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Q7M6U3

- TEX14_MOUSE

UniProt

Q7M6U3 - TEX14_MOUSE

Protein

Inactive serine/threonine-protein kinase TEX14

Gene

Tex14

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 2 (25 Jul 2006)
      Previous versions | rss
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    Functioni

    Required both for the formation of intercellular bridges during meiosis and for kinetochore-microtubule attachment during mitosis. Intercellular bridges are evolutionarily conserved structures that connect differentiating germ cells and are required for spermatogenesis and male fertility. Acts by promoting the conversion of midbodies into intercellular bridges via its interaction with CEP55: interaction with CEP55 inhibits the interaction between CEP55 and PDCD6IP/ALIX and TSG101, blocking cell abscission and leading to transform midbodies into intercellular bridges. Also plays a role during mitosis: recruited to kinetochores by PLK1 during early mitosis and regulates the maturation of the outer kinetochores and microtubule attachment. Has no protein kinase activity in vitro.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei267 – 2671ATPPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi205 – 2139ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. protein kinase activity Source: InterPro

    GO - Biological processi

    1. attachment of spindle microtubules to kinetochore Source: UniProtKB
    2. intercellular bridge organization Source: UniProtKB
    3. male meiosis Source: UniProtKB
    4. mitotic sister chromatid separation Source: UniProtKB
    5. mitotic spindle assembly checkpoint Source: UniProtKB
    6. negative regulation of cytokinesis Source: MGI
    7. negative regulation of protein binding Source: MGI

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inactive serine/threonine-protein kinase TEX14
    Alternative name(s):
    Testis-expressed sequence 14
    Testis-expressed sequence 14 protein
    Gene namesi
    Name:Tex14
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:1933227. Tex14.

    Subcellular locationi

    Cytoplasm. Midbody. Chromosomecentromerekinetochore
    Note: Detected in the intercellular bridges that connect male germ cell daughter cells after cell division.

    GO - Cellular componenti

    1. cell Source: UniProtKB
    2. condensed chromosome kinetochore Source: UniProtKB-SubCell
    3. cytoplasm Source: UniProtKB-SubCell
    4. intercellular bridge Source: UniProtKB
    5. kinetochore Source: UniProtKB
    6. midbody Source: UniProtKB

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Kinetochore

    Pathology & Biotechi

    Disruption phenotypei

    Male mice are sterile, due to the absence of intercellular bridges. Intercellular bridges do not form during spermatogenesis, and male mice are sterile. In females, embryonic intercellular bridges are also absent, mice have fewer oocytes, but they are fertile.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi431 – 4311S → A: Reduced phosphorylation by PLK1 and abolishes depletion from kinetochores and subsequent degradation by the APC/C complex. 1 Publication
    Mutagenesisi431 – 4311S → D or E: Mimicks phosphorylation state; inducing early depletion from kinetochores and subsequent degradation by the APC/C complex. 1 Publication
    Mutagenesisi791 – 7911G → A: Does not affect interaction with CEP55. 1 Publication
    Mutagenesisi792 – 7921P → A: Abolishes interaction with CEP55. 1 Publication
    Mutagenesisi797 – 7971Y → A: Abolishes interaction with CEP55. 1 Publication
    Mutagenesisi889 – 8979Missing: Prevents degradation during metaphase.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14501450Inactive serine/threonine-protein kinase TEX14PRO_0000246996Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei431 – 4311Phosphoserine; by PLK11 Publication

    Post-translational modificationi

    Phosphorylated on Thr residues by CDK1 during early phases of mitosis, promoting the interaction with PLK1 and recruitment to kinetochores. Phosphorylated on Ser-431 by PLK1 during late prometaphase promotes the rapid depletion from kinetochores and its subsequent degradation by the APC/C complex.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ7M6U3.
    PRIDEiQ7M6U3.

    PTM databases

    PhosphoSiteiQ7M6U3.

    Expressioni

    Tissue specificityi

    Detected in testis and spermatogonia. Not detectable in the other tissues tested.3 Publications

    Developmental stagei

    Detected at low levels in developing testis at 5 and 10 days after birth. Highly expressed in testis 15 and 20 days after birth. Highly expressed in pachytene, diplotene and meiotically dividing spermatocytes and in early round spermatids.1 Publication

    Gene expression databases

    ArrayExpressiQ7M6U3.
    BgeeiQ7M6U3.
    CleanExiMM_TEX14.
    GenevestigatoriQ7M6U3.

    Interactioni

    Subunit structurei

    Interacts with KIF23 and RBM44. Interacts with CEP55; inhibiting interaction between CEP55 and PDCD6IP/ALIX and TSG101.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Cep55Q8BT0711EBI-6674575,EBI-2552328

    Protein-protein interaction databases

    IntActiQ7M6U3. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7M6U3.
    SMRiQ7M6U3. Positions 23-133, 225-533.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati27 – 5428ANK 1Add
    BLAST
    Repeati55 – 8430ANK 2Add
    BLAST
    Repeati88 – 11730ANK 3Add
    BLAST
    Domaini199 – 512314Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi791 – 7977GPPX3Y
    Motifi889 – 8979D-box

    Domaini

    The protein kinase domain is predicted to be catalytically inactive.
    The GPPX3Y motif mediates interaction with CEP55.1 Publication

    Sequence similaritiesi

    Belongs to the protein kinase superfamily.Curated
    Contains 3 ANK repeats.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, Repeat

    Phylogenomic databases

    eggNOGiCOG0666.
    GeneTreeiENSGT00390000015123.
    HOVERGENiHBG094035.
    InParanoidiQ7M6U3.
    KOiK17540.
    OMAiFSFFSGP.
    OrthoDBiEOG75F4C9.
    PhylomeDBiQ7M6U3.
    TreeFamiTF328704.

    Family and domain databases

    Gene3Di1.25.40.20. 1 hit.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    [Graphical view]
    PfamiPF12796. Ank_2. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view]
    SMARTiSM00248. ANK. 3 hits.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 2 hits.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q7M6U3-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSRGAPFPVP CPVLLGTFTD DSLEAQLHEY AKQGNCVKLK KILKKGVCVD     50
    AVNTQGQSAL FVAALLGHVK LVDVLVDYGS DPNHRCFDGS TPVHAAAFSG 100
    NQWILSKLLT AGGDLRLHDE KGRNPQAWAL TAGKDRSTQM VEFMQRCTSH 150
    MKAIIQGFSY DLLKKIDSPQ RLIGSPPWFG SLIQGSPNSS PNRQLKPGII 200
    SAQNIYSFGF GKFYLTSGMQ LTYPGSLPVI GEKEVVQADD EPTFSFFSGP 250
    YMVMTNLVWN RSRVTVKELN LPTRPHCSRL RLADLLIAEQ EHSSNLRHPN 300
    LLQLMAVCLS RDLEKIRLVY ERITVGTLFS VLHERRSQFP VLHMEVIVHL 350
    LLQVADALIY LHSRGFIHRS LSSYAVHIVS AGEARLTNLE YLTESQDSGA 400
    HRNVTRMPLP TQLYNWAAPE VVLQKAATVK SDIYSFSVII QEILTDSIPW 450
    NGLDGSLVKE TIALGNYLEA DVRLPEPYYD IVKSGIHAKQ KNRTMNLQDI 500
    RYILKNDLKE FIGAQKTQPT ESPRGQSYEP HPDVNICLGL TSEYQKDPPD 550
    LDIKELKEMG SQPHSPTDHS FLTVKPTLAP QTLDSSLSAQ KPDNANVPSP 600
    PAACLAEEVR SPTASQDSLC SFEINEIYSG CLTLGTDKEE ECLGTAASPE 650
    GDRPNQGDEL PSLEEELDKM ERELHCFCEE DKSISEVDTD LLFEDDDWQS 700
    DSLGSLNLPE PTREAKGKTS SWSKTDEYVS KCVLNLKISQ VMMQQSAEWL 750
    RKLEQEVEEL EWAQKELDSQ CSSLRDASLK FANAKFQPAV GPPSLAYLPP 800
    VMQLPGLKQP ENGGTWLTLA RSPGNEREFQ EGHFSKKPEK LSACGWKPFT 850
    QVSEESRGDC SELNNQLPTL RGPGKQSTGE QLPSTQEARE SLEKNTNQNS 900
    RSMASVSSEI YATKSRNNED NGEAHLKWRL AVKEMAEKAV SGQLLLPPWN 950
    PQSSAPFESK VENESTPLPR PPIRGPESTE WQHILEYQRE NDEPKGNTKF 1000
    GKMDNSDCDK NKHSRWTGLQ RFTGIRYPFF RNHEQPEQNE ASQASCDTSV 1050
    GTEKFYSTSS PIGDDFERFQ DSFAQRQGYV EENFQIREIF EKNAEILTKP 1100
    QFQAIQCAED KQDETLGETP KELKEKNTSL TDIQDLSSIT YDQDGYFKET 1150
    SYKTPKLKHA PTSASTPLSP ESISSAASHY EDCLENTTFH VKRGSTFCWN 1200
    GQEAMRTLSA KFTTVRERAK SLESLLASSK SLPAKLTDSK RLCMLSETGS 1250
    SNVSAAFVTS THATKRKSLP RELAEATSQQ HLDELPPPAQ ELLDEIEQLK 1300
    QQQVSSLASH ENTARDLSVT NKDKKHLEEQ ETNSSKDSSF LSSREIQDLE 1350
    DTERAHSSLD EDLERFLQSP EENTALLDPT KGSTREKKNK DQDVVEQKRK 1400
    KKESIKPERR ESDSSLGTLE EDELKPCFWK RLGWSEPSRI IVLDQSDLSD 1450
    Length:1,450
    Mass (Da):162,541
    Last modified:July 25, 2006 - v2
    Checksum:i0628605EBE0FF0A4
    GO
    Isoform 2 (identifier: Q7M6U3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-218: Missing.

    Show »
    Length:1,232
    Mass (Da):138,851
    Checksum:iA2CDBD69A483AF39
    GO

    Sequence cautioni

    The sequence CAI35965.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti324 – 3241T → A in AAK31963. (PubMed:11279525)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 218218Missing in isoform 2. 1 PublicationVSP_019870Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF285584 mRNA. Translation: AAK31963.1.
    AL596086, AL669902 Genomic DNA. Translation: CAI35127.1.
    AL669902 Genomic DNA. Translation: CAI35965.1. Different initiation.
    AL669902, AL596086 Genomic DNA. Translation: CAI35966.1.
    CU406969, CU406988 Genomic DNA. Translation: CAQ52018.1.
    CU406988, CU406969 Genomic DNA. Translation: CAQ52278.1.
    AY193717 mRNA. Translation: AAN86761.1.
    AY193718 mRNA. Translation: AAN86762.1.
    BK000966 mRNA. Translation: DAA01357.1.
    BK000967 mRNA. Translation: DAA01358.1.
    AK139808 mRNA. Translation: BAE24144.1.
    CCDSiCCDS48877.1. [Q7M6U3-1]
    RefSeqiNP_001186222.1. NM_001199293.1.
    NP_113563.2. NM_031386.2. [Q7M6U3-1]
    XP_006534611.1. XM_006534548.1. [Q7M6U3-2]
    XP_006534612.1. XM_006534549.1. [Q7M6U3-2]
    XP_006536545.1. XM_006536482.1. [Q7M6U3-2]
    XP_006536546.1. XM_006536483.1. [Q7M6U3-2]
    UniGeneiMm.440758.

    Genome annotation databases

    EnsembliENSMUST00000060835; ENSMUSP00000054444; ENSMUSG00000010342. [Q7M6U3-1]
    GeneIDi83560.
    KEGGimmu:83560.
    UCSCiuc007ktr.2. mouse. [Q7M6U3-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF285584 mRNA. Translation: AAK31963.1 .
    AL596086 , AL669902 Genomic DNA. Translation: CAI35127.1 .
    AL669902 Genomic DNA. Translation: CAI35965.1 . Different initiation.
    AL669902 , AL596086 Genomic DNA. Translation: CAI35966.1 .
    CU406969 , CU406988 Genomic DNA. Translation: CAQ52018.1 .
    CU406988 , CU406969 Genomic DNA. Translation: CAQ52278.1 .
    AY193717 mRNA. Translation: AAN86761.1 .
    AY193718 mRNA. Translation: AAN86762.1 .
    BK000966 mRNA. Translation: DAA01357.1 .
    BK000967 mRNA. Translation: DAA01358.1 .
    AK139808 mRNA. Translation: BAE24144.1 .
    CCDSi CCDS48877.1. [Q7M6U3-1 ]
    RefSeqi NP_001186222.1. NM_001199293.1.
    NP_113563.2. NM_031386.2. [Q7M6U3-1 ]
    XP_006534611.1. XM_006534548.1. [Q7M6U3-2 ]
    XP_006534612.1. XM_006534549.1. [Q7M6U3-2 ]
    XP_006536545.1. XM_006536482.1. [Q7M6U3-2 ]
    XP_006536546.1. XM_006536483.1. [Q7M6U3-2 ]
    UniGenei Mm.440758.

    3D structure databases

    ProteinModelPortali Q7M6U3.
    SMRi Q7M6U3. Positions 23-133, 225-533.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q7M6U3. 2 interactions.

    PTM databases

    PhosphoSitei Q7M6U3.

    Proteomic databases

    PaxDbi Q7M6U3.
    PRIDEi Q7M6U3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000060835 ; ENSMUSP00000054444 ; ENSMUSG00000010342 . [Q7M6U3-1 ]
    GeneIDi 83560.
    KEGGi mmu:83560.
    UCSCi uc007ktr.2. mouse. [Q7M6U3-1 ]

    Organism-specific databases

    CTDi 56155.
    MGIi MGI:1933227. Tex14.

    Phylogenomic databases

    eggNOGi COG0666.
    GeneTreei ENSGT00390000015123.
    HOVERGENi HBG094035.
    InParanoidi Q7M6U3.
    KOi K17540.
    OMAi FSFFSGP.
    OrthoDBi EOG75F4C9.
    PhylomeDBi Q7M6U3.
    TreeFami TF328704.

    Miscellaneous databases

    NextBioi 350646.
    PROi Q7M6U3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7M6U3.
    Bgeei Q7M6U3.
    CleanExi MM_TEX14.
    Genevestigatori Q7M6U3.

    Family and domain databases

    Gene3Di 1.25.40.20. 1 hit.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    [Graphical view ]
    Pfami PF12796. Ank_2. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view ]
    SMARTi SM00248. ANK. 3 hits.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 2 hits.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "An abundance of X-linked genes expressed in spermatogonia."
      Wang P.J., McCarrey J.R., Yang F., Page D.C.
      Nat. Genet. 27:422-426(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
      Tissue: Testis.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "Sequence and expression of testis-expressed gene 14 (Tex14): a gene encoding a protein kinase preferentially expressed during spermatogenesis."
      Wu M.-H., Rajkovic A., Burns K.H., Yan W., Lin Y.-N., Matzuk M.M.
      Gene Expr. Patterns 3:231-236(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-227 (ISOFORM 1), IDENTIFICATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 714-1396.
      Strain: C57BL/6J.
      Tissue: Egg.
    5. Cited for: FUNCTION, ABSENCE OF PROTEIN KINASE ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    6. "Conversion of midbodies into germ cell intercellular bridges."
      Greenbaum M.P., Ma L., Matzuk M.M.
      Dev. Biol. 305:389-396(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH KIF23.
    7. "Mouse TEX14 is required for embryonic germ cell intercellular bridges but not female fertility."
      Greenbaum M.P., Iwamori N., Agno J.E., Matzuk M.M.
      Biol. Reprod. 80:449-457(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.
    8. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CEP55, MUTAGENESIS OF GLY-791; PRO-792 AND TYR-797.
    9. "Identification and characterization of RBM44 as a novel intercellular bridge protein."
      Iwamori T., Lin Y.N., Ma L., Iwamori N., Matzuk M.M.
      PLoS ONE 6:E17066-E17066(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RBM44.
    10. "Mouse germ cell clusters form by aggregation as well as clonal divisions."
      Mork L., Tang H., Batchvarov I., Capel B.
      Mech. Dev. 128:591-596(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    11. "Tex14, a plk1-regulated protein, is required for kinetochore-microtubule attachment and regulation of the spindle assembly checkpoint."
      Mondal G., Ohashi A., Yang L., Rowley M., Couch F.J.
      Mol. Cell 45:680-695(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-431, MUTAGENESIS OF SER-431 AND 889-ARG--ASN-897.

    Entry informationi

    Entry nameiTEX14_MOUSE
    AccessioniPrimary (citable) accession number: Q7M6U3
    Secondary accession number(s): B2KGL0
    , Q3UT36, Q5NC10, Q5NC11, Q8CGK1, Q8CGK2, Q99MV8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 25, 2006
    Last sequence update: July 25, 2006
    Last modified: October 1, 2014
    This is version 104 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Used as a marker for intercellular bridges.1 Publication

    Caution

    Ser-370 is present instead of the conserved Asp which is expected to be an active site residue.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3