078624
CEP70_HUMANCEP70physical
21078624
CEP72_HUMANCEP72physical
21078624
COG6_HUMANCOG6physical
21078624
CRIM1_HUMANCRIM1physical
21078624
FBLN3_HUMANEFEMP1physical
21078624
FBLN4_HUMANEFEMP2physical
21078624
FBN1_HUMANFBN1physical
21078624
FINC_HUMANFN1physical
21078624
GOGA2_HUMANGOLGA2physical
21078624
GOGA3_HUMANGOLGA3physical
21078624
GASP1_HUMANGPRASP1physical
21078624
GRN_HUMANGRNphysical
21078624
JAG2_HUMANJAG2physical
21078624
KALRN_HUMANKALRNphysical
21078624
LAMB1_HUMANLAMB1physical
21078624
LAMB2_HUMANLAMB2physical
21078624
LRSM1_HUMANLRSAM1physical
21078624
LTBP4_HUMANLTBP4physical
21078624
MATN2_HUMANMATN2physical
21078624
MEGF6_HUMANMEGF6physical
21078624
MEGF8_HUMANMEGF8physical
21078624
MPRIP_HUMANMPRIPphysical
21078624
NELL1_HUMANNELL1physical
21078624
NELL2_HUMANNELL2physical
21078624
NOC2L_HUMANNOC2Lphysical
21078624
NUP62_HUMANNUP62physical
21078624
PNMA1_HUMANPNMA1physical
21078624
PP12C_HUMANPPP1R12Cphysical
21078624
RABE1_HUMANRABEP1physical
21078624
TRI27_HUMANTRIM27physical
21078624
RNF31_HUMANRNF31physical
21078624
SIAH1_HUMANSIAH1physical
21078624
SNX1_HUMANSNX1physical
21078624
SPY1_HUMANSPRY1physical
21078624
SSFA2_HUMANSSFA2physical
21078624
THY1_HUMANTHY1physical
21078624
TRAF2_HUMANTRAF2physical
21078624
TRI23_HUMANTRIM23physical
21078624
TRI54_HUMANTRIM54physical
21078624
TXD11_HUMANTXNDC11physical
21078624
UBQL2_HUMANUBQLN2physical
21078624
VWF_HUMANVWFphysical
21078624
SUMO1_HUMANSUMO1physical
19843541
SUMO2_HUMANSUMO2physical
19843541
UBP22_HUMANUSP22physical
21746879
AT7L3_HUMANATXN7L3physical
21746879
ENY2_HUMANENY2physical
21746879
PICK1_HUMANPICK1physical
16713569
ASPP2_HUMANTP53BP2physical
16713569
RD23A_HUMANRAD23Aphysical
16713569
GCN5_YEASTGCN5physical
24129567
UBP22_HUMANUSP22physical
26195632
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
164500Spinocerebellar ataxia 7 (SCA7)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ATX7_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-840; SER-849 ANDTHR-854, AND MASS SPECTROMETRY.
Sumoylation
ReferencePubMed
"SUMOylation attenuates the aggregation propensity and cellulartoxicity of the polyglutamine expanded ataxin-7.";
Janer A., Werner A., Takahashi-Fujigasaki J., Daret A., Fujigasaki H.,Takada K., Duyckaerts C., Brice A., Dejean A., Sittler A.;
Hum. Mol. Genet. 19:181-195(2010).
Cited for: SUMOYLATION AT LYS-257, AND MUTAGENESIS OF LYS-257 AND LYS-858.

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