P54259 (ATN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Atrophin-1

Alternative name(s):
Dentatorubral-pallidoluysian atrophy protein

Gene names

Name:	ATN1
Synonyms:	D12S755E, DRPLA

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	1190 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcriptional corepressor. Recruits NR2E1 to repress transcription. Promotes vascular smooth cell (VSMC) migration and orientation By similarity. Corepressor of MTG8 transcriptional repression. Has some intrinsic repression activity which is independent of the number of poly-Asn (polyQ) repeats. Ref.10 Ref.12
Subunit structure	Interacts with NR2E1; the interaction represses the transcriptional activity of NR2E1. Interacts (via its N-terminus) with FAT1 (via a C-terminus domain) By similarity. Interacts with BAIAP2, WWP1, WWP2, WWP3 and RERE. Interacts (via its N-terminus) with MTG8; the interaction enhances transcriptional repression of MTG8. Ref.8 Ref.9 Ref.11 Ref.12 Ref.17
Subcellular location	Nucleus. Cytoplasm › perinuclear region. Cell junction By similarity. Note: Shuttles between nucleus and cytoplasm. Colocalizes with FAT1 in the perinuclear area, at cell-cell junctions and leading edges of cells By similarity. Colocalizes with MTG8 in discrete nuclear dots. Proteolytic fragment F1 appears to remain in nucleus. Fragment F2 is exported into the cytoplasm. Fragment F2 from mutant sequences with longer poly-Asn (polyQ) tracts are additionally located to the cytoplasmic membrane and to certain organelles. Ref.9 Ref.10 Ref.12 Ref.14 Ref.19
Tissue specificity	Widely expressed in various tissues including heart, lung, kidney, ovary, testis, prostate, placenta, skeletal Low levels in the liver, thymus and leukocytes. In the adult brain, broadly expressed in amygdala, caudate nucleus, corpus callosum, hippocampus, hypothalamus, substantia nigra, subthalamic nucleus, and thalamus. High levels in fetal tissues, especially brain. Ref.1 Ref.2 Ref.3
Post-translational modification	Phosphorylated in vitro by MAPK8/JNK1 on Ser-739. Mutant ATN1 sequences with expanded poly-Asn (polyQ) traits are more slowly phosphorylated. Ref.13 Proteolytically cleaved, probably in the nucleus, to produce two C-terminal fragments of 140 kDa (F1) and 125 kDa (F2) each containing poly-Asn (polyQ) tracts. F2 is produced by cleavage by caspases and is exported into the cytoplasm. In vitro, cleavage increases with an increase in the number of polyQ tracts. C-terminal proteolytic products appear to be the cause of cell toxicity. In vitro cleavage at Asp-109. Ref.7 Ref.10 Ref.14 Ref.19
Polymorphism	The poly-Gln region of ATN1 is highly polymorphic (7 to 23 repeats) in the normal population and is expanded to about 49-75 repeats in DRPLA and HRS patients. Longer expansions result in earlier onset and more severe clinical manifestations of the disease.
Involvement in disease	Dentatorubral-pallidoluysian atrophy (DRPLA) [MIM:125370]: Autosomal dominant neurodegenerative disorder characterized by a loss of neurons in the dentate nucleus, rubrum, glogus pallidus and Luys'body. Clinical features are myoclonus epilepsy, dementia, and cerebellar ataxia. Onset of the disease occurs usually in the second decade of life and death in the fourth. Note: The disease is caused by mutations affecting the gene represented in this entry.
Sequence caution	The sequence BAA07534.1 differs from that shown. Reason: Frameshift at positions 961, 970, 977, 980, 983 and 1005.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cell junction Cytoplasm Nucleus
Coding sequence diversity	Polymorphism Triplet repeat expansion
Disease	Epilepsy Neurodegeneration
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell migration Inferred from electronic annotation. Source: Compara central nervous system development Traceable author statement PubMed 7647802. Source: ProtInc maintenance of cell polarity Inferred from electronic annotation. Source: Compara negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.12. Source: UniProtKB neuron apoptotic process Inferred from direct assay Ref.10. Source: UniProtKB toxin metabolic process Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cell junction Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Traceable author statement PubMed 7647802. Source: ProtInc nuclear matrix Inferred from direct assay Ref.12. Source: UniProtKB perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	transcription corepressor activity Inferred from direct assay Ref.12. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EFEMP1	Q12805	3	EBI-945980,EBI-536772
EFEMP2	O95967	3	EBI-945980,EBI-743414
PLEKHA5	Q9HAU0	2	EBI-945980,EBI-945934
PSME3	P61289	3	EBI-945980,EBI-355546
RBFOX1	Q9NWB1	2	EBI-945980,EBI-945906
RERE	Q9P2R6	3	EBI-945980,EBI-948076
TRIP6	Q15654	2	EBI-945980,EBI-742327

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1190	1190	Atrophin-1		PRO_0000064730
Regions
	Region	517 – 567	51	Involved in binding BAIAP2
	Region	879 – 894	16	Required for interaction with FAT1
	Motif	16 – 32	17	Nuclear localization signal Ref.14
	Motif	1033 – 1041	9	Nuclear export signal
	Compositional bias	73 – 82	10	Glu/Ser-rich
	Compositional bias	302 – 305	4	Poly-Pro
	Compositional bias	376 – 382	7	Poly-Ser
	Compositional bias	386 – 397	12	Poly-Ser
	Compositional bias	442 – 447	6	Poly-Pro
	Compositional bias	479 – 483	5	Poly-His
	Compositional bias	484 – 502	19	Poly-Gln
	Compositional bias	509 – 512	4	Poly-Pro
	Compositional bias	569 – 579	11	Poly-Ser
	Compositional bias	709 – 712	4	Poly-Pro
	Compositional bias	807 – 820	14	Ala/Arg-rich
	Compositional bias	821 – 832	12	Arg/Glu-rich (mixed charge)
	Compositional bias	930 – 939	10	Arg/Glu-rich (mixed charge)
Sites
	Site	109 – 110	2	Cleavage
Amino acid modifications
	Modified residue	34	1	Phosphoserine Ref.20
	Modified residue	77	1	Phosphoserine Ref.16
	Modified residue	79	1	Phosphoserine Ref.16
	Modified residue	101	1	Phosphoserine Ref.16
	Modified residue	103	1	Phosphoserine Ref.16
	Modified residue	107	1	Phosphoserine Ref.16
	Modified residue	641	1	N6-acetyllysine Ref.18
	Modified residue	653	1	Phosphothreonine Ref.16
	Modified residue	661	1	Phosphoserine Ref.16 Ref.21
	Modified residue	739	1	Phosphoserine; by MAPK8 Ref.13
	Modified residue	746	1	Phosphoserine Ref.16
	Modified residue	748	1	Phosphoserine Ref.16
Natural variations
	Natural variant	339	1	M → I. Ref.3 Corresponds to variant rs1058045 [ dbSNP | Ensembl ].		VAR_030937
	Natural variant	484 – 488	5	Missing.		VAR_064038
Experimental info
	Mutagenesis	109	1	D → N: Prevents cleavage and suppresses apoptosis. Ref.10
	Mutagenesis	739	1	S → A: Abolishes phosphorylation.
	Sequence conflict	94	1	Missing in AAB50276. Ref.3
	Sequence conflict	333	1	H → Y in BAA06626. Ref.1
	Sequence conflict	1033	1	A → G in BAA06626. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P54259 [UniParc]. Last modified January 11, 2011. Version 3. Checksum: B47603486C672637	FASTA	1,190	125,414
	10 20 30 40 50 60 MKTRQNKDSM SMRSGRKKEA PGPREELRSR GRASPGGVST SSSDGKAEKS RQTAKKARVE 70 80 90 100 110 120 EASTPKVNKQ GRSEEISESE SEETNAPKKT KTEQELPRPQ SPSDLDSLDG RSLNDDGSSD 130 140 150 160 170 180 PRDIDQDNRS TSPSIYSPGS VENDSDSSSG LSQGPARPYH PPPLFPPSPQ PPDSTPRQPE 190 200 210 220 230 240 ASFEPHPSVT PTGYHAPMEP PTSRMFQAPP GAPPPHPQLY PGGTGGVLSG PPMGPKGGGA 250 260 270 280 290 300 ASSVGGPNGG KQHPPPTTPI SVSSSGASGA PPTKPPTTPV GGGNLPSAPP PANFPHVTPN 310 320 330 340 350 360 LPPPPALRPL NNASASPPGL GAQPLPGHLP SPHAMGQGMG GLPPGPEKGP TLAPSPHSLP 370 380 390 400 410 420 PASSSAPAPP MRFPYSSSSS SSAAASSSSS SSSSSASPFP ASQALPSYPH SFPPPTSLSV 430 440 450 460 470 480 SNQPPKYTQP SLPSQAVWSQ GPPPPPPYGR LLANSNAHPG PFPPSTGAQS TAHPPVSTHH 490 500 510 520 530 540 HHHQQQQQQQ QQQQQQQQQQ QQHHGNSGPP PPGAFPHPLE GGSSHHAHPY AMSPSLGSLR 550 560 570 580 590 600 PYPPGPAHLP PPHSQVSYSQ AGPNGPPVSS SSNSSSSTSQ GSYPCSHPSP SQGPQGAPYP 610 620 630 640 650 660 FPPVPTVTTS SATLSTVIAT VASSPAGYKT ASPPGPPPYG KRAPSPGAYK TATPPGYKPG 670 680 690 700 710 720 SPPSFRTGTP PGYRGTSPPA GPGTFKPGSP TVGPGPLPPA GPSGLPSLPP PPAAPASGPP 730 740 750 760 770 780 LSATQIKQEP AEEYETPESP VPPARSPSPP PKVVDVPSHA SQSARFNKHL DRGFNSCARS 790 800 810 820 830 840 DLYFVPLEGS KLAKKRADLV EKVRREAEQR AREEKERERE REREKERERE KERELERSVK 850 860 870 880 890 900 LAQEGRAPVE CPSLGPVPHR PPFEPGSAVA TVPPYLGPDT PALRTLSEYA RPHVMSPGNR 910 920 930 940 950 960 NHPFYVPLGA VDPGLLGYNV PALYSSDPAA REREREARER DLRDRLKPGF EVKPSELEPL 970 980 990 1000 1010 1020 HGVPGPGLDP FPRHGGLALQ PGPPGLHPFP FHPSLGPLER ERLALAAGPA LRPDMSYAER 1030 1040 1050 1060 1070 1080 LAAERQHAER VAALGNDPLA RLQMLNVTPH HHQHSHIHSH LHLHQQDAIH AASASVHPLI 1090 1100 1110 1120 1130 1140 DPLASGSHLT RIPYPAGTLP NPLLPHPLHE NEVLRHQLFA APYRDLPASL SAPMSAAHQL 1150 1160 1170 1180 1190 QAMHAQSAEL QRLALEQQQW LHAHHPLHSV PLPAQEDYYS HLKKESDKPL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and expression of the gene responsible for the triplet repeat disorder, dentatorubral and pallidoluysian atrophy (DRPLA)." Nagafuchi S., Yanagisawa H., Ohsaki E., Shirayama T., Tadokoro K., Inoue T., Yamada M. Nat. Genet. 8:177-182(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANT 484-GLN--GLN-488 DEL. Tissue: Brain.
[2]	"Molecular cloning of a full-length cDNA for dentatorubral-pallidoluysian atrophy and regional expressions of the expanded alleles in the CNS." Onodera O., Oyake M., Takano H., Ikeuchi T., Igarashi S., Tsuji S. Am. J. Hum. Genet. 57:1050-1060(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANT 484-GLN--GLN-488 DEL. Tissue: Brain.
[3]	"DRPLA gene (atrophin-1) sequence and mRNA expression in human brain." Margolis R.L., Li S.-H., Young W.S., Wagster M.V., Stine O.C., Kidwai A.S., Ashworth R.G., Ross C.A. Brain Res. Mol. Brain Res. 36:219-226(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANTS ILE-339 AND 484-GLN--GLN-488 DEL.
[4]	"Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination." Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A. Genome Res. 7:268-280(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], POLYMORPHISM OF POLY-GLN REGION. Tissue: Brain.
[5]	"A unique origin and multistep process for the generation of expanded DRPLA triplet repeats." Yanagisawa H., Fujii K., Nagafuchi S., Nakahori Y., Nakagome Y., Akane A., Nakamura M., Sano A., Komure O., Kondo I., Jin D.K., Soerensen S.A., Potter N.T., Young S.R., Nakamura K., Nukina N., Nagao Y., Tadokoro K. , Okuyama T., Miyashita T., Inoue T., Kanazawa I., Yamada M. Hum. Mol. Genet. 5:373-379(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-76.
[6]	"The Haw River syndrome: dentatorubropallidoluysian atrophy (DRPLA) in an African-American family." Burke J.R., Wingfield M.S., Lewis K.E., Roses A.D., Lee J.E., Hulette C., Pericak-Vance M.A., Vance J.M. Nat. Genet. 7:521-524(1994) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN HRS.
[7]	"Dentatorubral pallidoluysian atrophy (DRPLA) protein is cleaved by caspase-3 during apoptosis." Miyashita T., Okamura-Oho Y., Mito Y., Nagafuchi S., Yamada M. J. Biol. Chem. 272:29238-29242(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEOLYTIC PROCESSING.
[8]	"Atrophin-1, the DRPLA gene product, interacts with two families of WW domain-containing proteins." Wood J.D., Yuan J., Margolis R.L., Colomer V., Duan K., Kushi J., Kaminsky Z., Kleiderlein J.J. Jr., Sharp A.H., Ross C.A. Mol. Cell. Neurosci. 11:149-160(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH WWP1; WWP2 AND WWP3.
[9]	"Dentatorubral-pallidoluysian atrophy protein interacts through a proline-rich region near polyglutamine with the SH3 domain of an insulin receptor tyrosine kinase substrate." Okamura-Oho Y., Miyashita T., Ohmi K., Yamada M. Hum. Mol. Genet. 8:947-957(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BAIAP2, SUBCELLULAR LOCATION.
[10]	"Cleavage of atrophin-1 at caspase site aspartic acid 109 modulates cytotoxicity." Ellerby L.M., Andrusiak R.L., Wellington C.L., Hackam A.S., Propp S.S., Wood J.D., Sharp A.H., Margolis R.L., Ross C.A., Salvesen G.S., Hayden M.R., Bredesen D.E. J. Biol. Chem. 274:8730-8736(1999) [PubMed] [Europe PMC] [Abstract] Cited for: CLEAVAGE AT ASP-109, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-109.
[11]	"Protein binding of a DRPLA family through arginine-glutamic acid dipeptide repeats is enhanced by extended polyglutamine." Yanagisawa H., Bundo M., Miyashita T., Okamura-Oho Y., Tadokoro K., Tokunaga K., Yamada M. Hum. Mol. Genet. 9:1433-1442(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RERE.
[12]	"Atrophin-1, the dentato-rubral and pallido-luysian atrophy gene product, interacts with ETO/MTG8 in the nuclear matrix and represses transcription." Wood J.D., Nucifora F.C. Jr., Duan K., Zhang C., Wang J., Kim Y., Schilling G., Sacchi N., Liu J.M., Ross C.A. J. Cell Biol. 150:939-948(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MTG8, SUBCELLULAR LOCATION, FUNCTION.
[13]	"Dentatorubral-pallidoluysian atrophy protein is phosphorylated by c-Jun NH2-terminal kinase." Okamura-Oho Y., Miyashita T., Nagao K., Shima S., Ogata Y., Katada T., Nishina H., Yamada M. Hum. Mol. Genet. 12:1535-1542(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-739.
[14]	"Nuclear localization of a non-caspase truncation product of atrophin-1, with an expanded polyglutamine repeat, increases cellular toxicity." Nucifora F.C. Jr., Ellerby L.M., Wellington C.L., Wood J.D., Herring W.J., Sawa A., Hayden M.R., Dawson V.L., Dawson T.M., Ross C.A. J. Biol. Chem. 278:13047-13055(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEOLYTIC PROCESSING, NUCLEAR LOCALIZATION SIGNAL, NUCLEAR EXPORT SIGNAL, SUBCELLULAR LOCATION.
[15]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[16]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-79; SER-101; SER-103; SER-107; THR-653; SER-661; SER-746 AND SER-748, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Atrophin proteins interact with the Fat1 cadherin and regulate migration and orientation in vascular smooth muscle cells." Hou R., Sibinga N.E. J. Biol. Chem. 284:6955-6965(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FAT1.
[18]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-641, MASS SPECTROMETRY.
[19]	"Proteolytic processing regulates pathological accumulation in dentatorubral-pallidoluysian atrophy." Suzuki Y., Nakayama K., Hashimoto N., Yazawa I. FEBS J. 277:4873-4887(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION.
[20]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-661, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	D31840 mRNA. Translation: BAA06626.1. D38529 mRNA. Translation: BAA07534.1. Frameshift. U23851 mRNA. Translation: AAB50276.1. U47924 Genomic DNA. Translation: AAB51321.1. D63808 Genomic DNA. Translation: BAA23631.1.
IPI	IPI00005502.
PIR	G01763. S50832.
RefSeq	NP_001007027.1. NM_001007026.1. NP_001931.2. NM_001940.3.
UniGene	Hs.143766.
3D structure databases
ProteinModelPortal	P54259.
ModBase	Search...
Protein-protein interaction databases
IntAct	P54259. 85 interactions.
MINT	MINT-92928.
STRING	9606.ENSP00000349076.
PTM databases
PhosphoSite	P54259.
Polymorphism databases
DMDM	29429203.
Proteomic databases
PaxDb	P54259.
PRIDE	P54259.
Protocols and materials databases
DNASU	1822.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000356654; ENSP00000349076; ENSG00000111676. ENST00000396684; ENSP00000379915; ENSG00000111676. ENST00000544325; ENSP00000441744; ENSG00000111676. ENST00000594779; ENSP00000469054; ENSG00000268872. ENST00000599184; ENSP00000469977; ENSG00000268872. ENST00000600565; ENSP00000473144; ENSG00000268872.
GeneID	1822.
KEGG	hsa:1822.
UCSC	uc001qrw.1. human.
Organism-specific databases
CTD	1822.
GeneCards	GC12P007033.
H-InvDB	HIX0079489.
HGNC	HGNC:3033. ATN1.
HPA	HPA031619.
MIM	125370. phenotype. 607462. gene.
neXtProt	NX_P54259.
Orphanet	101. Dentatorubral-pallidoluysian atrophy.
PharmGKB	PA27487.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG331121.
HOVERGEN	HBG075369.
InParanoid	P54259.
KO	K05626.
OMA	ATFPHVT.
OrthoDB	EOG4RFKT4.
PhylomeDB	P54259.
Gene expression databases
ArrayExpress	P54259.
Bgee	P54259.
CleanEx	HS_ATN1.
Genevestigator	P54259.
GermOnline	ENSG00000111676. Homo sapiens.
Family and domain databases
InterPro	IPR017993. Atrophin-1. IPR002951. Atrophin-like. [Graphical view]
Pfam	PF03154. Atrophin-1. 2 hits. [Graphical view]
PRINTS	PR01222. ATROPHIN.
ProtoNet	Search...
Other
ChiTaRS	ATN1. human.
GenomeRNAi	1822.
NextBio	7425.
SOURCE	Search...

Entry information

Entry name

ATN1_HUMAN

Accession

Primary (citable) accession number: P54259
Secondary accession number(s): Q99495, Q99621, Q9UEK7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 11, 2011
Last modified:	May 1, 2013
This is version 123 of the entry and version 3 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.