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O75962

- TRIO_HUMAN

UniProt

O75962 - TRIO_HUMAN

Protein

Triple functional domain protein

Gene

TRIO

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 2 (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.

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei2825 – 28251ATPPROSITE-ProRule annotation
    Active sitei2915 – 29151By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi2802 – 28109ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. apoptotic signaling pathway Source: Reactome
    2. axon guidance Source: Reactome
    3. neurotrophin TRK receptor signaling pathway Source: Reactome
    4. positive regulation of apoptotic process Source: Reactome
    5. positive regulation of GTPase activity Source: GOC
    6. regulation of small GTPase mediated signal transduction Source: Reactome
    7. small GTPase mediated signal transduction Source: Reactome
    8. transmembrane receptor protein tyrosine phosphatase signaling pathway Source: ProtInc

    Keywords - Molecular functioni

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

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.
    REACT_13638. NRAGE signals death through JNK.
    REACT_18283. G alpha (q) signalling events.
    REACT_18407. G alpha (12/13) signalling events.
    REACT_22351. DCC mediated attractive signaling.
    SignaLinkiO75962.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Triple functional domain protein (EC:2.7.11.1)
    Alternative name(s):
    PTPRF-interacting protein
    Gene namesi
    Name:TRIO
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:12303. TRIO.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1299 – 12991E → A: 50% decrease in nucleotide exchange activity. 1 Publication
    Mutagenesisi1303 – 13031T → A: 40% decrease in nucleotide exchange activity. 1 Publication
    Mutagenesisi1389 – 13891N → A: No change in nucleotide exchange activity. 1 Publication
    Mutagenesisi1426 – 14261V → A: 90% decrease in nucleotide exchange activity. 1 Publication
    Mutagenesisi1427 – 14271Q → A: 80% decrease in nucleotide exchange activity. 1 Publication
    Mutagenesisi1428 – 14281R → A: 80% decrease in nucleotide exchange activity. 1 Publication
    Mutagenesisi1430 – 14301T → A: 80% decrease in nucleotide exchange activity. 1 Publication
    Mutagenesisi1431 – 14311K → A: Loss of nucleotide exchange activity. 1 Publication
    Mutagenesisi1434 – 14341L → A: 40% decrease in nucleotide exchange activity. 1 Publication
    Mutagenesisi1437 – 14371K → A: No change in nucleotide exchange activity. 1 Publication
    Mutagenesisi1438 – 14381E → A: 30% decrease in nucleotide exchange activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA36982.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 30973097Triple functional domain proteinPRO_0000080978Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2282 – 22821Phosphoserine1 Publication
    Modified residuei2455 – 24551Phosphoserine2 Publications
    Modified residuei2459 – 24591Phosphoserine1 Publication
    Disulfide bondi2696 ↔ 2759PROSITE-ProRule annotation

    Post-translational modificationi

    Phosphorylated on serine residue(s).2 Publications

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiO75962.
    PaxDbiO75962.
    PRIDEiO75962.

    PTM databases

    PhosphoSiteiO75962.

    Expressioni

    Tissue specificityi

    Highly expressed in heart, skeletal muscle, brain, pancreas, placenta, liver, kidney and lung.

    Gene expression databases

    ArrayExpressiO75962.
    BgeeiO75962.
    CleanExiHS_TRIO.
    GenevestigatoriO75962.

    Organism-specific databases

    HPAiHPA008157.

    Interactioni

    Subunit structurei

    Interacts to form a complex with leukocyte antigen related protein.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DISC1Q9NRI53EBI-718519,EBI-529989

    Protein-protein interaction databases

    BioGridi113055. 13 interactions.
    DIPiDIP-37578N.
    IntActiO75962. 6 interactions.
    MINTiMINT-1397752.
    STRINGi9606.ENSP00000339299.

    Structurei

    Secondary structure

    1
    3097
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1291 – 131626
    Helixi1318 – 13247
    Turni1331 – 13355
    Helixi1337 – 13415
    Helixi1344 – 135310
    Helixi1355 – 13617
    Turni1362 – 13643
    Helixi1366 – 13694
    Helixi1370 – 13756
    Turni1376 – 13805
    Helixi1381 – 140020
    Turni1401 – 14033
    Helixi1404 – 14129
    Helixi1418 – 14225
    Helixi1424 – 144118
    Helixi1450 – 147021
    Beta strandi1473 – 14753
    Helixi1481 – 14833
    Beta strandi1486 – 149510
    Beta strandi1497 – 15015
    Beta strandi1504 – 152320
    Beta strandi1529 – 153810
    Helixi1539 – 15413
    Beta strandi1542 – 15454
    Beta strandi1549 – 15524
    Beta strandi1554 – 15629
    Turni1565 – 15673
    Beta strandi1569 – 15724
    Helixi1576 – 159217

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NTYX-ray1.70A1284-1594[»]
    2NZ8X-ray2.00B1285-1594[»]
    ProteinModelPortaliO75962.
    SMRiO75962. Positions 220-440, 801-1006, 1290-1594, 1655-1721, 1960-2291, 2555-2612, 2628-3072.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75962.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini65 – 210146CRAL-TRIOPROSITE-ProRule annotationAdd
    BLAST
    Repeati311 – 418108Spectrin 1Add
    BLAST
    Repeati538 – 644107Spectrin 2Add
    BLAST
    Repeati878 – 984107Spectrin 3Add
    BLAST
    Repeati1109 – 1216108Spectrin 4Add
    BLAST
    Domaini1292 – 1467176DH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1480 – 1591112PH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1656 – 171257SH3 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1969 – 2145177DH 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini2157 – 2271115PH 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini2551 – 261666SH3 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini2685 – 277591Ig-like C2-typeAdd
    BLAST
    Domaini2796 – 3052257Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi715 – 7184Poly-Gln
    Compositional biasi1845 – 18506Poly-Ser
    Compositional biasi2292 – 231221Poly-GlyAdd
    BLAST
    Compositional biasi2545 – 25517Poly-Ser

    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.

    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 2 SH3 domains.PROSITE-ProRule annotation
    Contains 4 spectrin repeats.Curated

    Keywords - Domaini

    Immunoglobulin domain, Repeat, SH3 domain

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000044462.
    HOVERGENiHBG108598.
    InParanoidiO75962.
    KOiK08810.
    OMAiIEERGRN.
    OrthoDBiEOG7B8S3F.
    PhylomeDBiO75962.
    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 (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O75962-1) [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

    MSGSSGGAAA PAASSGPAAA ASAAGSGCGG GAGEGAEEAA KDLADIAAFF     50
    RSGFRKNDEM KAMDVLPILK EKVAYLSGGR DKRGGPILTF PARSNHDRIR 100
    QEDLRRLISY LACIPSEEVC KRGFTVIVDM RGSKWDSIKP LLKILQESFP 150
    CCIHVALIIK PDNFWQKQRT NFGSSKFEFE TNMVSLEGLT KVVDPSQLTP 200
    EFDGCLEYNH EEWIEIRVAF EDYISNATHM LSRLEELQDI LAKKELPQDL 250
    EGARNMIEEH SQLKKKVIKA PIEDLDLEGQ KLLQRIQSSE SFPKKNSGSG 300
    NADLQNLLPK VSTMLDRLHS TRQHLHQMWH VRKLKLDQCF QLRLFEQDAE 350
    KMFDWITHNK GLFLNSYTEI GTSHPHAMEL QTQHNHFAMN CMNVYVNINR 400
    IMSVANRLVE SGHYASQQIR QIASQLEQEW 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 NSVNMPGMVT 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 QERTIHLKGA 1600
    LKEPIHIPKT APATRQKGRR DGEDLDSQGD GSSQPDTISI ASRTSQNTLD 1650
    SDKLSGGCEL TVVIHDFTAC NSNELTIRRG QTVEVLERPH DKPDWCLVRT 1700
    TDRSPAAEGL VPCGSLCIAH SRSSMEMEGI FNHKDSLSVS SNDASPPASV 1750
    ASLQPHMIGA QSSPGPKRPG NTLRKWLTSP VRRLSSGKAD GHVKKLAHKH 1800
    KKSREVRKSA DAGSQKDSDD SAATPQDETV EERGRNEGLS SGTLSKSSSS 1850
    GMQSCGEEEG EEGADAVPLP PPMAIQQHSL LQPDSQDDKA SSRLLVRPTS 1900
    SETPSAAELV SAIEELVKSK MALEDRPSSL LVDQGDSSSP SFNPSDNSLL 1950
    SSSSPIDEME ERKSSSLKRR HYVLQELVET ERDYVRDLGY VVEGYMALMK 2000
    EDGVPDDMKG KDKIVFGNIH QIYDWHRDFF LGELEKCLED PEKLGSLFVK 2050
    HERRLHMYIA YCQNKPKSEH IVSEYIDTFF EDLKQRLGHR LQLTDLLIKP 2100
    VQRIMKYQLL LKDFLKYSKK ASLDTSELER AVEVMCIVPR RCNDMMNVGR 2150
    LQGFDGKIVA QGKLLLQDTF LVTDQDAGLL PRCRERRIFL FEQIVIFSEP 2200
    LDKKKGFSMP GFLFKNSIKV SCLCLEENVE NDPCKFALTS RTGDVVETFI 2250
    LHSSSPSVRQ TWIHEINQIL ENQRNFLNAL TSPIEYQRNH SGGGGGGGSG 2300
    GSGGGGGSGG GGAPSGGSGH SGGPSSCGGA PSTSRSRPSR IPQPVRHHPP 2350
    VLVSSAASSQ AEADKMSGTS TPGPSLPPPG AAPEAGPSAP SRRPPGADAE 2400
    GSEREAEPIP KMKVLESPRK GAANASGSSP DAPAKDARAS LGTLPLGKPR 2450
    AGAASPLNSP LSSAVPSLGK EPFPPSSPLQ KGGSFWSSIP ASPASRPGSF 2500
    TFPGDSDSLQ RQTPRHAAPG KDTDRMSTCS SASEQSVQST QSNGSESSSS 2550
    SNISTMLVTH DYTAVKEDEI NVYQGEVVQI LASNQQNMFL VFRAATDQCP 2600
    AAEGWIPGFV LGHTSAVIVE NPDGTLKKST SWHTALRLRK KSEKKDKDGK 2650
    REGKLENGYR KSREGLSNKV SVKLLNPNYI YDVPPEFVIP LSEVTCETGE 2700
    TVVLRCRVCG RPKASITWKG PEHNTLNNDG HYSISYSDLG EATLKIVGVT 2750
    TEDDGIYTCI AVNDMGSASS SASLRVLGPG MDGIMVTWKD NFDSFYSEVA 2800
    ELGRGRFSVV KKCDQKGTKR AVATKFVNKK LMKRDQVTHE LGILQSLQHP 2850
    LLVGLLDTFE TPTSYILVLE MADQGRLLDC VVRWGSLTEG KIRAHLGEVL 2900
    EAVRYLHNCR IAHLDLKPEN ILVDESLAKP TIKLADFGDA VQLNTTYYIH 2950
    QLLGNPEFAA PEIILGNPVS LTSDTWSVGV LTYVLLSGVS PFLDDSVEET 3000
    CLNICRLDFS FPDDYFKGVS QKAKEFVCFL LQEDPAKRPS AALALQEQWL 3050
    QAGNGRSTGV LDTSRLTSFI ERRKHQNDVR PIRSIKNFLQ SRLLPRV 3097
    Length:3,097
    Mass (Da):346,900
    Last modified:September 1, 2009 - v2
    Checksum:iEA9236DF88B0EA24
    GO
    Isoform 2 (identifier: O75962-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2368-2368: G → E
         2369-2544: Missing.

    Show »
    Length:2,921
    Mass (Da):329,389
    Checksum:i7F2AEF630EF984C9
    GO
    Isoform 3 (identifier: O75962-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-2501: Missing.
         2502-2544: FPGDSDSLQR...QSVQSTQSNG → MLPSQAQGLL...LARNTFLKAC

    Note: No experimental confirmation available.

    Show »
    Length:596
    Mass (Da):66,206
    Checksum:iF6DA7D25AE9E7F0C
    GO
    Isoform 4 (identifier: O75962-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-59: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:3,038
    Mass (Da):341,598
    Checksum:i2E9F96D84514638C
    GO
    Isoform 5 (identifier: O75962-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2545-2563: SESSSSSNISTMLVTHDYT → VSASGGPRPPAPLPLSRQL
         2564-3097: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:2,563
    Mass (Da):287,377
    Checksum:iD55716EE24B33EFE
    GO

    Sequence cautioni

    The sequence AAC34245.1 differs from that shown. Reason: Frameshift at position 2301.
    Isoform 2 : The sequence AAC34245.1 differs from that shown. Reason: Frameshift at position 2301.
    The sequence AAC34245.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAC43042.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti550 – 5534QLEN → HVRT in AAC34245. (PubMed:8643598)Curated
    Sequence conflicti550 – 5534QLEN → HVRT in AAC43042. 1 PublicationCurated
    Sequence conflicti574 – 5741D → E in AAC34245. (PubMed:8643598)Curated
    Sequence conflicti574 – 5741D → E in AAC43042. 1 PublicationCurated
    Sequence conflicti787 – 7882QL → HV in AAC34245. (PubMed:8643598)Curated
    Sequence conflicti787 – 7882QL → HV in AAC43042. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti291 – 2911S → T.1 Publication
    Corresponds to variant rs55772118 [ dbSNP | Ensembl ].
    VAR_041899
    Natural varianti348 – 3481D → E.
    Corresponds to variant rs16903367 [ dbSNP | Ensembl ].
    VAR_059802
    Natural varianti1368 – 13681D → V.1 Publication
    VAR_069371
    Natural varianti1613 – 16131A → T.
    Corresponds to variant rs16903474 [ dbSNP | Ensembl ].
    VAR_059803
    Natural varianti1644 – 16441T → M.1 Publication
    Corresponds to variant rs55687522 [ dbSNP | Ensembl ].
    VAR_041900
    Natural varianti1690 – 16901H → R.1 Publication
    Corresponds to variant rs56292586 [ dbSNP | Ensembl ].
    VAR_041901
    Natural varianti1978 – 19781V → M in a metastatic melanoma sample; somatic mutation. 1 Publication
    VAR_041902
    Natural varianti2242 – 22421T → M.1 Publication
    Corresponds to variant rs55916212 [ dbSNP | Ensembl ].
    VAR_041903
    Natural varianti2563 – 25631T → M.1 Publication
    VAR_069372

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 25012501Missing in isoform 3. 1 PublicationVSP_023306Add
    BLAST
    Alternative sequencei1 – 5959Missing in isoform 4. 1 PublicationVSP_037860Add
    BLAST
    Alternative sequencei2368 – 23681G → E in isoform 2. 1 PublicationVSP_004467
    Alternative sequencei2369 – 2544176Missing in isoform 2. 1 PublicationVSP_004468Add
    BLAST
    Alternative sequencei2502 – 254443FPGDS…TQSNG → MLPSQAQGLLWWVFPLFPAS SLSYPPVSYRADGLARNTFL KAC in isoform 3. 1 PublicationVSP_023307Add
    BLAST
    Alternative sequencei2545 – 256319SESSS…THDYT → VSASGGPRPPAPLPLSRQL in isoform 5. 1 PublicationVSP_037861Add
    BLAST
    Alternative sequencei2564 – 3097534Missing in isoform 5. 1 PublicationVSP_037862Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK131423 mRNA. Translation: BAD18570.1.
    AC010419 Genomic DNA. No translation available.
    AC016549 Genomic DNA. No translation available.
    AC016654 Genomic DNA. No translation available.
    AC016656 Genomic DNA. No translation available.
    AC026456 Genomic DNA. No translation available.
    CH471102 Genomic DNA. Translation: EAX08047.1.
    CH471102 Genomic DNA. Translation: EAX08048.1.
    BC035585 mRNA. Translation: AAH35585.1.
    BC017268 mRNA. Translation: AAH17268.1.
    U42390 mRNA. Translation: AAC34245.1. Sequence problems.
    AF091395 mRNA. Translation: AAC43042.1. Different initiation.
    AB209754 mRNA. Translation: BAD92991.1.
    CCDSiCCDS3883.1. [O75962-1]
    RefSeqiNP_009049.2. NM_007118.2. [O75962-1]
    UniGeneiHs.130031.

    Genome annotation databases

    EnsembliENST00000344135; ENSP00000339291; ENSG00000038382. [O75962-3]
    ENST00000344204; ENSP00000339299; ENSG00000038382. [O75962-1]
    GeneIDi7204.
    KEGGihsa:7204.
    UCSCiuc003jff.3. human. [O75962-1]
    uc003jfh.1. human. [O75962-5]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK131423 mRNA. Translation: BAD18570.1 .
    AC010419 Genomic DNA. No translation available.
    AC016549 Genomic DNA. No translation available.
    AC016654 Genomic DNA. No translation available.
    AC016656 Genomic DNA. No translation available.
    AC026456 Genomic DNA. No translation available.
    CH471102 Genomic DNA. Translation: EAX08047.1 .
    CH471102 Genomic DNA. Translation: EAX08048.1 .
    BC035585 mRNA. Translation: AAH35585.1 .
    BC017268 mRNA. Translation: AAH17268.1 .
    U42390 mRNA. Translation: AAC34245.1 . Sequence problems.
    AF091395 mRNA. Translation: AAC43042.1 . Different initiation.
    AB209754 mRNA. Translation: BAD92991.1 .
    CCDSi CCDS3883.1. [O75962-1 ]
    RefSeqi NP_009049.2. NM_007118.2. [O75962-1 ]
    UniGenei Hs.130031.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NTY X-ray 1.70 A 1284-1594 [» ]
    2NZ8 X-ray 2.00 B 1285-1594 [» ]
    ProteinModelPortali O75962.
    SMRi O75962. Positions 220-440, 801-1006, 1290-1594, 1655-1721, 1960-2291, 2555-2612, 2628-3072.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113055. 13 interactions.
    DIPi DIP-37578N.
    IntActi O75962. 6 interactions.
    MINTi MINT-1397752.
    STRINGi 9606.ENSP00000339299.

    PTM databases

    PhosphoSitei O75962.

    Proteomic databases

    MaxQBi O75962.
    PaxDbi O75962.
    PRIDEi O75962.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000344135 ; ENSP00000339291 ; ENSG00000038382 . [O75962-3 ]
    ENST00000344204 ; ENSP00000339299 ; ENSG00000038382 . [O75962-1 ]
    GeneIDi 7204.
    KEGGi hsa:7204.
    UCSCi uc003jff.3. human. [O75962-1 ]
    uc003jfh.1. human. [O75962-5 ]

    Organism-specific databases

    CTDi 7204.
    GeneCardsi GC05P014143.
    HGNCi HGNC:12303. TRIO.
    HPAi HPA008157.
    MIMi 601893. gene.
    neXtProti NX_O75962.
    PharmGKBi PA36982.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000044462.
    HOVERGENi HBG108598.
    InParanoidi O75962.
    KOi K08810.
    OMAi IEERGRN.
    OrthoDBi EOG7B8S3F.
    PhylomeDBi O75962.
    TreeFami TF318080.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.
    REACT_13638. NRAGE signals death through JNK.
    REACT_18283. G alpha (q) signalling events.
    REACT_18407. G alpha (12/13) signalling events.
    REACT_22351. DCC mediated attractive signaling.
    SignaLinki O75962.

    Miscellaneous databases

    ChiTaRSi TRIO. human.
    EvolutionaryTracei O75962.
    GeneWikii TRIO_(gene).
    GenomeRNAii 7204.
    NextBioi 28234.
    PROi O75962.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75962.
    Bgeei O75962.
    CleanExi HS_TRIO.
    Genevestigatori O75962.

    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. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Brain.
    2. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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 1-1686 (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2715-3097 (ISOFORM 1).
      Tissue: Kidney and Lymph.
    5. "The multidomain protein Trio binds the LAR transmembrane tyrosine phosphatase, contains a protein kinase domain, and has separate rac-specific and rho-specific guanine nucleotide exchange factor domains."
      Debant A., Serra-Pages C., Seipel K., O'Brien S., Tang M., Park S.-H., Streuli M.
      Proc. Natl. Acad. Sci. U.S.A. 93:5466-5471(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 38-3097 (ISOFORM 2).
      Tissue: Fibroblast.
    6. Streuli M.
      Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 38-3097 (ISOFORM 1).
    7. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 362-3097 (ISOFORM 5).
      Tissue: Brain.
    8. "Trio amino-terminal guanine nucleotide exchange factor domain expression promotes actin cytoskeleton reorganization, cell migration and anchorage-independent cell growth."
      Seipel K., Medley Q.G., Kedersha N.L., Zhang X.A., O'Brien S.P., Serra-Pages C., Hemler M.E., Streuli M.
      J. Cell Sci. 112:1825-1834(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2282 AND SER-2455, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2455 AND SER-2459, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "NMR structure and mutagenesis of the N-terminal Dbl homology domain of the nucleotide exchange factor Trio."
      Liu X., Wang H., Eberstadt M., Schnuchel A., Olejniczak E.T., Meadows R.P., Schkeryantz J.M., Janowick D.A., Harlan J.E., Harris E.A.S., Staunton D.E., Fesik S.W.
      Cell 95:269-277(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1286-1466, MUTAGENESIS.
    16. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] THR-291; MET-1644; ARG-1690; MET-1978 AND MET-2242.
    17. Cited for: VARIANTS VAL-1368 AND MET-2563.

    Entry informationi

    Entry nameiTRIO_HUMAN
    AccessioniPrimary (citable) accession number: O75962
    Secondary accession number(s): D3DTD1
    , Q13458, Q59EQ7, Q6PJC9, Q6ZN05, Q8IWK8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: September 1, 2009
    Last modified: October 1, 2014
    This is version 153 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3