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Protein

Atrophin-1

Gene

Atn1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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. Corepressor of MTG8 transcriptional repression. Has some intrinsic repression activity (By similarity).By similarity

GO - Molecular functioni

  • JUN kinase binding Source: RGD

GO - Biological processi

  • regulation of neuron differentiation Source: RGD
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • 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 homolog
Gene namesi
Name:Atn1
Synonyms:Drpla
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi61832. Atn1.

Subcellular locationi

  • Nucleus 1 Publication
  • Cytoplasmperinuclear region 1 Publication
  • Cell junction 1 Publication

  • Note: Shuttles between nucleus and cytoplasm. Colocalizes with MTG8 in discrete nuclear dots (By similarity). Colocalizes with FAT1 in the perinuclear area, at cell-cell junctions and leading edges of cells.By similarity

GO - Cellular componenti

  • cell junction Source: UniProtKB-SubCell
  • cell leading edge Source: UniProtKB
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000647321 – 1183Atrophin-1Add BLAST1183

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei34PhosphoserineBy similarity1
Modified residuei77PhosphoserineCombined sources1
Modified residuei79PhosphoserineCombined sources1
Modified residuei100PhosphoserineCombined sources1
Modified residuei102PhosphoserineBy similarity1
Modified residuei106PhosphoserineCombined sources1
Modified residuei625PhosphoserineBy similarity1
Modified residuei634N6-acetyllysineBy similarity1
Modified residuei646PhosphothreonineBy similarity1
Modified residuei654PhosphoserineBy similarity1
Modified residuei662PhosphothreonineBy similarity1
Modified residuei732Phosphoserine; by MAPK8By similarity1
Modified residuei739PhosphoserineBy similarity1
Modified residuei741PhosphoserineBy similarity1
Modified residuei889PhosphoserineBy similarity1
Modified residuei1108Asymmetric dimethylarginineBy similarity1

Post-translational modificationi

Phosphorylated in vitro by MAPK8/JNK1 on Ser-732.By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP54258.
PRIDEiP54258.

PTM databases

iPTMnetiP54258.
PhosphoSitePlusiP54258.

Expressioni

Tissue specificityi

Predominant neuronal expression, Expressed in most brain regions including striatum, hippocampus, cerebral cortex, diencephalon, brain stem and cerebellum. Highest levels in cerebellum. Also highly expressed in kidney and testis, low expression in skeletal muscle and heart.1 Publication

Developmental stagei

Similar expression at all development stages (14.5 dpc, 17.5 dpc, newborns and adults).1 Publication

Inductioni

Induced after vascular injury and by growth factors. Decreased levels with INF-gamma.1 Publication

Interactioni

Subunit structurei

Interacts with NR2E1; the interaction represses the transcriptional activity of NR2E1. Interact (via its N-terminus) with FAT1 (via a C-terminal domain). 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 similarity).By similarity

GO - Molecular functioni

  • JUN kinase binding Source: RGD

Protein-protein interaction databases

MINTiMINT-93051.
STRINGi10116.ENSRNOP00000045475.

Structurei

3D structure databases

ProteinModelPortaliP54258.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni510 – 560Involved in binding BAIAP2By similarityAdd BLAST51
Regioni872 – 887Required for interaction with FAT1By similarityAdd BLAST16

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi16 – 32Nuclear localization signalBy similarityAdd BLAST17
Motifi1026 – 1034Nuclear export signalBy similarity9

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi165 – 171Poly-Pro7
Compositional biasi303 – 306Poly-Pro4
Compositional biasi377 – 383Poly-Ser7
Compositional biasi387 – 391Poly-Ser5
Compositional biasi440 – 446Poly-Pro7
Compositional biasi477 – 480Poly-His4
Compositional biasi481 – 489Poly-Gln9
Compositional biasi502 – 505Poly-Pro4
Compositional biasi562 – 572Poly-SerAdd BLAST11
Compositional biasi702 – 705Poly-Pro4
Compositional biasi800 – 813Ala/Arg-richAdd BLAST14
Compositional biasi814 – 825Arg/Glu-rich (mixed charge)Add BLAST12
Compositional biasi923 – 932Arg/Glu-rich (mixed charge)10
Compositional biasi1043 – 1070His-richAdd BLAST28

Phylogenomic databases

eggNOGiKOG2133. Eukaryota.
ENOG410ZIND. LUCA.
HOGENOMiHOG000231091.
HOVERGENiHBG075369.
InParanoidiP54258.
PhylomeDBiP54258.

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.

P54258-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTRQNKDSM SMRSGRKKEA PGPREELRSR GRASPGGVST SSSDGKAEKS
60 70 80 90 100
RQTAKKARVE ETSTPKANKQ GRSEEISESE SEETSAPKKT KTEELPRPQS
110 120 130 140 150
PSDLDSLDGR SINDDGSSDP RDIDQDNRST SPSIYSPGSV ENDSDSSSGL
160 170 180 190 200
SQGPARPYHP PPLFPPSPPP PDSIPRQPES GFEPHPSVPP TGYHAPMEPP
210 220 230 240 250
TSRLFQGPPP GAPPPHPQLY PGSAGGGVLS GPPMGPKGGA AASSVGPPSG
260 270 280 290 300
GKQHPPPTTP IPISSSGASG APPAKPPNTP VGAGNLPSAP PPATFPHVTP
310 320 330 340 350
NLPPPPALRP LNNASASPPG MGAQPIPGHL PSPHAMGQGM SGLPPGPEKG
360 370 380 390 400
PTLAPSPHPL PPASSSAPGP PMRYPYSSCS SSSVAASSSS SAATSQYPAS
410 420 430 440 450
QTLPSYPHSF PPPTSMSVSN QPPKYTQPSL PSQAVWSQGP PPPPPPYGRL
460 470 480 490 500
LPNNNTHPGP FPPTGGQSTA HPPAPAHHHH QQQQQPQPQP QPQQHHHGNS
510 520 530 540 550
GPPPPGAYPH PLESSNSHHA HPYNMSPSLG SLRPYPPGPA HLPPSHGQVS
560 570 580 590 600
YSQAGPNGPP VSSSSNSSGS SSQAAYSCSH PSSSQGPQGA SYPFPPVPPI
610 620 630 640 650
TTSSATLSTV IATVASSPAG YKTASPPGPP QYSKRAPSPG SYKTATPPGY
660 670 680 690 700
KPGSPPSFRT GTPPGYRGTS PPAGPGTFKP GSPTVGPGPL PPAGPSSLSS
710 720 730 740 750
LPPPPAAPTT GPPLTATQIK QEPAEEYETP ESPVPPARSP SPPPKVVDVP
760 770 780 790 800
SHASQSARFN KHLDRGFNSC ARSDLYFVPL EGSKLAKKRA DLVEKVRREA
810 820 830 840 850
EQRAREEKER EREREREKER EREKERELER SVKLAQEGRA PVECPSLGPV
860 870 880 890 900
PHRPPFEPGS AVATVPPYLG PDTPALRTLS EYARPHVMSP GNRNHPFYVP
910 920 930 940 950
LGAVDPGLLG YNVPALYSSD PAAREREREA RERDLRDRLK PGFEVKPSEL
960 970 980 990 1000
EPLHGVPGPG LDPFPRHGGL ALQPGPPGLH PFPFHPSLGP LERERLALAA
1010 1020 1030 1040 1050
GPALRPDMSY AERLAAERQH AERVAALGND PLARLQMLNV TPHHHQHSHI
1060 1070 1080 1090 1100
HSHLHLHQQD AIHAASASVH PLIDPLASGS HLTRIPYPAG TLPNPLLPHP
1110 1120 1130 1140 1150
LHENEVLRHQ LFAAPYRDLP ASLSAPMSAA HQLQAMHAQS AELQRLALEQ
1160 1170 1180
QQWLHAHHPL HSVPLPAQED YYSHLKKESD KPL
Length:1,183
Mass (Da):124,779
Last modified:October 1, 1996 - v1
Checksum:i7FB9928DCADF9B1F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti455N → S in CAA61623 (PubMed:8541849).Curated1
Sequence conflicti594F → L in CAA61623 (PubMed:8541849).Curated1
Sequence conflicti689P → R in CAA61623 (PubMed:8541849).Curated1
Sequence conflicti717T → M in CAA61623 (PubMed:8541849).Curated1
Sequence conflicti737A → V in CAA61623 (PubMed:8541849).Curated1
Sequence conflicti965Missing in CAA61623 (PubMed:8541849).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31777 mRNA. Translation: AAA80337.1.
X89453 Genomic DNA. Translation: CAA61623.1.
UniGeneiRn.11305.

Genome annotation databases

UCSCiRGD:61832. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31777 mRNA. Translation: AAA80337.1.
X89453 Genomic DNA. Translation: CAA61623.1.
UniGeneiRn.11305.

3D structure databases

ProteinModelPortaliP54258.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-93051.
STRINGi10116.ENSRNOP00000045475.

PTM databases

iPTMnetiP54258.
PhosphoSitePlusiP54258.

Proteomic databases

PaxDbiP54258.
PRIDEiP54258.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:61832. rat.

Organism-specific databases

RGDi61832. Atn1.

Phylogenomic databases

eggNOGiKOG2133. Eukaryota.
ENOG410ZIND. LUCA.
HOGENOMiHOG000231091.
HOVERGENiHBG075369.
InParanoidiP54258.
PhylomeDBiP54258.

Miscellaneous databases

PROiP54258.

Family and domain databases

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

Entry informationi

Entry nameiATN1_RAT
AccessioniPrimary (citable) accession number: P54258
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.