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P54259

- ATN1_HUMAN

UniProt

P54259 - ATN1_HUMAN

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Protein

Atrophin-1

Gene

ATN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 domain specific binding Source: UniProtKB
  2. 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
Complete GO annotation...

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-KW
  2. cytoplasm Source: ProtInc
  3. nuclear matrix Source: UniProtKB
  4. nucleus Source: UniProtKB
Complete GO annotation...

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

BgeeiP54259.
CleanExiHS_ATN1.
ExpressionAtlasiP54259. baseline and differential.
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.
GeneTreeiENSGT00580000081398.
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

« Hide

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

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.3 Publications
VAR_064038

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
GeneTreei ENSGT00580000081398.
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

Bgeei P54259.
CleanExi HS_ATN1.
ExpressionAtlasi P54259. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 136 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

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