JUPI1_MOUSE
ID JUPI1_MOUSE Reviewed; 154 AA.
AC P97825;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Jupiter microtubule associated homolog 1 {ECO:0000250|UniProtKB:Q9UK76};
DE AltName: Full=Hematological and neurological expressed 1 protein {ECO:0000312|MGI:MGI:1096361};
DE Contains:
DE RecName: Full=Jupiter microtubule associated homolog 1, N-terminally processed;
GN Name=Jpt1 {ECO:0000312|MGI:MGI:1096361};
GN Synonyms=Hn1 {ECO:0000312|MGI:MGI:1096361};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Erythroid cell;
RX PubMed=9271675; DOI=10.1007/s003359900540;
RA Tang W., Lai Y.H., Han X.D., Wong P.M.C., Peters L.L., Chui D.H.K.;
RT "Murine Hn1 on chromosome 11 is expressed in hemopoietic and brain
RT tissues.";
RL Mamm. Genome 8:695-696(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, and C57BL/6J;
RC TISSUE=Bone marrow, Embryo, Fetal head, Fetal heart, Placenta, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54; SER-87 AND SER-88, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-148, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8]
RP FUNCTION, AND INDUCTION BY MIR-132.
RX PubMed=25450365; DOI=10.1016/j.bbrc.2014.10.049;
RA Zhang Z.G., Chen W.X., Wu Y.H., Liang H.F., Zhang B.X.;
RT "MiR-132 prohibits proliferation, invasion, migration, and metastasis in
RT breast cancer by targeting HN1.";
RL Biochem. Biophys. Res. Commun. 454:109-114(2014).
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 (By similarity). Plays a role in
CC the regulation of cell cycle and cell adhesion (PubMed:25450365). Has
CC an inhibitory role on AR-signaling pathway through the induction of
CC receptor proteosomal degradation (By similarity).
CC {ECO:0000250|UniProtKB:Q9UK76, ECO:0000269|PubMed:25450365}.
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 -!- TISSUE SPECIFICITY: Expressed in yolk sac, fetal brain, brain, spleen
CC and bone marrow. {ECO:0000269|PubMed:9271675}.
CC -!- INDUCTION: Negatively regulated by the microRNA miR-132.
CC {ECO:0000269|PubMed:25450365}.
CC -!- SIMILARITY: Belongs to the JUPITER family. {ECO:0000305}.
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DR EMBL; U90123; AAB70094.1; -; mRNA.
DR EMBL; AK152560; BAE31313.1; -; mRNA.
DR EMBL; AK010057; BAB26672.1; -; mRNA.
DR EMBL; AK013122; BAB28661.1; -; mRNA.
DR EMBL; AK014212; BAB29208.1; -; mRNA.
DR EMBL; AK159784; BAE35368.1; -; mRNA.
DR EMBL; AK167466; BAE39550.1; -; mRNA.
DR EMBL; AK167961; BAE39958.1; -; mRNA.
DR EMBL; AK168632; BAE40492.1; -; mRNA.
DR EMBL; BC003758; AAH03758.1; -; mRNA.
DR CCDS; CCDS25638.1; -.
DR RefSeq; NP_032284.1; NM_008258.1.
DR AlphaFoldDB; P97825; -.
DR BioGRID; 200350; 2.
DR IntAct; P97825; 1.
DR MINT; P97825; -.
DR STRING; 10090.ENSMUSP00000021083; -.
DR iPTMnet; P97825; -.
DR PhosphoSitePlus; P97825; -.
DR EPD; P97825; -.
DR jPOST; P97825; -.
DR MaxQB; P97825; -.
DR PaxDb; P97825; -.
DR PeptideAtlas; P97825; -.
DR PRIDE; P97825; -.
DR ProteomicsDB; 269125; -.
DR DNASU; 15374; -.
DR Ensembl; ENSMUST00000021083; ENSMUSP00000021083; ENSMUSG00000020737.
DR GeneID; 15374; -.
DR KEGG; mmu:15374; -.
DR UCSC; uc007mhv.1; mouse.
DR CTD; 51155; -.
DR MGI; MGI:1096361; Jpt1.
DR VEuPathDB; HostDB:ENSMUSG00000020737; -.
DR eggNOG; ENOG502S346; Eukaryota.
DR GeneTree; ENSGT00940000162422; -.
DR HOGENOM; CLU_123394_0_0_1; -.
DR InParanoid; P97825; -.
DR OMA; EQGNDEC; -.
DR OrthoDB; 1438333at2759; -.
DR PhylomeDB; P97825; -.
DR TreeFam; TF327169; -.
DR BioGRID-ORCS; 15374; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Hn1; mouse.
DR PRO; PR:P97825; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P97825; protein.
DR Bgee; ENSMUSG00000020737; Expressed in barrel cortex and 266 other tissues.
DR Genevisible; P97825; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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..154
FT /note="Jupiter microtubule associated homolog 1"
FT /id="PRO_0000054919"
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_0000424488"
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 51..93
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:0007744|PubMed:21183079"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK76"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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:0007744|PubMed:23806337"
SQ SEQUENCE 154 AA; 16081 MW; F358F8F697ED221F CRC64;
MTTTTTFKGV DPNSRNSSRV LRPPGGGSNF SLGFDEPAEQ PVRKNKMASN IFGTPEENPP
SWAKSAGSKS SGGREDSESP GTQRSNSSEA SSGDFLDLKG EGDMHENVDT DFQANLAQME
EKPVPAAPVP SPVAPAPVPS RRNPPGGKSS LVLG
