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Q0KL02 (TRIO_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Triple functional domain protein

EC=2.7.11.1
Gene names
Name:Trio
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length3102 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

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

Subcellular location

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

Tissue specificity

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. Ref.1

Domain

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 similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family.

Contains 1 CRAL-TRIO domain.

Contains 2 DH (DBL-homology) domains.

Contains 1 Ig-like C2-type (immunoglobulin-like) domain.

Contains 2 PH domains.

Contains 1 protein kinase domain.

Contains 1 SH3 domain.

Contains 6 spectrin repeats.

Sequence caution

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

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q0KL02-1)

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.
Isoform 2 (identifier: Q0KL02-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1890-1908: ASSRLLVRPTSSETPSAAE → HYVDLCSVSVLAQFPYLSI
     1909-3102: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q0KL02-3)

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.
Isoform 4 (identifier: Q0KL02-4)

The sequence of this isoform differs from the canonical sequence as follows:
     2548-2548: G → GS
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 31023102Triple functional domain protein
PRO_0000278474

Regions

Domain65 – 210146CRAL-TRIO
Repeat218 – 338121Spectrin 1
Repeat340 – 446107Spectrin 2
Repeat566 – 672107Spectrin 3
Repeat673 – 784112Spectrin 4
Repeat907 – 1012106Spectrin 5
Repeat1138 – 1244107Spectrin 6
Domain1292 – 1467176DH 1
Domain1479 – 1591113PH 1
Domain1656 – 172166SH3
Domain1969 – 2145177DH 2
Domain2157 – 2271115PH 2
Domain2688 – 277891Ig-like C2-type
Domain2799 – 3053255Protein kinase
Nucleotide binding2805 – 28139ATP By similarity
Compositional bias715 – 7184Poly-Gln
Compositional bias1845 – 18506Poly-Ser
Compositional bias1951 – 19544Poly-Ser
Compositional bias2292 – 232433Gly-rich
Compositional bias2296 – 2557262Ser-rich

Sites

Active site29181Proton acceptor By similarity
Binding site28281ATP By similarity

Amino acid modifications

Modified residue22821Phosphoserine By similarity
Modified residue24581Phosphoserine Ref.5
Modified residue24621Phosphoserine By similarity
Disulfide bond2709 ↔ 2762 By similarity

Natural variations

Alternative sequence1890 – 190819ASSRL…PSAAE → HYVDLCSVSVLAQFPYLSI in isoform 2.
VSP_023308
Alternative sequence1909 – 31021194Missing in isoform 2.
VSP_023309
Alternative sequence25481G → GS in isoform 3 and isoform 4.
VSP_037863
Alternative sequence2549 – 256820EGSSS…EYTAV → VRVPGSLRPSTPPPLSRQLF in isoform 3.
VSP_037864
Alternative sequence2569 – 3102534Missing in isoform 3.
VSP_037865

Experimental info

Mutagenesis14271Q → A: Abolishes Rac1 activation; when associated with E-1435. Ref.1
Mutagenesis14351L → E: Abolishes Rac1 activation; when associated with A-1427. Ref.1
Sequence conflict28631E → K in BAE32258. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 1, 2009. Version 3.
Checksum: 8E8F7C44CB4F72D0

FASTA3,102347,861
        10         20         30         40         50         60 
MSGSSGGATA PAASSGPAAA ASAAGSGCGG GAGEGAEEAA KDLADIAAFF RSGFRKNDEM 

        70         80         90        100        110        120 
KAMDVLPILK EKVAYLSGGR DKRGGPILTF PARSNHDRIR QEDLRRLISY LACIPSEEVC 

       130        140        150        160        170        180 
KRGFTVIVDM RGSKWDSIKP LLKILQESFP CCIHIALIIK PDNFWQKQRT NFGSSKFEFE 

       190        200        210        220        230        240 
TNMVSLEGLT KVVDPSQLTP EFDGCLEYNH EEWIEIRVAF EEYISNAAHM LSRLEELQDV 

       250        260        270        280        290        300 
LAKKELPQDL EGARNMIDEH SQLKKKVIKA PIEDLDLEGQ KLLQRIQSSD SFPKKNSGSG 

       310        320        330        340        350        360 
NADLQNLLPK VSTMLDRLHS TRQHLHQMWH VRKLKLDQCF QLRLFEQDAE KMFDWITHNK 

       370        380        390        400        410        420 
GLFLNSYTEI GTSHPHAMEL QTQHNHFAMN CMNVYVNINR IMSVANRLVE SGHYASQQIK 

       430        440        450        460        470        480 
QIANQLEQEW KAFAAALDER STLLDMSSIF HQKAEKYMSN VDSWCKACGE VDLPSELQDL 

       490        500        510        520        530        540 
EDAIHHHQGI YEHITLAYSE VSQDGKSLLD KLQRPLTPGS SDSLTASANY SKAVHHVLDV 

       550        560        570        580        590        600 
IHEVLHHQRQ LENIWQHRKV RLHQRLQLCV FQQDVQQVLD WIENHGEAFL SKHTGVGKSL 

       610        620        630        640        650        660 
HRARALQKRH EDFEEVAQNT YTNADKLLEA AEQLAQTGEC DPEEIYQAAH QLEDRIQDFV 

       670        680        690        700        710        720 
RRVEQRKILL DMSVSFHTHV KELWTWLEEL QKELLDDVYA ESVEAVQDLI KRFGQQQQTT 

       730        740        750        760        770        780 
LQVTVNVIKE GEDLIQQLRD SAISSNKTPH NSSINHIETV LQQLDEAQSQ MEELFQERKI 

       790        800        810        820        830        840 
KLELFLQLRI FERDAIDIIS DLESWNDELS QQMNDFDTED LTIAEQRLQH HADKALTMNN 

       850        860        870        880        890        900 
LTFDVIHQGQ DLLQYVNEVQ ASGVELLCDR DVDMATRVQD LLEFLHEKQQ ELDLAAEQHR 

       910        920        930        940        950        960 
KHLEQCVQLR HLQAEVKQVL GWIRNGESML NAGLITASSL QEAEQLQREH EQFQHAIEKT 

       970        980        990       1000       1010       1020 
HQSALQVQQK AEAMLQANHY DMDMIRDCAE KVASHWQQLM LKMEDRLKLV NASVAFYKTS 

      1030       1040       1050       1060       1070       1080 
EQVCSVLESL EQEYKREEDW CGGADKLGPN SETDHVTPMI SKHLEQKEAF LKACTLARRN 

      1090       1100       1110       1120       1130       1140 
ADVFLKYLHR NSVSMPGMVT HIKAPEQQVK NILNELFQRE NRVLHYWTMR KRRLDQCQQY 

      1150       1160       1170       1180       1190       1200 
VVFERSAKQA LEWIHDNGEF YLSTHTSTGS SIQHTQELLK EHEEFQITAK QTKERVKLLI 

      1210       1220       1230       1240       1250       1260 
QLADGFCEKG HAHAAEIKKC VTAVDKRYRD FSLRMEKYRT SLEKALGISS DSNKSSKSLQ 

      1270       1280       1290       1300       1310       1320 
LDIIPASIPG SEVKLRDAAH ELNEEKRKSA RRKEFIMAEL IQTEKAYVRD LRECMDTYLW 

      1330       1340       1350       1360       1370       1380 
EMTSGVEEIP PGIVNKELII FGNMQEIYEF HNNIFLKELE KYEQLPEDVG HCFVTWADKF 

      1390       1400       1410       1420       1430       1440 
QMYVTYCKNK PDSTQLILEH AGSYFDEIQQ RHGLANSISS YLIKPVQRIT KYQLLLKELL 

      1450       1460       1470       1480       1490       1500 
TCCEEGKGEI KDGLEVMLSV PKRANDAMHL SMLEGFDENI ESQGELILQE SFQVWDPKTL 

      1510       1520       1530       1540       1550       1560 
IRKGRERHLF LFEMSLVFSK EVKDSSGRSK YLYKSKLFTS ELGVTEHVEG DPCKFALWVG 

      1570       1580       1590       1600       1610       1620 
RTPTSDNKIV LKASSIENKQ DWIKHIREVI QERTVHLRGA LKEPIHIPKT APAARQKGRR 

      1630       1640       1650       1660       1670       1680 
DGEDLDSQGD GSSQPDTISI ASRTSQNTLD SDKLSGGCEL TVVIHDFTAC NSNELTIRRG 

      1690       1700       1710       1720       1730       1740 
QTVEVLERPH DKPDWCLVRT TDRSPAAEGL VPCGSLCIAH SRSSMEMEGI FNHKDSLSVS 

      1750       1760       1770       1780       1790       1800 
SNDASPPASV ASLQPHMIGA QSSPGPKRPG NTLRKWLTSP VRRLSSGKAD GHAKKLAHKH 

      1810       1820       1830       1840       1850       1860 
KKSREVRKSA DAGSQKDSDD SAATPQDETI EERGRNEGLS SGTLSKSSSS GMQSCGEEEG 

      1870       1880       1890       1900       1910       1920 
EEGADAVPLP PPMAIQQHSL LQPDSQDDKA SSRLLVRPTS SETPSAAELV SAIEELVKSK 

      1930       1940       1950       1960       1970       1980 
MALEDRPSSL LVDQGDSSSP SFNPSDNSLL SSSSPIDEME ERKCSSLKRR HYVLQELVET 

      1990       2000       2010       2020       2030       2040 
ERDYVRDLGC VVEGYMALMK EDGVPDDMKG KDKIVFGNIH QIYDWHRDFF LGELEKCLED 

      2050       2060       2070       2080       2090       2100 
PEKLGSLFVK HERRLHMYIV YCQNKPKSEH IVSEYIDTFF EDLKQRLGHR LQLTDLLIKP 

      2110       2120       2130       2140       2150       2160 
VQRIMKYQLL LKDFLKYSKK ASLDTSELEK AVEVMCIVPK RCNDMMNVGR LQGFDGKIVA 

      2170       2180       2190       2200       2210       2220 
QGKLLLQDTF LVTDQDAGLL PRCKERRVFL FEQIVIFSEP LDKKKGFSMP GFLFKNSIKV 

      2230       2240       2250       2260       2270       2280 
SCLCLEENVE SDPCKFALTS RTGDAVETFV LHSSSPSVRQ TWIHEINQIL ENQRNFLNAL 

      2290       2300       2310       2320       2330       2340 
TSPIEYQRNH SGGGGSGSGG SSGGGGGSGG SGASSGGSSS HGSGPSSCSS GPSSSRSRPS 

      2350       2360       2370       2380       2390       2400 
RIPQPVRHHP PMLVSSAASS QAEADKMSGM SAPSPSLPTP SSSLALEASL GQPSRLPLSG 

      2410       2420       2430       2440       2450       2460 
DSEGHERETE PIPKMKVMES PRKAPGSTSG TSQDGNTKDA RGNLGSLPLG KTRPGAVSPL 

      2470       2480       2490       2500       2510       2520 
NSPLSTTFPS PFGKEAFPPS SPLQKGGSFW SSIPASPASR PSSFTFPGDS DSLQRQTHRH 

      2530       2540       2550       2560       2570       2580 
AAPSKDTDRM STCSSASEQS VQSTQSNGEG SSSSNISTML VTHEYTAVKE DEINVYQGEV 

      2590       2600       2610       2620       2630       2640 
VQILASNQQN MFLVFRAATD QCPAAEGWIP GFVLGHTSAV IMENPDGTLK KSTSWHTALR 

      2650       2660       2670       2680       2690       2700 
LRKKSEKKDK DGKRDGKLEN GYRKPREGLS NKVSVKLLNP NYIYDVPPEF VIPLSEVTCE 

      2710       2720       2730       2740       2750       2760 
TGETVVFRCR VCGRPKASIT WKGPEHNTLN NDDHYSISYS DIGEATLKII GVSTEDDGIY 

      2770       2780       2790       2800       2810       2820 
TCIAVNDMGS ASSSASLRVL GPGSDGIVVT WKDNFDAFYS EVAELGRGRF AVVKKCDQKG 

      2830       2840       2850       2860       2870       2880 
TKRAVATKFV NKKLMKRDQV THELGILQNL QHPLLVSLLD TFETPTSYVL VLEMADQGRL 

      2890       2900       2910       2920       2930       2940 
LDCVVRWGSL TEGKVRAHLG EVLEAVRYLH NCRIAHLDLK PENILVDQSL AKPTIKLADF 

      2950       2960       2970       2980       2990       3000 
GDAVQLNTTY YIHQLLGNPE FAAPEIILGN PVSLTADTWS VGVLTYVLLS GVSPFLDDSV 

      3010       3020       3030       3040       3050       3060 
EETCLNICRL DFSFPEDYFQ GVSQKAKEFV CFLLQEDPAK RPSAALALQE QWLQAGNGSG 

      3070       3080       3090       3100 
KGTGVLDTSR LTSFIERRKH QNDVRPIRSI KNFLQSRLLP RV 

« Hide

Isoform 2 [UniParc].

Checksum: CB3E6B6BB738F7F1
Show »

FASTA1,908217,005
Isoform 3 [UniParc].

Checksum: 5869317875FB1134
Show »

FASTA2,569288,709
Isoform 4 [UniParc].

Checksum: 3471FAD8B46480A6
Show »

FASTA3,103347,948

References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS49587.1. [Q0KL02-4]
RefSeqNP_001074771.1. NM_001081302.1. [Q0KL02-4]
XP_006520117.1. XM_006520054.1. [Q0KL02-2]
UniGeneMm.485422.

3D structure databases

ProteinModelPortalQ0KL02.
SMRQ0KL02. Positions 220-440, 801-1006, 1290-1594, 1655-1721, 1960-2291, 2558-2615, 2631-3085.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid230148. 1 interaction.
STRING10090.ENSMUSP00000087714.

PTM databases

PhosphoSiteQ0KL02.

Proteomic databases

MaxQBQ0KL02.
PaxDbQ0KL02.
PRIDEQ0KL02.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000090247; ENSMUSP00000087714; ENSMUSG00000022263. [Q0KL02-4]
GeneID223435.
KEGGmmu:223435.
UCSCuc007vjw.1. mouse. [Q0KL02-4]
uc007vjx.1. mouse. [Q0KL02-3]

Organism-specific databases

CTD7204.
MGIMGI:1927230. Trio.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00720000108506.
HOGENOMHOG000044462.
HOVERGENHBG108598.
InParanoidQ0KL02.
KOK08810.
OMAIEERGRN.
OrthoDBEOG7B8S3F.
PhylomeDBQ0KL02.
TreeFamTF318080.

Gene expression databases

BgeeQ0KL02.
CleanExMM_TRIO.
GenevestigatorQ0KL02.

Family and domain databases

Gene3D1.20.900.10. 2 hits.
2.30.29.30. 2 hits.
2.60.40.10. 1 hit.
3.40.525.10. 1 hit.
InterProIPR001251. 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.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
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]
PANTHERPTHR22826:SF104. PTHR22826:SF104. 1 hit.
PfamPF13716. 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]
SMARTSM00408. 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]
SUPFAMSSF48065. SSF48065. 2 hits.
SSF50044. SSF50044. 2 hits.
SSF52087. SSF52087. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS50191. 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]
ProtoNetSearch...

Other

ChiTaRSTRIO. mouse.
NextBio376714.
PROQ0KL02.
SOURCESearch...

Entry information

Entry nameTRIO_MOUSE
AccessionPrimary (citable) accession number: Q0KL02
Secondary accession number(s): Q3U522, Q6P9K6, Q80W23
Entry history
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: September 1, 2009
Last modified: July 9, 2014
This is version 76 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot