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Q0KL02

- TRIO_MOUSE

UniProt

Q0KL02 - TRIO_MOUSE

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Protein
Triple functional domain protein
Gene
Trio
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei2828 – 28281ATP By similarity
Active sitei2918 – 29181Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi2805 – 28139ATP By similarity

GO - Molecular functioni

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

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
Note: Isoform 2 localizes to early endosomes.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

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 protein
PRO_0000278474Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2282 – 22821Phosphoserine By similarity
Modified residuei2458 – 24581Phosphoserine1 Publication
Modified residuei2462 – 24621Phosphoserine By similarity
Disulfide bondi2709 ↔ 2762 By similarity

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini65 – 210146CRAL-TRIO
Add
BLAST
Repeati218 – 338121Spectrin 1
Add
BLAST
Repeati340 – 446107Spectrin 2
Add
BLAST
Repeati566 – 672107Spectrin 3
Add
BLAST
Repeati673 – 784112Spectrin 4
Add
BLAST
Repeati907 – 1012106Spectrin 5
Add
BLAST
Repeati1138 – 1244107Spectrin 6
Add
BLAST
Domaini1292 – 1467176DH 1
Add
BLAST
Domaini1479 – 1591113PH 1
Add
BLAST
Domaini1656 – 172166SH3
Add
BLAST
Domaini1969 – 2145177DH 2
Add
BLAST
Domaini2157 – 2271115PH 2
Add
BLAST
Domaini2688 – 277891Ig-like C2-type
Add
BLAST
Domaini2799 – 3053255Protein kinase
Add
BLAST

Compositional bias

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

Sequence similaritiesi

Contains 1 CRAL-TRIO domain.
Contains 2 PH domains.
Contains 1 SH3 domain.
Contains 6 spectrin repeats.

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1890 – 190819ASSRL…PSAAE → HYVDLCSVSVLAQFPYLSI in isoform 2.
VSP_023308Add
BLAST
Alternative sequencei1909 – 31021194Missing in isoform 2.
VSP_023309Add
BLAST
Alternative sequencei2548 – 25481G → GS in isoform 3 and isoform 4.
VSP_037863
Alternative sequencei2549 – 256820EGSSS…EYTAV → VRVPGSLRPSTPPPLSRQLF in isoform 3.
VSP_037864Add
BLAST
Alternative sequencei2569 – 3102534Missing in isoform 3.
VSP_037865Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2863 – 28631E → K in BAE32258. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 77 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

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