SCA7
entrez
6314
canonical
uniprot
O15265
canonical
ensembl
ENSG00000163635
resolver
ensp
ENSP00000295900
resolver
ensp
ENSP00000420234
resolver
ensp
ENSP00000428067
resolver
ensp
ENSP00000428277
resolver
ensp
ENSP00000501377
resolver
genesymbol
ATXN7
resolver
genesymbol
SCA7
resolver
genesymbol_syn
SCA7
resolver
hgnc
HGNC:10560
resolver
uniprot
A0A0A6YYU1
resolver
uniprot
A0A0K0K1H5
resolver
uniprot
B4E207
resolver
uniprot
E9PHP9
resolver
uniprot
F6U365
resolver
uniprot
O75328
resolver
uniprot
O75329
resolver
uniprot
Q9UPD8
resolver
uniprot
Q9Y6P8
resolver
uniprot_entry
ATX7_HUMAN
resolver
uniprot_entry
Q9UPD8_HUMAN
resolver
uniprot_sec
A0A0A6YYU1
resolver
uniprot_sec
A0A0K0K1H5
resolver
uniprot_sec
B4E207
resolver
uniprot_sec
E9PHP9
resolver
uniprot_sec
F6U365
resolver
uniprot_sec
O75328
resolver
uniprot_sec
O75329
resolver
uniprot_sec
Q9Y6P8
resolver
amino_acid_sequence
MSERAADDVRGEPRRAAAAAGGAAAAAARQQQQQQQQQQPPPPQPQRQQHPPPPPRRTRPEDGGPGAASTSAAAMATVGERRPLPSPEVMLGQSWNLWVEASKLPGKDGTELDESFKEFGKNREVMGLCREDMPIFGFCPAHDDFYLVVCNDCNQVVKPQAFQSHYERRHSSSSKPPLAVPPTSVFSFFPSLSKSKGGSASGSNRSSSGGVLSASSSSSKLLKSPKEKLQLRGNTRPMHPIQQSRVPHGRIMTPSVKVEKIHPKMDGTLLKSAVGPTCPATVSSLVKPGLNCPSIPKPTLPSPGQILNGKGLPAPPTLEKKPEDNSNNRKFLNKRLSEREFDPDIHCGVIDLDTKKPCTRSLTCKTHSLTQRRAVQGRRKRFDVLLAEHKNKTREKELIRHPDSQQPPQPLRDPHPAPPRTSQEPHQNPHGVIPSESKPFVASKPKPHTPSLPRPPGCPAQQGGSAPIDPPPVHESPHPPLPATEPASRLSSEEGEGDDKEESVEKLDCHYSGHHPQPASFCTFGSRQIGRGYYVFDSRWNRLRCALNLMVEKHLNAQLWKKIPPVPSTTSPISTRIPHRTNSVPTSQCGVSYLAAATVSTSPVLLSSTCISPNSKSVPAHGTTLNAQPAASGAMDPVCSMQSRQVSSSSSSPSTPSGLSSVPSSPMSRKPQKLKSSKSLRPKESSGNSTNCQNASSSTSGGSGKKRKNSSPLLVHSSSSSSSSSSSSHSMESFRKNCVAHSGPPYPSTVTSSHSIGLNCVTNKANAVNVRHDQSGRGPPTGSPAESIKRMSVMVNSSDSTLSLGPFIHQSNELPVNSHGSFSHSHTPLDKLIGKKRKCSPSSSSINNSSSKPTKVAKVPAVNNVHMKHTGTIPGAQGLMNSSLLHQPKARP
uniprot
proteins
disease_involvement
DISEASE: Spinocerebellar ataxia 7 (SCA7) [MIM:164500]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA7 belongs to the autosomal dominant cerebellar ataxias type II (ADCA II) which are characterized by cerebellar ataxia with retinal degeneration and pigmentary macular dystrophy. {ECO:0000269|PubMed:9288099}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Acts as a component of the SAGA (aka STAGA) transcription coactivator-HAT complex (PubMed:15932940, PubMed:18206972). Mediates the interaction of SAGA complex with the CRX and is involved in CRX-dependent gene activation (PubMed:15932940, PubMed:18206972). Probably involved in tethering the deubiquitination module within the SAGA complex (PubMed:24493646). Necessary for microtubule cytoskeleton stabilization (PubMed:22100762). Involved in neurodegeneration (PubMed:9288099). {ECO:0000269|PubMed:15932940, ECO:0000269|PubMed:18206972, ECO:0000269|PubMed:22100762, ECO:0000269|PubMed:24493646, ECO:0000269|PubMed:9288099}.
uniprot
proteins
mass_dalton
95451
uniprot
proteins
mutagenesis
MUTAGEN 257; /note="K->R: Almost completely abolishes sumoylation."; /evidence="ECO:0000269|PubMed:19843541"; MUTAGEN 266; /note="D->N: Abolished cleavage by caspase-7 and attenuates formation of protein aggregates in SCA7 degeneration; when associated with N-344."; /evidence="ECO:0000269|PubMed:17646170"; MUTAGEN 344; /note="D->N: Abolished cleavage by caspase-7 and attenuates formation of protein aggregates in SCA7 degeneration; when associated with N-266."; /evidence="ECO:0000269|PubMed:17646170"; MUTAGEN 858; /note="K->R: No effect on sumoylation."; /evidence="ECO:0000269|PubMed:19843541
uniprot
proteins
post_translational_modification
PTM: Proteolytically cleaved by caspase-7 (CASP7) (PubMed:17646170). The cleavage may be involved in SCA7 degeneration: the isoform fragments may exert distinct toxic influences that could contribute to selective neurodegeneration (PubMed:17646170). {ECO:0000269|PubMed:17646170}.; PTM: Sumoylation decreases the aggregation propensity and cellular toxicity of forms with an expanded poly-Gln region but has no effect on subcellular location or interaction with components of the STAGA complex. {ECO:0000269|PubMed:19843541}.
uniprot
proteins
protein_family
Ataxin-7 family
uniprot
proteins
pubmed
10441328
uniprot
proteins
pubmed
11371513
uniprot
proteins
pubmed
11734547
uniprot
proteins
pubmed
12533095
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15115762
uniprot
proteins
pubmed
15932940
uniprot
proteins
pubmed
16314424
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
17646170
uniprot
proteins
pubmed
18206972
uniprot
proteins
pubmed
19843541
uniprot
proteins
pubmed
22100762
uniprot
proteins
pubmed
24493646
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
9288099
uniprot
proteins
pubmed
9425224
uniprot
proteins
sequence_length
892
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform a]: Nucleus {ECO:0000269|PubMed:12533095, ECO:0000269|PubMed:16314424, ECO:0000269|PubMed:22100762}. Nucleus, nucleolus {ECO:0000269|PubMed:10441328}. Nucleus matrix {ECO:0000269|PubMed:10441328}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22100762}. Note=In addition to a diffuse distribution throughout the nucleus, it is associated with the nuclear matrix and the nucleolus (PubMed:10441328). It is able to shuttle between the nucleus and cytoplasm (PubMed:16314424). {ECO:0000269|PubMed:10441328, ECO:0000269|PubMed:16314424}.; SUBCELLULAR LOCATION: [Isoform b]: Cytoplasm {ECO:0000269|PubMed:12533095}.
uniprot
proteins