O15265 (ATX7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ataxin-7

Alternative name(s):
Spinocerebellar ataxia type 7 protein

Gene names

Name:	ATXN7
Synonyms:	SCA7

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	892 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.14
Subunit structure	Component of the STAGA transcription coactivator-HAT complex, at least composed of SUPT3H, GCN5L2, TAF5L, TAF6L, SUPT7L, TADA3L, TAD1L, TAF10, TAF12, TRRAP, TAF9 and ATXN7. The STAGA core complex is associated with a subcomplex required for histone deubiquitination composed of ATXN7L3, ENY2 and USP22. Interacts with SORBS1, PSMC1 and CRX. Interacts with TRRAP, GCN5L2 and TAF10. Interacts with alpha tubulin. Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.14
Subcellular location	Isoform a: Nucleus. Nucleus › nucleolus. Nucleus matrix. Cytoplasm › cytoskeleton. Note: 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 cytoplasm. Ref.6 Ref.11 Ref.14 Isoform b: Cytoplasm Ref.6 Ref.11 Ref.14.
Tissue specificity	Isoform a and isoform b are expressed in CNS, but isoform a is expressed predominantly in the peripherical tissues. Isoform b is also highly expressed in the frontal lobe, skeletal muscle and spinal cord and is expressed at a lower level in the lung, lymphoblast and intestine.
Post-translational modification	Proteolytically cleaved. The cleavage may be involved in SCA7 degeneration: the isoform fragments may exert distinct toxic influences that could contribute to selective neurodegeneration. 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. Ref.13
Polymorphism	The poly-Gln region of ATXN7 is highly polymorphic (4 to 18 repeats) in the normal population and is expanded to about 38-130 repeats in SCA7 patients. Intermediate alleles with 28 to 35 repeats are prone to further expansion.
Involvement in 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1
Sequence similarities	Belongs to the ataxin-7 family. Contains 1 SCA7 domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing Polymorphism Triplet repeat expansion
Disease	Disease mutation Neurodegeneration Spinocerebellar ataxia
PTM	Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell death Inferred from electronic annotation. Source: UniProtKB-KW histone deubiquitination Inferred from direct assay Ref.12. Source: UniProtKB microtubule cytoskeleton organization Inferred from mutant phenotype Ref.14. Source: UniProtKB negative regulation of insulin-like growth factor receptor signaling pathway Inferred from electronic annotation. Source: Compara negative regulation of phosphorylation Inferred from electronic annotation. Source: Compara nucleus organization Traceable author statement Ref.6. Source: ProtInc positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW visual perception Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA microtubule cytoskeleton Inferred from direct assay Ref.14. Source: UniProtKB nuclear matrix Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.14. Source: UniProtKB
Molecular_function	chromatin binding Inferred from electronic annotation. Source: Compara zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AGRN	O00468	2	EBI-708350,EBI-947482
CEP72	Q9P209	2	EBI-708350,EBI-739498
LTBP4	Q8N2S1	2	EBI-708350,EBI-947718
MATN2	O00339	2	EBI-708350,EBI-949020
MEGF6	O75095	2	EBI-708350,EBI-947597
MEGF8	Q7Z7M0	2	EBI-708350,EBI-947617
NOC2L	Q9Y3T9	2	EBI-708350,EBI-751547
NUP62	P37198	2	EBI-708350,EBI-347978
SIAH1	Q8IUQ4	2	EBI-708350,EBI-747107
TAF10	Q12962	6	EBI-708350,EBI-708376
TRRAP	Q9Y4A5	6	EBI-708350,EBI-399128

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform a (identifier: O15265-1)

Also known as: Ataxin-7a;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform b (identifier: O15265-2)

Also known as: Ataxin-7b; SCA7b;

The sequence of this isoform differs from the canonical sequence as follows:
     888-892: PKARP → DISSPCLRTGISATSPQSPDLKSKGTSLTAENSTGRNNADTFEDKLHLHSALWTPRCL

Isoform 3 (identifier: O15265-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-166: MSERAADDVR...VKPQAFQSHY → MEGSKTPLQSSPSAQELKAPL

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 892

892

Ataxin-7

PRO_0000064759

Regions

Domain

334 – 401

68

SCA7

Compositional bias

16 – 20

5

Poly-Ala

Compositional bias

23 – 28

6

Poly-Ala

Compositional bias

30 – 49

20

Gln-rich

Compositional bias

30 – 39

10

Poly-Gln

Compositional bias

40 – 65

26

Pro-rich

Compositional bias

40 – 45

6

Poly-Pro

Compositional bias

51 – 55

5

Poly-Pro

Compositional bias

171 – 219

49

Ser-rich

Compositional bias

171 – 174

4

Poly-Ser

Compositional bias

213 – 219

7

Poly-Ser

Compositional bias

402 – 486

85

Pro-rich

Compositional bias

640 – 851

212

Ser-rich

Compositional bias

647 – 654

8

Poly-Ser

Compositional bias

717 – 730

14

Poly-Ser

Compositional bias

840 – 845

6

Poly-Ser

Amino acid modifications

Cross-link

257

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.13

Natural variations

Alternative sequence

1 – 166

166

MSERA…FQSHY → MEGSKTPLQSSPSAQELKAP L in isoform 3.

VSP_044456

Alternative sequence

888 – 892

5

PKARP → DISSPCLRTGISATSPQSPD LKSKGTSLTAENSTGRNNAD TFEDKLHLHSALWTPRCL in isoform b.

VSP_007695

Natural variant

264

1

K → R. Ref.2 Ref.3
Corresponds to variant rs1053338 [ dbSNP | Ensembl ].

VAR_011823

Natural variant

573

1

I → V.
Corresponds to variant rs3733124 [ dbSNP | Ensembl ].

VAR_053779

Natural variant

663

1

P → S.
Corresponds to variant rs1053340 [ dbSNP | Ensembl ].

VAR_011824

Natural variant

862

1

V → M. Ref.2 Ref.3
Corresponds to variant rs3774729 [ dbSNP | Ensembl ].

VAR_020143

Experimental info

Mutagenesis

257

1

K → R: Almost completely abolishes sumoylation. Ref.13

Mutagenesis

858

1

K → R: No effect on sumoylation. Ref.13

Sequence conflict

105

1

P → H in AAC19162. Ref.2

Sequence conflict

129

1

C → S in AAC19162. Ref.2

Sequence conflict

888 – 892

5

PKARP → VGNGL in AAC39765. Ref.2

Sequence conflict

888 – 892

5

PKARP → VGNGL in AAC19163. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

892

Helix Strand Turn

Details...

Turn

343 – 345

3

Turn

352 – 354

3

Helix

369 – 374

6

Beta strand

378 – 380

3

Helix

382 – 393

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform a (Ataxin-7a) [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 9AEA787D77103C5F	FASTA	892	95,451
	10 20 30 40 50 60 MSERAADDVR GEPRRAAAAA GGAAAAAARQ QQQQQQQQQP PPPQPQRQQH PPPPPRRTRP 70 80 90 100 110 120 EDGGPGAAST SAAAMATVGE RRPLPSPEVM LGQSWNLWVE ASKLPGKDGT ELDESFKEFG 130 140 150 160 170 180 KNREVMGLCR EDMPIFGFCP AHDDFYLVVC NDCNQVVKPQ AFQSHYERRH SSSSKPPLAV 190 200 210 220 230 240 PPTSVFSFFP SLSKSKGGSA SGSNRSSSGG VLSASSSSSK LLKSPKEKLQ LRGNTRPMHP 250 260 270 280 290 300 IQQSRVPHGR IMTPSVKVEK IHPKMDGTLL KSAVGPTCPA TVSSLVKPGL NCPSIPKPTL 310 320 330 340 350 360 PSPGQILNGK GLPAPPTLEK KPEDNSNNRK FLNKRLSERE FDPDIHCGVI DLDTKKPCTR 370 380 390 400 410 420 SLTCKTHSLT QRRAVQGRRK RFDVLLAEHK NKTREKELIR HPDSQQPPQP LRDPHPAPPR 430 440 450 460 470 480 TSQEPHQNPH GVIPSESKPF VASKPKPHTP SLPRPPGCPA QQGGSAPIDP PPVHESPHPP 490 500 510 520 530 540 LPATEPASRL SSEEGEGDDK EESVEKLDCH YSGHHPQPAS FCTFGSRQIG RGYYVFDSRW 550 560 570 580 590 600 NRLRCALNLM VEKHLNAQLW KKIPPVPSTT SPISTRIPHR TNSVPTSQCG VSYLAAATVS 610 620 630 640 650 660 TSPVLLSSTC ISPNSKSVPA HGTTLNAQPA ASGAMDPVCS MQSRQVSSSS SSPSTPSGLS 670 680 690 700 710 720 SVPSSPMSRK PQKLKSSKSL RPKESSGNST NCQNASSSTS GGSGKKRKNS SPLLVHSSSS 730 740 750 760 770 780 SSSSSSSSHS MESFRKNCVA HSGPPYPSTV TSSHSIGLNC VTNKANAVNV RHDQSGRGPP 790 800 810 820 830 840 TGSPAESIKR MSVMVNSSDS TLSLGPFIHQ SNELPVNSHG SFSHSHTPLD KLIGKKRKCS 850 860 870 880 890 PSSSSINNSS SKPTKVAKVP AVNNVHMKHT GTIPGAQGLM NSSLLHQPKA RP
	Isoform b (Ataxin-7b) (SCA7b) [UniParc]. Checksum: B230F94D3D468D77	FASTA	945	101,112
	10 20 30 40 50 60 MSERAADDVR GEPRRAAAAA GGAAAAAARQ QQQQQQQQQP PPPQPQRQQH PPPPPRRTRP 70 80 90 100 110 120 EDGGPGAAST SAAAMATVGE RRPLPSPEVM LGQSWNLWVE ASKLPGKDGT ELDESFKEFG 130 140 150 160 170 180 KNREVMGLCR EDMPIFGFCP AHDDFYLVVC NDCNQVVKPQ AFQSHYERRH SSSSKPPLAV 190 200 210 220 230 240 PPTSVFSFFP SLSKSKGGSA SGSNRSSSGG VLSASSSSSK LLKSPKEKLQ LRGNTRPMHP 250 260 270 280 290 300 IQQSRVPHGR IMTPSVKVEK IHPKMDGTLL KSAVGPTCPA TVSSLVKPGL NCPSIPKPTL 310 320 330 340 350 360 PSPGQILNGK GLPAPPTLEK KPEDNSNNRK FLNKRLSERE FDPDIHCGVI DLDTKKPCTR 370 380 390 400 410 420 SLTCKTHSLT QRRAVQGRRK RFDVLLAEHK NKTREKELIR HPDSQQPPQP LRDPHPAPPR 430 440 450 460 470 480 TSQEPHQNPH GVIPSESKPF VASKPKPHTP SLPRPPGCPA QQGGSAPIDP PPVHESPHPP 490 500 510 520 530 540 LPATEPASRL SSEEGEGDDK EESVEKLDCH YSGHHPQPAS FCTFGSRQIG RGYYVFDSRW 550 560 570 580 590 600 NRLRCALNLM VEKHLNAQLW KKIPPVPSTT SPISTRIPHR TNSVPTSQCG VSYLAAATVS 610 620 630 640 650 660 TSPVLLSSTC ISPNSKSVPA HGTTLNAQPA ASGAMDPVCS MQSRQVSSSS SSPSTPSGLS 670 680 690 700 710 720 SVPSSPMSRK PQKLKSSKSL RPKESSGNST NCQNASSSTS GGSGKKRKNS SPLLVHSSSS 730 740 750 760 770 780 SSSSSSSSHS MESFRKNCVA HSGPPYPSTV TSSHSIGLNC VTNKANAVNV RHDQSGRGPP 790 800 810 820 830 840 TGSPAESIKR MSVMVNSSDS TLSLGPFIHQ SNELPVNSHG SFSHSHTPLD KLIGKKRKCS 850 860 870 880 890 900 PSSSSINNSS SKPTKVAKVP AVNNVHMKHT GTIPGAQGLM NSSLLHQDIS SPCLRTGISA 910 920 930 940 TSPQSPDLKS KGTSLTAENS TGRNNADTFE DKLHLHSALW TPRCL
	Isoform 3 [UniParc]. Checksum: AE6215958E714C8E	FASTA	747	79,535
	10 20 30 40 50 60 MEGSKTPLQS SPSAQELKAP LERRHSSSSK PPLAVPPTSV FSFFPSLSKS KGGSASGSNR 70 80 90 100 110 120 SSSGGVLSAS SSSSKLLKSP KEKLQLRGNT RPMHPIQQSR VPHGRIMTPS VKVEKIHPKM 130 140 150 160 170 180 DGTLLKSAVG PTCPATVSSL VKPGLNCPSI PKPTLPSPGQ ILNGKGLPAP PTLEKKPEDN 190 200 210 220 230 240 SNNRKFLNKR LSEREFDPDI HCGVIDLDTK KPCTRSLTCK THSLTQRRAV QGRRKRFDVL 250 260 270 280 290 300 LAEHKNKTRE KELIRHPDSQ QPPQPLRDPH PAPPRTSQEP HQNPHGVIPS ESKPFVASKP 310 320 330 340 350 360 KPHTPSLPRP PGCPAQQGGS APIDPPPVHE SPHPPLPATE PASRLSSEEG EGDDKEESVE 370 380 390 400 410 420 KLDCHYSGHH PQPASFCTFG SRQIGRGYYV FDSRWNRLRC ALNLMVEKHL NAQLWKKIPP 430 440 450 460 470 480 VPSTTSPIST RIPHRTNSVP TSQCGVSYLA AATVSTSPVL LSSTCISPNS KSVPAHGTTL 490 500 510 520 530 540 NAQPAASGAM DPVCSMQSRQ VSSSSSSPST PSGLSSVPSS PMSRKPQKLK SSKSLRPKES 550 560 570 580 590 600 SGNSTNCQNA SSSTSGGSGK KRKNSSPLLV HSSSSSSSSS SSSHSMESFR KNCVAHSGPP 610 620 630 640 650 660 YPSTVTSSHS IGLNCVTNKA NAVNVRHDQS GRGPPTGSPA ESIKRMSVMV NSSDSTLSLG 670 680 690 700 710 720 PFIHQSNELP VNSHGSFSHS HTPLDKLIGK KRKCSPSSSS INNSSSKPTK VAKVPAVNNV 730 740 HMKHTGTIPG AQGLMNSSLL HQPKARP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of the SCA7 gene reveals a highly unstable CAG repeat expansion." David G., Abbas N., Stevanin G., Duerr A., Yvert G., Cancel G., Weber C., Imbert G., Saudou F., Antoniou E., Drabkin H., Gemmill R., Giunti P., Benomar A., Wood N., Ruberg M., Agid Y., Mandel J.-L., Brice A. Nat. Genet. 17:65-70(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), INVOLVEMENT IN SCA7. Tissue: Lymphoblast.
[2]	"Molecular genetic analysis of autosomal dominant cerebellar ataxia with retinal degeneration (ADCA type II) caused by CAG triplet repeat expansion." Del-Favero J., Krols L., Michalik A., Theuns J., Loefgren A., Goossens D., Wehnert A., Van den Bossche D., Van Zand K., Backhovens H., van Regenmorter N., Martin J.-J., Van Broeckhoven C. Hum. Mol. Genet. 7:177-186(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-131, POLYMORPHISM, VARIANTS ARG-264 AND MET-862. Tissue: Colon.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANTS ARG-264 AND MET-862. Tissue: Trachea.
[4]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"A novel central nervous system-enriched spinocerebellar ataxia type 7 gene product." Einum D.D., Clark A.M., Townsend J.J., Ptacek L.J., Fu Y.H. Arch. Neurol. 60:97-103(2003) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORMS A AND B). Tissue: Testis.
[6]	"Nuclear localization of the spinocerebellar ataxia type 7 protein, ataxin-7." Kaytor M.D., Duvick L.A., Skinner P.J., Koob M.D., Ranum L.P., Orr H.T. Hum. Mol. Genet. 8:1657-1664(1999) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[7]	"Ataxin-7 interacts with a Cbl-associated protein that it recruits into neuronal intranuclear inclusions." Lebre A.-S., Jamot L., Takahashi J., Spassky N., Leprince C., Ravise N., Zander C., Fujigasaki H., Kussel-Andermann P., Duyckaerts C., Camonis J.H., Brice A. Hum. Mol. Genet. 10:1201-1213(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SORBS1.
[8]	"Association of ataxin-7 with the proteasome subunit S4 of the 19S regulatory complex." Matilla A., Gorbea C., Einum D.D., Townsend J., Michalik A., van Broeckhoven C., Jensen C.C., Murphy K.J., Ptacek L.J., Fu Y.H. Hum. Mol. Genet. 10:2821-2831(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PSMC1.
[9]	"Ataxin-7 is a subunit of GCN5 histone acetyltransferase-containing complexes." Helmlinger D., Hardy S., Sasorith S., Klein F., Robert F., Weber C., Miguet L., Potier N., Van-Dorsselaer A., Wurtz J.M., Mandel J.L., Tora L., Devys D. Hum. Mol. Genet. 13:1257-1265(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TRRAP; GCN5L2 AND TAF10.
[10]	"Polyglutamine-expanded ataxin-7 inhibits STAGA histone acetyltransferase activity to produce retinal degeneration." Palhan V.B., Chen S., Peng G.H., Tjernberg A., Gamper A.M., Fan Y., Chait B.T., La Spada A.R., Roeder R.G. Proc. Natl. Acad. Sci. U.S.A. 102:8472-8477(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE STAGA COMPLEX.
[11]	"Ataxin-7 can export from the nucleus via a conserved exportin-dependent signal." Taylor J., Grote S.K., Xia J., Vandelft M., Graczyk J., Ellerby L.M., La Spada A.R., Truant R. J. Biol. Chem. 281:2730-2739(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[12]	"A TFTC/STAGA module mediates histone H2A and H2B deubiquitination, coactivates nuclear receptors, and counteracts heterochromatin silencing." Zhao Y., Lang G., Ito S., Bonnet J., Metzger E., Sawatsubashi S., Suzuki E., Le Guezennec X., Stunnenberg H.G., Krasnov A., Georgieva S.G., Schuele R., Takeyama K., Kato S., Tora L., Devys D. Mol. Cell 29:92-101(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN STAGA COMPLEX.
[13]	"SUMOylation attenuates the aggregation propensity and cellular toxicity 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) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION AT LYS-257, MUTAGENESIS OF LYS-257 AND LYS-858.
[14]	"Ataxin-7 associates with microtubules and stabilizes the cytoskeletal network." Nakamura Y., Tagawa K., Oka T., Sasabe T., Ito H., Shiwaku H., La Spada A.R., Okazawa H. Hum. Mol. Genet. 21:1099-1110(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ALPHA TUBULIN, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ000517 mRNA. Translation: CAA04154.1.
AF032102 Genomic DNA. Translation: AAC19162.1.
AF032103 mRNA. Translation: AAC19163.1.
AF032105 mRNA. Translation: AAC39765.1.
AK304062 mRNA. Translation: BAG64969.1.
AC012557 Genomic DNA. No translation available.
AC104162 Genomic DNA. No translation available.
AA398030 mRNA. No translation available.

IPI

IPI00005743.
IPI00332082.

PIR

T09193.

RefSeq

NP_000324.1. NM_000333.3.
NP_001121621.2. NM_001128149.2.
NP_001170858.1. NM_001177387.1.

UniGene

Hs.476595.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KKR	NMR	-	A	330-401	[»]

ProteinModelPortal

O15265.

ModBase

Search...

Protein-protein interaction databases

IntAct

O15265. 57 interactions.

MINT

MINT-2862470.

STRING

9606.ENSP00000381590.

PTM databases

PhosphoSite

O15265.

Proteomic databases

PaxDb

O15265.

PRIDE

O15265.

Protocols and materials databases

DNASU

6314.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000295900; ENSP00000295900; ENSG00000163635.
ENST00000398590; ENSP00000381590; ENSG00000163635.
ENST00000484332; ENSP00000428277; ENSG00000163635.
ENST00000487717; ENSP00000420234; ENSG00000163635.
ENST00000538065; ENSP00000439585; ENSG00000163635.

GeneID

6314.

KEGG

hsa:6314.

UCSC

uc003dlv.3. human.
uc021wzy.1. human.

Organism-specific databases

CTD

6314.

GeneCards

GC03P063825.

HGNC

HGNC:10560. ATXN7.

HPA

HPA034989.

MIM

164500. phenotype.
607640. gene.

neXtProt

NX_O15265.

Orphanet

94147. Spinocerebellar ataxia type 7.

PharmGKB

PA34973.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG270433.

HOGENOM

HOG000252910.

HOVERGEN

HBG004320.

KO

K11318.

OMA

RKNSSPL.

OrthoDB

EOG4DV5KV.

Gene expression databases

ArrayExpress

O15265.

Bgee

O15265.

CleanEx

HS_ATXN7.

Genevestigator

O15265.

GermOnline

ENSG00000163635. Homo sapiens.

Family and domain databases

InterPro

IPR013243. SCA7_dom.
IPR015880. Znf_C2H2-like.
[Graphical view]

Pfam

PF08313. SCA7. 1 hit.
[Graphical view]

SMART

SM00355. ZnF_C2H2. 1 hit.
[Graphical view]

PROSITE

PS51505. SCA7. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ATXN7. human.

EvolutionaryTrace

O15265.

GenomeRNAi

6314.

NextBio

24505.

PMAP-CutDB

O15265.

SOURCE

Search...

Entry information

Entry name

ATX7_HUMAN

Accession

Primary (citable) accession number: O15265
Secondary accession number(s): B4E207 , E9PHP9, O75328, O75329, Q9Y6P8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 126 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.