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

GO - Biological processi

  • 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)DescriptionActionsGraphical viewLength
ChainiPRO_00000809361 – 1149Guanine nucleotide exchange factor DBSAdd BLAST1149

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei457PhosphoserineBy similarity1
Modified residuei462PhosphoserineBy similarity1
Modified residuei471PhosphoserineBy similarity1
Modified residuei480PhosphoserineBy similarity1
Modified residuei621PhosphoserineCombined sources1
Modified residuei622PhosphothreonineCombined sources1
Modified residuei1033PhosphoserineCombined sources1
Modified residuei1034PhosphoserineCombined sources1
Modified residuei1041PhosphoserineCombined sources1
Modified residuei1042PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ64096.
MaxQBiQ64096.
PRIDEiQ64096.

PTM databases

iPTMnetiQ64096.
PhosphoSitePlusiQ64096.

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 interactors.
MINTiMINT-1658374.

Structurei

Secondary structure

11149
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi625 – 657Combined sources33
Helixi660 – 663Combined sources4
Turni665 – 670Combined sources6
Helixi673 – 677Combined sources5
Helixi679 – 683Combined sources5
Helixi686 – 695Combined sources10
Helixi697 – 702Combined sources6
Turni703 – 706Combined sources4
Helixi708 – 710Combined sources3
Helixi711 – 716Combined sources6
Turni717 – 720Combined sources4
Helixi721 – 723Combined sources3
Helixi724 – 742Combined sources19
Helixi746 – 755Combined sources10
Helixi761 – 765Combined sources5
Helixi767 – 784Combined sources18
Turni785 – 788Combined sources4
Helixi792 – 815Combined sources24
Beta strandi818 – 820Combined sources3
Helixi825 – 828Combined sources4
Beta strandi831 – 841Combined sources11
Beta strandi848 – 851Combined sources4
Beta strandi855 – 857Combined sources3
Beta strandi859 – 876Combined sources18
Turni880 – 883Combined sources4
Beta strandi888 – 896Combined sources9
Helixi897 – 899Combined sources3
Beta strandi900 – 903Combined sources4
Beta strandi912 – 917Combined sources6
Turni918 – 921Combined sources4
Beta strandi922 – 927Combined sources6
Helixi931 – 958Combined sources28
Turni959 – 964Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ64096.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini52 – 224CRAL-TRIOPROSITE-ProRule annotationAdd BLAST173
Repeati351 – 456SpectrinAdd BLAST106
Domaini632 – 812DHPROSITE-ProRule annotationAdd BLAST181
Domaini841 – 950PHPROSITE-ProRule annotationAdd BLAST110
Domaini1058 – 1112SH3PROSITE-ProRule annotationAdd BLAST55

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili503 – 529Sequence analysisAdd BLAST27

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi624 – 627Poly-Glu4

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.
3.40.525.10. 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)DescriptionActionsGraphical viewLength
Sequence conflicti495 – 496AL → SF in AAB33461 (PubMed:7862449).Curated2
Sequence conflicti701L → V in AAB33461 (PubMed:7862449).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiQ64096.
PhosphoSitePlusiQ64096.

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.
3.40.525.10. 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...

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: November 30, 2016
This is version 147 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.