JUPI1_BOVIN
ID JUPI1_BOVIN Reviewed; 154 AA.
AC Q3T0T5;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Jupiter microtubule associated homolog 1 {ECO:0000250|UniProtKB:Q9UK76};
DE AltName: Full=Hematological and neurological expressed 1 protein {ECO:0000250|UniProtKB:Q9UK76};
DE Contains:
DE RecName: Full=Jupiter microtubule associated homolog 1, N-terminally processed;
GN Name=JPT1 {ECO:0000250|UniProtKB:Q9UK76};
GN Synonyms=HN1 {ECO:0000250|UniProtKB:Q9UK76};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; BC102268; AAI02269.1; -; mRNA.
DR RefSeq; NP_001029906.1; NM_001034734.2.
DR AlphaFoldDB; Q3T0T5; -.
DR STRING; 9913.ENSBTAP00000040191; -.
DR PaxDb; Q3T0T5; -.
DR PeptideAtlas; Q3T0T5; -.
DR PRIDE; Q3T0T5; -.
DR Ensembl; ENSBTAT00000081279; ENSBTAP00000074060; ENSBTAG00000030170.
DR GeneID; 613381; -.
DR KEGG; bta:613381; -.
DR CTD; 51155; -.
DR VEuPathDB; HostDB:ENSBTAG00000030170; -.
DR VGNC; VGNC:55841; JPT1.
DR eggNOG; ENOG502S346; Eukaryota.
DR GeneTree; ENSGT00940000164037; -.
DR HOGENOM; CLU_123394_0_0_1; -.
DR InParanoid; Q3T0T5; -.
DR OMA; YQGMEPG; -.
DR OrthoDB; 1438333at2759; -.
DR TreeFam; TF327169; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000030170; Expressed in Ammon's horn and 106 other tissues.
DR ExpressionAtlas; Q3T0T5; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR InterPro; IPR033335; JUPITER.
DR PANTHER; PTHR34930; PTHR34930; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..154
FT /note="Jupiter microtubule associated homolog 1"
FT /id="PRO_0000054917"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UK76"
FT CHAIN 2..154
FT /note="Jupiter microtubule associated homolog 1, N-
FT terminally processed"
FT /id="PRO_0000424486"
FT REGION 1..154
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 125..142
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:0000250|UniProtKB:Q9UK76"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK76"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK76"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK76"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK76"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK76"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK76"
FT MOD_RES 148
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK76"
SQ SEQUENCE 154 AA; 16010 MW; 9F17C856636B889F CRC64;
MTTTTTFKGV DPNSRNSSRV LRPPGGGSNF SLGFDEPTEQ PVRRNKMASS IFGTPEENPP
SWAKSAGAKS SGGREDAESS GPQRRNSSEA NSGDFLDLKG EGDVHENVDT DLQASLGQSE
EKPVPAAPVP SPVAPAPVPS RRNPPGGKSS LVLG
