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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
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 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. 2 interactions.
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.
GeneTreeiENSGT00760000119030.
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.
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

        10         20         30         40         50
MSGSSGGATA PAASSGPAAA ASAAGSGCGG GAGEGAEEAA KDLADIAAFF
60 70 80 90 100
RSGFRKNDEM KAMDVLPILK EKVAYLSGGR DKRGGPILTF PARSNHDRIR
110 120 130 140 150
QEDLRRLISY LACIPSEEVC KRGFTVIVDM RGSKWDSIKP LLKILQESFP
160 170 180 190 200
CCIHIALIIK PDNFWQKQRT NFGSSKFEFE TNMVSLEGLT KVVDPSQLTP
210 220 230 240 250
EFDGCLEYNH EEWIEIRVAF EEYISNAAHM LSRLEELQDV LAKKELPQDL
260 270 280 290 300
EGARNMIDEH SQLKKKVIKA PIEDLDLEGQ KLLQRIQSSD SFPKKNSGSG
310 320 330 340 350
NADLQNLLPK VSTMLDRLHS TRQHLHQMWH VRKLKLDQCF QLRLFEQDAE
360 370 380 390 400
KMFDWITHNK GLFLNSYTEI GTSHPHAMEL QTQHNHFAMN CMNVYVNINR
410 420 430 440 450
IMSVANRLVE SGHYASQQIK QIANQLEQEW KAFAAALDER STLLDMSSIF
460 470 480 490 500
HQKAEKYMSN VDSWCKACGE VDLPSELQDL EDAIHHHQGI YEHITLAYSE
510 520 530 540 550
VSQDGKSLLD KLQRPLTPGS SDSLTASANY SKAVHHVLDV IHEVLHHQRQ
560 570 580 590 600
LENIWQHRKV RLHQRLQLCV FQQDVQQVLD WIENHGEAFL SKHTGVGKSL
610 620 630 640 650
HRARALQKRH EDFEEVAQNT YTNADKLLEA AEQLAQTGEC DPEEIYQAAH
660 670 680 690 700
QLEDRIQDFV RRVEQRKILL DMSVSFHTHV KELWTWLEEL QKELLDDVYA
710 720 730 740 750
ESVEAVQDLI KRFGQQQQTT LQVTVNVIKE GEDLIQQLRD SAISSNKTPH
760 770 780 790 800
NSSINHIETV LQQLDEAQSQ MEELFQERKI KLELFLQLRI FERDAIDIIS
810 820 830 840 850
DLESWNDELS QQMNDFDTED LTIAEQRLQH HADKALTMNN LTFDVIHQGQ
860 870 880 890 900
DLLQYVNEVQ ASGVELLCDR DVDMATRVQD LLEFLHEKQQ ELDLAAEQHR
910 920 930 940 950
KHLEQCVQLR HLQAEVKQVL GWIRNGESML NAGLITASSL QEAEQLQREH
960 970 980 990 1000
EQFQHAIEKT HQSALQVQQK AEAMLQANHY DMDMIRDCAE KVASHWQQLM
1010 1020 1030 1040 1050
LKMEDRLKLV NASVAFYKTS EQVCSVLESL EQEYKREEDW CGGADKLGPN
1060 1070 1080 1090 1100
SETDHVTPMI SKHLEQKEAF LKACTLARRN ADVFLKYLHR NSVSMPGMVT
1110 1120 1130 1140 1150
HIKAPEQQVK NILNELFQRE NRVLHYWTMR KRRLDQCQQY VVFERSAKQA
1160 1170 1180 1190 1200
LEWIHDNGEF YLSTHTSTGS SIQHTQELLK EHEEFQITAK QTKERVKLLI
1210 1220 1230 1240 1250
QLADGFCEKG HAHAAEIKKC VTAVDKRYRD FSLRMEKYRT SLEKALGISS
1260 1270 1280 1290 1300
DSNKSSKSLQ LDIIPASIPG SEVKLRDAAH ELNEEKRKSA RRKEFIMAEL
1310 1320 1330 1340 1350
IQTEKAYVRD LRECMDTYLW EMTSGVEEIP PGIVNKELII FGNMQEIYEF
1360 1370 1380 1390 1400
HNNIFLKELE KYEQLPEDVG HCFVTWADKF QMYVTYCKNK PDSTQLILEH
1410 1420 1430 1440 1450
AGSYFDEIQQ RHGLANSISS YLIKPVQRIT KYQLLLKELL TCCEEGKGEI
1460 1470 1480 1490 1500
KDGLEVMLSV PKRANDAMHL SMLEGFDENI ESQGELILQE SFQVWDPKTL
1510 1520 1530 1540 1550
IRKGRERHLF LFEMSLVFSK EVKDSSGRSK YLYKSKLFTS ELGVTEHVEG
1560 1570 1580 1590 1600
DPCKFALWVG RTPTSDNKIV LKASSIENKQ DWIKHIREVI QERTVHLRGA
1610 1620 1630 1640 1650
LKEPIHIPKT APAARQKGRR DGEDLDSQGD GSSQPDTISI ASRTSQNTLD
1660 1670 1680 1690 1700
SDKLSGGCEL TVVIHDFTAC NSNELTIRRG QTVEVLERPH DKPDWCLVRT
1710 1720 1730 1740 1750
TDRSPAAEGL VPCGSLCIAH SRSSMEMEGI FNHKDSLSVS SNDASPPASV
1760 1770 1780 1790 1800
ASLQPHMIGA QSSPGPKRPG NTLRKWLTSP VRRLSSGKAD GHAKKLAHKH
1810 1820 1830 1840 1850
KKSREVRKSA DAGSQKDSDD SAATPQDETI EERGRNEGLS SGTLSKSSSS
1860 1870 1880 1890 1900
GMQSCGEEEG EEGADAVPLP PPMAIQQHSL LQPDSQDDKA SSRLLVRPTS
1910 1920 1930 1940 1950
SETPSAAELV SAIEELVKSK MALEDRPSSL LVDQGDSSSP SFNPSDNSLL
1960 1970 1980 1990 2000
SSSSPIDEME ERKCSSLKRR HYVLQELVET ERDYVRDLGC VVEGYMALMK
2010 2020 2030 2040 2050
EDGVPDDMKG KDKIVFGNIH QIYDWHRDFF LGELEKCLED PEKLGSLFVK
2060 2070 2080 2090 2100
HERRLHMYIV YCQNKPKSEH IVSEYIDTFF EDLKQRLGHR LQLTDLLIKP
2110 2120 2130 2140 2150
VQRIMKYQLL LKDFLKYSKK ASLDTSELEK AVEVMCIVPK RCNDMMNVGR
2160 2170 2180 2190 2200
LQGFDGKIVA QGKLLLQDTF LVTDQDAGLL PRCKERRVFL FEQIVIFSEP
2210 2220 2230 2240 2250
LDKKKGFSMP GFLFKNSIKV SCLCLEENVE SDPCKFALTS RTGDAVETFV
2260 2270 2280 2290 2300
LHSSSPSVRQ TWIHEINQIL ENQRNFLNAL TSPIEYQRNH SGGGGSGSGG
2310 2320 2330 2340 2350
SSGGGGGSGG SGASSGGSSS HGSGPSSCSS GPSSSRSRPS RIPQPVRHHP
2360 2370 2380 2390 2400
PMLVSSAASS QAEADKMSGM SAPSPSLPTP SSSLALEASL GQPSRLPLSG
2410 2420 2430 2440 2450
DSEGHERETE PIPKMKVMES PRKAPGSTSG TSQDGNTKDA RGNLGSLPLG
2460 2470 2480 2490 2500
KTRPGAVSPL NSPLSTTFPS PFGKEAFPPS SPLQKGGSFW SSIPASPASR
2510 2520 2530 2540 2550
PSSFTFPGDS DSLQRQTHRH AAPSKDTDRM STCSSASEQS VQSTQSNGEG
2560 2570 2580 2590 2600
SSSSNISTML VTHEYTAVKE DEINVYQGEV VQILASNQQN MFLVFRAATD
2610 2620 2630 2640 2650
QCPAAEGWIP GFVLGHTSAV IMENPDGTLK KSTSWHTALR LRKKSEKKDK
2660 2670 2680 2690 2700
DGKRDGKLEN GYRKPREGLS NKVSVKLLNP NYIYDVPPEF VIPLSEVTCE
2710 2720 2730 2740 2750
TGETVVFRCR VCGRPKASIT WKGPEHNTLN NDDHYSISYS DIGEATLKII
2760 2770 2780 2790 2800
GVSTEDDGIY TCIAVNDMGS ASSSASLRVL GPGSDGIVVT WKDNFDAFYS
2810 2820 2830 2840 2850
EVAELGRGRF AVVKKCDQKG TKRAVATKFV NKKLMKRDQV THELGILQNL
2860 2870 2880 2890 2900
QHPLLVSLLD TFETPTSYVL VLEMADQGRL LDCVVRWGSL TEGKVRAHLG
2910 2920 2930 2940 2950
EVLEAVRYLH NCRIAHLDLK PENILVDQSL AKPTIKLADF GDAVQLNTTY
2960 2970 2980 2990 3000
YIHQLLGNPE FAAPEIILGN PVSLTADTWS VGVLTYVLLS GVSPFLDDSV
3010 3020 3030 3040 3050
EETCLNICRL DFSFPEDYFQ GVSQKAKEFV CFLLQEDPAK RPSAALALQE
3060 3070 3080 3090 3100
QWLQAGNGSG KGTGVLDTSR LTSFIERRKH QNDVRPIRSI KNFLQSRLLP

RV
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. 2 interactions.
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 ENSGT00760000119030.
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.
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: October 29, 2014
This is version 79 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