ID   JTB_MOUSE               Reviewed;         146 AA.
AC   O88824;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 139.
DE   RecName: Full=Protein JTB;
DE   Flags: Precursor;
GN   Name=Jtb; Synonyms=Gm622;
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].
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 [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
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   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING OF N-TERMINUS,
RP   MUTAGENESIS OF 13-ALA-GLY-14, AND INDUCTION.
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).
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 (By similarity). Inhibits apoptosis
CC       induced by TGFB1. Overexpression induces swelling of mitochondria and
CC       reduces mitochondrial membrane potential. {ECO:0000250,
CC       ECO:0000269|PubMed:17369841}.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}. Mitochondrion
CC       {ECO:0000269|PubMed:17369841}. Cytoplasm {ECO:0000250}. Cytoplasm,
CC       cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
CC       Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Detected at the
CC       centrosome and along spindle fibers during prophase and metaphase.
CC       Detected at the midbody during telophase (By similarity).
CC       {ECO:0000250}.
CC   -!- INDUCTION: Up-regulated by TGFB1 in mammary epithelial cells.
CC       {ECO:0000269|PubMed:17369841}.
CC   -!- PTM: Undergoes N-terminal proteolytic processing, removing a peptide of
CC       about 1 kDa from the N-terminus of the protein.
CC       {ECO:0000269|PubMed:17369841}.
CC   -!- SIMILARITY: Belongs to the JTB family. {ECO:0000305}.
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DR   EMBL; AB016490; BAA33733.1; -; mRNA.
DR   EMBL; BC008139; AAH08139.1; -; mRNA.
DR   CCDS; CCDS17523.1; -.
DR   RefSeq; NP_996807.1; NM_206924.2.
DR   AlphaFoldDB; O88824; -.
DR   SMR; O88824; -.
DR   STRING; 10090.ENSMUSP00000029546; -.
DR   iPTMnet; O88824; -.
DR   PhosphoSitePlus; O88824; -.
DR   PaxDb; 10090-ENSMUSP00000029546; -.
DR   ProteomicsDB; 269428; -.
DR   Pumba; O88824; -.
DR   Ensembl; ENSMUST00000029546.15; ENSMUSP00000029546.9; ENSMUSG00000027937.16.
DR   GeneID; 23922; -.
DR   KEGG; mmu:23922; -.
DR   UCSC; uc008qbo.1; mouse.
DR   AGR; MGI:1346082; -.
DR   CTD; 10899; -.
DR   MGI; MGI:1346082; Jtb.
DR   VEuPathDB; HostDB:ENSMUSG00000027937; -.
DR   eggNOG; KOG4084; Eukaryota.
DR   GeneTree; ENSGT00390000016136; -.
DR   HOGENOM; CLU_130083_1_0_1; -.
DR   InParanoid; O88824; -.
DR   OMA; TITRSCD; -.
DR   OrthoDB; 5347248at2759; -.
DR   PhylomeDB; O88824; -.
DR   TreeFam; TF316934; -.
DR   BioGRID-ORCS; 23922; 9 hits in 80 CRISPR screens.
DR   ChiTaRS; Jtb; mouse.
DR   PRO; PR:O88824; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; O88824; Protein.
DR   Bgee; ENSMUSG00000027937; Expressed in parotid gland and 259 other cell types or tissues.
DR   ExpressionAtlas; O88824; baseline and differential.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR   GO; GO:0008637; P:apoptotic mitochondrial changes; IDA:MGI.
DR   GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR   GO; GO:0045860; P:positive regulation of protein kinase activity; ISS:UniProtKB.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IMP:UniProtKB.
DR   Gene3D; 3.30.720.220; -; 1.
DR   InterPro; IPR008657; JTB.
DR   PANTHER; PTHR13041; JTB PROTEIN-RELATED; 1.
DR   PANTHER; PTHR13041:SF3; PROTEIN JTB; 1.
DR   Pfam; PF05439; JTB; 1.
DR   Genevisible; O88824; MM.
PE   1: Evidence at protein level;
KW   Apoptosis; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Membrane;
KW   Mitochondrion; Mitosis; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..146
FT                   /note="Protein JTB"
FT                   /id="PRO_0000021536"
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   MUTAGEN         13..14
FT                   /note="AG->DD: Abolishes N-terminal proteolytic
FT                   processing."
FT                   /evidence="ECO:0000269|PubMed:17369841"
SQ   SEQUENCE   146 AA;  16329 MW;  9E4DAF394B2A2107 CRC64;
     MLAGAGRRGL PRAGHLCWLL CAFTLKLCEA EAPVREEKLS VSTSTSPCWL AEEFVVTEEC
     TPCSNFQIKT TPECGSTGYV EKITCSSSKR NEFKSCRSAL LEQHLFWKFE GVVVAVALVF
     ACLVIVRQRQ LDRKALEKVR KQIESI
//