JUPI2_HUMAN
ID JUPI2_HUMAN Reviewed; 190 AA.
AC Q9H910; B1AJY2; B4DLH4; Q6EIC7;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Jupiter microtubule associated homolog 2 {ECO:0000312|HGNC:HGNC:14137};
DE AltName: Full=Hematological and neurological expressed 1-like protein {ECO:0000303|PubMed:15094197};
DE Short=HN1-like protein;
GN Name=JPT2 {ECO:0000312|HGNC:HGNC:14137};
GN Synonyms=C16orf34, HN1L {ECO:0000303|PubMed:15094197}; ORFNames=L11;
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 AND 2), SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain, and Liver;
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), INDUCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15334068; DOI=10.1038/sj.onc.1207921;
RA Petroziello J., Yamane A., Westendorf L., Thompson M., McDonagh C.,
RA Cerveny C., Law C.-L., Wahl A., Carter P.;
RT "Suppression subtractive hybridization and expression profiling identifies
RT a unique set of genes overexpressed in non-small-cell lung cancer.";
RL Oncogene 23:7734-7745(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Teratocarcinoma, and Tongue;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; THR-35; SER-97 AND
RP SER-144, AND 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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND IDENTIFICATION BY
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND IDENTIFICATION BY
RP 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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, 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 [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-69; SER-97; SER-132
RP AND SER-144, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [18]
RP FUNCTION, FUNCTION (MICROBIAL INFECTION), SUBUNIT, AND INTERACTION WITH
RP TPCN1.
RX PubMed=33758061; DOI=10.1126/scisignal.abd5605;
RA Gunaratne G.S., Brailoiu E., He S., Unterwald E.M., Patel S., Slama J.T.,
RA Walseth T.F., Marchant J.S.;
RT "Essential requirement for JPT2 in NAADP-evoked Ca2+ signaling.";
RL Sci. Signal. 14:0-0(2021).
RN [19]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=33758062; DOI=10.1126/scisignal.abd5647;
RA Roggenkamp H.G., Khansahib I., Hernandez C.L.C., Zhang Y., Lodygin D.,
RA Krueger A., Gu F., Moeckl F., Loehndorf A., Wolters V., Woike D.,
RA Rosche A., Bauche A., Schetelig D., Werner R., Schlueter H., Failla A.V.,
RA Meier C., Fliegert R., Walseth T.F., Fluegel A., Diercks B.P., Guse A.H.;
RT "HN1L/JPT2: A signaling protein that connects NAADP generation to Ca2+
RT microdomain formation.";
RL Sci. Signal. 14:0-0(2021).
CC -!- FUNCTION: Nicotinic acid adenine dinucleotide phosphate (NAADP) binding
CC protein required for NAADP-evoked intracellular calcium release
CC (PubMed:33758061, PubMed:33758062). Confers NAADP-sensitivity to the
CC two pore channels (TPCs) complex (PubMed:33758061). Enables NAADP to
CC activate Ca(2+) release from the endoplasmic reticulum through
CC ryanodine receptors (PubMed:33758062). {ECO:0000269|PubMed:33758061,
CC ECO:0000269|PubMed:33758062}.
CC -!- FUNCTION: (Microbial infection) Involved in the endolysosomal
CC trafficking of coronaviruse SARS-CoV-2. {ECO:0000269|PubMed:33758061}.
CC -!- SUBUNIT: Monomer (PubMed:33758062). Dimer (PubMed:33758062). Interacts
CC with TPCN1 (PubMed:33758061). {ECO:0000269|PubMed:33758061,
CC ECO:0000269|PubMed:33758062}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15094197,
CC ECO:0000269|PubMed:33758062}. Nucleus {ECO:0000269|PubMed:15094197}.
CC Note=Colocalizes with type 1 ryanodine receptor (RYR1).
CC {ECO:0000269|PubMed:33758062}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=HN1LA;
CC IsoId=Q9H910-1; Sequence=Displayed;
CC Name=2; Synonyms=HN1LB, HN1LC;
CC IsoId=Q9H910-2; Sequence=VSP_014706;
CC Name=3;
CC IsoId=Q9H910-3; Sequence=VSP_057423;
CC -!- TISSUE SPECIFICITY: Expressed in liver, kidney, prostate, testis and
CC uterus. {ECO:0000269|PubMed:15094197}.
CC -!- INDUCTION: Up-regulated in squamous cell carcinoma (SCC) adenocarcinoma
CC (AC), adenosquamous cell carcinoma (ASCC), bronchioalveolar carcinoma
CC (BAC), breast and uterus tumors. {ECO:0000269|PubMed:15334068}.
CC -!- SIMILARITY: Belongs to the JUPITER family. {ECO:0000305}.
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DR EMBL; AY323831; AAP72616.1; -; Genomic_DNA.
DR EMBL; AY323978; AAP83791.1; -; mRNA.
DR EMBL; AY323979; AAP83792.1; -; mRNA.
DR EMBL; AY598330; AAT06741.1; -; mRNA.
DR EMBL; AK023154; BAB14434.1; -; mRNA.
DR EMBL; AE006639; AAK61289.1; -; Genomic_DNA.
DR EMBL; AK296998; BAG59536.1; -; mRNA.
DR EMBL; AL031009; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL031710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85635.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85638.1; -; Genomic_DNA.
DR EMBL; BC014438; AAH14438.1; -; mRNA.
DR EMBL; BC060853; AAH60853.1; -; mRNA.
DR CCDS; CCDS10441.1; -. [Q9H910-1]
DR RefSeq; NP_653171.1; NM_144570.2. [Q9H910-1]
DR AlphaFoldDB; Q9H910; -.
DR BioGRID; 124774; 33.
DR IntAct; Q9H910; 11.
DR STRING; 9606.ENSP00000248098; -.
DR ChEMBL; CHEMBL4295946; -.
DR GlyGen; Q9H910; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H910; -.
DR MetOSite; Q9H910; -.
DR PhosphoSitePlus; Q9H910; -.
DR BioMuta; JPT2; -.
DR EPD; Q9H910; -.
DR jPOST; Q9H910; -.
DR MassIVE; Q9H910; -.
DR MaxQB; Q9H910; -.
DR PaxDb; Q9H910; -.
DR PeptideAtlas; Q9H910; -.
DR PRIDE; Q9H910; -.
DR ProteomicsDB; 4534; -.
DR ProteomicsDB; 81270; -. [Q9H910-1]
DR ProteomicsDB; 81271; -. [Q9H910-2]
DR TopDownProteomics; Q9H910-1; -. [Q9H910-1]
DR Antibodypedia; 23196; 81 antibodies from 15 providers.
DR DNASU; 90861; -.
DR Ensembl; ENST00000248098.8; ENSP00000248098.3; ENSG00000206053.13. [Q9H910-1]
DR Ensembl; ENST00000382711.9; ENSP00000372158.5; ENSG00000206053.13. [Q9H910-2]
DR Ensembl; ENST00000562684.5; ENSP00000457694.1; ENSG00000206053.13. [Q9H910-3]
DR GeneID; 90861; -.
DR KEGG; hsa:90861; -.
DR MANE-Select; ENST00000248098.8; ENSP00000248098.3; NM_144570.3; NP_653171.1.
DR UCSC; uc002cmg.4; human. [Q9H910-1]
DR UCSC; uc010uvi.3; human.
DR CTD; 90861; -.
DR DisGeNET; 90861; -.
DR GeneCards; JPT2; -.
DR HGNC; HGNC:14137; JPT2.
DR HPA; ENSG00000206053; Low tissue specificity.
DR MIM; 619241; gene.
DR neXtProt; NX_Q9H910; -.
DR OpenTargets; ENSG00000206053; -.
DR PharmGKB; PA162391043; -.
DR VEuPathDB; HostDB:ENSG00000206053; -.
DR eggNOG; ENOG502S1G7; Eukaryota.
DR GeneTree; ENSGT00390000007652; -.
DR HOGENOM; CLU_111612_0_0_1; -.
DR InParanoid; Q9H910; -.
DR OMA; MLKNHEP; -.
DR OrthoDB; 1620782at2759; -.
DR PhylomeDB; Q9H910; -.
DR TreeFam; TF327169; -.
DR PathwayCommons; Q9H910; -.
DR SignaLink; Q9H910; -.
DR BioGRID-ORCS; 90861; 10 hits in 1072 CRISPR screens.
DR ChiTaRS; HN1L; human.
DR GeneWiki; HN1L; -.
DR GenomeRNAi; 90861; -.
DR Pharos; Q9H910; Tbio.
DR PRO; PR:Q9H910; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9H910; protein.
DR Bgee; ENSG00000206053; Expressed in epithelium of bronchus and 197 other tissues.
DR ExpressionAtlas; Q9H910; baseline and differential.
DR Genevisible; Q9H910; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IDA:UniProtKB.
DR GO; GO:0050848; P:regulation of calcium-mediated signaling; IMP:UniProtKB.
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; Host-virus interaction;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..190
FT /note="Jupiter microtubule associated homolog 2"
FT /id="PRO_0000054921"
FT REGION 1..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..171
FT /note="Basic and acidic 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 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 35
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..17
FT /note="MFQVPDSEGGRAGSRAM -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15094197"
FT /id="VSP_014706"
FT VAR_SEQ 14
FT /note="S -> SRKWQLLTGSLASTSPSLLSGQGPWAPLQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057423"
SQ SEQUENCE 190 AA; 20063 MW; 9132F17687193192 CRC64;
MFQVPDSEGG RAGSRAMKPP GGESSNLFGS PEEATPSSRP NRMASNIFGP TEEPQNIPKR
TNPPGGKGSG IFDESTPVQT RQHLNPPGGK TSDIFGSPVT ATSRLAHPNK PKDHVFLCEG
EEPKSDLKAA RSIPAGAEPG EKGSARKAGP AKEQEPMPTV DSHEPRLGPR PRSHNKVLNP
PGGKSSISFY
