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O75962 (TRIO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Triple functional domain protein

EC=2.7.11.1
Alternative name(s):
PTPRF-interacting protein
Gene names
Name:TRIO
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length3097 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.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Interacts to form a complex with leukocyte antigen related protein.

Subcellular location

Cytoplasm By similarity.

Tissue specificity

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

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.

Post-translational modification

Phosphorylated on serine residue(s).

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 2 SH3 domains.

Contains 4 spectrin repeats.

Sequence caution

The sequence AAC34245.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAC34245.1 differs from that shown. Reason: Frameshift at position 2301.

The sequence AAC43042.1 differs from that shown. Reason: Erroneous initiation.

Isoform 2: The sequence AAC34245.1 differs from that shown. Reason: Frameshift at position 2301.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainImmunoglobulin domain
Repeat
SH3 domain
   LigandATP-binding
Nucleotide-binding
   Molecular functionGuanine-nucleotide releasing factor
Kinase
Serine/threonine-protein kinase
Transferase
   PTMDisulfide bond
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic signaling pathway

Traceable author statement. Source: Reactome

axon guidance

Traceable author statement. Source: Reactome

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

positive regulation of apoptotic process

Traceable author statement. Source: Reactome

regulation of GTPase activity

Traceable author statement Ref.5. Source: GOC

regulation of small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

transmembrane receptor protein tyrosine phosphatase signaling pathway

Traceable author statement Ref.5. Source: ProtInc

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Rho guanyl-nucleotide exchange factor activity

Inferred from electronic annotation. Source: InterPro

guanyl-nucleotide exchange factor activity

Traceable author statement Ref.5. Source: ProtInc

protein serine/threonine kinase activity

Traceable author statement Ref.5. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DISC1Q9NRI53EBI-718519,EBI-529989

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75962-1)

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: O75962-2)

The sequence of this isoform differs from the canonical sequence as follows:
     2368-2368: G → E
     2369-2544: Missing.
Isoform 3 (identifier: O75962-3)

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.
Isoform 4 (identifier: O75962-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-59: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: O75962-5)

The sequence of this isoform differs from the canonical sequence as follows:
     2545-2563: SESSSSSNISTMLVTHDYT → VSASGGPRPPAPLPLSRQL
     2564-3097: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 30973097Triple functional domain protein
PRO_0000080978

Regions

Domain65 – 210146CRAL-TRIO
Repeat311 – 418108Spectrin 1
Repeat538 – 644107Spectrin 2
Repeat878 – 984107Spectrin 3
Repeat1109 – 1216108Spectrin 4
Domain1292 – 1467176DH 1
Domain1480 – 1591112PH 1
Domain1656 – 171257SH3 1
Domain1969 – 2145177DH 2
Domain2157 – 2271115PH 2
Domain2551 – 261666SH3 2
Domain2685 – 277591Ig-like C2-type
Domain2796 – 3052257Protein kinase
Nucleotide binding2802 – 28109ATP By similarity
Compositional bias715 – 7184Poly-Gln
Compositional bias1845 – 18506Poly-Ser
Compositional bias2292 – 231221Poly-Gly
Compositional bias2545 – 25517Poly-Ser

Sites

Active site29151 By similarity
Binding site28251ATP By similarity

Amino acid modifications

Modified residue22821Phosphoserine Ref.10
Modified residue24551Phosphoserine Ref.10 Ref.13
Modified residue24591Phosphoserine Ref.13
Disulfide bond2696 ↔ 2759 Potential

Natural variations

Alternative sequence1 – 25012501Missing in isoform 3.
VSP_023306
Alternative sequence1 – 5959Missing in isoform 4.
VSP_037860
Alternative sequence23681G → E in isoform 2.
VSP_004467
Alternative sequence2369 – 2544176Missing in isoform 2.
VSP_004468
Alternative sequence2502 – 254443FPGDS…TQSNG → MLPSQAQGLLWWVFPLFPAS SLSYPPVSYRADGLARNTFL KAC in isoform 3.
VSP_023307
Alternative sequence2545 – 256319SESSS…THDYT → VSASGGPRPPAPLPLSRQL in isoform 5.
VSP_037861
Alternative sequence2564 – 3097534Missing in isoform 5.
VSP_037862
Natural variant2911S → T. Ref.16
Corresponds to variant rs55772118 [ dbSNP | Ensembl ].
VAR_041899
Natural variant3481D → E.
Corresponds to variant rs16903367 [ dbSNP | Ensembl ].
VAR_059802
Natural variant13681D → V. Ref.17
VAR_069371
Natural variant16131A → T.
Corresponds to variant rs16903474 [ dbSNP | Ensembl ].
VAR_059803
Natural variant16441T → M. Ref.16
Corresponds to variant rs55687522 [ dbSNP | Ensembl ].
VAR_041900
Natural variant16901H → R. Ref.16
Corresponds to variant rs56292586 [ dbSNP | Ensembl ].
VAR_041901
Natural variant19781V → M in a metastatic melanoma sample; somatic mutation. Ref.16
VAR_041902
Natural variant22421T → M. Ref.16
Corresponds to variant rs55916212 [ dbSNP | Ensembl ].
VAR_041903
Natural variant25631T → M. Ref.17
VAR_069372

Experimental info

Mutagenesis12991E → A: 50% decrease in nucleotide exchange activity.
Mutagenesis13031T → A: 40% decrease in nucleotide exchange activity.
Mutagenesis13891N → A: No change in nucleotide exchange activity.
Mutagenesis14261V → A: 90% decrease in nucleotide exchange activity.
Mutagenesis14271Q → A: 80% decrease in nucleotide exchange activity.
Mutagenesis14281R → A: 80% decrease in nucleotide exchange activity.
Mutagenesis14301T → A: 80% decrease in nucleotide exchange activity.
Mutagenesis14311K → A: Loss of nucleotide exchange activity.
Mutagenesis14341L → A: 40% decrease in nucleotide exchange activity.
Mutagenesis14371K → A: No change in nucleotide exchange activity.
Mutagenesis14381E → A: 30% decrease in nucleotide exchange activity.
Sequence conflict550 – 5534QLEN → HVRT in AAC34245. Ref.5
Sequence conflict550 – 5534QLEN → HVRT in AAC43042. Ref.6
Sequence conflict5741D → E in AAC34245. Ref.5
Sequence conflict5741D → E in AAC43042. Ref.6
Sequence conflict787 – 7882QL → HV in AAC34245. Ref.5
Sequence conflict787 – 7882QL → HV in AAC43042. Ref.6

Secondary structure

................................................... 3097
Helix Strand Turn

Details...

Sequences

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

Last modified September 1, 2009. Version 2.
Checksum: EA9236DF88B0EA24

FASTA3,097346,900
        10         20         30         40         50         60 
MSGSSGGAAA 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 CCIHVALIIK PDNFWQKQRT NFGSSKFEFE 

       190        200        210        220        230        240 
TNMVSLEGLT KVVDPSQLTP EFDGCLEYNH EEWIEIRVAF EDYISNATHM LSRLEELQDI 

       250        260        270        280        290        300 
LAKKELPQDL EGARNMIEEH SQLKKKVIKA PIEDLDLEGQ KLLQRIQSSE SFPKKNSGSG 

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

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

       430        440        450        460        470        480 
QIASQLEQEW 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 NSVNMPGMVT 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 QERTIHLKGA LKEPIHIPKT APATRQKGRR 

      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 GHVKKLAHKH 

      1810       1820       1830       1840       1850       1860 
KKSREVRKSA DAGSQKDSDD SAATPQDETV 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 ERKSSSLKRR HYVLQELVET 

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

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

      2110       2120       2130       2140       2150       2160 
VQRIMKYQLL LKDFLKYSKK ASLDTSELER AVEVMCIVPR RCNDMMNVGR LQGFDGKIVA 

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

      2230       2240       2250       2260       2270       2280 
SCLCLEENVE NDPCKFALTS RTGDVVETFI LHSSSPSVRQ TWIHEINQIL ENQRNFLNAL 

      2290       2300       2310       2320       2330       2340 
TSPIEYQRNH SGGGGGGGSG GSGGGGGSGG GGAPSGGSGH SGGPSSCGGA PSTSRSRPSR 

      2350       2360       2370       2380       2390       2400 
IPQPVRHHPP VLVSSAASSQ AEADKMSGTS TPGPSLPPPG AAPEAGPSAP SRRPPGADAE 

      2410       2420       2430       2440       2450       2460 
GSEREAEPIP KMKVLESPRK GAANASGSSP DAPAKDARAS LGTLPLGKPR AGAASPLNSP 

      2470       2480       2490       2500       2510       2520 
LSSAVPSLGK EPFPPSSPLQ KGGSFWSSIP ASPASRPGSF TFPGDSDSLQ RQTPRHAAPG 

      2530       2540       2550       2560       2570       2580 
KDTDRMSTCS SASEQSVQST QSNGSESSSS SNISTMLVTH DYTAVKEDEI NVYQGEVVQI 

      2590       2600       2610       2620       2630       2640 
LASNQQNMFL VFRAATDQCP AAEGWIPGFV LGHTSAVIVE NPDGTLKKST SWHTALRLRK 

      2650       2660       2670       2680       2690       2700 
KSEKKDKDGK REGKLENGYR KSREGLSNKV SVKLLNPNYI YDVPPEFVIP LSEVTCETGE 

      2710       2720       2730       2740       2750       2760 
TVVLRCRVCG RPKASITWKG PEHNTLNNDG HYSISYSDLG EATLKIVGVT TEDDGIYTCI 

      2770       2780       2790       2800       2810       2820 
AVNDMGSASS SASLRVLGPG MDGIMVTWKD NFDSFYSEVA ELGRGRFSVV KKCDQKGTKR 

      2830       2840       2850       2860       2870       2880 
AVATKFVNKK LMKRDQVTHE LGILQSLQHP LLVGLLDTFE TPTSYILVLE MADQGRLLDC 

      2890       2900       2910       2920       2930       2940 
VVRWGSLTEG KIRAHLGEVL EAVRYLHNCR IAHLDLKPEN ILVDESLAKP TIKLADFGDA 

      2950       2960       2970       2980       2990       3000 
VQLNTTYYIH QLLGNPEFAA PEIILGNPVS LTSDTWSVGV LTYVLLSGVS PFLDDSVEET 

      3010       3020       3030       3040       3050       3060 
CLNICRLDFS FPDDYFKGVS QKAKEFVCFL LQEDPAKRPS AALALQEQWL QAGNGRSTGV 

      3070       3080       3090 
LDTSRLTSFI ERRKHQNDVR PIRSIKNFLQ SRLLPRV 

« Hide

Isoform 2 [UniParc].

Checksum: 7F2AEF630EF984C9
Show »

FASTA2,921329,389
Isoform 3 [UniParc].

Checksum: F6DA7D25AE9E7F0C
Show »

FASTA59666,206
Isoform 4 [UniParc].

Checksum: 2E9F96D84514638C
Show »

FASTA3,038341,598
Isoform 5 [UniParc].

Checksum: D55716EE24B33EFE
Show »

FASTA2,563287,377

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Diagnostic exome sequencing in persons with severe intellectual disability."
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G., Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G., Veltman J.A., Vissers L.E.
N. Engl. J. Med. 367:1921-1929(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VAL-1368 AND MET-2563.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_009049.2. NM_007118.2.
UniGeneHs.130031.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NTYX-ray1.70A1284-1594[»]
2NZ8X-ray2.00B1285-1594[»]
ProteinModelPortalO75962.
SMRO75962. Positions 220-440, 801-1006, 1101-1239, 1290-1594, 1655-1721, 1960-2291, 2555-2612, 2628-3086.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113055. 13 interactions.
DIPDIP-37578N.
IntActO75962. 6 interactions.
MINTMINT-1397752.
STRING9606.ENSP00000339299.

PTM databases

PhosphoSiteO75962.

Proteomic databases

PaxDbO75962.
PRIDEO75962.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000344135; ENSP00000339291; ENSG00000038382. [O75962-3]
ENST00000344204; ENSP00000339299; ENSG00000038382. [O75962-1]
ENST00000537187; ENSP00000446348; ENSG00000038382. [O75962-2]
GeneID7204.
KEGGhsa:7204.
UCSCuc003jff.3. human. [O75962-1]
uc003jfh.1. human. [O75962-5]

Organism-specific databases

CTD7204.
GeneCardsGC05P014143.
HGNCHGNC:12303. TRIO.
HPAHPA008157.
MIM601893. gene.
neXtProtNX_O75962.
PharmGKBPA36982.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000044462.
HOVERGENHBG108598.
InParanoidO75962.
KOK08810.
OMAIEERGRN.
OrthoDBEOG7B8S3F.
PhylomeDBO75962.
TreeFamTF318080.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
SignaLinkO75962.

Gene expression databases

ArrayExpressO75962.
BgeeO75962.
CleanExHS_TRIO.
GenevestigatorO75962.

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:SF78. PTHR22826:SF78. 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. human.
EvolutionaryTraceO75962.
GeneWikiTRIO_(gene).
GenomeRNAi7204.
NextBio28234.
PROO75962.
SOURCESearch...

Entry information

Entry nameTRIO_HUMAN
AccessionPrimary (citable) accession number: O75962
Secondary accession number(s): D3DTD1 expand/collapse secondary AC list , Q13458, Q59EQ7, Q6PJC9, Q6ZN05, Q8IWK8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: September 1, 2009
Last modified: April 16, 2014
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM