JTB_HUMAN
ID JTB_HUMAN Reviewed; 146 AA.
AC O76095; O95442; Q6IB19; Q9P0Q4;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Protein JTB;
DE AltName: Full=Jumping translocation breakpoint protein;
DE AltName: Full=Prostate androgen-regulated protein;
DE Short=PAR protein;
DE Flags: Precursor;
GN Name=JTB; ORFNames=HSPC222;
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] (ISOFORM 1), SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=10321732; DOI=10.1038/sj.onc.1202510;
RA Hatakeyama S., Osawa M., Omine M., Ishikawa F.;
RT "JTB: a novel membrane protein gene at 1q21 rearranged in a jumping
RT translocation.";
RL Oncogene 18:2085-2090(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Mammary cancer, and Prostatic carcinoma;
RX PubMed=10762645; DOI=10.3892/ijo.16.5.1055;
RA Platica O., Chen S., Ivan E., Lopingco M.C., Holland J.F., Platica M.;
RT "PAR, a novel androgen regulated gene, ubiquitously expressed in normal and
RT malignant cells.";
RL Int. J. Oncol. 16:1055-1061(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Mei G., Yu W., Gibbs R.A.;
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [9]
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 [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cervix, Lung, Skin, and Uterus;
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 [11]
RP TISSUE SPECIFICITY.
RX PubMed=17369841; DOI=10.1038/sj.onc.1210423;
RA Kanome T., Itoh N., Ishikawa F., Mori K., Kim-Kaneyama J.R., Nose K.,
RA Shibanuma M.;
RT "Characterization of Jumping translocation breakpoint (JTB) gene product
RT isolated as a TGF-beta1-inducible clone involved in regulation of
RT mitochondrial function, cell growth and cell death.";
RL Oncogene 26:5991-6001(2007).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH AURKA; AURKB AND BIRC5,
RP SUBUNIT, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=21225229; DOI=10.3892/ijo.2011.900;
RA Platica M., Ionescu A., Ivan E., Holland J.F., Mandeli J., Platica O.;
RT "PAR, a protein involved in the cell cycle, is functionally related to
RT chromosomal passenger proteins.";
RL Int. J. Oncol. 38:777-785(2011).
RN [13]
RP STRUCTURE BY NMR OF 47-104.
RX PubMed=22079049; DOI=10.1016/j.jmb.2011.10.048;
RA Rousseau F., Pan B., Fairbrother W.J., Bazan J.F., Lingel A.;
RT "The structure of the extracellular domain of the jumping translocation
RT breakpoint protein reveals a variation of the midkine fold.";
RL J. Mol. Biol. 415:22-28(2012).
CC -!- FUNCTION: Required for normal cytokinesis during mitosis. Plays a role
CC in the regulation of cell proliferation. May be a component of the
CC chromosomal passenger complex (CPC), a complex that acts as a key
CC regulator of mitosis. The CPC complex has essential functions at the
CC centromere in ensuring correct chromosome alignment and segregation and
CC is required for chromatin-induced microtubule stabilization and spindle
CC assembly. Increases AURKB activity. Inhibits apoptosis induced by TGFB1
CC (By similarity). Overexpression induces swelling of mitochondria and
CC reduces mitochondrial membrane potential (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:21225229}.
CC -!- SUBUNIT: Interacts with AURKA, AURKB, BIRC5 and INCENP. May be a
CC component of the CPC at least composed of BIRC5/survivin,
CC CDCA8/borealin, INCENP and AURKB/Aurora-B.
CC {ECO:0000269|PubMed:21225229}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Mitochondrion {ECO:0000250}. Cytoplasm.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
CC Cytoplasm, cytoskeleton, spindle. Note=Detected at the centrosome and
CC along spindle fibers during prophase and metaphase. Detected at the
CC midbody during telophase.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O76095-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O76095-2; Sequence=VSP_041400;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed in all normal human tissues
CC studied but overexpressed or underexpressed in many of their malignant
CC counterparts. {ECO:0000269|PubMed:10321732,
CC ECO:0000269|PubMed:10762645, ECO:0000269|PubMed:17369841,
CC ECO:0000269|PubMed:21225229}.
CC -!- INDUCTION: Protein levels increase during the S phase of the cell
CC cycle, are highest during G2 and mitosis, and decrease to low levels at
CC G1. Levels are lowest at the transition from G1 to S phase.
CC {ECO:0000269|PubMed:21225229}.
CC -!- SIMILARITY: Belongs to the JTB family. {ECO:0000305}.
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DR EMBL; AB016492; BAA33735.1; -; Genomic_DNA.
DR EMBL; AB016488; BAA33731.1; -; mRNA.
DR EMBL; AB016493; BAA33736.1; -; Genomic_DNA.
DR EMBL; AF115850; AAD09822.2; -; mRNA.
DR EMBL; AF131797; AAD20045.1; -; mRNA.
DR EMBL; AF151056; AAF36142.1; -; mRNA.
DR EMBL; BT007285; AAP35949.1; -; mRNA.
DR EMBL; CR456985; CAG33266.1; -; mRNA.
DR EMBL; AK312106; BAG35042.1; -; mRNA.
DR EMBL; AL358472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53241.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53242.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53244.1; -; Genomic_DNA.
DR EMBL; BC000499; AAH00499.1; -; mRNA.
DR EMBL; BC000996; AAH00996.1; -; mRNA.
DR EMBL; BC001363; AAH01363.1; -; mRNA.
DR EMBL; BC001667; AAH01667.1; -; mRNA.
DR EMBL; BC004239; AAH04239.1; -; mRNA.
DR EMBL; BC019277; AAH19277.1; -; mRNA.
DR CCDS; CCDS1057.1; -. [O76095-1]
DR RefSeq; NP_006685.1; NM_006694.3. [O76095-1]
DR PDB; 2KJX; NMR; -; A=47-104.
DR PDBsum; 2KJX; -.
DR AlphaFoldDB; O76095; -.
DR SMR; O76095; -.
DR BioGRID; 116105; 40.
DR IntAct; O76095; 6.
DR MINT; O76095; -.
DR STRING; 9606.ENSP00000271843; -.
DR GlyGen; O76095; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O76095; -.
DR PhosphoSitePlus; O76095; -.
DR BioMuta; JTB; -.
DR EPD; O76095; -.
DR jPOST; O76095; -.
DR MassIVE; O76095; -.
DR MaxQB; O76095; -.
DR PaxDb; O76095; -.
DR PeptideAtlas; O76095; -.
DR PRIDE; O76095; -.
DR ProteomicsDB; 50413; -. [O76095-1]
DR ProteomicsDB; 50414; -. [O76095-2]
DR Antibodypedia; 1668; 110 antibodies from 22 providers.
DR DNASU; 10899; -.
DR Ensembl; ENST00000271843.9; ENSP00000271843.4; ENSG00000143543.15. [O76095-1]
DR Ensembl; ENST00000356648.5; ENSP00000349069.1; ENSG00000143543.15. [O76095-2]
DR Ensembl; ENST00000368589.5; ENSP00000357578.1; ENSG00000143543.15. [O76095-2]
DR Ensembl; ENST00000428469.1; ENSP00000395250.1; ENSG00000143543.15. [O76095-2]
DR GeneID; 10899; -.
DR KEGG; hsa:10899; -.
DR MANE-Select; ENST00000271843.9; ENSP00000271843.4; NM_006694.4; NP_006685.1.
DR UCSC; uc001fds.4; human. [O76095-1]
DR CTD; 10899; -.
DR DisGeNET; 10899; -.
DR GeneCards; JTB; -.
DR HGNC; HGNC:6201; JTB.
DR HPA; ENSG00000143543; Low tissue specificity.
DR MIM; 604671; gene.
DR neXtProt; NX_O76095; -.
DR OpenTargets; ENSG00000143543; -.
DR PharmGKB; PA30003; -.
DR VEuPathDB; HostDB:ENSG00000143543; -.
DR eggNOG; KOG4084; Eukaryota.
DR GeneTree; ENSGT00390000016136; -.
DR HOGENOM; CLU_130083_1_0_1; -.
DR InParanoid; O76095; -.
DR OMA; GRRLCWL; -.
DR OrthoDB; 1375062at2759; -.
DR PhylomeDB; O76095; -.
DR TreeFam; TF316934; -.
DR PathwayCommons; O76095; -.
DR SignaLink; O76095; -.
DR BioGRID-ORCS; 10899; 87 hits in 1083 CRISPR screens.
DR ChiTaRS; JTB; human.
DR EvolutionaryTrace; O76095; -.
DR GeneWiki; JTB_(gene); -.
DR GenomeRNAi; 10899; -.
DR Pharos; O76095; Tbio.
DR PRO; PR:O76095; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O76095; protein.
DR Bgee; ENSG00000143543; Expressed in parotid gland and 202 other tissues.
DR Genevisible; O76095; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0019901; F:protein kinase binding; IDA:UniProtKB.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; IEA:Ensembl.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IMP:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR InterPro; IPR008657; JTB.
DR PANTHER; PTHR13041; PTHR13041; 1.
DR Pfam; PF05439; JTB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Cell cycle; Cell division;
KW Cytoplasm; Cytoskeleton; Membrane; Mitochondrion; Mitosis;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..146
FT /note="Protein JTB"
FT /id="PRO_0000021535"
FT TOPO_DOM 31..105
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..38
FT /note="MLAGAGRPGLPQGRHLCWLLCAFTLKLCQAEAPVQEEK -> MAWGWHLSF
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11042152,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_041400"
FT VARIANT 16
FT /note="L -> F (in dbSNP:rs34686244)"
FT /id="VAR_033994"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:2KJX"
FT STRAND 54..62
FT /evidence="ECO:0007829|PDB:2KJX"
FT HELIX 65..70
FT /evidence="ECO:0007829|PDB:2KJX"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:2KJX"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:2KJX"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:2KJX"
FT TURN 86..89
FT /evidence="ECO:0007829|PDB:2KJX"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:2KJX"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:2KJX"
SQ SEQUENCE 146 AA; 16358 MW; CA7080543591C319 CRC64;
MLAGAGRPGL PQGRHLCWLL CAFTLKLCQA EAPVQEEKLS ASTSNLPCWL VEEFVVAEEC
SPCSNFRAKT TPECGPTGYV EKITCSSSKR NEFKSCRSAL MEQRLFWKFE GAVVCVALIF
ACLVIIRQRQ LDRKALEKVR KQIESI
