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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 – 28251ATP By similarity
Active sitei2915 – 29151 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi2802 – 28109ATP By similarity

GO - Molecular functioni

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

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. 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.
Mutagenesisi1303 – 13031T → A: 40% decrease in nucleotide exchange activity.
Mutagenesisi1389 – 13891N → A: No change in nucleotide exchange activity.
Mutagenesisi1426 – 14261V → A: 90% decrease in nucleotide exchange activity.
Mutagenesisi1427 – 14271Q → A: 80% decrease in nucleotide exchange activity.
Mutagenesisi1428 – 14281R → A: 80% decrease in nucleotide exchange activity.
Mutagenesisi1430 – 14301T → A: 80% decrease in nucleotide exchange activity.
Mutagenesisi1431 – 14311K → A: Loss of nucleotide exchange activity.
Mutagenesisi1434 – 14341L → A: 40% decrease in nucleotide exchange activity.
Mutagenesisi1437 – 14371K → A: No change in nucleotide exchange activity.
Mutagenesisi1438 – 14381E → A: 30% decrease in nucleotide exchange activity.

Organism-specific databases

PharmGKBiPA36982.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 30973097Triple functional domain protein
PRO_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 ↔ 2759 Reviewed prediction

Post-translational modificationi

Phosphorylated on serine residue(s).

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiO75962.
PaxDbiO75962.
PRIDEiO75962.

PTM databases

PhosphoSiteiO75962.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiO75962.
BgeeiO75962.
CleanExiHS_TRIO.
GenevestigatoriO75962.

Organism-specific databases

HPAiHPA008157.

Interactioni

Subunit structurei

Interacts to form a complex with leukocyte antigen related protein.

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiO75962.

Family & Domainsi

Domains and Repeats

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi715 – 7184Poly-Gln
Compositional biasi1845 – 18506Poly-Ser
Compositional biasi2292 – 231221Poly-Gly
Add
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.
Contains 2 PH domains.
Contains 2 SH3 domains.
Contains 4 spectrin repeats.

Keywords - Domaini

Immunoglobulin domain, Repeat, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000044462.
HOVERGENiHBG108598.
InParanoidiO75962.
KOiK08810.
OMAiIEERGRN.
OrthoDBiEOG7B8S3F.
PhylomeDBiO75962.
TreeFamiTF318080.

Family and domain databases

Gene3Di1.20.900.10. 2 hits.
2.30.29.30. 2 hits.
2.60.40.10. 1 hit.
3.40.525.10. 1 hit.
InterProiIPR001251. CRAL-TRIO_dom.
IPR000219. DH-domain.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR001452. SH3_domain.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
IPR028570. TRIO.
[Graphical view]
PANTHERiPTHR22826:SF104. PTHR22826:SF104. 1 hit.
PfamiPF13716. CRAL_TRIO_2. 1 hit.
PF07679. I-set. 1 hit.
PF00069. Pkinase. 1 hit.
PF00621. RhoGEF. 2 hits.
PF00018. SH3_1. 1 hit.
PF00435. Spectrin. 4 hits.
[Graphical view]
SMARTiSM00408. IGc2. 1 hit.
SM00233. PH. 2 hits.
SM00325. RhoGEF. 2 hits.
SM00220. S_TKc. 1 hit.
SM00516. SEC14. 1 hit.
SM00326. SH3. 2 hits.
SM00150. SPEC. 6 hits.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 2 hits.
SSF50044. SSF50044. 2 hits.
SSF52087. SSF52087. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50191. CRAL_TRIO. 1 hit.
PS50010. DH_2. 2 hits.
PS50835. IG_LIKE. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O75962-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MSGSSGGAAA PAASSGPAAA ASAAGSGCGG GAGEGAEEAA KDLADIAAFF     50
RSGFRKNDEM KAMDVLPILK EKVAYLSGGR DKRGGPILTF PARSNHDRIR 100
QEDLRRLISY LACIPSEEVC KRGFTVIVDM RGSKWDSIKP LLKILQESFP 150
CCIHVALIIK PDNFWQKQRT NFGSSKFEFE TNMVSLEGLT KVVDPSQLTP 200
EFDGCLEYNH EEWIEIRVAF EDYISNATHM LSRLEELQDI LAKKELPQDL 250
EGARNMIEEH SQLKKKVIKA PIEDLDLEGQ KLLQRIQSSE SFPKKNSGSG 300
NADLQNLLPK VSTMLDRLHS TRQHLHQMWH VRKLKLDQCF QLRLFEQDAE 350
KMFDWITHNK GLFLNSYTEI GTSHPHAMEL QTQHNHFAMN CMNVYVNINR 400
IMSVANRLVE SGHYASQQIR QIASQLEQEW KAFAAALDER STLLDMSSIF 450
HQKAEKYMSN VDSWCKACGE VDLPSELQDL EDAIHHHQGI YEHITLAYSE 500
VSQDGKSLLD KLQRPLTPGS SDSLTASANY SKAVHHVLDV IHEVLHHQRQ 550
LENIWQHRKV RLHQRLQLCV FQQDVQQVLD WIENHGEAFL SKHTGVGKSL 600
HRARALQKRH EDFEEVAQNT YTNADKLLEA AEQLAQTGEC DPEEIYQAAH 650
QLEDRIQDFV RRVEQRKILL DMSVSFHTHV KELWTWLEEL QKELLDDVYA 700
ESVEAVQDLI KRFGQQQQTT LQVTVNVIKE GEDLIQQLRD SAISSNKTPH 750
NSSINHIETV LQQLDEAQSQ MEELFQERKI KLELFLQLRI FERDAIDIIS 800
DLESWNDELS QQMNDFDTED LTIAEQRLQH HADKALTMNN LTFDVIHQGQ 850
DLLQYVNEVQ ASGVELLCDR DVDMATRVQD LLEFLHEKQQ ELDLAAEQHR 900
KHLEQCVQLR HLQAEVKQVL GWIRNGESML NAGLITASSL QEAEQLQREH 950
EQFQHAIEKT HQSALQVQQK AEAMLQANHY DMDMIRDCAE KVASHWQQLM 1000
LKMEDRLKLV NASVAFYKTS EQVCSVLESL EQEYKREEDW CGGADKLGPN 1050
SETDHVTPMI SKHLEQKEAF LKACTLARRN ADVFLKYLHR NSVNMPGMVT 1100
HIKAPEQQVK NILNELFQRE NRVLHYWTMR KRRLDQCQQY VVFERSAKQA 1150
LEWIHDNGEF YLSTHTSTGS SIQHTQELLK EHEEFQITAK QTKERVKLLI 1200
QLADGFCEKG HAHAAEIKKC VTAVDKRYRD FSLRMEKYRT SLEKALGISS 1250
DSNKSSKSLQ LDIIPASIPG SEVKLRDAAH ELNEEKRKSA RRKEFIMAEL 1300
IQTEKAYVRD LRECMDTYLW EMTSGVEEIP PGIVNKELII FGNMQEIYEF 1350
HNNIFLKELE KYEQLPEDVG HCFVTWADKF QMYVTYCKNK PDSTQLILEH 1400
AGSYFDEIQQ RHGLANSISS YLIKPVQRIT KYQLLLKELL TCCEEGKGEI 1450
KDGLEVMLSV PKRANDAMHL SMLEGFDENI ESQGELILQE SFQVWDPKTL 1500
IRKGRERHLF LFEMSLVFSK EVKDSSGRSK YLYKSKLFTS ELGVTEHVEG 1550
DPCKFALWVG RTPTSDNKIV LKASSIENKQ DWIKHIREVI QERTIHLKGA 1600
LKEPIHIPKT APATRQKGRR DGEDLDSQGD GSSQPDTISI ASRTSQNTLD 1650
SDKLSGGCEL TVVIHDFTAC NSNELTIRRG QTVEVLERPH DKPDWCLVRT 1700
TDRSPAAEGL VPCGSLCIAH SRSSMEMEGI FNHKDSLSVS SNDASPPASV 1750
ASLQPHMIGA QSSPGPKRPG NTLRKWLTSP VRRLSSGKAD GHVKKLAHKH 1800
KKSREVRKSA DAGSQKDSDD SAATPQDETV EERGRNEGLS SGTLSKSSSS 1850
GMQSCGEEEG EEGADAVPLP PPMAIQQHSL LQPDSQDDKA SSRLLVRPTS 1900
SETPSAAELV SAIEELVKSK MALEDRPSSL LVDQGDSSSP SFNPSDNSLL 1950
SSSSPIDEME ERKSSSLKRR HYVLQELVET ERDYVRDLGY VVEGYMALMK 2000
EDGVPDDMKG KDKIVFGNIH QIYDWHRDFF LGELEKCLED PEKLGSLFVK 2050
HERRLHMYIA YCQNKPKSEH IVSEYIDTFF EDLKQRLGHR LQLTDLLIKP 2100
VQRIMKYQLL LKDFLKYSKK ASLDTSELER AVEVMCIVPR RCNDMMNVGR 2150
LQGFDGKIVA QGKLLLQDTF LVTDQDAGLL PRCRERRIFL FEQIVIFSEP 2200
LDKKKGFSMP GFLFKNSIKV SCLCLEENVE NDPCKFALTS RTGDVVETFI 2250
LHSSSPSVRQ TWIHEINQIL ENQRNFLNAL TSPIEYQRNH SGGGGGGGSG 2300
GSGGGGGSGG GGAPSGGSGH SGGPSSCGGA PSTSRSRPSR IPQPVRHHPP 2350
VLVSSAASSQ AEADKMSGTS TPGPSLPPPG AAPEAGPSAP SRRPPGADAE 2400
GSEREAEPIP KMKVLESPRK GAANASGSSP DAPAKDARAS LGTLPLGKPR 2450
AGAASPLNSP LSSAVPSLGK EPFPPSSPLQ KGGSFWSSIP ASPASRPGSF 2500
TFPGDSDSLQ RQTPRHAAPG KDTDRMSTCS SASEQSVQST QSNGSESSSS 2550
SNISTMLVTH DYTAVKEDEI NVYQGEVVQI LASNQQNMFL VFRAATDQCP 2600
AAEGWIPGFV LGHTSAVIVE NPDGTLKKST SWHTALRLRK KSEKKDKDGK 2650
REGKLENGYR KSREGLSNKV SVKLLNPNYI YDVPPEFVIP LSEVTCETGE 2700
TVVLRCRVCG RPKASITWKG PEHNTLNNDG HYSISYSDLG EATLKIVGVT 2750
TEDDGIYTCI AVNDMGSASS SASLRVLGPG MDGIMVTWKD NFDSFYSEVA 2800
ELGRGRFSVV KKCDQKGTKR AVATKFVNKK LMKRDQVTHE LGILQSLQHP 2850
LLVGLLDTFE TPTSYILVLE MADQGRLLDC VVRWGSLTEG KIRAHLGEVL 2900
EAVRYLHNCR IAHLDLKPEN ILVDESLAKP TIKLADFGDA VQLNTTYYIH 2950
QLLGNPEFAA PEIILGNPVS LTSDTWSVGV LTYVLLSGVS PFLDDSVEET 3000
CLNICRLDFS FPDDYFKGVS QKAKEFVCFL LQEDPAKRPS AALALQEQWL 3050
QAGNGRSTGV LDTSRLTSFI ERRKHQNDVR PIRSIKNFLQ SRLLPRV 3097
Length:3,097
Mass (Da):346,900
Last modified:September 1, 2009 - v2
Checksum:iEA9236DF88B0EA24
GO
Isoform 2 (identifier: O75962-2) [UniParc]FASTAAdd to Basket

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

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

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

Note: No experimental confirmation available.

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

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

Note: No experimental confirmation available.

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

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

Note: No experimental confirmation available.

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

Sequence cautioni

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

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.
VSP_023306Add
BLAST
Alternative sequencei1 – 5959Missing in isoform 4.
VSP_037860Add
BLAST
Alternative sequencei2368 – 23681G → E in isoform 2.
VSP_004467
Alternative sequencei2369 – 2544176Missing in isoform 2.
VSP_004468Add
BLAST
Alternative sequencei2502 – 254443FPGDS…TQSNG → MLPSQAQGLLWWVFPLFPAS SLSYPPVSYRADGLARNTFL KAC in isoform 3.
VSP_023307Add
BLAST
Alternative sequencei2545 – 256319SESSS…THDYT → VSASGGPRPPAPLPLSRQL in isoform 5.
VSP_037861Add
BLAST
Alternative sequencei2564 – 3097534Missing in isoform 5.
VSP_037862Add
BLAST

Sequence conflict

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

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]
ENST00000537187; ENSP00000446348; ENSG00000038382. [O75962-2]
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...

Protein-protein interaction databases

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

PTM databases

PhosphoSitei O75962.

Proteomic databases

MaxQBi O75962.
PaxDbi O75962.
PRIDEi O75962.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000344135 ; ENSP00000339291 ; ENSG00000038382 . [O75962-3 ]
ENST00000344204 ; ENSP00000339299 ; ENSG00000038382 . [O75962-1 ]
ENST00000537187 ; ENSP00000446348 ; ENSG00000038382 . [O75962-2 ]
GeneIDi 7204.
KEGGi hsa:7204.
UCSCi uc003jff.3. human. [O75962-1 ]
uc003jfh.1. human. [O75962-5 ]

Organism-specific databases

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

Phylogenomic databases

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

Enzyme and pathway databases

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

Miscellaneous databases

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

Gene expression databases

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

Family and domain databases

Gene3Di 1.20.900.10. 2 hits.
2.30.29.30. 2 hits.
2.60.40.10. 1 hit.
3.40.525.10. 1 hit.
InterProi IPR001251. CRAL-TRIO_dom.
IPR000219. DH-domain.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR001452. SH3_domain.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
IPR028570. TRIO.
[Graphical view ]
PANTHERi PTHR22826:SF104. PTHR22826:SF104. 1 hit.
Pfami PF13716. CRAL_TRIO_2. 1 hit.
PF07679. I-set. 1 hit.
PF00069. Pkinase. 1 hit.
PF00621. RhoGEF. 2 hits.
PF00018. SH3_1. 1 hit.
PF00435. Spectrin. 4 hits.
[Graphical view ]
SMARTi SM00408. IGc2. 1 hit.
SM00233. PH. 2 hits.
SM00325. RhoGEF. 2 hits.
SM00220. S_TKc. 1 hit.
SM00516. SEC14. 1 hit.
SM00326. SH3. 2 hits.
SM00150. SPEC. 6 hits.
[Graphical view ]
SUPFAMi SSF48065. SSF48065. 2 hits.
SSF50044. SSF50044. 2 hits.
SSF52087. SSF52087. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS50191. CRAL_TRIO. 1 hit.
PS50010. DH_2. 2 hits.
PS50835. IG_LIKE. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« 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: September 3, 2014
This is version 152 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

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