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Protein

Triple functional domain protein

Gene

TRIO

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei2825ATPPROSITE-ProRule annotation1
Active sitei2915By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi2802 – 2810ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

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

BioCyciZFISH:HS00534-MONOMER.
ReactomeiR-HSA-193648. NRAGE signals death through JNK.
R-HSA-194840. Rho GTPase cycle.
R-HSA-416476. G alpha (q) signalling events.
R-HSA-416482. G alpha (12/13) signalling events.
R-HSA-418885. DCC mediated attractive signaling.
SignaLinkiO75962.
SIGNORiO75962.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:12303. TRIO.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1299E → A: 50% decrease in nucleotide exchange activity. 1 Publication1
Mutagenesisi1303T → A: 40% decrease in nucleotide exchange activity. 1 Publication1
Mutagenesisi1389N → A: No change in nucleotide exchange activity. 1 Publication1
Mutagenesisi1426V → A: 90% decrease in nucleotide exchange activity. 1 Publication1
Mutagenesisi1427Q → A: 80% decrease in nucleotide exchange activity. 1 Publication1
Mutagenesisi1428R → A: 80% decrease in nucleotide exchange activity. 1 Publication1
Mutagenesisi1430T → A: 80% decrease in nucleotide exchange activity. 1 Publication1
Mutagenesisi1431K → A: Loss of nucleotide exchange activity. 1 Publication1
Mutagenesisi1434L → A: 40% decrease in nucleotide exchange activity. 1 Publication1
Mutagenesisi1437K → A: No change in nucleotide exchange activity. 1 Publication1
Mutagenesisi1438E → A: 30% decrease in nucleotide exchange activity. 1 Publication1

Organism-specific databases

DisGeNETi7204.
OpenTargetsiENSG00000038382.
PharmGKBiPA36982.

Polymorphism and mutation databases

BioMutaiTRIO.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000809781 – 3097Triple functional domain proteinAdd BLAST3097

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1627PhosphoserineBy similarity1
Modified residuei2282PhosphoserineCombined sources1
Modified residuei2455PhosphoserineCombined sources1
Modified residuei2459PhosphoserineCombined sources1
Modified residuei2631PhosphoserineCombined sources1
Disulfide bondi2696 ↔ 2759PROSITE-ProRule annotation

Post-translational modificationi

Phosphorylated on serine residue(s).

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

EPDiO75962.
MaxQBiO75962.
PaxDbiO75962.
PeptideAtlasiO75962.
PRIDEiO75962.

PTM databases

iPTMnetiO75962.
PhosphoSitePlusiO75962.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000038382.
CleanExiHS_TRIO.
ExpressionAtlasiO75962. baseline and differential.
GenevisibleiO75962. HS.

Organism-specific databases

HPAiHPA008157.
HPA064664.

Interactioni

Subunit structurei

Interacts with CARMIL1 (PubMed:19846667). Interacts to form a complex with leukocyte antigen related protein.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi113055. 28 interactors.
DIPiDIP-37578N.
IntActiO75962. 12 interactors.
MINTiMINT-1397752.
STRINGi9606.ENSP00000339299.

Structurei

Secondary structure

13097
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1291 – 1316Combined sources26
Helixi1318 – 1324Combined sources7
Turni1331 – 1335Combined sources5
Helixi1337 – 1341Combined sources5
Helixi1344 – 1353Combined sources10
Helixi1355 – 1361Combined sources7
Turni1362 – 1364Combined sources3
Helixi1366 – 1369Combined sources4
Helixi1370 – 1375Combined sources6
Turni1376 – 1380Combined sources5
Helixi1381 – 1400Combined sources20
Turni1401 – 1403Combined sources3
Helixi1404 – 1412Combined sources9
Helixi1418 – 1422Combined sources5
Helixi1424 – 1441Combined sources18
Helixi1450 – 1470Combined sources21
Beta strandi1473 – 1475Combined sources3
Helixi1481 – 1483Combined sources3
Beta strandi1486 – 1495Combined sources10
Beta strandi1497 – 1501Combined sources5
Beta strandi1504 – 1523Combined sources20
Beta strandi1529 – 1538Combined sources10
Helixi1539 – 1541Combined sources3
Beta strandi1542 – 1545Combined sources4
Beta strandi1549 – 1552Combined sources4
Beta strandi1554 – 1562Combined sources9
Turni1565 – 1567Combined sources3
Beta strandi1569 – 1572Combined sources4
Helixi1576 – 1592Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NTYX-ray1.70A1284-1594[»]
2NZ8X-ray2.00B1285-1594[»]
ProteinModelPortaliO75962.
SMRiO75962.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75962.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini65 – 210CRAL-TRIOPROSITE-ProRule annotationAdd BLAST146
Repeati311 – 418Spectrin 1Add BLAST108
Repeati538 – 644Spectrin 2Add BLAST107
Repeati878 – 984Spectrin 3Add BLAST107
Repeati1109 – 1216Spectrin 4Add BLAST108
Domaini1292 – 1467DH 1PROSITE-ProRule annotationAdd BLAST176
Domaini1480 – 1591PH 1PROSITE-ProRule annotationAdd BLAST112
Domaini1656 – 1712SH3 1PROSITE-ProRule annotationAdd BLAST57
Domaini1969 – 2145DH 2PROSITE-ProRule annotationAdd BLAST177
Domaini2157 – 2271PH 2PROSITE-ProRule annotationAdd BLAST115
Domaini2551 – 2616SH3 2PROSITE-ProRule annotationAdd BLAST66
Domaini2685 – 2775Ig-like C2-typeAdd BLAST91
Domaini2796 – 3052Protein kinasePROSITE-ProRule annotationAdd BLAST257

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi715 – 718Poly-Gln4
Compositional biasi1845 – 1850Poly-Ser6
Compositional biasi2292 – 2312Poly-GlyAdd BLAST21
Compositional biasi2545 – 2551Poly-Ser7

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

eggNOGiKOG0032. Eukaryota.
KOG4240. Eukaryota.
ENOG410XPCA. LUCA.
GeneTreeiENSGT00760000119030.
HOGENOMiHOG000044462.
HOVERGENiHBG108598.
InParanoidiO75962.
KOiK08810.
OMAiAEPIPKM.
OrthoDBiEOG091G00JY.
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.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR001452. SH3_domain.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
IPR028570. TRIO.
[Graphical view]
PANTHERiPTHR22826:SF104. PTHR22826:SF104. 2 hits.
PfamiPF00650. CRAL_TRIO. 1 hit.
PF07679. I-set. 1 hit.
PF00169. PH. 2 hits.
PF00069. Pkinase. 1 hit.
PF00621. RhoGEF. 2 hits.
PF00018. SH3_1. 1 hit.
PF00435. Spectrin. 4 hits.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
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]
SUPFAMiSSF48065. SSF48065. 2 hits.
SSF48726. SSF48726. 1 hit.
SSF50044. SSF50044. 2 hits.
SSF50729. SSF50729. 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. AlignAdd to basket

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti550 – 553QLEN → HVRT in AAC34245 (PubMed:8643598).Curated4
Sequence conflicti550 – 553QLEN → HVRT in AAC43042 (Ref. 6) Curated4
Sequence conflicti574D → E in AAC34245 (PubMed:8643598).Curated1
Sequence conflicti574D → E in AAC43042 (Ref. 6) Curated1
Sequence conflicti787 – 788QL → HV in AAC34245 (PubMed:8643598).Curated2
Sequence conflicti787 – 788QL → HV in AAC43042 (Ref. 6) Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_041899291S → T.1 PublicationCorresponds to variant rs55772118dbSNPEnsembl.1
Natural variantiVAR_059802348D → E.Corresponds to variant rs16903367dbSNPEnsembl.1
Natural variantiVAR_0693711368D → V.1 Publication1
Natural variantiVAR_0598031613A → T.Corresponds to variant rs16903474dbSNPEnsembl.1
Natural variantiVAR_0419001644T → M.1 PublicationCorresponds to variant rs55687522dbSNPEnsembl.1
Natural variantiVAR_0419011690H → R.1 PublicationCorresponds to variant rs56292586dbSNPEnsembl.1
Natural variantiVAR_0419021978V → M in a metastatic melanoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_0419032242T → M.1 PublicationCorresponds to variant rs55916212dbSNPEnsembl.1
Natural variantiVAR_0693722563T → M.1 PublicationCorresponds to variant rs751663099dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0233061 – 2501Missing in isoform 3. 1 PublicationAdd BLAST2501
Alternative sequenceiVSP_0378601 – 59Missing in isoform 4. 1 PublicationAdd BLAST59
Alternative sequenceiVSP_0044672368G → E in isoform 2. 1 Publication1
Alternative sequenceiVSP_0044682369 – 2544Missing in isoform 2. 1 PublicationAdd BLAST176
Alternative sequenceiVSP_0233072502 – 2544FPGDS…TQSNG → MLPSQAQGLLWWVFPLFPAS SLSYPPVSYRADGLARNTFL KAC in isoform 3. 1 PublicationAdd BLAST43
Alternative sequenceiVSP_0378612545 – 2563SESSS…THDYT → VSASGGPRPPAPLPLSRQL in isoform 5. 1 PublicationAdd BLAST19
Alternative sequenceiVSP_0378622564 – 3097Missing in isoform 5. 1 PublicationAdd BLAST534

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_007118.3. [O75962-1]
XP_011512412.1. XM_011514110.2. [O75962-4]
UniGeneiHs.130031.

Genome annotation databases

EnsembliENST00000344135; ENSP00000339291; ENSG00000038382. [O75962-3]
ENST00000344204; ENSP00000339299; ENSG00000038382. [O75962-1]
GeneIDi7204.
KEGGihsa:7204.
UCSCiuc003jff.4. human. [O75962-1]

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:
EMBLi
GenBanki
DDBJi
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_007118.3. [O75962-1]
XP_011512412.1. XM_011514110.2. [O75962-4]
UniGeneiHs.130031.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NTYX-ray1.70A1284-1594[»]
2NZ8X-ray2.00B1285-1594[»]
ProteinModelPortaliO75962.
SMRiO75962.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113055. 28 interactors.
DIPiDIP-37578N.
IntActiO75962. 12 interactors.
MINTiMINT-1397752.
STRINGi9606.ENSP00000339299.

PTM databases

iPTMnetiO75962.
PhosphoSitePlusiO75962.

Polymorphism and mutation databases

BioMutaiTRIO.

Proteomic databases

EPDiO75962.
MaxQBiO75962.
PaxDbiO75962.
PeptideAtlasiO75962.
PRIDEiO75962.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000344135; ENSP00000339291; ENSG00000038382. [O75962-3]
ENST00000344204; ENSP00000339299; ENSG00000038382. [O75962-1]
GeneIDi7204.
KEGGihsa:7204.
UCSCiuc003jff.4. human. [O75962-1]

Organism-specific databases

CTDi7204.
DisGeNETi7204.
GeneCardsiTRIO.
HGNCiHGNC:12303. TRIO.
HPAiHPA008157.
HPA064664.
MIMi601893. gene.
neXtProtiNX_O75962.
OpenTargetsiENSG00000038382.
PharmGKBiPA36982.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0032. Eukaryota.
KOG4240. Eukaryota.
ENOG410XPCA. LUCA.
GeneTreeiENSGT00760000119030.
HOGENOMiHOG000044462.
HOVERGENiHBG108598.
InParanoidiO75962.
KOiK08810.
OMAiAEPIPKM.
OrthoDBiEOG091G00JY.
PhylomeDBiO75962.
TreeFamiTF318080.

Enzyme and pathway databases

BioCyciZFISH:HS00534-MONOMER.
ReactomeiR-HSA-193648. NRAGE signals death through JNK.
R-HSA-194840. Rho GTPase cycle.
R-HSA-416476. G alpha (q) signalling events.
R-HSA-416482. G alpha (12/13) signalling events.
R-HSA-418885. DCC mediated attractive signaling.
SignaLinkiO75962.
SIGNORiO75962.

Miscellaneous databases

ChiTaRSiTRIO. human.
EvolutionaryTraceiO75962.
GeneWikiiTRIO_(gene).
GenomeRNAii7204.
PROiO75962.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000038382.
CleanExiHS_TRIO.
ExpressionAtlasiO75962. baseline and differential.
GenevisibleiO75962. HS.

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.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR001452. SH3_domain.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
IPR028570. TRIO.
[Graphical view]
PANTHERiPTHR22826:SF104. PTHR22826:SF104. 2 hits.
PfamiPF00650. CRAL_TRIO. 1 hit.
PF07679. I-set. 1 hit.
PF00169. PH. 2 hits.
PF00069. Pkinase. 1 hit.
PF00621. RhoGEF. 2 hits.
PF00018. SH3_1. 1 hit.
PF00435. Spectrin. 4 hits.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
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]
SUPFAMiSSF48065. SSF48065. 2 hits.
SSF48726. SSF48726. 1 hit.
SSF50044. SSF50044. 2 hits.
SSF50729. SSF50729. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 177 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.