JUPI1_RAT
ID JUPI1_RAT Reviewed; 149 AA.
AC Q6AXU6;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Jupiter microtubule associated homolog 1 {ECO:0000250|UniProtKB:Q9UK76};
DE AltName: Full=Hematological and neurological expressed 1 protein {ECO:0000312|RGD:1359325};
DE Contains:
DE RecName: Full=Jupiter microtubule associated homolog 1, N-terminally processed;
GN Name=JPT1 {ECO:0000250|UniProtKB:Q9UK76};
GN Synonyms=Hn1 {ECO:0000312|RGD:1359325};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54; SER-82; SER-83 AND
RP SER-87, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Modulates negatively AKT-mediated GSK3B signaling. Induces
CC CTNNB1 'Ser-33' phosphorylation and degradation through the suppression
CC of the inhibitory 'Ser-9' phosphorylation of GSK3B, which represses the
CC function of the APC:CTNNB1:GSK3B complex and the interaction with
CC CDH1/E-cadherin in adherent junctions. Plays a role in the regulation
CC of cell cycle and cell adhesion. Has an inhibitory role on AR-signaling
CC pathway through the induction of receptor proteosomal degradation.
CC {ECO:0000250|UniProtKB:Q9UK76}.
CC -!- SUBUNIT: Interacts with the complex composed, at least, of APC, CTNNB1
CC and GSK3B; the interaction takes place with the inactive form of GSK3B
CC (phosphorylated at 'Ser-9'). {ECO:0000250|UniProtKB:Q9UK76}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UK76}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9UK76}.
CC -!- SIMILARITY: Belongs to the JUPITER family. {ECO:0000305}.
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DR EMBL; BC079311; AAH79311.1; -; mRNA.
DR RefSeq; NP_001005876.1; NM_001005876.1.
DR AlphaFoldDB; Q6AXU6; -.
DR BioGRID; 252352; 1.
DR STRING; 10116.ENSRNOP00000004862; -.
DR iPTMnet; Q6AXU6; -.
DR PhosphoSitePlus; Q6AXU6; -.
DR jPOST; Q6AXU6; -.
DR PaxDb; Q6AXU6; -.
DR PRIDE; Q6AXU6; -.
DR GeneID; 287828; -.
DR KEGG; rno:287828; -.
DR CTD; 51155; -.
DR RGD; 1359325; Hn1.
DR VEuPathDB; HostDB:ENSRNOG00000003661; -.
DR eggNOG; ENOG502S346; Eukaryota.
DR HOGENOM; CLU_123394_0_0_1; -.
DR InParanoid; Q6AXU6; -.
DR OMA; EQGNDEC; -.
DR OrthoDB; 1438333at2759; -.
DR PRO; PR:Q6AXU6; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000003661; Expressed in duodenum and 20 other tissues.
DR ExpressionAtlas; Q6AXU6; baseline and differential.
DR Genevisible; Q6AXU6; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR InterPro; IPR033335; JUPITER.
DR PANTHER; PTHR34930; PTHR34930; 1.
DR Pfam; PF17054; JUPITER; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..149
FT /note="Jupiter microtubule associated homolog 1"
FT /id="PRO_0000054920"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UK76"
FT CHAIN 2..149
FT /note="Jupiter microtubule associated homolog 1, N-
FT terminally processed"
FT /id="PRO_0000424489"
FT REGION 1..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..137
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK76"
FT MOD_RES 2
FT /note="N-acetylthreonine; in Hematological and neurological
FT expressed 1 protein, N-terminally processed"
FT /evidence="ECO:0000250|UniProtKB:Q9UK76"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK76"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK76"
FT MOD_RES 54
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK76"
FT MOD_RES 143
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK76"
SQ SEQUENCE 149 AA; 15575 MW; 46E5EE8E32D5F413 CRC64;
MTTTTTFKGV DPNSRNSSRV LRPPGGGSNF SLGFDEPTEQ PVRKNKMASN IFGTPEENPP
SWAKSAGGRE DSESPGTQRS NSSEASSGDF LDLKGESDVH ENVDTDFQAS LAQVEEKPVP
AAPVPSPVAP APAPSRRNPP GGKSSLVLG
