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P54259

- ATN1_HUMAN

UniProt

P54259 - ATN1_HUMAN

Protein

Atrophin-1

Gene

ATN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 3 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    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.By similarity2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei109 – 1102Cleavage

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein domain specific binding Source: UniProtKB
    3. transcription corepressor activity Source: UniProtKB

    GO - Biological processi

    1. cell migration Source: Ensembl
    2. central nervous system development Source: ProtInc
    3. maintenance of cell polarity Source: Ensembl
    4. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    5. neuron apoptotic process Source: UniProtKB
    6. toxin metabolic process Source: Ensembl
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Biological processi

    Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Atrophin-1
    Alternative name(s):
    Dentatorubral-pallidoluysian atrophy protein
    Gene namesi
    Name:ATN1
    Synonyms:D12S755E, DRPLA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:3033. ATN1.

    Subcellular locationi

    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.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-SubCell
    2. cytoplasm Source: ProtInc
    3. nuclear matrix Source: UniProtKB
    4. nucleus Source: UniProtKB
    5. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi109 – 1091D → N: Prevents cleavage and suppresses apoptosis. 1 Publication
    Mutagenesisi739 – 7391S → A: Abolishes phosphorylation.

    Keywords - Diseasei

    Epilepsy, Neurodegeneration

    Organism-specific databases

    MIMi125370. phenotype.
    Orphaneti101. Dentatorubral pallidoluysian atrophy.
    PharmGKBiPA27487.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11901190Atrophin-1PRO_0000064730Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei34 – 341Phosphoserine1 Publication
    Modified residuei77 – 771Phosphoserine1 Publication
    Modified residuei79 – 791Phosphoserine1 Publication
    Modified residuei101 – 1011Phosphoserine1 Publication
    Modified residuei103 – 1031Phosphoserine1 Publication
    Modified residuei107 – 1071Phosphoserine1 Publication
    Modified residuei641 – 6411N6-acetyllysine1 Publication
    Modified residuei653 – 6531Phosphothreonine1 Publication
    Modified residuei661 – 6611Phosphoserine2 Publications
    Modified residuei739 – 7391Phosphoserine; by MAPK81 Publication
    Modified residuei746 – 7461Phosphoserine1 Publication
    Modified residuei748 – 7481Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated in vitro by MAPK8/JNK1 on Ser-739. Mutant ATN1 sequences with expanded poly-Asn (polyQ) traits are more slowly phosphorylated.4 Publications
    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-109.4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP54259.
    PaxDbiP54259.
    PRIDEiP54259.

    PTM databases

    PhosphoSiteiP54259.

    Expressioni

    Tissue specificityi

    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.3 Publications

    Gene expression databases

    ArrayExpressiP54259.
    BgeeiP54259.
    CleanExiHS_ATN1.
    GenevestigatoriP54259.

    Organism-specific databases

    HPAiHPA031619.

    Interactioni

    Subunit structurei

    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. Interacts with PQBP1.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EFEMP1Q128053EBI-945980,EBI-536772
    EFEMP2O959673EBI-945980,EBI-743414
    PLEKHA5Q9HAU02EBI-945980,EBI-945934
    PSME3P612893EBI-945980,EBI-355546
    RBFOX1Q9NWB12EBI-945980,EBI-945906
    REREQ9P2R63EBI-945980,EBI-948076
    TRIP6Q156542EBI-945980,EBI-742327

    Protein-protein interaction databases

    BioGridi108156. 98 interactions.
    IntActiP54259. 87 interactions.
    MINTiMINT-92928.
    STRINGi9606.ENSP00000349076.

    Structurei

    3D structure databases

    ProteinModelPortaliP54259.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni517 – 56751Involved in binding BAIAP2Add
    BLAST
    Regioni879 – 89416Required for interaction with FAT1Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi16 – 3217Nuclear localization signal1 PublicationAdd
    BLAST
    Motifi1033 – 10419Nuclear export signal

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi73 – 8210Glu/Ser-rich
    Compositional biasi302 – 3054Poly-Pro
    Compositional biasi376 – 3827Poly-Ser
    Compositional biasi386 – 39712Poly-SerAdd
    BLAST
    Compositional biasi442 – 4476Poly-Pro
    Compositional biasi479 – 4835Poly-His
    Compositional biasi484 – 50219Poly-GlnAdd
    BLAST
    Compositional biasi509 – 5124Poly-Pro
    Compositional biasi569 – 57911Poly-SerAdd
    BLAST
    Compositional biasi709 – 7124Poly-Pro
    Compositional biasi807 – 82014Ala/Arg-richAdd
    BLAST
    Compositional biasi821 – 83212Arg/Glu-rich (mixed charge)Add
    BLAST
    Compositional biasi930 – 93910Arg/Glu-rich (mixed charge)

    Phylogenomic databases

    eggNOGiNOG331121.
    HOVERGENiHBG075369.
    InParanoidiP54259.
    KOiK05626.
    OMAiGPEKGPT.
    OrthoDBiEOG7D59MN.
    PhylomeDBiP54259.
    TreeFamiTF328554.

    Family and domain databases

    InterProiIPR017993. Atrophin-1.
    IPR002951. Atrophin-like.
    [Graphical view]
    PfamiPF03154. Atrophin-1. 2 hits.
    [Graphical view]
    PRINTSiPR01222. ATROPHIN.

    Sequencei

    Sequence statusi: Complete.

    P54259-1 [UniParc]FASTAAdd to Basket

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    MKTRQNKDSM SMRSGRKKEA PGPREELRSR GRASPGGVST SSSDGKAEKS     50
    RQTAKKARVE EASTPKVNKQ GRSEEISESE SEETNAPKKT KTEQELPRPQ 100
    SPSDLDSLDG RSLNDDGSSD PRDIDQDNRS TSPSIYSPGS VENDSDSSSG 150
    LSQGPARPYH PPPLFPPSPQ PPDSTPRQPE ASFEPHPSVT PTGYHAPMEP 200
    PTSRMFQAPP GAPPPHPQLY PGGTGGVLSG PPMGPKGGGA ASSVGGPNGG 250
    KQHPPPTTPI SVSSSGASGA PPTKPPTTPV GGGNLPSAPP PANFPHVTPN 300
    LPPPPALRPL NNASASPPGL GAQPLPGHLP SPHAMGQGMG GLPPGPEKGP 350
    TLAPSPHSLP PASSSAPAPP MRFPYSSSSS SSAAASSSSS SSSSSASPFP 400
    ASQALPSYPH SFPPPTSLSV SNQPPKYTQP SLPSQAVWSQ GPPPPPPYGR 450
    LLANSNAHPG PFPPSTGAQS TAHPPVSTHH HHHQQQQQQQ QQQQQQQQQQ 500
    QQHHGNSGPP PPGAFPHPLE GGSSHHAHPY AMSPSLGSLR PYPPGPAHLP 550
    PPHSQVSYSQ AGPNGPPVSS SSNSSSSTSQ GSYPCSHPSP SQGPQGAPYP 600
    FPPVPTVTTS SATLSTVIAT VASSPAGYKT ASPPGPPPYG KRAPSPGAYK 650
    TATPPGYKPG SPPSFRTGTP PGYRGTSPPA GPGTFKPGSP TVGPGPLPPA 700
    GPSGLPSLPP PPAAPASGPP LSATQIKQEP AEEYETPESP VPPARSPSPP 750
    PKVVDVPSHA SQSARFNKHL DRGFNSCARS DLYFVPLEGS KLAKKRADLV 800
    EKVRREAEQR AREEKERERE REREKERERE KERELERSVK LAQEGRAPVE 850
    CPSLGPVPHR PPFEPGSAVA TVPPYLGPDT PALRTLSEYA RPHVMSPGNR 900
    NHPFYVPLGA VDPGLLGYNV PALYSSDPAA REREREARER DLRDRLKPGF 950
    EVKPSELEPL HGVPGPGLDP FPRHGGLALQ PGPPGLHPFP FHPSLGPLER 1000
    ERLALAAGPA LRPDMSYAER LAAERQHAER VAALGNDPLA RLQMLNVTPH 1050
    HHQHSHIHSH LHLHQQDAIH AASASVHPLI DPLASGSHLT RIPYPAGTLP 1100
    NPLLPHPLHE NEVLRHQLFA APYRDLPASL SAPMSAAHQL QAMHAQSAEL 1150
    QRLALEQQQW LHAHHPLHSV PLPAQEDYYS HLKKESDKPL 1190
    Length:1,190
    Mass (Da):125,414
    Last modified:January 11, 2011 - v3
    Checksum:iB47603486C672637
    GO

    Sequence cautioni

    The sequence BAA07534.1 differs from that shown. Reason: Frameshift at positions 961, 970, 977, 980, 983 and 1005.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti94 – 941Missing in AAB50276. (PubMed:8965642)Curated
    Sequence conflicti333 – 3331H → Y in BAA06626. (PubMed:7842016)Curated
    Sequence conflicti1033 – 10331A → G in BAA06626. (PubMed:7842016)Curated

    Polymorphismi

    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.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti339 – 3391M → I.1 Publication
    Corresponds to variant rs1058045 [ dbSNP | Ensembl ].
    VAR_030937
    Natural varianti484 – 4885Missing.2 Publications
    VAR_064038

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS31734.1.
    PIRiG01763.
    S50832.
    RefSeqiNP_001007027.1. NM_001007026.1.
    NP_001931.2. NM_001940.3.
    UniGeneiHs.143766.

    Genome annotation databases

    EnsembliENST00000356654; ENSP00000349076; ENSG00000111676.
    ENST00000396684; ENSP00000379915; ENSG00000111676.
    GeneIDi1822.
    KEGGihsa:1822.
    UCSCiuc001qrw.1. human.

    Polymorphism databases

    DMDMi317373480.

    Keywords - Coding sequence diversityi

    Polymorphism, Triplet repeat expansion

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS31734.1.
    PIRi G01763.
    S50832.
    RefSeqi NP_001007027.1. NM_001007026.1.
    NP_001931.2. NM_001940.3.
    UniGenei Hs.143766.

    3D structure databases

    ProteinModelPortali P54259.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108156. 98 interactions.
    IntActi P54259. 87 interactions.
    MINTi MINT-92928.
    STRINGi 9606.ENSP00000349076.

    PTM databases

    PhosphoSitei P54259.

    Polymorphism databases

    DMDMi 317373480.

    Proteomic databases

    MaxQBi P54259.
    PaxDbi P54259.
    PRIDEi P54259.

    Protocols and materials databases

    DNASUi 1822.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000356654 ; ENSP00000349076 ; ENSG00000111676 .
    ENST00000396684 ; ENSP00000379915 ; ENSG00000111676 .
    GeneIDi 1822.
    KEGGi hsa:1822.
    UCSCi uc001qrw.1. human.

    Organism-specific databases

    CTDi 1822.
    GeneCardsi GC12P007033.
    GeneReviewsi ATN1.
    H-InvDB HIX0079489.
    HGNCi HGNC:3033. ATN1.
    HPAi HPA031619.
    MIMi 125370. phenotype.
    607462. gene.
    neXtProti NX_P54259.
    Orphaneti 101. Dentatorubral pallidoluysian atrophy.
    PharmGKBi PA27487.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG331121.
    HOVERGENi HBG075369.
    InParanoidi P54259.
    KOi K05626.
    OMAi GPEKGPT.
    OrthoDBi EOG7D59MN.
    PhylomeDBi P54259.
    TreeFami TF328554.

    Miscellaneous databases

    ChiTaRSi ATN1. human.
    GeneWikii ATN1.
    GenomeRNAii 1822.
    NextBioi 7425.
    PROi P54259.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P54259.
    Bgeei P54259.
    CleanExi HS_ATN1.
    Genevestigatori P54259.

    Family and domain databases

    InterProi IPR017993. Atrophin-1.
    IPR002951. Atrophin-like.
    [Graphical view ]
    Pfami PF03154. Atrophin-1. 2 hits.
    [Graphical view ]
    PRINTSi PR01222. ATROPHIN.
    ProtoNeti Search...

    Publicationsi

    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. 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. 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. 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. 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. "Y65C missense mutation in the WW domain of the Golabi-Ito-Hall syndrome protein PQBP1 affects its binding activity and deregulates pre-mRNA splicing."
      Tapia V.E., Nicolaescu E., McDonald C.B., Musi V., Oka T., Inayoshi Y., Satteson A.C., Mazack V., Humbert J., Gaffney C.J., Beullens M., Schwartz C.E., Landgraf C., Volkmer R., Pastore A., Farooq A., Bollen M., Sudol M.
      J. Biol. Chem. 285:19391-19401(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PQBP1.
    21. "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.
    22. "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].

    Entry informationi

    Entry nameiATN1_HUMAN
    AccessioniPrimary (citable) accession number: P54259
    Secondary accession number(s): Q99495, Q99621, Q9UEK7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 135 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

    External Data

    Dasty 3