MCF2_HUMAN
ID MCF2_HUMAN Reviewed; 925 AA.
AC P10911; B7Z3Y5; B7Z869; B7ZAV1; E9PH77; F5H091; P14919; Q5JYJ2; Q5JYJ3;
AC Q5JYJ4; Q8IUF3; Q8IUF4; Q9UJB3;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 3.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=Proto-oncogene DBL;
DE AltName: Full=Proto-oncogene MCF-2;
DE Contains:
DE RecName: Full=MCF2-transforming protein;
DE Contains:
DE RecName: Full=DBL-transforming protein;
GN Name=MCF2; Synonyms=DBL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=3056717; DOI=10.1002/j.1460-2075.1988.tb03093.x;
RA Ron D., Tronick S.R., Aaronson S.A., Eva A.;
RT "Molecular cloning and characterization of the human dbl proto-oncogene:
RT evidence that its overexpression is sufficient to transform NIH/3T3
RT cells.";
RL EMBO J. 7:2465-2473(1988).
RN [2]
RP SEQUENCE REVISION.
RA Ron D.;
RL Submitted (JUN-1989) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), TISSUE SPECIFICITY, AND
RP CHARACTERIZATION.
RX PubMed=12445822; DOI=10.1016/s0006-291x(02)02645-1;
RA Komai K., Okayama R., Kitagawa M., Yagi H., Chihara K., Shiozawa S.;
RT "Alternative splicing variants of the human DBL (MCF-2) proto-oncogene.";
RL Biochem. Biophys. Res. Commun. 299:455-458(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Rhodes S., Huckle E.;
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6).
RC TISSUE=Testis, and Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 498-925 (ISOFORM 1).
RX PubMed=3281159; DOI=10.1073/pnas.85.7.2061;
RA Eva A., Vecchio G., Rao C.D., Tronick S.R., Aaronson S.A.;
RT "The predicted DBL oncogene product defines a distinct class of
RT transforming proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:2061-2065(1988).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 398-925 (ISOFORM 1).
RX PubMed=2577874;
RA Noguchi T., Galland F., Batoz M., Mattei M.-G., Birnbaum D.;
RT "Activation of a mcf.2 oncogene by deletion of amino-terminal coding
RT sequences.";
RL Oncogene 3:709-715(1988).
RN [10]
RP DOMAIN DBL-HOMOLOGY, AND MUTAGENESIS.
RX PubMed=2065022;
RA Ron D., Zannini M., Lewis M., Wickner R.B., Hunt L.T., Graziani G.,
RA Tronick S.R., Aaronson S.A., Eva A.;
RT "A region of proto-dbl essential for its transforming activity shows
RT sequence similarity to a yeast cell cycle gene, CDC24, and the human
RT breakpoint cluster gene, bcr.";
RL New Biol. 3:372-379(1991).
RN [11]
RP CHARACTERIZATION OF DBL DOMAIN.
RX PubMed=8276860; DOI=10.1016/s0021-9258(17)42313-1;
RA Hart M.J., Eva A., Zangrilli D., Aaronson S.A., Evans T., Cerione R.A.,
RA Zheng Y.;
RT "Cellular transformation and guanine nucleotide exchange activity are
RT catalyzed by a common domain on the dbl oncogene product.";
RL J. Biol. Chem. 269:62-65(1994).
RN [12]
RP PHOSPHORYLATION BY TNK2.
RX PubMed=10652228; DOI=10.1006/bbrc.2000.2106;
RA Kato J., Kaziro Y., Satoh T.;
RT "Activation of the guanine nucleotide exchange factor Dbl following ACK1-
RT dependent tyrosine phosphorylation.";
RL Biochem. Biophys. Res. Commun. 268:141-147(2000).
RN [13]
RP SUBCELLULAR LOCATION, DOMAIN CRAL-TRIO, AND INTERACTION WITH INOSITOL
RP PHOSPHOLIPIDS.
RX PubMed=15157669; DOI=10.1016/j.cellsig.2004.01.007;
RA Ueda S., Kataoka T., Satoh T.;
RT "Role of the Sec14-like domain of Dbl family exchange factors in the
RT regulation of Rho family GTPases in different subcellular sites.";
RL Cell. Signal. 16:899-906(2004).
RN [14]
RP POSSIBLE INTERACTION WITH CCPG1.
RX PubMed=17000758; DOI=10.1128/mcb.00670-06;
RA Kostenko E.V., Olabisi O.O., Sahay S., Rodriguez P.L., Whitehead I.P.;
RT "Ccpg1, a novel scaffold protein that regulates the activity of the Rho
RT guanine nucleotide exchange factor Dbs.";
RL Mol. Cell. Biol. 26:8964-8975(2006).
CC -!- FUNCTION: Guanine nucleotide exchange factor (GEF) that modulates the
CC Rho family of GTPases. Promotes the conversion of some member of the
CC Rho family GTPase from the GDP-bound to the GTP-bound form. Isoform 1
CC exhibits no activity toward RHOA, RAC1 or CDC42. Isoform 2 exhibits
CC decreased GEF activity toward CDC42. Isoform 3 exhibits a weak but
CC significant activity toward RAC1 and CDC42. Isoform 4 exhibits
CC significant activity toward RHOA and CDC42. The truncated DBL oncogene
CC is active toward RHOA, RAC1 and CDC42.
CC -!- SUBUNIT: Interacts with an array of inositol phospholipids such as
CC phosphatidylinositol 3-phosphate (PI3P), phosphatidylinositol 4-
CC phosphate (PI4P) and phosphatidylinositol 5-phosphate (PI5P). May
CC interact with CCPG1. {ECO:0000269|PubMed:15157669}.
CC -!- INTERACTION:
CC P10911; P15531: NME1; NbExp=4; IntAct=EBI-1914514, EBI-741141;
CC PRO_0000030434; P15531: NME1; NbExp=9; IntAct=EBI-1915491, EBI-741141;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15157669}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Membrane.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Membrane. Note=Colocalizes with
CC CDC42 to plasma membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=Var.1;
CC IsoId=P10911-1; Sequence=Displayed;
CC Name=2; Synonyms=Var.2;
CC IsoId=P10911-2; Sequence=VSP_008151, VSP_008152;
CC Name=3; Synonyms=Var.3;
CC IsoId=P10911-3; Sequence=VSP_008150;
CC Name=4; Synonyms=Var.4;
CC IsoId=P10911-4; Sequence=VSP_008153;
CC Name=5;
CC IsoId=P10911-5; Sequence=VSP_008150, VSP_008153;
CC Name=6;
CC IsoId=P10911-6; Sequence=VSP_046118, VSP_008151, VSP_008152;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed only in brain. Isoform 3 is
CC expressed in heart, kidney, spleen, liver and testis. Isoform 4 is
CC expressed in brain, heart, kidney, testis, placenta, stomach and
CC peripheral blood. The protein is detectable in brain, heart, kidney,
CC intestine, muscle, lung and testis. {ECO:0000269|PubMed:12445822}.
CC -!- DOMAIN: The CRAL-TRIO domain is involved in interaction with inositol
CC phospholipids.
CC -!- DOMAIN: The DH domain is essential for transforming activity and
CC directly catalyzes GDP-GTP exchange activity. It may interact with
CC CCPG1.
CC -!- PTM: Phosphorylation by TNK2 enhances guanine nucleotide exchange
CC factor (GEF) activity toward Rho family proteins.
CC {ECO:0000269|PubMed:10652228}.
CC -!- DISEASE: Note=MCF2 and DBL represent two activated versions of the same
CC proto-oncogene. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MCF2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA52172.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X12556; CAA31069.1; -; mRNA.
DR EMBL; AB085901; BAC41200.1; -; mRNA.
DR EMBL; AB085902; BAC41201.1; -; mRNA.
DR EMBL; AL117234; CAB55301.1; -; mRNA.
DR EMBL; AK296488; BAH12371.1; -; mRNA.
DR EMBL; AK302957; BAH13855.1; -; mRNA.
DR EMBL; AK316416; BAH14787.1; -; mRNA.
DR EMBL; AL033403; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161777; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471150; EAW88427.1; -; Genomic_DNA.
DR EMBL; CH471150; EAW88430.1; -; Genomic_DNA.
DR EMBL; J03639; AAA52172.1; ALT_INIT; mRNA.
DR EMBL; X13230; CAA31617.1; ALT_SEQ; mRNA.
DR CCDS; CCDS14667.1; -. [P10911-1]
DR CCDS; CCDS48175.1; -. [P10911-3]
DR CCDS; CCDS55514.1; -. [P10911-6]
DR CCDS; CCDS55515.1; -. [P10911-2]
DR CCDS; CCDS55516.1; -. [P10911-4]
DR CCDS; CCDS55517.1; -. [P10911-5]
DR PIR; A28051; TVHUBD.
DR PIR; A30040; TVHUDB.
DR PIR; S10138; S10138.
DR RefSeq; NP_001093325.1; NM_001099855.1. [P10911-3]
DR RefSeq; NP_001165347.1; NM_001171876.1. [P10911-5]
DR RefSeq; NP_001165348.1; NM_001171877.1. [P10911-6]
DR RefSeq; NP_001165349.1; NM_001171878.1. [P10911-2]
DR RefSeq; NP_001165350.1; NM_001171879.1. [P10911-4]
DR RefSeq; NP_005360.3; NM_005369.4. [P10911-1]
DR RefSeq; XP_011529641.1; XM_011531339.2. [P10911-5]
DR RefSeq; XP_016885020.1; XM_017029531.1. [P10911-5]
DR AlphaFoldDB; P10911; -.
DR SMR; P10911; -.
DR BioGRID; 110336; 16.
DR CORUM; P10911; -.
DR IntAct; P10911; 5.
DR MINT; P10911; -.
DR STRING; 9606.ENSP00000430276; -.
DR ChEMBL; CHEMBL4523650; -.
DR SwissLipids; SLP:000001545; -.
DR iPTMnet; P10911; -.
DR PhosphoSitePlus; P10911; -.
DR BioMuta; MCF2; -.
DR DMDM; 92087039; -.
DR MassIVE; P10911; -.
DR PaxDb; P10911; -.
DR PeptideAtlas; P10911; -.
DR PRIDE; P10911; -.
DR ProteomicsDB; 20475; -.
DR ProteomicsDB; 25269; -.
DR ProteomicsDB; 52668; -. [P10911-1]
DR ProteomicsDB; 52669; -. [P10911-2]
DR ProteomicsDB; 52670; -. [P10911-3]
DR ProteomicsDB; 52671; -. [P10911-4]
DR Antibodypedia; 4174; 115 antibodies from 23 providers.
DR DNASU; 4168; -.
DR Ensembl; ENST00000338585.6; ENSP00000342204.6; ENSG00000101977.21. [P10911-4]
DR Ensembl; ENST00000370573.8; ENSP00000359605.4; ENSG00000101977.21. [P10911-2]
DR Ensembl; ENST00000370576.9; ENSP00000359608.4; ENSG00000101977.21. [P10911-1]
DR Ensembl; ENST00000414978.5; ENSP00000397055.1; ENSG00000101977.21. [P10911-3]
DR Ensembl; ENST00000519895.5; ENSP00000430276.1; ENSG00000101977.21. [P10911-5]
DR Ensembl; ENST00000536274.5; ENSP00000438155.1; ENSG00000101977.21. [P10911-6]
DR GeneID; 4168; -.
DR KEGG; hsa:4168; -.
DR MANE-Select; ENST00000519895.6; ENSP00000430276.1; NM_001171876.2; NP_001165347.1. [P10911-5]
DR UCSC; uc004fau.4; human. [P10911-1]
DR CTD; 4168; -.
DR DisGeNET; 4168; -.
DR GeneCards; MCF2; -.
DR HGNC; HGNC:6940; MCF2.
DR HPA; ENSG00000101977; Tissue enhanced (adrenal gland, seminal vesicle, testis).
DR MIM; 311030; gene.
DR neXtProt; NX_P10911; -.
DR OpenTargets; ENSG00000101977; -.
DR PharmGKB; PA30684; -.
DR VEuPathDB; HostDB:ENSG00000101977; -.
DR eggNOG; KOG4240; Eukaryota.
DR GeneTree; ENSGT00940000156974; -.
DR HOGENOM; CLU_007130_1_0_1; -.
DR InParanoid; P10911; -.
DR OMA; DWIITFP; -.
DR OrthoDB; 118479at2759; -.
DR PhylomeDB; P10911; -.
DR TreeFam; TF318080; -.
DR PathwayCommons; P10911; -.
DR Reactome; R-HSA-193634; Axonal growth inhibition (RHOA activation).
DR Reactome; R-HSA-193648; NRAGE signals death through JNK.
DR Reactome; R-HSA-416482; G alpha (12/13) signalling events.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR SignaLink; P10911; -.
DR SIGNOR; P10911; -.
DR BioGRID-ORCS; 4168; 9 hits in 695 CRISPR screens.
DR ChiTaRS; MCF2; human.
DR GeneWiki; MCF2; -.
DR GenomeRNAi; 4168; -.
DR Pharos; P10911; Tbio.
DR PRO; PR:P10911; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P10911; protein.
DR Bgee; ENSG00000101977; Expressed in adrenal tissue and 140 other tissues.
DR ExpressionAtlas; P10911; baseline and differential.
DR Genevisible; P10911; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0016358; P:dendrite development; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0050771; P:negative regulation of axonogenesis; TAS:Reactome.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd00176; SPEC; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00150; SPEC; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Guanine-nucleotide releasing factor;
KW Membrane; Phosphoprotein; Proto-oncogene; Reference proteome.
FT CHAIN 1..925
FT /note="Proto-oncogene DBL"
FT /id="PRO_0000030432"
FT CHAIN 398..925
FT /note="MCF2-transforming protein"
FT /id="PRO_0000030433"
FT CHAIN 498..925
FT /note="DBL-transforming protein"
FT /id="PRO_0000030434"
FT DOMAIN 1..88
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT REPEAT 221..322
FT /note="Spectrin"
FT DOMAIN 495..675
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 687..809
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT VAR_SEQ 1..17
FT /note="MAEANPRRGKMRFRRNA -> MQDIAFLSGGRGKDNAWIITFPENCNFRCIP
FT EEVIAKVLTYLTSIARQNGSDSRFTIILDRRLDTWSSLKISLQKIS (in isoform
FT 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:12445822,
FT ECO:0000303|PubMed:14702039, ECO:0000303|Ref.4"
FT /id="VSP_008150"
FT VAR_SEQ 58..96
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046118"
FT VAR_SEQ 454
FT /note="Q -> QVGVGYSFFQACKLFSK (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:12445822,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_008153"
FT VAR_SEQ 842..860
FT /note="KQQGAFISTEETELEHTST -> DLCRRWLSYIDEATMSNGK (in
FT isoform 2 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:12445822,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_008151"
FT VAR_SEQ 861..925
FT /note="Missing (in isoform 2 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:12445822,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_008152"
FT MUTAGEN 640..646
FT /note="LLLKELL->IIIRDII: Transformation capability reduced;
FT no stimulation of GDP dissociation."
FT /evidence="ECO:0000269|PubMed:2065022"
FT CONFLICT 54
FT /note="L -> P (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="C -> S (in Ref. 5; BAH12371)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="L -> F (in Ref. 5; BAH14787)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="D -> Y (in Ref. 5; BAH12371)"
FT /evidence="ECO:0000305"
FT CONFLICT 634
FT /note="R -> Q (in Ref. 8)"
FT /evidence="ECO:0000305"
FT CONFLICT 687
FT /note="N -> I (in Ref. 5; BAH14787)"
FT /evidence="ECO:0000305"
FT CONFLICT 886
FT /note="A -> V (in Ref. 9)"
FT /evidence="ECO:0000305"
FT CONFLICT 900
FT /note="F -> S (in Ref. 5; BAH13855)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 925 AA; 107673 MW; 96233C7AFC85D637 CRC64;
MAEANPRRGK MRFRRNAASF PGNLHLVLVL RPTSFLQRTF TDIGFWFSQE DFMLKLPVVM
LSSVSDLLTY IDDKQLTPEL GGTLQYCHSE WIIFRNAIEN FALTVKEMAQ MLQSFGTELA
ETELPDDIPS IEEILAIRAE RYHLLKNDIT AVTKEGKILL TNLEVPDTEG AVSSRLECHR
QISGDWQTIN KLLTQVHDME TAFDGFWEKH QLKMEQYLQL WKFEQDFQQL VTEVEFLLNQ
QAELADVTGT IAQVKQKIKK LENLDENSQE LLSKAQFVIL HGHKLAANHH YALDLICQRC
NELRYLSDIL VNEIKAKRIQ LSRTFKMHKL LQQARQCCDE GECLLANQEI DKFQSKEDAQ
KALQDIENFL EMALPFINYE PETLQYEFDV ILSPELKVQM KTIQLKLENI RSIFENQQAG
FRNLADKHVR PIQFVVPTPE NLVTSGTPFF SSKQGKKTWR QNQSNLKIEV VPDCQEKRSS
GPSSSLDNGN SLDVLKNHVL NELIQTERVY VRELYTVLLG YRAEMDNPEM FDLMPPLLRN
KKDILFGNMA EIYEFHNDIF LSSLENCAHA PERVGPCFLE RKDDFQMYAK YCQNKPRSET
IWRKYSECAF FQECQRKLKH RLRLDSYLLK PVQRITKYQL LLKELLKYSK DCEGSALLKK
ALDAMLDLLK SVNDSMHQIA INGYIGNLNE LGKMIMQGGF SVWIGHKKGA TKMKDLARFK
PMQRHLFLYE KAIVFCKRRV ESGEGSDRYP SYSFKHCWKM DEVGITEYVK GDNRKFEIWY
GEKEEVYIVQ ASNVDVKMTW LKEIRNILLK QQELLTVKKR KQQDQLTERD KFQISLQQND
EKQQGAFIST EETELEHTST VVEVCEAIAS VQAEANTVWT EASQSAEISE EPAEWSSNYF
YPTYDENEEE NRPLMRPVSE MALLY
