Reviewed, UniProtKB/Swiss-Prot O75962 (TRIO_HUMAN)

Names and origin

Protein names

Recommended name:
    Triple functional domain protein
    EC=2.7.11.1
Alternative name(s):
    PTPRF-interacting protein

Gene names

Name:

TRIO

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	3038 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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). Ref.7 Ref.8 Ref.9
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.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Immunoglobulin domain Repeat SH3 domain
Ligand	ATP-binding Nucleotide-binding
Molecular function	Guanine-nucleotide releasing factor Kinase Serine/threonine-protein kinase Transferase
PTM	Disulfide bond Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro regulation of Rho protein signal transduction Inferred from electronic annotation. Source: InterPro transmembrane receptor protein tyrosine phosphatase signaling pathway Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW Rho guanyl-nucleotide exchange factor activity Inferred from electronic annotation. Source: InterPro protein serine/threonine kinase activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 3 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:
     2309-2309: G → E
     2310-3038: Missing.

Note: Ref.1 (AAC43042) sequence differs from that shown due to a frameshift in position 2241.

Isoform 3 (identifier: O75962-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-2442: Missing.
     2443-2485: FPGDSDSLQR...QSVQSTQSNG → MLPSQAQGLL...LARNTFLKAC

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 3038

3038

Triple functional domain protein

PRO_0000080978

Regions

Domain

6 – 151

146

CRAL-TRIO

Repeat

252 – 359

108

Spectrin 1

Repeat

479 – 585

107

Spectrin 2

Repeat

819 – 925

107

Spectrin 3

Repeat

1050 – 1157

108

Spectrin 4

Domain

1233 – 1408

176

DH 1

Domain

1421 – 1532

112

PH 1

Domain

1597 – 1653

57

SH3 1

Domain

1910 – 2086

177

DH 2

Domain

2098 – 2212

115

PH 2

Domain

2492 – 2557

66

SH3 2

Domain

2626 – 2716

91

Ig-like C2-type

Domain

2737 – 2993

257

Protein kinase

Nucleotide binding

2743 – 2751

9

ATP By similarity

Compositional bias

656 – 659

4

Poly-Gln

Compositional bias

1786 – 1791

6

Poly-Ser

Compositional bias

2233 – 2253

21

Poly-Gly

Compositional bias

2486 – 2492

7

Poly-Ser

Sites

Active site

2856

1

By similarity

Binding site

2766

1

ATP By similarity

Amino acid modifications

Modified residue

1486

1

Phosphothreonine Ref.7

Modified residue

1844

1

Phosphothreonine Ref.8

Modified residue

2223

1

Phosphoserine Ref.9

Modified residue

2396

1

Phosphoserine Ref.9

Modified residue

2408

1

Phosphoserine Ref.9

Disulfide bond

2637 ↔ 2700

Potential

Natural variations

Alternative sequence

1 – 2442

2442

Missing in isoform 3.

VSP_023306

Alternative sequence

2309

1

G → E in isoform 2.

VSP_004467

Alternative sequence

2310 – 3038

729

Missing in isoform 2.

VSP_004468

Alternative sequence

2443 – 2485

43

FPGDS…TQSNG → MLPSQAQGLLWWVFPLFPAS SLSYPPVSYRADGLARNTFL KAC in isoform 3.

VSP_023307

Natural variant

232

1

S → T Ref.12

VAR_041899

Natural variant

1585

1

T → M Ref.12

VAR_041900

Natural variant

1631

1

H → R Ref.12

VAR_041901

Natural variant

1919

1

V → M in a metastatic melanoma sample; somatic mutation. Ref.12

VAR_041902

Natural variant

2183

1

T → M Ref.12

VAR_041903

Experimental info

Mutagenesis

1240

1

E → A: 50% decrease in nucleotide exchange activity.

Mutagenesis

1244

1

T → A: 40% decrease in nucleotide exchange activity.

Mutagenesis

1330

1

N → A: No change in nucleotide exchange activity.

Mutagenesis

1367

1

V → A: 90% decrease in nucleotide exchange activity.

Mutagenesis

1368

1

Q → A: 80% decrease in nucleotide exchange activity.

Mutagenesis

1369

1

R → A: 80% decrease in nucleotide exchange activity.

Mutagenesis

1371

1

T → A: 80% decrease in nucleotide exchange activity.

Mutagenesis

1372

1

K → A: Loss of nucleotide exchange activity.

Mutagenesis

1375

1

L → A: 40% decrease in nucleotide exchange activity.

Mutagenesis

1378

1

K → A: No change in nucleotide exchange activity.

Mutagenesis

1379

1

E → A: 30% decrease in nucleotide exchange activity.

Sequence conflict

491 – 494

4

HVRT → QLEN in AAH35585. Ref.4

Sequence conflict

491 – 494

4

HVRT → QLEN in BAD92991. Ref.5

Sequence conflict

515

1

E → D in AAH35585. Ref.4

Sequence conflict

515

1

E → D in BAD92991. Ref.5

Sequence conflict

728 – 729

2

HV → QL in AAH35585. Ref.4

Sequence conflict

728 – 729

2

HV → QL in BAD92991. Ref.5

Sequence conflict

2486 – 2504

19

SESSS…THDYT → VSASGGPRPPAPLPLSRQL in BAD92991. Ref.5

Secondary structure

1

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3038

Helix Strand Turn

Details...

Helix

1232 – 1257

26

Helix

1259 – 1265

7

Turn

1272 – 1276

5

Helix

1278 – 1282

5

Helix

1285 – 1294

10

Helix

1296 – 1302

7

Turn

1303 – 1305

3

Helix

1307 – 1310

4

Helix

1311 – 1316

6

Turn

1317 – 1321

5

Helix

1322 – 1341

20

Turn

1342 – 1344

3

Helix

1345 – 1353

9

Helix

1359 – 1363

5

Helix

1365 – 1382

18

Helix

1391 – 1411

21

Beta strand

1414 – 1416

3

Helix

1422 – 1424

3

Beta strand

1427 – 1436

10

Beta strand

1438 – 1442

5

Beta strand

1445 – 1464

20

Beta strand

1470 – 1479

10

Helix

1480 – 1482

3

Beta strand

1483 – 1486

4

Beta strand

1495 – 1503

9

Turn

1506 – 1508

3

Beta strand

1510 – 1513

4

Helix

1517 – 1533

17

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 28620F3B513EB74B	FASTA	3,038	341,617
	10 20 30 40 50 60 MKAMDVLPIL KEKVAYLSGG RDKRGGPILT FPARSNHDRI RQEDLRRLIS YLACIPSEEV 70 80 90 100 110 120 CKRGFTVIVD MRGSKWDSIK PLLKILQESF PCCIHVALII KPDNFWQKQR TNFGSSKFEF 130 140 150 160 170 180 ETNMVSLEGL TKVVDPSQLT PEFDGCLEYN HEEWIEIRVA FEDYISNATH MLSRLEELQD 190 200 210 220 230 240 ILAKKELPQD LEGARNMIEE HSQLKKKVIK APIEDLDLEG QKLLQRIQSS ESFPKKNSGS 250 260 270 280 290 300 GNADLQNLLP KVSTMLDRLH STRQHLHQMW HVRKLKLDQC FQLRLFEQDA EKMFDWITHN 310 320 330 340 350 360 KGLFLNSYTE IGTSHPHAME LQTQHNHFAM NCMNVYVNIN RIMSVANRLV ESGHYASQQI 370 380 390 400 410 420 RQIASQLEQE WKAFAAALDE RSTLLDMSSI FHQKAEKYMS NVDSWCKACG EVDLPSELQD 430 440 450 460 470 480 LEDAIHHHQG IYEHITLAYS EVSQDGKSLL DKLQRPLTPG SSDSLTASAN YSKAVHHVLD 490 500 510 520 530 540 VIHEVLHHQR HVRTIWQHRK VRLHQRLQLC VFQQEVQQVL DWIENHGEAF LSKHTGVGKS 550 560 570 580 590 600 LHRARALQKR HEDFEEVAQN TYTNADKLLE AAEQLAQTGE CDPEEIYQAA HQLEDRIQDF 610 620 630 640 650 660 VRRVEQRKIL LDMSVSFHTH VKELWTWLEE LQKELLDDVY AESVEAVQDL IKRFGQQQQT 670 680 690 700 710 720 TLQVTVNVIK EGEDLIQQLR DSAISSNKTP HNSSINHIET VLQQLDEAQS QMEELFQERK 730 740 750 760 770 780 IKLELFLHVR IFERDAIDII SDLESWNDEL SQQMNDFDTE DLTIAEQRLQ HHADKALTMN 790 800 810 820 830 840 NLTFDVIHQG QDLLQYVNEV QASGVELLCD RDVDMATRVQ DLLEFLHEKQ QELDLAAEQH 850 860 870 880 890 900 RKHLEQCVQL RHLQAEVKQV LGWIRNGESM LNAGLITASS LQEAEQLQRE HEQFQHAIEK 910 920 930 940 950 960 THQSALQVQQ KAEAMLQANH YDMDMIRDCA EKVASHWQQL MLKMEDRLKL VNASVAFYKT 970 980 990 1000 1010 1020 SEQVCSVLES LEQEYKREED WCGGADKLGP NSETDHVTPM ISKHLEQKEA FLKACTLARR 1030 1040 1050 1060 1070 1080 NADVFLKYLH RNSVNMPGMV THIKAPEQQV KNILNELFQR ENRVLHYWTM RKRRLDQCQQ 1090 1100 1110 1120 1130 1140 YVVFERSAKQ ALEWIHDNGE FYLSTHTSTG SSIQHTQELL KEHEEFQITA KQTKERVKLL 1150 1160 1170 1180 1190 1200 IQLADGFCEK GHAHAAEIKK CVTAVDKRYR DFSLRMEKYR TSLEKALGIS SDSNKSSKSL 1210 1220 1230 1240 1250 1260 QLDIIPASIP GSEVKLRDAA HELNEEKRKS ARRKEFIMAE LIQTEKAYVR DLRECMDTYL 1270 1280 1290 1300 1310 1320 WEMTSGVEEI PPGIVNKELI IFGNMQEIYE FHNNIFLKEL EKYEQLPEDV GHCFVTWADK 1330 1340 1350 1360 1370 1380 FQMYVTYCKN KPDSTQLILE HAGSYFDEIQ QRHGLANSIS SYLIKPVQRI TKYQLLLKEL 1390 1400 1410 1420 1430 1440 LTCCEEGKGE IKDGLEVMLS VPKRANDAMH LSMLEGFDEN IESQGELILQ ESFQVWDPKT 1450 1460 1470 1480 1490 1500 LIRKGRERHL FLFEMSLVFS KEVKDSSGRS KYLYKSKLFT SELGVTEHVE GDPCKFALWV 1510 1520 1530 1540 1550 1560 GRTPTSDNKI VLKASSIENK QDWIKHIREV IQERTIHLKG ALKEPIHIPK TAPATRQKGR 1570 1580 1590 1600 1610 1620 RDGEDLDSQG DGSSQPDTIS IASRTSQNTL DSDKLSGGCE LTVVIHDFTA CNSNELTIRR 1630 1640 1650 1660 1670 1680 GQTVEVLERP HDKPDWCLVR TTDRSPAAEG LVPCGSLCIA HSRSSMEMEG IFNHKDSLSV 1690 1700 1710 1720 1730 1740 SSNDASPPAS VASLQPHMIG AQSSPGPKRP GNTLRKWLTS PVRRLSSGKA DGHVKKLAHK 1750 1760 1770 1780 1790 1800 HKKSREVRKS ADAGSQKDSD DSAATPQDET VEERGRNEGL SSGTLSKSSS SGMQSCGEEE 1810 1820 1830 1840 1850 1860 GEEGADAVPL PPPMAIQQHS LLQPDSQDDK ASSRLLVRPT SSETPSAAEL VSAIEELVKS 1870 1880 1890 1900 1910 1920 KMALEDRPSS LLVDQGDSSS PSFNPSDNSL LSSSSPIDEM EERKSSSLKR RHYVLQELVE 1930 1940 1950 1960 1970 1980 TERDYVRDLG YVVEGYMALM KEDGVPDDMK GKDKIVFGNI HQIYDWHRDF FLGELEKCLE 1990 2000 2010 2020 2030 2040 DPEKLGSLFV KHERRLHMYI AYCQNKPKSE HIVSEYIDTF FEDLKQRLGH RLQLTDLLIK 2050 2060 2070 2080 2090 2100 PVQRIMKYQL LLKDFLKYSK KASLDTSELE RAVEVMCIVP RRCNDMMNVG RLQGFDGKIV 2110 2120 2130 2140 2150 2160 AQGKLLLQDT FLVTDQDAGL LPRCRERRIF LFEQIVIFSE PLDKKKGFSM PGFLFKNSIK 2170 2180 2190 2200 2210 2220 VSCLCLEENV ENDPCKFALT SRTGDVVETF ILHSSSPSVR QTWIHEINQI LENQRNFLNA 2230 2240 2250 2260 2270 2280 LTSPIEYQRN HSGGGGGGGS GGSGGGGGSG GGGAPSGGSG HSGGPSSCGG APSTSRSRPS 2290 2300 2310 2320 2330 2340 RIPQPVRHHP PVLVSSAASS QAEADKMSGT STPGPSLPPP GAAPEAGPSA PSRRPPGADA 2350 2360 2370 2380 2390 2400 EGSEREAEPI PKMKVLESPR KGAANASGSS PDAPAKDARA SLGTLPLGKP RAGAASPLNS 2410 2420 2430 2440 2450 2460 PLSSAVPSLG KEPFPPSSPL QKGGSFWSSI PASPASRPGS FTFPGDSDSL QRQTPRHAAP 2470 2480 2490 2500 2510 2520 GKDTDRMSTC SSASEQSVQS TQSNGSESSS SSNISTMLVT HDYTAVKEDE INVYQGEVVQ 2530 2540 2550 2560 2570 2580 ILASNQQNMF LVFRAATDQC PAAEGWIPGF VLGHTSAVIV ENPDGTLKKS TSWHTALRLR 2590 2600 2610 2620 2630 2640 KKSEKKDKDG KREGKLENGY RKSREGLSNK VSVKLLNPNY IYDVPPEFVI PLSEVTCETG 2650 2660 2670 2680 2690 2700 ETVVLRCRVC GRPKASITWK GPEHNTLNND GHYSISYSDL GEATLKIVGV TTEDDGIYTC 2710 2720 2730 2740 2750 2760 IAVNDMGSAS SSASLRVLGP GMDGIMVTWK DNFDSFYSEV AELGRGRFSV VKKCDQKGTK 2770 2780 2790 2800 2810 2820 RAVATKFVNK KLMKRDQVTH ELGILQSLQH PLLVGLLDTF ETPTSYILVL EMADQGRLLD 2830 2840 2850 2860 2870 2880 CVVRWGSLTE GKIRAHLGEV LEAVRYLHNC RIAHLDLKPE NILVDESLAK PTIKLADFGD 2890 2900 2910 2920 2930 2940 AVQLNTTYYI HQLLGNPEFA APEIILGNPV SLTSDTWSVG VLTYVLLSGV SPFLDDSVEE 2950 2960 2970 2980 2990 3000 TCLNICRLDF SFPDDYFKGV SQKAKEFVCF LLQEDPAKRP SAALALQEQW LQAGNGRSTG 3010 3020 3030 VLDTSRLTSF IERRKHQNDV RPIRSIKNFL QSRLLPRV
	Isoform 2. Checksum: A6ED6C8C95A50AD2	FASTA	2,309	262,700
	10 20 30 40 50 60 MKAMDVLPIL KEKVAYLSGG RDKRGGPILT FPARSNHDRI RQEDLRRLIS YLACIPSEEV 70 80 90 100 110 120 CKRGFTVIVD MRGSKWDSIK PLLKILQESF PCCIHVALII KPDNFWQKQR TNFGSSKFEF 130 140 150 160 170 180 ETNMVSLEGL TKVVDPSQLT PEFDGCLEYN HEEWIEIRVA FEDYISNATH MLSRLEELQD 190 200 210 220 230 240 ILAKKELPQD LEGARNMIEE HSQLKKKVIK APIEDLDLEG QKLLQRIQSS ESFPKKNSGS 250 260 270 280 290 300 GNADLQNLLP KVSTMLDRLH STRQHLHQMW HVRKLKLDQC FQLRLFEQDA EKMFDWITHN 310 320 330 340 350 360 KGLFLNSYTE IGTSHPHAME LQTQHNHFAM NCMNVYVNIN RIMSVANRLV ESGHYASQQI 370 380 390 400 410 420 RQIASQLEQE WKAFAAALDE RSTLLDMSSI FHQKAEKYMS NVDSWCKACG EVDLPSELQD 430 440 450 460 470 480 LEDAIHHHQG IYEHITLAYS EVSQDGKSLL DKLQRPLTPG SSDSLTASAN YSKAVHHVLD 490 500 510 520 530 540 VIHEVLHHQR HVRTIWQHRK VRLHQRLQLC VFQQEVQQVL DWIENHGEAF LSKHTGVGKS 550 560 570 580 590 600 LHRARALQKR HEDFEEVAQN TYTNADKLLE AAEQLAQTGE CDPEEIYQAA HQLEDRIQDF 610 620 630 640 650 660 VRRVEQRKIL LDMSVSFHTH VKELWTWLEE LQKELLDDVY AESVEAVQDL IKRFGQQQQT 670 680 690 700 710 720 TLQVTVNVIK EGEDLIQQLR DSAISSNKTP HNSSINHIET VLQQLDEAQS QMEELFQERK 730 740 750 760 770 780 IKLELFLHVR IFERDAIDII SDLESWNDEL SQQMNDFDTE DLTIAEQRLQ HHADKALTMN 790 800 810 820 830 840 NLTFDVIHQG QDLLQYVNEV QASGVELLCD RDVDMATRVQ DLLEFLHEKQ QELDLAAEQH 850 860 870 880 890 900 RKHLEQCVQL RHLQAEVKQV LGWIRNGESM LNAGLITASS LQEAEQLQRE HEQFQHAIEK 910 920 930 940 950 960 THQSALQVQQ KAEAMLQANH YDMDMIRDCA EKVASHWQQL MLKMEDRLKL VNASVAFYKT 970 980 990 1000 1010 1020 SEQVCSVLES LEQEYKREED WCGGADKLGP NSETDHVTPM ISKHLEQKEA FLKACTLARR 1030 1040 1050 1060 1070 1080 NADVFLKYLH RNSVNMPGMV THIKAPEQQV KNILNELFQR ENRVLHYWTM RKRRLDQCQQ 1090 1100 1110 1120 1130 1140 YVVFERSAKQ ALEWIHDNGE FYLSTHTSTG SSIQHTQELL KEHEEFQITA KQTKERVKLL 1150 1160 1170 1180 1190 1200 IQLADGFCEK GHAHAAEIKK CVTAVDKRYR DFSLRMEKYR TSLEKALGIS SDSNKSSKSL 1210 1220 1230 1240 1250 1260 QLDIIPASIP GSEVKLRDAA HELNEEKRKS ARRKEFIMAE LIQTEKAYVR DLRECMDTYL 1270 1280 1290 1300 1310 1320 WEMTSGVEEI PPGIVNKELI IFGNMQEIYE FHNNIFLKEL EKYEQLPEDV GHCFVTWADK 1330 1340 1350 1360 1370 1380 FQMYVTYCKN KPDSTQLILE HAGSYFDEIQ QRHGLANSIS SYLIKPVQRI TKYQLLLKEL 1390 1400 1410 1420 1430 1440 LTCCEEGKGE IKDGLEVMLS VPKRANDAMH LSMLEGFDEN IESQGELILQ ESFQVWDPKT 1450 1460 1470 1480 1490 1500 LIRKGRERHL FLFEMSLVFS KEVKDSSGRS KYLYKSKLFT SELGVTEHVE GDPCKFALWV 1510 1520 1530 1540 1550 1560 GRTPTSDNKI VLKASSIENK QDWIKHIREV IQERTIHLKG ALKEPIHIPK TAPATRQKGR 1570 1580 1590 1600 1610 1620 RDGEDLDSQG DGSSQPDTIS IASRTSQNTL DSDKLSGGCE LTVVIHDFTA CNSNELTIRR 1630 1640 1650 1660 1670 1680 GQTVEVLERP HDKPDWCLVR TTDRSPAAEG LVPCGSLCIA HSRSSMEMEG IFNHKDSLSV 1690 1700 1710 1720 1730 1740 SSNDASPPAS VASLQPHMIG AQSSPGPKRP GNTLRKWLTS PVRRLSSGKA DGHVKKLAHK 1750 1760 1770 1780 1790 1800 HKKSREVRKS ADAGSQKDSD DSAATPQDET VEERGRNEGL SSGTLSKSSS SGMQSCGEEE 1810 1820 1830 1840 1850 1860 GEEGADAVPL PPPMAIQQHS LLQPDSQDDK ASSRLLVRPT SSETPSAAEL VSAIEELVKS 1870 1880 1890 1900 1910 1920 KMALEDRPSS LLVDQGDSSS PSFNPSDNSL LSSSSPIDEM EERKSSSLKR RHYVLQELVE 1930 1940 1950 1960 1970 1980 TERDYVRDLG YVVEGYMALM KEDGVPDDMK GKDKIVFGNI HQIYDWHRDF FLGELEKCLE 1990 2000 2010 2020 2030 2040 DPEKLGSLFV KHERRLHMYI AYCQNKPKSE HIVSEYIDTF FEDLKQRLGH RLQLTDLLIK 2050 2060 2070 2080 2090 2100 PVQRIMKYQL LLKDFLKYSK KASLDTSELE RAVEVMCIVP RRCNDMMNVG RLQGFDGKIV 2110 2120 2130 2140 2150 2160 AQGKLLLQDT FLVTDQDAGL LPRCRERRIF LFEQIVIFSE PLDKKKGFSM PGFLFKNSIK 2170 2180 2190 2200 2210 2220 VSCLCLEENV ENDPCKFALT SRTGDVVETF ILHSSSPSVR QTWIHEINQI LENQRNFLNA 2230 2240 2250 2260 2270 2280 LTSPIEYQRN HSGGGGGGGS GGSGGGGGSG GGGAPSGGSG HSGGPSSCGG APSTSRSRPS 2290 2300 RIPQPVRHHP PVLVSSAASS QAEADKMSE
	Isoform 3. Checksum: F6DA7D25AE9E7F0C	FASTA	596	66,206
	10 20 30 40 50 60 MLPSQAQGLL WWVFPLFPAS SLSYPPVSYR ADGLARNTFL KACSESSSSS NISTMLVTHD 70 80 90 100 110 120 YTAVKEDEIN VYQGEVVQIL ASNQQNMFLV FRAATDQCPA AEGWIPGFVL GHTSAVIVEN 130 140 150 160 170 180 PDGTLKKSTS WHTALRLRKK SEKKDKDGKR EGKLENGYRK SREGLSNKVS VKLLNPNYIY 190 200 210 220 230 240 DVPPEFVIPL SEVTCETGET VVLRCRVCGR PKASITWKGP EHNTLNNDGH YSISYSDLGE 250 260 270 280 290 300 ATLKIVGVTT EDDGIYTCIA VNDMGSASSS ASLRVLGPGM DGIMVTWKDN FDSFYSEVAE 310 320 330 340 350 360 LGRGRFSVVK KCDQKGTKRA VATKFVNKKL MKRDQVTHEL GILQSLQHPL LVGLLDTFET 370 380 390 400 410 420 PTSYILVLEM ADQGRLLDCV VRWGSLTEGK IRAHLGEVLE AVRYLHNCRI AHLDLKPENI 430 440 450 460 470 480 LVDESLAKPT IKLADFGDAV QLNTTYYIHQ LLGNPEFAAP EIILGNPVSL TSDTWSVGVL 490 500 510 520 530 540 TYVLLSGVSP FLDDSVEETC LNICRLDFSF PDDYFKGVSQ KAKEFVCFLL QEDPAKRPSA 550 560 570 580 590 ALALQEQWLQ AGNGRSTGVL DTSRLTSFIE RRKHQNDVRP IRSIKNFLQS RLLPRV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 8643598] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Fibroblast.
[2]	Streuli M. Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Brain.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1627 AND 2656-3038. Tissue: Kidney and Lymph.
[5]	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 303-2573 (ISOFORM 1). Tissue: Brain.
[6]	"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: 10341202] [Abstract] Cited for: CHARACTERIZATION.
[7]	"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry." Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R. Nat. Methods 2:591-598(2005) [PubMed: 16094384] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1486, MASS SPECTROMETRY. Tissue: T-cell.
[8]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1844, MASS SPECTROMETRY. Tissue: Epithelium.
[9]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2223; SER-2396 AND SER-2408, MASS SPECTROMETRY.
[10]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[11]	"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: 9790533] [Abstract] Cited for: STRUCTURE BY NMR OF 1227-1407, MUTAGENESIS.
[12]	"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: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] THR-232; MET-1585; ARG-1631; MET-1919 AND MET-2183.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF091395 mRNA. Translation: AAC43042.1.
U42390 mRNA. Translation: AAC34245.1. Frameshift.
AK131423 mRNA. Translation: BAD18570.1.
BC017268 mRNA. Translation: AAH17268.1.
BC035585 mRNA. Translation: AAH35585.1.
AB209754 mRNA. Translation: BAD92991.1.

IPI

IPI00442035.
IPI00479523.
IPI00657953.

RefSeq

NP_009049.2.

UniGene

Hs.130031

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NTY	X-ray	1.70	A	1225-1535	[»]
2NZ8	X-ray	2.00	B	1226-1535	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

O75962. 4 interactions.

PTM databases

PhosphoSite

O75962.

Proteomic databases

PRIDE

O75962.

Genome annotation databases

Ensembl

ENSG00000038382. Homo sapiens. [Contig view]

GeneID

7204.

KEGG

hsa:7204.

Organism-specific databases

GeneCards

GC05P014196.

H-InvDB

HIX0004754.

HGNC

HGNC:12303. TRIO.

HPA

HPA008157.

MIM

601893. gene.

PharmGKB

PA36982.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

O75962.

HOVERGEN

O75962.

Enzyme and pathway databases

BRENDA

2.7.11.1. 247.

Reactome

REACT_11044. Signaling by Rho GTPases.

Gene expression databases

ArrayExpress

O75962.

Bgee

O75962.

CleanEx

HS_TRIO.

GermOnline

ENSG00000038382. Homo sapiens.

Family and domain databases

InterPro

IPR001251. CRAL_bd_TRIO_C.
IPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR011993. PH_type.
IPR001849. Pleckstrin_homology.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
IPR001452. SH3_domain.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view]

Gene3D

G3DSA:3.40.525.10. CRAL_bd_TRIO_C. 1 hit.
G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
G3DSA:2.30.29.30. PH_type. 2 hits.
G3DSA:1.20.900.10. RhoGEF. 2 hits.

Pfam

PF07679. I-set. 1 hit.
PF00169. PH. 2 hits.
PF00069. Pkinase. 1 hit.
PF00621. RhoGEF. 2 hits.
PF00018. SH3_1. 1 hit.
PF00435. Spectrin. 6 hits.
[Graphical view]

ProDom

PD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

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]

PROSITE

PS50191. CRAL_TRIO. 1 hit.
PS00741. DH_1. False negative.
PS50010. DH_2. 2 hits.
PS50835. IG_LIKE. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
PS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

28234.

SOURCE

Search...

Entry information

Entry name

TRIO_HUMAN

Accession

Primary (citable) accession number: O75962
Secondary accession number(s): Q13458 , Q59EQ7, Q6PJC9, Q6ZN05, Q8IWK8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1998
Last modified:	June 16, 2009
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)