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O75962

- TRIO_HUMAN

UniProt

O75962 - TRIO_HUMAN

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Protein

Triple functional domain protein

Gene

TRIO

Organism
Homo sapiens (Human)
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.

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 serine/threonine kinase activity Source: ProtInc
  4. 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
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_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
Complete GO annotation...

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

BgeeiO75962.
CleanExiHS_TRIO.
ExpressionAtlasiO75962. baseline and differential.
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. 18 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.
GeneTreeiENSGT00760000119030.
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.
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

        10         20         30         40         50
MSGSSGGAAA 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
CCIHVALIIK PDNFWQKQRT NFGSSKFEFE TNMVSLEGLT KVVDPSQLTP
210 220 230 240 250
EFDGCLEYNH EEWIEIRVAF EDYISNATHM LSRLEELQDI LAKKELPQDL
260 270 280 290 300
EGARNMIEEH SQLKKKVIKA PIEDLDLEGQ KLLQRIQSSE 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 SGHYASQQIR QIASQLEQEW 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 NSVNMPGMVT
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 QERTIHLKGA
1610 1620 1630 1640 1650
LKEPIHIPKT APATRQKGRR 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 GHVKKLAHKH
1810 1820 1830 1840 1850
KKSREVRKSA DAGSQKDSDD SAATPQDETV 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 ERKSSSLKRR HYVLQELVET ERDYVRDLGY VVEGYMALMK
2010 2020 2030 2040 2050
EDGVPDDMKG KDKIVFGNIH QIYDWHRDFF LGELEKCLED PEKLGSLFVK
2060 2070 2080 2090 2100
HERRLHMYIA YCQNKPKSEH IVSEYIDTFF EDLKQRLGHR LQLTDLLIKP
2110 2120 2130 2140 2150
VQRIMKYQLL LKDFLKYSKK ASLDTSELER AVEVMCIVPR RCNDMMNVGR
2160 2170 2180 2190 2200
LQGFDGKIVA QGKLLLQDTF LVTDQDAGLL PRCRERRIFL FEQIVIFSEP
2210 2220 2230 2240 2250
LDKKKGFSMP GFLFKNSIKV SCLCLEENVE NDPCKFALTS RTGDVVETFI
2260 2270 2280 2290 2300
LHSSSPSVRQ TWIHEINQIL ENQRNFLNAL TSPIEYQRNH SGGGGGGGSG
2310 2320 2330 2340 2350
GSGGGGGSGG GGAPSGGSGH SGGPSSCGGA PSTSRSRPSR IPQPVRHHPP
2360 2370 2380 2390 2400
VLVSSAASSQ AEADKMSGTS TPGPSLPPPG AAPEAGPSAP SRRPPGADAE
2410 2420 2430 2440 2450
GSEREAEPIP KMKVLESPRK GAANASGSSP DAPAKDARAS LGTLPLGKPR
2460 2470 2480 2490 2500
AGAASPLNSP LSSAVPSLGK EPFPPSSPLQ KGGSFWSSIP ASPASRPGSF
2510 2520 2530 2540 2550
TFPGDSDSLQ RQTPRHAAPG KDTDRMSTCS SASEQSVQST QSNGSESSSS
2560 2570 2580 2590 2600
SNISTMLVTH DYTAVKEDEI NVYQGEVVQI LASNQQNMFL VFRAATDQCP
2610 2620 2630 2640 2650
AAEGWIPGFV LGHTSAVIVE NPDGTLKKST SWHTALRLRK KSEKKDKDGK
2660 2670 2680 2690 2700
REGKLENGYR KSREGLSNKV SVKLLNPNYI YDVPPEFVIP LSEVTCETGE
2710 2720 2730 2740 2750
TVVLRCRVCG RPKASITWKG PEHNTLNNDG HYSISYSDLG EATLKIVGVT
2760 2770 2780 2790 2800
TEDDGIYTCI AVNDMGSASS SASLRVLGPG MDGIMVTWKD NFDSFYSEVA
2810 2820 2830 2840 2850
ELGRGRFSVV KKCDQKGTKR AVATKFVNKK LMKRDQVTHE LGILQSLQHP
2860 2870 2880 2890 2900
LLVGLLDTFE TPTSYILVLE MADQGRLLDC VVRWGSLTEG KIRAHLGEVL
2910 2920 2930 2940 2950
EAVRYLHNCR IAHLDLKPEN ILVDESLAKP TIKLADFGDA VQLNTTYYIH
2960 2970 2980 2990 3000
QLLGNPEFAA PEIILGNPVS LTSDTWSVGV LTYVLLSGVS PFLDDSVEET
3010 3020 3030 3040 3050
CLNICRLDFS FPDDYFKGVS QKAKEFVCFL LQEDPAKRPS AALALQEQWL
3060 3070 3080 3090
QAGNGRSTGV LDTSRLTSFI ERRKHQNDVR PIRSIKNFLQ SRLLPRV
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. 18 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.
GeneTreei ENSGT00760000119030.
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

Bgeei O75962.
CleanExi HS_TRIO.
ExpressionAtlasi O75962. baseline and differential.
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.
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. "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 29, 2014
This is version 154 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