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Q0KL02

- TRIO_MOUSE

UniProt

Q0KL02 - TRIO_MOUSE

Protein

Triple functional domain protein

Gene

Trio

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 3 (01 Sep 2009)
      Previous versions | rss
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    Functioni

    Promotes the exchange of GDP by GTP. Together with leukocyte antigen-related (LAR) protein, it could play a role in coordinating cell-matrix and cytoskeletal rearrangements necessary for cell migration and cell growth By similarity.By similarity

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei2828 – 28281ATPPROSITE-ProRule annotation
    Active sitei2918 – 29181Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi2805 – 28139ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein serine/threonine kinase activity Source: UniProtKB-KW
    3. Rho guanyl-nucleotide exchange factor activity Source: InterPro

    Keywords - Molecular functioni

    Guanine-nucleotide releasing factor, Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_204733. G alpha (12/13) signalling events.
    REACT_207651. G alpha (q) signalling events.
    REACT_209641. NRAGE signals death through JNK.
    REACT_210090. Rho GTPase cycle.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Triple functional domain protein (EC:2.7.11.1)
    Gene namesi
    Name:Trio
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:1927230. Trio.

    Subcellular locationi

    Cytoplasm 1 Publication
    Note: Isoform 2 localizes to early endosomes.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1427 – 14271Q → A: Abolishes Rac1 activation; when associated with E-1435. 1 Publication
    Mutagenesisi1435 – 14351L → E: Abolishes Rac1 activation; when associated with A-1427. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 31023102Triple functional domain proteinPRO_0000278474Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2282 – 22821PhosphoserineBy similarity
    Modified residuei2458 – 24581Phosphoserine1 Publication
    Modified residuei2462 – 24621PhosphoserineBy similarity
    Disulfide bondi2709 ↔ 2762PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiQ0KL02.
    PaxDbiQ0KL02.
    PRIDEiQ0KL02.

    PTM databases

    PhosphoSiteiQ0KL02.

    Expressioni

    Tissue specificityi

    Widespread in the brain, with more intense signals in the hippocampus, olfactory bulb, cortical layers and cerebellum. Isoform 2 is predominantly expressed in Purkinje neurons of brain.1 Publication

    Gene expression databases

    BgeeiQ0KL02.
    CleanExiMM_TRIO.
    GenevestigatoriQ0KL02.

    Interactioni

    Subunit structurei

    Interacts to form a complex with leukocyte antigen related protein.By similarity

    Protein-protein interaction databases

    BioGridi230148. 1 interaction.
    STRINGi10090.ENSMUSP00000087714.

    Structurei

    3D structure databases

    ProteinModelPortaliQ0KL02.
    SMRiQ0KL02. Positions 220-440, 801-1006, 1290-1594, 1655-1721, 1960-2291, 2558-2615, 2631-3085.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini65 – 210146CRAL-TRIOPROSITE-ProRule annotationAdd
    BLAST
    Repeati218 – 338121Spectrin 1Add
    BLAST
    Repeati340 – 446107Spectrin 2Add
    BLAST
    Repeati566 – 672107Spectrin 3Add
    BLAST
    Repeati673 – 784112Spectrin 4Add
    BLAST
    Repeati907 – 1012106Spectrin 5Add
    BLAST
    Repeati1138 – 1244107Spectrin 6Add
    BLAST
    Domaini1292 – 1467176DH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1479 – 1591113PH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1656 – 172166SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini1969 – 2145177DH 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini2157 – 2271115PH 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini2688 – 277891Ig-like C2-typeAdd
    BLAST
    Domaini2799 – 3053255Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi715 – 7184Poly-Gln
    Compositional biasi1845 – 18506Poly-Ser
    Compositional biasi1951 – 19544Poly-Ser
    Compositional biasi2292 – 232433Gly-richAdd
    BLAST
    Compositional biasi2296 – 2557262Ser-richAdd
    BLAST

    Domaini

    The N-terminal DBL/GEF domain specifically catalyzes nucleotide exchange for RAC1, leading to the activation of Jun kinase and the production of membrane ruffles. The second DBL/GEF domain is an exchange factor for rhoa and induces the formation of stress fibers By similarity.By similarity

    Sequence similaritiesi

    Contains 1 CRAL-TRIO domain.PROSITE-ProRule annotation
    Contains 2 DH (DBL-homology) domains.PROSITE-ProRule annotation
    Contains 2 PH domains.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation
    Contains 6 spectrin repeats.Curated

    Keywords - Domaini

    Immunoglobulin domain, Repeat, SH3 domain

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00720000108506.
    HOGENOMiHOG000044462.
    HOVERGENiHBG108598.
    InParanoidiQ0KL02.
    KOiK08810.
    OMAiIEERGRN.
    OrthoDBiEOG7B8S3F.
    PhylomeDBiQ0KL02.
    TreeFamiTF318080.

    Family and domain databases

    Gene3Di1.20.900.10. 2 hits.
    2.30.29.30. 2 hits.
    2.60.40.10. 1 hit.
    3.40.525.10. 1 hit.
    InterProiIPR001251. CRAL-TRIO_dom.
    IPR000219. DH-domain.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003598. Ig_sub2.
    IPR011009. Kinase-like_dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR000719. Prot_kinase_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    IPR001452. SH3_domain.
    IPR018159. Spectrin/alpha-actinin.
    IPR002017. Spectrin_repeat.
    IPR028570. TRIO.
    [Graphical view]
    PANTHERiPTHR22826:SF104. PTHR22826:SF104. 1 hit.
    PfamiPF13716. CRAL_TRIO_2. 1 hit.
    PF07679. I-set. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF00621. RhoGEF. 2 hits.
    PF00018. SH3_1. 1 hit.
    PF00435. Spectrin. 4 hits.
    [Graphical view]
    SMARTiSM00408. IGc2. 1 hit.
    SM00233. PH. 2 hits.
    SM00325. RhoGEF. 2 hits.
    SM00220. S_TKc. 1 hit.
    SM00516. SEC14. 1 hit.
    SM00326. SH3. 2 hits.
    SM00150. SPEC. 6 hits.
    [Graphical view]
    SUPFAMiSSF48065. SSF48065. 2 hits.
    SSF50044. SSF50044. 2 hits.
    SSF52087. SSF52087. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS50191. CRAL_TRIO. 1 hit.
    PS50010. DH_2. 2 hits.
    PS50835. IG_LIKE. 1 hit.
    PS50003. PH_DOMAIN. 2 hits.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q0KL02-1) [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

    MSGSSGGATA PAASSGPAAA ASAAGSGCGG GAGEGAEEAA KDLADIAAFF     50
    RSGFRKNDEM KAMDVLPILK EKVAYLSGGR DKRGGPILTF PARSNHDRIR 100
    QEDLRRLISY LACIPSEEVC KRGFTVIVDM RGSKWDSIKP LLKILQESFP 150
    CCIHIALIIK PDNFWQKQRT NFGSSKFEFE TNMVSLEGLT KVVDPSQLTP 200
    EFDGCLEYNH EEWIEIRVAF EEYISNAAHM LSRLEELQDV LAKKELPQDL 250
    EGARNMIDEH SQLKKKVIKA PIEDLDLEGQ KLLQRIQSSD SFPKKNSGSG 300
    NADLQNLLPK VSTMLDRLHS TRQHLHQMWH VRKLKLDQCF QLRLFEQDAE 350
    KMFDWITHNK GLFLNSYTEI GTSHPHAMEL QTQHNHFAMN CMNVYVNINR 400
    IMSVANRLVE SGHYASQQIK QIANQLEQEW KAFAAALDER STLLDMSSIF 450
    HQKAEKYMSN VDSWCKACGE VDLPSELQDL EDAIHHHQGI YEHITLAYSE 500
    VSQDGKSLLD KLQRPLTPGS SDSLTASANY SKAVHHVLDV IHEVLHHQRQ 550
    LENIWQHRKV RLHQRLQLCV FQQDVQQVLD WIENHGEAFL SKHTGVGKSL 600
    HRARALQKRH EDFEEVAQNT YTNADKLLEA AEQLAQTGEC DPEEIYQAAH 650
    QLEDRIQDFV RRVEQRKILL DMSVSFHTHV KELWTWLEEL QKELLDDVYA 700
    ESVEAVQDLI KRFGQQQQTT LQVTVNVIKE GEDLIQQLRD SAISSNKTPH 750
    NSSINHIETV LQQLDEAQSQ MEELFQERKI KLELFLQLRI FERDAIDIIS 800
    DLESWNDELS QQMNDFDTED LTIAEQRLQH HADKALTMNN LTFDVIHQGQ 850
    DLLQYVNEVQ ASGVELLCDR DVDMATRVQD LLEFLHEKQQ ELDLAAEQHR 900
    KHLEQCVQLR HLQAEVKQVL GWIRNGESML NAGLITASSL QEAEQLQREH 950
    EQFQHAIEKT HQSALQVQQK AEAMLQANHY DMDMIRDCAE KVASHWQQLM 1000
    LKMEDRLKLV NASVAFYKTS EQVCSVLESL EQEYKREEDW CGGADKLGPN 1050
    SETDHVTPMI SKHLEQKEAF LKACTLARRN ADVFLKYLHR NSVSMPGMVT 1100
    HIKAPEQQVK NILNELFQRE NRVLHYWTMR KRRLDQCQQY VVFERSAKQA 1150
    LEWIHDNGEF YLSTHTSTGS SIQHTQELLK EHEEFQITAK QTKERVKLLI 1200
    QLADGFCEKG HAHAAEIKKC VTAVDKRYRD FSLRMEKYRT SLEKALGISS 1250
    DSNKSSKSLQ LDIIPASIPG SEVKLRDAAH ELNEEKRKSA RRKEFIMAEL 1300
    IQTEKAYVRD LRECMDTYLW EMTSGVEEIP PGIVNKELII FGNMQEIYEF 1350
    HNNIFLKELE KYEQLPEDVG HCFVTWADKF QMYVTYCKNK PDSTQLILEH 1400
    AGSYFDEIQQ RHGLANSISS YLIKPVQRIT KYQLLLKELL TCCEEGKGEI 1450
    KDGLEVMLSV PKRANDAMHL SMLEGFDENI ESQGELILQE SFQVWDPKTL 1500
    IRKGRERHLF LFEMSLVFSK EVKDSSGRSK YLYKSKLFTS ELGVTEHVEG 1550
    DPCKFALWVG RTPTSDNKIV LKASSIENKQ DWIKHIREVI QERTVHLRGA 1600
    LKEPIHIPKT APAARQKGRR DGEDLDSQGD GSSQPDTISI ASRTSQNTLD 1650
    SDKLSGGCEL TVVIHDFTAC NSNELTIRRG QTVEVLERPH DKPDWCLVRT 1700
    TDRSPAAEGL VPCGSLCIAH SRSSMEMEGI FNHKDSLSVS SNDASPPASV 1750
    ASLQPHMIGA QSSPGPKRPG NTLRKWLTSP VRRLSSGKAD GHAKKLAHKH 1800
    KKSREVRKSA DAGSQKDSDD SAATPQDETI EERGRNEGLS SGTLSKSSSS 1850
    GMQSCGEEEG EEGADAVPLP PPMAIQQHSL LQPDSQDDKA SSRLLVRPTS 1900
    SETPSAAELV SAIEELVKSK MALEDRPSSL LVDQGDSSSP SFNPSDNSLL 1950
    SSSSPIDEME ERKCSSLKRR HYVLQELVET ERDYVRDLGC VVEGYMALMK 2000
    EDGVPDDMKG KDKIVFGNIH QIYDWHRDFF LGELEKCLED PEKLGSLFVK 2050
    HERRLHMYIV YCQNKPKSEH IVSEYIDTFF EDLKQRLGHR LQLTDLLIKP 2100
    VQRIMKYQLL LKDFLKYSKK ASLDTSELEK AVEVMCIVPK RCNDMMNVGR 2150
    LQGFDGKIVA QGKLLLQDTF LVTDQDAGLL PRCKERRVFL FEQIVIFSEP 2200
    LDKKKGFSMP GFLFKNSIKV SCLCLEENVE SDPCKFALTS RTGDAVETFV 2250
    LHSSSPSVRQ TWIHEINQIL ENQRNFLNAL TSPIEYQRNH SGGGGSGSGG 2300
    SSGGGGGSGG SGASSGGSSS HGSGPSSCSS GPSSSRSRPS RIPQPVRHHP 2350
    PMLVSSAASS QAEADKMSGM SAPSPSLPTP SSSLALEASL GQPSRLPLSG 2400
    DSEGHERETE PIPKMKVMES PRKAPGSTSG TSQDGNTKDA RGNLGSLPLG 2450
    KTRPGAVSPL NSPLSTTFPS PFGKEAFPPS SPLQKGGSFW SSIPASPASR 2500
    PSSFTFPGDS DSLQRQTHRH AAPSKDTDRM STCSSASEQS VQSTQSNGEG 2550
    SSSSNISTML VTHEYTAVKE DEINVYQGEV VQILASNQQN MFLVFRAATD 2600
    QCPAAEGWIP GFVLGHTSAV IMENPDGTLK KSTSWHTALR LRKKSEKKDK 2650
    DGKRDGKLEN GYRKPREGLS NKVSVKLLNP NYIYDVPPEF VIPLSEVTCE 2700
    TGETVVFRCR VCGRPKASIT WKGPEHNTLN NDDHYSISYS DIGEATLKII 2750
    GVSTEDDGIY TCIAVNDMGS ASSSASLRVL GPGSDGIVVT WKDNFDAFYS 2800
    EVAELGRGRF AVVKKCDQKG TKRAVATKFV NKKLMKRDQV THELGILQNL 2850
    QHPLLVSLLD TFETPTSYVL VLEMADQGRL LDCVVRWGSL TEGKVRAHLG 2900
    EVLEAVRYLH NCRIAHLDLK PENILVDQSL AKPTIKLADF GDAVQLNTTY 2950
    YIHQLLGNPE FAAPEIILGN PVSLTADTWS VGVLTYVLLS GVSPFLDDSV 3000
    EETCLNICRL DFSFPEDYFQ GVSQKAKEFV CFLLQEDPAK RPSAALALQE 3050
    QWLQAGNGSG KGTGVLDTSR LTSFIERRKH QNDVRPIRSI KNFLQSRLLP 3100
    RV 3102
    Length:3,102
    Mass (Da):347,861
    Last modified:September 1, 2009 - v3
    Checksum:i8E8F7C44CB4F72D0
    GO
    Isoform 2 (identifier: Q0KL02-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1890-1908: ASSRLLVRPTSSETPSAAE → HYVDLCSVSVLAQFPYLSI
         1909-3102: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,908
    Mass (Da):217,005
    Checksum:iCB3E6B6BB738F7F1
    GO
    Isoform 3 (identifier: Q0KL02-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2548-2548: G → GS
         2549-2568: EGSSSSNISTMLVTHEYTAV → VRVPGSLRPSTPPPLSRQLF
         2569-3102: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:2,569
    Mass (Da):288,709
    Checksum:i5869317875FB1134
    GO
    Isoform 4 (identifier: Q0KL02-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2548-2548: G → GS

    Note: No experimental confirmation available.

    Show »
    Length:3,103
    Mass (Da):347,948
    Checksum:i3471FAD8B46480A6
    GO

    Sequence cautioni

    The sequence BAE32258.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2863 – 28631E → K in BAE32258. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1890 – 190819ASSRL…PSAAE → HYVDLCSVSVLAQFPYLSI in isoform 2. 1 PublicationVSP_023308Add
    BLAST
    Alternative sequencei1909 – 31021194Missing in isoform 2. 1 PublicationVSP_023309Add
    BLAST
    Alternative sequencei2548 – 25481G → GS in isoform 3 and isoform 4. 2 PublicationsVSP_037863
    Alternative sequencei2549 – 256820EGSSS…EYTAV → VRVPGSLRPSTPPPLSRQLF in isoform 3. 1 PublicationVSP_037864Add
    BLAST
    Alternative sequencei2569 – 3102534Missing in isoform 3. 1 PublicationVSP_037865Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB106872 mRNA. Translation: BAF30811.1.
    AC107452 Genomic DNA. No translation available.
    AC116808 Genomic DNA. No translation available.
    AC120373 Genomic DNA. No translation available.
    AC130219 Genomic DNA. No translation available.
    BC051169 mRNA. Translation: AAH51169.1.
    BC060724 mRNA. No translation available.
    AK153924 mRNA. Translation: BAE32258.1. Different initiation.
    CCDSiCCDS49587.1. [Q0KL02-4]
    RefSeqiNP_001074771.1. NM_001081302.1. [Q0KL02-4]
    XP_006520117.1. XM_006520054.1. [Q0KL02-2]
    UniGeneiMm.485422.

    Genome annotation databases

    EnsembliENSMUST00000090247; ENSMUSP00000087714; ENSMUSG00000022263. [Q0KL02-4]
    GeneIDi223435.
    KEGGimmu:223435.
    UCSCiuc007vjw.1. mouse. [Q0KL02-4]
    uc007vjx.1. mouse. [Q0KL02-3]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB106872 mRNA. Translation: BAF30811.1 .
    AC107452 Genomic DNA. No translation available.
    AC116808 Genomic DNA. No translation available.
    AC120373 Genomic DNA. No translation available.
    AC130219 Genomic DNA. No translation available.
    BC051169 mRNA. Translation: AAH51169.1 .
    BC060724 mRNA. No translation available.
    AK153924 mRNA. Translation: BAE32258.1 . Different initiation.
    CCDSi CCDS49587.1. [Q0KL02-4 ]
    RefSeqi NP_001074771.1. NM_001081302.1. [Q0KL02-4 ]
    XP_006520117.1. XM_006520054.1. [Q0KL02-2 ]
    UniGenei Mm.485422.

    3D structure databases

    ProteinModelPortali Q0KL02.
    SMRi Q0KL02. Positions 220-440, 801-1006, 1290-1594, 1655-1721, 1960-2291, 2558-2615, 2631-3085.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 230148. 1 interaction.
    STRINGi 10090.ENSMUSP00000087714.

    PTM databases

    PhosphoSitei Q0KL02.

    Proteomic databases

    MaxQBi Q0KL02.
    PaxDbi Q0KL02.
    PRIDEi Q0KL02.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000090247 ; ENSMUSP00000087714 ; ENSMUSG00000022263 . [Q0KL02-4 ]
    GeneIDi 223435.
    KEGGi mmu:223435.
    UCSCi uc007vjw.1. mouse. [Q0KL02-4 ]
    uc007vjx.1. mouse. [Q0KL02-3 ]

    Organism-specific databases

    CTDi 7204.
    MGIi MGI:1927230. Trio.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00720000108506.
    HOGENOMi HOG000044462.
    HOVERGENi HBG108598.
    InParanoidi Q0KL02.
    KOi K08810.
    OMAi IEERGRN.
    OrthoDBi EOG7B8S3F.
    PhylomeDBi Q0KL02.
    TreeFami TF318080.

    Enzyme and pathway databases

    Reactomei REACT_204733. G alpha (12/13) signalling events.
    REACT_207651. G alpha (q) signalling events.
    REACT_209641. NRAGE signals death through JNK.
    REACT_210090. Rho GTPase cycle.

    Miscellaneous databases

    ChiTaRSi TRIO. mouse.
    NextBioi 376714.
    PROi Q0KL02.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q0KL02.
    CleanExi MM_TRIO.
    Genevestigatori Q0KL02.

    Family and domain databases

    Gene3Di 1.20.900.10. 2 hits.
    2.30.29.30. 2 hits.
    2.60.40.10. 1 hit.
    3.40.525.10. 1 hit.
    InterProi IPR001251. CRAL-TRIO_dom.
    IPR000219. DH-domain.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003598. Ig_sub2.
    IPR011009. Kinase-like_dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR000719. Prot_kinase_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    IPR001452. SH3_domain.
    IPR018159. Spectrin/alpha-actinin.
    IPR002017. Spectrin_repeat.
    IPR028570. TRIO.
    [Graphical view ]
    PANTHERi PTHR22826:SF104. PTHR22826:SF104. 1 hit.
    Pfami PF13716. CRAL_TRIO_2. 1 hit.
    PF07679. I-set. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF00621. RhoGEF. 2 hits.
    PF00018. SH3_1. 1 hit.
    PF00435. Spectrin. 4 hits.
    [Graphical view ]
    SMARTi SM00408. IGc2. 1 hit.
    SM00233. PH. 2 hits.
    SM00325. RhoGEF. 2 hits.
    SM00220. S_TKc. 1 hit.
    SM00516. SEC14. 1 hit.
    SM00326. SH3. 2 hits.
    SM00150. SPEC. 6 hits.
    [Graphical view ]
    SUPFAMi SSF48065. SSF48065. 2 hits.
    SSF50044. SSF50044. 2 hits.
    SSF52087. SSF52087. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS50191. CRAL_TRIO. 1 hit.
    PS50010. DH_2. 2 hits.
    PS50835. IG_LIKE. 1 hit.
    PS50003. PH_DOMAIN. 2 hits.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Solo/Trio8, a membrane-associated short isoform of Trio, modulates endosome dynamics and neurite elongation."
      Sun Y.-J., Nishikawa K., Yuda K., Wang Y.-L., Osaka H., Fukazawa N., Naito A., Wada K., Aoki S.
      Mol. Cell. Biol. 26:6923-6935(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, MUTAGENESIS OF GLN-1427 AND LEU-1435, SUBCELLULAR LOCATION.
      Strain: C57BL/6J.
      Tissue: Cerebellum.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2062-3102 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1145-3102 (ISOFORM 3).
      Strain: C57BL/6.
      Tissue: Brain and Olfactory epithelium.
    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 2521-3102 (ISOFORM 4).
      Strain: NOD.
      Tissue: Thymus.
    5. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2458, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiTRIO_MOUSE
    AccessioniPrimary (citable) accession number: Q0KL02
    Secondary accession number(s): Q3U522, Q6P9K6, Q80W23
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 20, 2007
    Last sequence update: September 1, 2009
    Last modified: October 1, 2014
    This is version 78 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3