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Protein

Guanine nucleotide exchange factor DBS

Gene

Mcf2l

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Guanine nucleotide exchange factor that catalyzes guanine nucleotide exchange on RHOA and CDC42, and thereby contributes to the regulation of RHOA and CDC42 signaling pathways (PubMed:17000758, PubMed:11889037, PubMed:12006984). Seems to lack activity with RAC1. Becomes activated and highly tumorigenic by truncation of the N-terminus (By similarity).By similarity2 Publications

GO - Molecular functioni

  • 1-phosphatidylinositol binding Source: MGI
  • Rho guanyl-nucleotide exchange factor activity Source: MGI

GO - Biological processi

  • positive regulation of GTPase activity Source: GOC
  • positive regulation of Rho protein signal transduction Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • Rho protein signal transduction Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide exchange factor DBS
Alternative name(s):
DBL's big sister
MCF2-transforming sequence-like protein
Gene namesi
Name:Mcf2l
Synonyms:Dbs
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:103263. Mcf2l.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular space Source: MGI
  • extrinsic component of membrane Source: UniProtKB
  • lamellipodium Source: MGI
  • membrane Source: MGI
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11491149Guanine nucleotide exchange factor DBSPRO_0000080936Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei457 – 4571PhosphoserineBy similarity
Modified residuei462 – 4621PhosphoserineBy similarity
Modified residuei471 – 4711PhosphoserineBy similarity
Modified residuei480 – 4801PhosphoserineBy similarity
Modified residuei621 – 6211PhosphoserineCombined sources
Modified residuei622 – 6221PhosphothreonineCombined sources
Modified residuei1033 – 10331PhosphoserineCombined sources
Modified residuei1034 – 10341PhosphoserineCombined sources
Modified residuei1041 – 10411PhosphoserineCombined sources
Modified residuei1042 – 10421PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ64096.
MaxQBiQ64096.
PRIDEiQ64096.

PTM databases

PhosphoSiteiQ64096.

Expressioni

Tissue specificityi

Expressed at low levels in several hemopoietic cell lines and in thymus and spleen, and at higher levels in other tissues, particularly in brain.1 Publication

Gene expression databases

CleanExiMM_MCF2L.

Interactioni

Subunit structurei

Interacts with GTP-bound RAC1 (By similarity). Interacts with CDC42 (PubMed:11889037). Interacts with RHOA (PubMed:12006984). Interacts with CCPG1, which results in specific inhibition of its exchange activity toward RHOA, but does not affect its activity on CDC42 (PubMed:17000758).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC42P60953-23EBI-602123,EBI-287394From a different organism.

Protein-protein interaction databases

DIPiDIP-34544N.
IntActiQ64096. 3 interactions.
MINTiMINT-1658374.

Structurei

Secondary structure

1
1149
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi625 – 65733Combined sources
Helixi660 – 6634Combined sources
Turni665 – 6706Combined sources
Helixi673 – 6775Combined sources
Helixi679 – 6835Combined sources
Helixi686 – 69510Combined sources
Helixi697 – 7026Combined sources
Turni703 – 7064Combined sources
Helixi708 – 7103Combined sources
Helixi711 – 7166Combined sources
Turni717 – 7204Combined sources
Helixi721 – 7233Combined sources
Helixi724 – 74219Combined sources
Helixi746 – 75510Combined sources
Helixi761 – 7655Combined sources
Helixi767 – 78418Combined sources
Turni785 – 7884Combined sources
Helixi792 – 81524Combined sources
Beta strandi818 – 8203Combined sources
Helixi825 – 8284Combined sources
Beta strandi831 – 84111Combined sources
Beta strandi848 – 8514Combined sources
Beta strandi855 – 8573Combined sources
Beta strandi859 – 87618Combined sources
Turni880 – 8834Combined sources
Beta strandi888 – 8969Combined sources
Helixi897 – 8993Combined sources
Beta strandi900 – 9034Combined sources
Beta strandi912 – 9176Combined sources
Turni918 – 9214Combined sources
Beta strandi922 – 9276Combined sources
Helixi931 – 95828Combined sources
Turni959 – 9646Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KZ7X-ray2.40A/C623-967[»]
1KZGX-ray2.60A/C623-967[»]
1LB1X-ray2.81A/C/E/G623-967[»]
1RJ2X-ray3.00A/D/G/J623-968[»]
ProteinModelPortaliQ64096.
SMRiQ64096. Positions 624-965.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ64096.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini52 – 224173CRAL-TRIOPROSITE-ProRule annotationAdd
BLAST
Repeati351 – 456106SpectrinAdd
BLAST
Domaini632 – 812181DHPROSITE-ProRule annotationAdd
BLAST
Domaini841 – 950110PHPROSITE-ProRule annotationAdd
BLAST
Domaini1058 – 111255SH3PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili503 – 52927Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi624 – 6274Poly-Glu

Domaini

The DH domain is involved in interaction with CCPG1.1 Publication
The CRAL-TRIO domain mediates interaction with various inositol phospholipids, such as phosphatidylinositol 3-phosphate (PI3P), phosphatidylinositol 4-phosphate (PI4P) and phosphatidylinositol 5-phosphate (PI5P).By similarity

Sequence similaritiesi

Belongs to the MCF2 family.Curated
Contains 1 CRAL-TRIO domain.PROSITE-ProRule annotation
Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation
Contains 1 spectrin repeat.Curated

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

HOGENOMiHOG000231361.
HOVERGENiHBG062385.
InParanoidiQ64096.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR001251. CRAL-TRIO_dom.
IPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR001452. SH3_domain.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view]
PfamiPF13716. CRAL_TRIO_2. 1 hit.
PF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF00435. Spectrin. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
SM00516. SEC14. 1 hit.
SM00326. SH3. 1 hit.
SM00150. SPEC. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF52087. SSF52087. 1 hit.
PROSITEiPS50191. CRAL_TRIO. 1 hit.
PS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q64096-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDCWCFIFC KEHVRSNPLS PQHDGASREE ADHQVDVSDG IRLVPDKAEA
60 70 80 90 100
TAATASDEIM HQDIVPLCAA DIQEQLKKRF AYLSGGRGQD GSPVITFPDY
110 120 130 140 150
PAFSEIPDKE FQNVMTYLTS IPSLQDAGIG FILVIDRRQD KWTSVKASVL
160 170 180 190 200
RIAASFPANL QLVLVLRPTG FFQRTLSDIA FKFNRDEFKM KVPVMMLSSV
210 220 230 240 250
PELHGYIDKS QLTEDLGGTL DYCHSRWLCH RTAIESFALM VKQTAQMLQA
260 270 280 290 300
FGTELAETEL PNDVQSTSLV LSAHTEKKAK VKEDLQLALK EGNSILESLR
310 320 330 340 350
EPLAESAAHS VNQDQLDNQA TVQRLLAQLN ETEAAFDEFW AKHQQKLEQC
360 370 380 390 400
LQLRHFEQGF REVKTTLDSM SQKIAAFTDV GNSLAHVQHL LKDLTAFEEK
410 420 430 440 450
SSVAVDKARA LSLEGQQLIE NRHYAVDSIH PKCEELQHLC DHFASEVTRR
460 470 480 490 500
RGLLSKSLEL HSLLETSMKW SDEGIFLLAS QPVDKCQSQD GAEAALQEIE
510 520 530 540 550
KFLETGAENK IQELNEIYKE YECILNQDLL EHVQKVFQKQ ESTEEMFHRR
560 570 580 590 600
QASLKKLAAK QTRPVQPVAP RPEALTKSPS PSPGSWRSSE NSSSEGNALR
610 620 630 640 650
RGPYRRAKSE MSEPRQGRTS STGEEEESLA ILRRHVMNEL LDTERAYVEE
660 670 680 690 700
LLCVLEGYAA EMDNPLMAHL ISTGLQNKKN ILFGNMEEIY HFHNRNIPAG
710 720 730 740 750
LESCIDCPEL VGRCFLERME EFQIYEKYCQ NKPRSESLWR QCSDCPFFQE
760 770 780 790 800
CQKKLDHKLS LDSYLLKPVQ RITKYQLLLK EMLKYSKHCE GAEDLQEALS
810 820 830 840 850
SILGILKAVN DSMHLIAITG YDGNLGDLGK LLMQGSFSVW TDHKKGHTKV
860 870 880 890 900
KELARFKPMQ RHLFLHEKAV LFCKKREENG EGYEKAPSYS YKQSLNMTAV
910 920 930 940 950
GITENVKGDT KKFEIWYNAR EEVYIIQAPT PEIKAAWVNE IRKVLTSQLQ
960 970 980 990 1000
ACREASQHRA LEQSHSLPLP TPSSTSPTKG NTRNVKKLED RKTDPLSLEG
1010 1020 1030 1040 1050
YVSSSLPKPP EKGKGWSKTS HSLEAPEEDG GWSSAEELIN SSDAEEDGGV
1060 1070 1080 1090 1100
GPKKLVPGKY TVVMDDEKGG PDTLAMRSGD MVEVVEEGAE GLWYVRDLTS
1110 1120 1130 1140
SKEGWVPASS LSTLLGKSSS AQCLSSSGKI HCARQLCPEP AEILSPEPV
Length:1,149
Mass (Da):129,113
Last modified:July 27, 2011 - v2
Checksum:i0A325FB42E49BA6D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti495 – 4962AL → SF in AAB33461 (PubMed:7862449).Curated
Sequence conflicti701 – 7011L → V in AAB33461 (PubMed:7862449).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S76838 mRNA. Translation: AAB33461.2.
AC127308 Genomic DNA. No translation available.
AC134581 Genomic DNA. No translation available.
UniGeneiMm.334413.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S76838 mRNA. Translation: AAB33461.2.
AC127308 Genomic DNA. No translation available.
AC134581 Genomic DNA. No translation available.
UniGeneiMm.334413.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KZ7X-ray2.40A/C623-967[»]
1KZGX-ray2.60A/C623-967[»]
1LB1X-ray2.81A/C/E/G623-967[»]
1RJ2X-ray3.00A/D/G/J623-968[»]
ProteinModelPortaliQ64096.
SMRiQ64096. Positions 624-965.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-34544N.
IntActiQ64096. 3 interactions.
MINTiMINT-1658374.

PTM databases

PhosphoSiteiQ64096.

Proteomic databases

EPDiQ64096.
MaxQBiQ64096.
PRIDEiQ64096.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:103263. Mcf2l.

Phylogenomic databases

HOGENOMiHOG000231361.
HOVERGENiHBG062385.
InParanoidiQ64096.

Miscellaneous databases

ChiTaRSiMcf2l. mouse.
EvolutionaryTraceiQ64096.
PROiQ64096.
SOURCEiSearch...

Gene expression databases

CleanExiMM_MCF2L.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR001251. CRAL-TRIO_dom.
IPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR001452. SH3_domain.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view]
PfamiPF13716. CRAL_TRIO_2. 1 hit.
PF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF00435. Spectrin. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
SM00516. SEC14. 1 hit.
SM00326. SH3. 1 hit.
SM00150. SPEC. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF52087. SSF52087. 1 hit.
PROSITEiPS50191. CRAL_TRIO. 1 hit.
PS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Retroviral transduction and oncogenic selection of a cDNA encoding Dbs, a homolog of the Dbl guanine nucleotide exchange factor."
    Whitehead I., Kirk H., Kay R.
    Oncogene 10:713-721(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Hematopoietic.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  4. "Ccpg1, a novel scaffold protein that regulates the activity of the Rho guanine nucleotide exchange factor Dbs."
    Kostenko E.V., Olabisi O.O., Sahay S., Rodriguez P.L., Whitehead I.P.
    Mol. Cell. Biol. 26:8964-8975(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CCPG1, SUBCELLULAR LOCATION.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621; THR-622; SER-1033; SER-1034; SER-1041 AND SER-1042, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney and Lung.
  6. "A crystallographic view of interactions between Dbs and Cdc42: PH domain-assisted guanine nucleotide exchange."
    Rossman K.L., Worthylake D.K., Snyder J.T., Siderovski D.P., Campbell S.L., Sondek J.
    EMBO J. 21:1315-1326(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 623-967 IN COMPLEX WITH CDC42, FUNCTION.
  7. "Structural basis for the selective activation of Rho GTPases by Dbl exchange factors."
    Snyder J.T., Worthylake D.K., Rossman K.L., Betts L., Pruitt W.M., Siderovski D.P., Der C.J., Sondek J.
    Nat. Struct. Biol. 9:468-475(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 623-967 IN COMPLEX WITH RHOA, FUNCTION.
  8. "Crystal structure of the DH/PH fragment of Dbs without bound GTPase."
    Worthylake D.K., Rossman K.L., Sondek J.
    Structure 12:1078-1086(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 498-843.

Entry informationi

Entry nameiMCF2L_MOUSE
AccessioniPrimary (citable) accession number: Q64096
Secondary accession number(s): E9PV70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 27, 2011
Last modified: May 11, 2016
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.