JUPI1_HUMAN
ID JUPI1_HUMAN Reviewed; 154 AA.
AC Q9UK76; B2R6K3; Q53FG7; Q7Z2D2; Q7Z2F0;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Jupiter microtubule associated homolog 1 {ECO:0000312|HGNC:HGNC:14569};
DE AltName: Full=Androgen-regulated protein 2;
DE AltName: Full=Hematological and neurological expressed 1 protein;
DE Contains:
DE RecName: Full=Jupiter microtubule associated homolog 1, N-terminally processed;
GN Name=JPT1 {ECO:0000312|HGNC:HGNC:14569};
GN Synonyms=ARM2, HN1 {ECO:0000303|PubMed:21323578};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3), AND TISSUE
RP SPECIFICITY.
RX PubMed=15094197; DOI=10.1016/j.gene.2004.02.025;
RA Zhou G., Wang J., Zhang Y., Zhong C., Ni J., Wang L., Guo J., Zhang K.,
RA Yu L., Zhao S.;
RT "Cloning, expression and subcellular localization of HN1 and HN1L genes, as
RT well as characterization of their orthologs, defining an evolutionarily
RT conserved gene family.";
RL Gene 331:115-123(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=T-cell;
RA Ji Y., Huang T., Johnson B.H., Thompson E.B.;
RT "Cloning of human homolog of Hn1 cDNA.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC TISSUE=Prostatic carcinoma;
RA Korkmaz K.S., Korkmaz C.G., Saatcioglu F.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Thymus;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Placenta, and 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 [8]
RP PROTEIN SEQUENCE OF 85-99, ACETYLATION AT THR-2, PHOSPHORYLATION AT SER-87,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16602700; DOI=10.1021/pr050415p;
RA Zougman A., Wisniewski J.R.;
RT "Beyond linker histones and high mobility group proteins: global profiling
RT of perchloric acid soluble proteins.";
RL J. Proteome Res. 5:925-934(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54; SER-80 AND SER-87, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54; SER-87 AND SER-88, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-148, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54; SER-87; SER-88 AND
RP SER-131, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION BY EGF.
RX PubMed=21323578; DOI=10.1089/dna.2010.1128;
RA Varisli L., Gonen-Korkmaz C., Debelec-Butuner B., Erbaykent-Tepedelen B.,
RA Muhammed H.S., Bogurcu N., Saatcioglu F., Korkmaz K.S.;
RT "Ubiquitously expressed hematological and neurological expressed 1
RT downregulates Akt-mediated GSK3beta signaling, and its knockdown results in
RT deregulated G2/M transition in prostate cells.";
RL DNA Cell Biol. 30:419-429(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP FUNCTION, AND INDUCTION BY ANDROGENS.
RX PubMed=22155408; DOI=10.1016/j.mce.2011.11.027;
RA Varisli L., Gonen-Korkmaz C., Syed H.M., Bogurcu N., Debelec-Butuner B.,
RA Erbaykent-Tepedelen B., Korkmaz K.S.;
RT "Androgen regulated HN1 leads proteosomal degradation of androgen receptor
RT (AR) and negatively influences AR mediated transactivation in prostate
RT cells.";
RL Mol. Cell. Endocrinol. 350:107-117(2012).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-31; THR-54; SER-71;
RP SER-80; SER-87; SER-88 AND SER-92, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [23]
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).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [25]
RP FUNCTION, AND INTERACTION WITH A COMPLEX COMPOSED OF AXIN1; AXIN2; APC;
RP CSNK1A1 AND GSK3B.
RX PubMed=25169422; DOI=10.1002/jcb.24956;
RA Varisli L., Ozturk B.E., Akyuz G.K., Korkmaz K.S.;
RT "HN1 negatively influences the beta-catenin/E-cadherin interaction, and
RT contributes to migration in prostate cells.";
RL J. Cell. Biochem. 116:170-178(2015).
CC -!- FUNCTION: Modulates negatively AKT-mediated GSK3B signaling
CC (PubMed:21323578, PubMed:22155408). Induces CTNNB1 'Ser-33'
CC phosphorylation and degradation through the suppression of the
CC 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 (PubMed:25169422). Plays a role
CC in the regulation of cell cycle and cell adhesion (PubMed:25169422,
CC PubMed:25450365). Has an inhibitory role on AR-signaling pathway
CC through the induction of receptor proteosomal degradation
CC (PubMed:22155408). {ECO:0000269|PubMed:21323578,
CC ECO:0000269|PubMed:22155408, ECO:0000269|PubMed:25169422,
CC 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:0000269|PubMed:25169422}.
CC -!- INTERACTION:
CC Q9UK76; P55212: CASP6; NbExp=3; IntAct=EBI-720411, EBI-718729;
CC Q9UK76; P06307: CCK; NbExp=3; IntAct=EBI-720411, EBI-6624398;
CC Q9UK76; O00291: HIP1; NbExp=3; IntAct=EBI-720411, EBI-473886;
CC Q9UK76; P13473-2: LAMP2; NbExp=3; IntAct=EBI-720411, EBI-21591415;
CC Q9UK76; P32243-2: OTX2; NbExp=3; IntAct=EBI-720411, EBI-9087860;
CC Q9UK76; P62826: RAN; NbExp=3; IntAct=EBI-720411, EBI-286642;
CC Q9UK76; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-720411, EBI-2623095;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21323578}. Cytoplasm
CC {ECO:0000269|PubMed:25169422}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=HN1A;
CC IsoId=Q9UK76-1; Sequence=Displayed;
CC Name=2; Synonyms=HN1B;
CC IsoId=Q9UK76-2; Sequence=VSP_017133;
CC Name=3; Synonyms=HN1C;
CC IsoId=Q9UK76-3; Sequence=VSP_017132;
CC -!- TISSUE SPECIFICITY: Expressed in testis, skeletal muscle, thymus,
CC prostate, colon, peripheral blood cells, brain and placenta.
CC {ECO:0000269|PubMed:15094197}.
CC -!- INDUCTION: Induced by EGF growth factor at mRNA and protein levels
CC (PubMed:21323578). Induced by androgens (PubMed:22155408). Negatively
CC regulated by the microRNA miR-132 (PubMed:25450365).
CC {ECO:0000269|PubMed:21323578, ECO:0000269|PubMed:22155408,
CC ECO:0000269|PubMed:25450365}.
CC -!- SIMILARITY: Belongs to the JUPITER family. {ECO:0000305}.
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DR EMBL; AF086910; AAP97140.1; -; mRNA.
DR EMBL; AY322169; AAP83838.1; -; mRNA.
DR EMBL; AY322170; AAP83839.1; -; mRNA.
DR EMBL; AF348672; AAL83903.1; -; Genomic_DNA.
DR EMBL; AF348672; AAP83962.1; -; Genomic_DNA.
DR EMBL; AF348672; AAP83963.1; -; Genomic_DNA.
DR EMBL; AF177862; AAD53312.1; -; mRNA.
DR EMBL; AF266846; AAQ14298.1; -; mRNA.
DR EMBL; AF266847; AAQ14299.1; -; Genomic_DNA.
DR EMBL; AK223321; BAD97041.1; -; mRNA.
DR EMBL; AK312613; BAG35500.1; -; mRNA.
DR EMBL; CH471099; EAW89244.1; -; Genomic_DNA.
DR EMBL; BC001420; AAH01420.1; -; mRNA.
DR EMBL; BC039343; AAH39343.1; -; mRNA.
DR CCDS; CCDS32729.1; -. [Q9UK76-2]
DR CCDS; CCDS45771.1; -. [Q9UK76-1]
DR CCDS; CCDS45772.1; -. [Q9UK76-3]
DR RefSeq; NP_001002032.1; NM_001002032.2. [Q9UK76-2]
DR RefSeq; NP_001002033.1; NM_001002033.2. [Q9UK76-3]
DR RefSeq; NP_001275538.1; NM_001288609.1. [Q9UK76-3]
DR RefSeq; NP_001275539.1; NM_001288610.1. [Q9UK76-3]
DR RefSeq; NP_001275540.1; NM_001288611.1.
DR RefSeq; NP_057269.1; NM_016185.3. [Q9UK76-1]
DR AlphaFoldDB; Q9UK76; -.
DR BioGRID; 119338; 27.
DR IntAct; Q9UK76; 14.
DR MINT; Q9UK76; -.
DR STRING; 9606.ENSP00000348316; -.
DR GlyGen; Q9UK76; 1 site.
DR iPTMnet; Q9UK76; -.
DR MetOSite; Q9UK76; -.
DR PhosphoSitePlus; Q9UK76; -.
DR BioMuta; JPT1; -.
DR EPD; Q9UK76; -.
DR jPOST; Q9UK76; -.
DR MassIVE; Q9UK76; -.
DR MaxQB; Q9UK76; -.
DR PaxDb; Q9UK76; -.
DR PeptideAtlas; Q9UK76; -.
DR PRIDE; Q9UK76; -.
DR ProteomicsDB; 84734; -. [Q9UK76-1]
DR ProteomicsDB; 84735; -. [Q9UK76-2]
DR ProteomicsDB; 84736; -. [Q9UK76-3]
DR TopDownProteomics; Q9UK76-1; -. [Q9UK76-1]
DR TopDownProteomics; Q9UK76-2; -. [Q9UK76-2]
DR TopDownProteomics; Q9UK76-3; -. [Q9UK76-3]
DR Antibodypedia; 32102; 236 antibodies from 28 providers.
DR DNASU; 51155; -.
DR Ensembl; ENST00000356033.8; ENSP00000348316.4; ENSG00000189159.16. [Q9UK76-2]
DR Ensembl; ENST00000409753.8; ENSP00000387059.3; ENSG00000189159.16. [Q9UK76-1]
DR Ensembl; ENST00000470924.5; ENSP00000462784.1; ENSG00000189159.16. [Q9UK76-3]
DR Ensembl; ENST00000476258.5; ENSP00000464266.1; ENSG00000189159.16. [Q9UK76-3]
DR Ensembl; ENST00000481647.5; ENSP00000462478.1; ENSG00000189159.16. [Q9UK76-3]
DR Ensembl; ENST00000482348.5; ENSP00000462834.1; ENSG00000189159.16. [Q9UK76-3]
DR GeneID; 51155; -.
DR KEGG; hsa:51155; -.
DR MANE-Select; ENST00000409753.8; ENSP00000387059.3; NM_016185.4; NP_057269.1.
DR UCSC; uc002jna.3; human. [Q9UK76-1]
DR CTD; 51155; -.
DR DisGeNET; 51155; -.
DR GeneCards; JPT1; -.
DR HGNC; HGNC:14569; JPT1.
DR HPA; ENSG00000189159; Tissue enhanced (testis).
DR MIM; 619242; gene.
DR neXtProt; NX_Q9UK76; -.
DR OpenTargets; ENSG00000189159; -.
DR PharmGKB; PA29347; -.
DR VEuPathDB; HostDB:ENSG00000189159; -.
DR eggNOG; ENOG502TDPY; Eukaryota.
DR GeneTree; ENSGT00940000162422; -.
DR HOGENOM; CLU_123394_0_0_1; -.
DR InParanoid; Q9UK76; -.
DR OMA; EQGNDEC; -.
DR OrthoDB; 1279488at2759; -.
DR PhylomeDB; Q9UK76; -.
DR TreeFam; TF327169; -.
DR PathwayCommons; Q9UK76; -.
DR SignaLink; Q9UK76; -.
DR BioGRID-ORCS; 51155; 7 hits in 622 CRISPR screens.
DR ChiTaRS; JPT1; human.
DR GeneWiki; HN1_(gene); -.
DR GenomeRNAi; 51155; -.
DR Pharos; Q9UK76; Tbio.
DR PRO; PR:Q9UK76; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9UK76; protein.
DR Bgee; ENSG00000189159; Expressed in cortical plate and 192 other tissues.
DR ExpressionAtlas; Q9UK76; baseline and differential.
DR Genevisible; Q9UK76; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..154
FT /note="Jupiter microtubule associated homolog 1"
FT /id="PRO_0000424487"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|PubMed:16602700,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..154
FT /note="Jupiter microtubule associated homolog 1, N-
FT terminally processed"
FT /id="PRO_0000054918"
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 43..66
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:0007744|PubMed:22814378"
FT MOD_RES 2
FT /note="N-acetylthreonine; in Hematological and neurological
FT expressed 1 protein, N-terminally processed"
FT /evidence="ECO:0000269|PubMed:16602700,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 54
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16602700,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 148
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..46
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15094197,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_017132"
FT VAR_SEQ 100..154
FT /note="GEGDIHENVDTDLPGSLGQSEEKPVPAAPVPSPVAPAPVPSRRNPPGGKSSL
FT VLG -> KMWTQTCQAAWGRVKRSPCLLRLCPARWPRPQCHPEEIPLAASPASSWVSSD
FT CPERCRSVCFLHACELHNLSLTVHLLDLFH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15094197"
FT /id="VSP_017133"
FT CONFLICT 85
FT /note="R -> G (in Ref. 5; BAD97041)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 154 AA; 16015 MW; 1B443E4C7A28F093 CRC64;
MTTTTTFKGV DPNSRNSSRV LRPPGGGSNF SLGFDEPTEQ PVRKNKMASN IFGTPEENQA
SWAKSAGAKS SGGREDLESS GLQRRNSSEA SSGDFLDLKG EGDIHENVDT DLPGSLGQSE
EKPVPAAPVP SPVAPAPVPS RRNPPGGKSS LVLG
