(data stored in ACNUC5448 zone)

HOGENOM: HS5_PE229

ID   HS5_PE229                            STANDARD;      PRT;   3097 AA.
AC   HS5_PE229; O75962; D3DTD1; Q13458; Q59EQ7; Q6PJC9; Q6ZN05; Q8IWK8;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Triple functional domain protein; EC=2.7.11 1;AltName:
DE   Full=PTPRF-interacting protein; (HS5.PE229).
GN   Name=TRIO;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS5.PE229.
CC       Homo sapiens chromosome 5 GRCh37  sequence 1..180905260 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:TRIO_HUMAN
CC   -!- FUNCTION: Promotes the exchange of GDP by GTP. Together with
CC       leukocyte antigen-related (LAR) protein, it could play a role in
CC       coordinating cell-matrix and cytoskeletal rearrangements necessary
CC       for cell migration and cell growth.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Interacts to form a complex with leukocyte antigen
CC       related protein.
CC   -!- INTERACTION:
CC       Q9NRI5:DISC1; NbExp=3; IntAct=EBI-718519, EBI-529989;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=O75962-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O75962-2; Sequence=VSP_004467, VSP_004468;
CC         Note=Ref.5 (AAC34245) sequence differs from that shown due to a
CC         frameshift in position 2301;
CC       Name=3;
CC         IsoId=O75962-3; Sequence=VSP_023306, VSP_023307;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=O75962-4; Sequence=VSP_037860;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=O75962-5; Sequence=VSP_037861, VSP_037862;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle,
CC       brain, pancreas, placenta, liver, kidney and lung.
CC   -!- DOMAIN: The N-terminal DBL/GEF domain specifically catalyzes
CC       nucleotide exchange for RAC1, leading to the activation of Jun
CC       kinase and the production of membrane ruffles. The second DBL/GEF
CC       domain is an exchange factor for rhoa and induces the formation of
CC       stress fibers.
CC   -!- PTM: Phosphorylated on serine residue(s).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family.
CC   -!- SIMILARITY: Contains 1 CRAL-TRIO domain.
CC   -!- SIMILARITY: Contains 2 DH (DBL-homology) domains.
CC   -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC       domain.
CC   -!- SIMILARITY: Contains 2 PH domains.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 2 SH3 domains.
CC   -!- SIMILARITY: Contains 4 spectrin repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC34245.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=AAC34245.1; Type=Frameshift; Positions=2301;
CC       Sequence=AAC43042.1; Type=Erroneous initiation;
CC   -!- GENE_FAMILY: HOG000044462 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000038382;ENST00000344204;ENSP00000339299.
DR   EMBL; AB115332; - ;
DR   EMBL; AB209754; - ;
DR   EMBL; AC010419; - ;
DR   EMBL; AC016549; - ;
DR   EMBL; AC016654; - ;
DR   EMBL; AC016656; - ;
DR   EMBL; AC026456; - ;
DR   EMBL; AF091395; - ;
DR   EMBL; AK131423; - ;
DR   EMBL; AK304786; - ;
DR   EMBL; BC017268; - ;
DR   EMBL; BC035585; - ;
DR   EMBL; CH471102; - ;
DR   EMBL; U42390; - ;
DR   UniProtKB/Swiss-Prot; O75962; D3DTD1; Q13458; Q59EQ7; Q6PJC9; Q6ZN05; Q8IWK8; -.
DR   EMBL; AK131423; BAD18570.1; -; mRNA.
DR   EMBL; AC010419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC016549; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC016654; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC016656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC026456; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471102; EAX08047.1; -; Genomic_DNA.
DR   EMBL; CH471102; EAX08048.1; -; Genomic_DNA.
DR   EMBL; BC035585; AAH35585.1; -; mRNA.
DR   EMBL; BC017268; AAH17268.1; -; mRNA.
DR   EMBL; U42390; AAC34245.1; ALT_SEQ; mRNA.
DR   EMBL; AF091395; AAC43042.1; ALT_INIT; mRNA.
DR   EMBL; AB209754; BAD92991.1; -; mRNA.
DR   IPI; IPI00442035; -.
DR   IPI; IPI00479523; -.
DR   IPI; IPI00657953; -.
DR   IPI; IPI00943836; -.
DR   IPI; IPI00943984; -.
DR   RefSeq; NP_009049.2; NM_007118.2.
DR   UniGene; Hs.130031; -.
DR   PDB; 1NTY; X-ray; 1.70 A; A=1284-1594.
DR   PDB; 2NZ8; X-ray; 2.00 A; B=1285-1594.
DR   PDBsum; 1NTY; -.
DR   PDBsum; 2NZ8; -.
DR   ProteinModelPortal; O75962; -.
DR   SMR; O75962; 217-445, 566-714, 754-1007, 1252-1594, 1655-1721, 1960-2291, 2555-2612, 2684-3082.
DR   IntAct; O75962; 3.
DR   MINT; MINT-1397752; -.
DR   STRING; O75962; -.
DR   PhosphoSite; O75962; -.
DR   PRIDE; O75962; -.
DR   Ensembl; ENST00000344204; ENSP00000339299; ENSG00000038382.
DR   GeneID; 7204; -.
DR   KEGG; hsa:7204; -.
DR   UCSC; uc003jff.1; human.
DR   UCSC; uc003jfh.1; human.
DR   CTD; 7204; -.
DR   GeneCards; GC05P014196; -.
DR   HGNC; HGNC:12303; TRIO.
DR   HPA; HPA008157; -.
DR   MIM; 601893; gene.
DR   neXtProt; NX_O75962; -.
DR   PharmGKB; PA36982; -.
DR   eggNOG; prNOG18964; -.
DR   InParanoid; O75962; -.
DR   OMA; RQTHRHA; -.
DR   OrthoDB; EOG4H462T; -.
DR   Reactome; REACT_11044; Signaling by Rho GTPases.
DR   Reactome; REACT_11061; Signalling by NGF.
DR   Reactome; REACT_14797; Signaling by GPCR.
DR   Reactome; REACT_18266; Axon guidance.
DR   NextBio; 28234; -.
DR   ArrayExpress; O75962; -.
DR   Bgee; O75962; -.
DR   CleanEx; HS_TRIO; -.
DR   Genevestigator; O75962; -.
DR   GermOnline; ENSG00000038382; Homo sapiens.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:ProtInc.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; TAS:Reactome.
DR   GO; GO:0006915; P:apoptosis; EXP:Reactome.
DR   GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR   GO; GO:0008624; P:induction of apoptosis by extracellular signals; EXP:Reactome.
DR   GO; GO:0048011; P:nerve growth factor receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome.
DR   GO; GO:0007185; P:transmembrane receptor protein tyrosine phosphatase signaling pathway; TAS:ProtInc.
DR   InterPro; IPR001251; CRAL-bd_TRIO_C.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_kinase_dom.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Gene3D; G3DSA:3.40.525.10; CRAL_bd_TRIO_C; 1.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 2.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00621; RhoGEF; 2.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF00435; Spectrin; 4.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM00325; RhoGEF; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SMART; SM00326; SH3; 2.
DR   SMART; SM00150; SPEC; 6.
DR   SUPFAM; SSF52087; CRAL_TRIO_C; 1.
DR   SUPFAM; SSF48065; DH-domain; 2.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF50044; SH3; 2.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
DR   PROSITE; PS00741; DH_1; FALSE_NEG.
DR   PROSITE; PS50010; DH_2; 2.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   HOGENOMDNA; HS5.PE229; -.
KW   ENSG000000383821755old_1320000031; ENSP000003392997901old_1320000031;
KW   B4E3M5_HUMAN; D3DTD1_HUMAN; D3DTD2_HUMAN; Q7Z2K2_HUMAN; AB115332;
KW   AC010419; AC016549; AC016654; AC016656; AC026456; AF091395; AK131423;
KW   BC017268; BC035585; CH471102; U42390;
KW   3D-structure; Alternative splicing; ATP-binding; Complete proteome;
KW   Cytoplasm; Disulfide bond; Guanine-nucleotide releasing factor;
KW   Immunoglobulin domain; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Polymorphism; Reference proteome; Repeat;
KW   Serine/threonine-protein kinase; SH3 domain; Transferase.
SQ   SEQUENCE   3097 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSGSSGGAAA PAASSGPAAA ASAAGSGCGG GAGEGAEEAA KDLADIAAFF RSGFRKNDEM
     KAMDVLPILK EKVAYLSGGR DKRGGPILTF PARSNHDRIR QEDLRRLISY LACIPSEEVC
     KRGFTVIVDM RGSKWDSIKP LLKILQESFP CCIHVALIIK PDNFWQKQRT NFGSSKFEFE
     TNMVSLEGLT KVVDPSQLTP EFDGCLEYNH EEWIEIRVAF EDYISNATHM LSRLEELQDI
     LAKKELPQDL EGARNMIEEH SQLKKKVIKA PIEDLDLEGQ KLLQRIQSSE SFPKKNSGSG
     NADLQNLLPK VSTMLDRLHS TRQHLHQMWH VRKLKLDQCF QLRLFEQDAE KMFDWITHNK
     GLFLNSYTEI GTSHPHAMEL QTQHNHFAMN CMNVYVNINR IMSVANRLVE SGHYASQQIR
     QIASQLEQEW KAFAAALDER STLLDMSSIF HQKAEKYMSN VDSWCKACGE VDLPSELQDL
     EDAIHHHQGI YEHITLAYSE VSQDGKSLLD KLQRPLTPGS SDSLTASANY SKAVHHVLDV
     IHEVLHHQRQ LENIWQHRKV RLHQRLQLCV FQQDVQQVLD WIENHGEAFL SKHTGVGKSL
     HRARALQKRH EDFEEVAQNT YTNADKLLEA AEQLAQTGEC DPEEIYQAAH QLEDRIQDFV
     RRVEQRKILL DMSVSFHTHV KELWTWLEEL QKELLDDVYA ESVEAVQDLI KRFGQQQQTT
     LQVTVNVIKE GEDLIQQLRD SAISSNKTPH NSSINHIETV LQQLDEAQSQ MEELFQERKI
     KLELFLQLRI FERDAIDIIS DLESWNDELS QQMNDFDTED LTIAEQRLQH HADKALTMNN
     LTFDVIHQGQ DLLQYVNEVQ ASGVELLCDR DVDMATRVQD LLEFLHEKQQ ELDLAAEQHR
     KHLEQCVQLR HLQAEVKQVL GWIRNGESML NAGLITASSL QEAEQLQREH EQFQHAIEKT
     HQSALQVQQK AEAMLQANHY DMDMIRDCAE KVASHWQQLM LKMEDRLKLV NASVAFYKTS
     EQVCSVLESL EQEYKREEDW CGGADKLGPN SETDHVTPMI SKHLEQKEAF LKACTLARRN
     ADVFLKYLHR NSVNMPGMVT HIKAPEQQVK NILNELFQRE NRVLHYWTMR KRRLDQCQQY
     VVFERSAKQA LEWIHDNGEF YLSTHTSTGS SIQHTQELLK EHEEFQITAK QTKERVKLLI
     QLADGFCEKG HAHAAEIKKC VTAVDKRYRD FSLRMEKYRT SLEKALGISS DSNKSSKSLQ
     LDIIPASIPG SEVKLRDAAH ELNEEKRKSA RRKEFIMAEL IQTEKAYVRD LRECMDTYLW
     EMTSGVEEIP PGIVNKELII FGNMQEIYEF HNNIFLKELE KYEQLPEDVG HCFVTWADKF
     QMYVTYCKNK PDSTQLILEH AGSYFDEIQQ RHGLANSISS YLIKPVQRIT KYQLLLKELL
     TCCEEGKGEI KDGLEVMLSV PKRANDAMHL SMLEGFDENI ESQGELILQE SFQVWDPKTL
     IRKGRERHLF LFEMSLVFSK EVKDSSGRSK YLYKSKLFTS ELGVTEHVEG DPCKFALWVG
     RTPTSDNKIV LKASSIENKQ DWIKHIREVI QERTIHLKGA LKEPIHIPKT APATRQKGRR
     DGEDLDSQGD GSSQPDTISI ASRTSQNTLD SDKLSGGCEL TVVIHDFTAC NSNELTIRRG
     QTVEVLERPH DKPDWCLVRT TDRSPAAEGL VPCGSLCIAH SRSSMEMEGI FNHKDSLSVS
     SNDASPPASV ASLQPHMIGA QSSPGPKRPG NTLRKWLTSP VRRLSSGKAD GHVKKLAHKH
     KKSREVRKSA DAGSQKDSDD SAATPQDETV EERGRNEGLS SGTLSKSSSS GMQSCGEEEG
     EEGADAVPLP PPMAIQQHSL LQPDSQDDKA SSRLLVRPTS SETPSAAELV SAIEELVKSK
     MALEDRPSSL LVDQGDSSSP SFNPSDNSLL SSSSPIDEME ERKSSSLKRR HYVLQELVET
     ERDYVRDLGY VVEGYMALMK EDGVPDDMKG KDKIVFGNIH QIYDWHRDFF LGELEKCLED
     PEKLGSLFVK HERRLHMYIA YCQNKPKSEH IVSEYIDTFF EDLKQRLGHR LQLTDLLIKP
     VQRIMKYQLL LKDFLKYSKK ASLDTSELER AVEVMCIVPR RCNDMMNVGR LQGFDGKIVA
     QGKLLLQDTF LVTDQDAGLL PRCRERRIFL FEQIVIFSEP LDKKKGFSMP GFLFKNSIKV
     SCLCLEENVE NDPCKFALTS RTGDVVETFI LHSSSPSVRQ TWIHEINQIL ENQRNFLNAL
     TSPIEYQRNH SGGGGGGGSG GSGGGGGSGG GGAPSGGSGH SGGPSSCGGA PSTSRSRPSR
     IPQPVRHHPP VLVSSAASSQ AEADKMSGTS TPGPSLPPPG AAPEAGPSAP SRRPPGADAE
     GSEREAEPIP KMKVLESPRK GAANASGSSP DAPAKDARAS LGTLPLGKPR AGAASPLNSP
     LSSAVPSLGK EPFPPSSPLQ KGGSFWSSIP ASPASRPGSF TFPGDSDSLQ RQTPRHAAPG
     KDTDRMSTCS SASEQSVQST QSNGSESSSS SNISTMLVTH DYTAVKEDEI NVYQGEVVQI
     LASNQQNMFL VFRAATDQCP AAEGWIPGFV LGHTSAVIVE NPDGTLKKST SWHTALRLRK
     KSEKKDKDGK REGKLENGYR KSREGLSNKV SVKLLNPNYI YDVPPEFVIP LSEVTCETGE
     TVVLRCRVCG RPKASITWKG PEHNTLNNDG HYSISYSDLG EATLKIVGVT TEDDGIYTCI
     AVNDMGSASS SASLRVLGPG MDGIMVTWKD NFDSFYSEVA ELGRGRFSVV KKCDQKGTKR
     AVATKFVNKK LMKRDQVTHE LGILQSLQHP LLVGLLDTFE TPTSYILVLE MADQGRLLDC
     VVRWGSLTEG KIRAHLGEVL EAVRYLHNCR IAHLDLKPEN ILVDESLAKP TIKLADFGDA
     VQLNTTYYIH QLLGNPEFAA PEIILGNPVS LTSDTWSVGV LTYVLLSGVS PFLDDSVEET
     CLNICRLDFS FPDDYFKGVS QKAKEFVCFL LQEDPAKRPS AALALQEQWL QAGNGRSTGV
     LDTSRLTSFI ERRKHQNDVR PIRSIKNFLQ SRLLPRV
//

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