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P54259 (ATN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Atrophin-1
Alternative name(s):
Dentatorubral-pallidoluysian atrophy protein
Gene names
Name:ATN1
Synonyms:D12S755E, DRPLA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1190 AA.
Sequence statusComplete.
Protein existenceEvidence 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-terminal 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. Cytoplasmperinuclear 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 processTranscription
Transcription regulation
   Cellular componentCell junction
Cytoplasm
Nucleus
   Coding sequence diversityPolymorphism
Triplet repeat expansion
   DiseaseEpilepsy
Neurodegeneration
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell migration

Inferred from electronic annotation. Source: Ensembl

central nervous system development

Traceable author statement PubMed 7647802. Source: ProtInc

maintenance of cell polarity

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcell 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

nucleus

Inferred from direct assay Ref.10. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein binding

Inferred from physical interaction Ref.12PubMed 17577209Ref.17Ref.8. Source: UniProtKB

protein domain specific binding

Inferred from physical interaction PubMed 11984006. Source: UniProtKB

transcription corepressor activity

Inferred from direct assay Ref.12. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11901190Atrophin-1
PRO_0000064730

Regions

Region517 – 56751Involved in binding BAIAP2
Region879 – 89416Required for interaction with FAT1
Motif16 – 3217Nuclear localization signal Ref.14
Motif1033 – 10419Nuclear export signal
Compositional bias73 – 8210Glu/Ser-rich
Compositional bias302 – 3054Poly-Pro
Compositional bias376 – 3827Poly-Ser
Compositional bias386 – 39712Poly-Ser
Compositional bias442 – 4476Poly-Pro
Compositional bias479 – 4835Poly-His
Compositional bias484 – 50219Poly-Gln
Compositional bias509 – 5124Poly-Pro
Compositional bias569 – 57911Poly-Ser
Compositional bias709 – 7124Poly-Pro
Compositional bias807 – 82014Ala/Arg-rich
Compositional bias821 – 83212Arg/Glu-rich (mixed charge)
Compositional bias930 – 93910Arg/Glu-rich (mixed charge)

Sites

Site109 – 1102Cleavage

Amino acid modifications

Modified residue341Phosphoserine Ref.20
Modified residue771Phosphoserine Ref.16
Modified residue791Phosphoserine Ref.16
Modified residue1011Phosphoserine Ref.16
Modified residue1031Phosphoserine Ref.16
Modified residue1071Phosphoserine Ref.16
Modified residue6411N6-acetyllysine Ref.18
Modified residue6531Phosphothreonine Ref.16
Modified residue6611Phosphoserine Ref.16 Ref.21
Modified residue7391Phosphoserine; by MAPK8 Ref.13
Modified residue7461Phosphoserine Ref.16
Modified residue7481Phosphoserine Ref.16

Natural variations

Natural variant3391M → I. Ref.3
Corresponds to variant rs1058045 [ dbSNP | Ensembl ].
VAR_030937
Natural variant484 – 4885Missing.
VAR_064038

Experimental info

Mutagenesis1091D → N: Prevents cleavage and suppresses apoptosis. Ref.10
Mutagenesis7391S → A: Abolishes phosphorylation.
Sequence conflict941Missing in AAB50276. Ref.3
Sequence conflict3331H → Y in BAA06626. Ref.1
Sequence conflict10331A → G in BAA06626. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P54259 [UniParc].

Last modified January 11, 2011. Version 3.
Checksum: B47603486C672637

FASTA1,190125,414
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

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.
CCDSCCDS31734.1.
PIRG01763.
S50832.
RefSeqNP_001007027.1. NM_001007026.1.
NP_001931.2. NM_001940.3.
UniGeneHs.143766.

3D structure databases

ProteinModelPortalP54259.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108156. 98 interactions.
IntActP54259. 87 interactions.
MINTMINT-92928.
STRING9606.ENSP00000349076.

PTM databases

PhosphoSiteP54259.

Polymorphism databases

DMDM317373480.

Proteomic databases

MaxQBP54259.
PaxDbP54259.
PRIDEP54259.

Protocols and materials databases

DNASU1822.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356654; ENSP00000349076; ENSG00000111676.
ENST00000396684; ENSP00000379915; ENSG00000111676.
ENST00000594779; ENSP00000469054; ENSG00000268872.
ENST00000599184; ENSP00000469977; ENSG00000268872.
GeneID1822.
KEGGhsa:1822.
UCSCuc001qrw.1. human.

Organism-specific databases

CTD1822.
GeneCardsGC12P007033.
GeneReviewsATN1.
H-InvDBHIX0079489.
HGNCHGNC:3033. ATN1.
HPAHPA031619.
MIM125370. phenotype.
607462. gene.
neXtProtNX_P54259.
Orphanet101. Dentatorubral pallidoluysian atrophy.
PharmGKBPA27487.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG331121.
HOVERGENHBG075369.
InParanoidP54259.
KOK05626.
OMAGPEKGPT.
OrthoDBEOG7D59MN.
PhylomeDBP54259.
TreeFamTF328554.

Gene expression databases

ArrayExpressP54259.
BgeeP54259.
CleanExHS_ATN1.
GenevestigatorP54259.

Family and domain databases

InterProIPR017993. Atrophin-1.
IPR002951. Atrophin-like.
[Graphical view]
PfamPF03154. Atrophin-1. 2 hits.
[Graphical view]
PRINTSPR01222. ATROPHIN.
ProtoNetSearch...

Other

ChiTaRSATN1. human.
GeneWikiATN1.
GenomeRNAi1822.
NextBio7425.
PROP54259.
SOURCESearch...

Entry information

Entry nameATN1_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM