P10911 · MCF2_HUMAN
- ProteinProto-oncogene DBL
- GeneMCF2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids925 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Guanine nucleotide exchange factor (GEF) that modulates the Rho family of GTPases. Promotes the conversion of some member of the Rho family GTPase from the GDP-bound to the GTP-bound form. Isoform 1 exhibits no activity toward RHOA, RAC1 or CDC42. Isoform 2 exhibits decreased GEF activity toward CDC42. Isoform 3 exhibits a weak but significant activity toward RAC1 and CDC42. Isoform 4 exhibits significant activity toward RHOA and CDC42. The truncated DBL oncogene is active toward RHOA, RAC1 and CDC42.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytoskeleton | |
Cellular Component | cytosol | |
Cellular Component | extrinsic component of membrane | |
Cellular Component | membrane | |
Molecular Function | guanyl-nucleotide exchange factor activity | |
Biological Process | cellular response to leukemia inhibitory factor | |
Biological Process | dendrite development | |
Biological Process | intracellular signal transduction | |
Biological Process | negative regulation of axonogenesis | |
Biological Process | regulation of small GTPase mediated signal transduction |
Keywords
- Molecular function
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameProto-oncogene DBL
- Alternative names
- Cleaved into 2 chains
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP10911
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Involvement in disease
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 640-646 | Transformation capability reduced; no stimulation of GDP dissociation. | ||||
Sequence: LLLKELL → IIIRDII |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 985 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000030432 | 1-925 | Proto-oncogene DBL | |||
Sequence: MAEANPRRGKMRFRRNAASFPGNLHLVLVLRPTSFLQRTFTDIGFWFSQEDFMLKLPVVMLSSVSDLLTYIDDKQLTPELGGTLQYCHSEWIIFRNAIENFALTVKEMAQMLQSFGTELAETELPDDIPSIEEILAIRAERYHLLKNDITAVTKEGKILLTNLEVPDTEGAVSSRLECHRQISGDWQTINKLLTQVHDMETAFDGFWEKHQLKMEQYLQLWKFEQDFQQLVTEVEFLLNQQAELADVTGTIAQVKQKIKKLENLDENSQELLSKAQFVILHGHKLAANHHYALDLICQRCNELRYLSDILVNEIKAKRIQLSRTFKMHKLLQQARQCCDEGECLLANQEIDKFQSKEDAQKALQDIENFLEMALPFINYEPETLQYEFDVILSPELKVQMKTIQLKLENIRSIFENQQAGFRNLADKHVRPIQFVVPTPENLVTSGTPFFSSKQGKKTWRQNQSNLKIEVVPDCQEKRSSGPSSSLDNGNSLDVLKNHVLNELIQTERVYVRELYTVLLGYRAEMDNPEMFDLMPPLLRNKKDILFGNMAEIYEFHNDIFLSSLENCAHAPERVGPCFLERKDDFQMYAKYCQNKPRSETIWRKYSECAFFQECQRKLKHRLRLDSYLLKPVQRITKYQLLLKELLKYSKDCEGSALLKKALDAMLDLLKSVNDSMHQIAINGYIGNLNELGKMIMQGGFSVWIGHKKGATKMKDLARFKPMQRHLFLYEKAIVFCKRRVESGEGSDRYPSYSFKHCWKMDEVGITEYVKGDNRKFEIWYGEKEEVYIVQASNVDVKMTWLKEIRNILLKQQELLTVKKRKQQDQLTERDKFQISLQQNDEKQQGAFISTEETELEHTSTVVEVCEAIASVQAEANTVWTEASQSAEISEEPAEWSSNYFYPTYDENEEENRPLMRPVSEMALLY | ||||||
Chain | PRO_0000030433 | 398-925 | MCF2-transforming protein | |||
Sequence: VQMKTIQLKLENIRSIFENQQAGFRNLADKHVRPIQFVVPTPENLVTSGTPFFSSKQGKKTWRQNQSNLKIEVVPDCQEKRSSGPSSSLDNGNSLDVLKNHVLNELIQTERVYVRELYTVLLGYRAEMDNPEMFDLMPPLLRNKKDILFGNMAEIYEFHNDIFLSSLENCAHAPERVGPCFLERKDDFQMYAKYCQNKPRSETIWRKYSECAFFQECQRKLKHRLRLDSYLLKPVQRITKYQLLLKELLKYSKDCEGSALLKKALDAMLDLLKSVNDSMHQIAINGYIGNLNELGKMIMQGGFSVWIGHKKGATKMKDLARFKPMQRHLFLYEKAIVFCKRRVESGEGSDRYPSYSFKHCWKMDEVGITEYVKGDNRKFEIWYGEKEEVYIVQASNVDVKMTWLKEIRNILLKQQELLTVKKRKQQDQLTERDKFQISLQQNDEKQQGAFISTEETELEHTSTVVEVCEAIASVQAEANTVWTEASQSAEISEEPAEWSSNYFYPTYDENEEENRPLMRPVSEMALLY | ||||||
Chain | PRO_0000030434 | 498-925 | DBL-transforming protein | |||
Sequence: HVLNELIQTERVYVRELYTVLLGYRAEMDNPEMFDLMPPLLRNKKDILFGNMAEIYEFHNDIFLSSLENCAHAPERVGPCFLERKDDFQMYAKYCQNKPRSETIWRKYSECAFFQECQRKLKHRLRLDSYLLKPVQRITKYQLLLKELLKYSKDCEGSALLKKALDAMLDLLKSVNDSMHQIAINGYIGNLNELGKMIMQGGFSVWIGHKKGATKMKDLARFKPMQRHLFLYEKAIVFCKRRVESGEGSDRYPSYSFKHCWKMDEVGITEYVKGDNRKFEIWYGEKEEVYIVQASNVDVKMTWLKEIRNILLKQQELLTVKKRKQQDQLTERDKFQISLQQNDEKQQGAFISTEETELEHTSTVVEVCEAIASVQAEANTVWTEASQSAEISEEPAEWSSNYFYPTYDENEEENRPLMRPVSEMALLY |
Post-translational modification
Phosphorylation by TNK2 enhances guanine nucleotide exchange factor (GEF) activity toward Rho family proteins.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Isoform 1 is expressed only in brain. Isoform 3 is expressed in heart, kidney, spleen, liver and testis. Isoform 4 is expressed in brain, heart, kidney, testis, placenta, stomach and peripheral blood. The protein is detectable in brain, heart, kidney, intestine, muscle, lung and testis.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with an array of inositol phospholipids such as phosphatidylinositol 3-phosphate (PI3P), phosphatidylinositol 4-phosphate (PI4P) and phosphatidylinositol 5-phosphate (PI5P). May interact with CCPG1.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P10911 | NME1 P15531 | 4 | EBI-1914514, EBI-741141 | |
BINARY | PRO_0000030434 | NME1 P15531 | 9 | EBI-1915491, EBI-741141 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-88 | CRAL-TRIO | ||||
Sequence: MAEANPRRGKMRFRRNAASFPGNLHLVLVLRPTSFLQRTFTDIGFWFSQEDFMLKLPVVMLSSVSDLLTYIDDKQLTPELGGTLQYCH | ||||||
Repeat | 221-322 | Spectrin | ||||
Sequence: WKFEQDFQQLVTEVEFLLNQQAELADVTGTIAQVKQKIKKLENLDENSQELLSKAQFVILHGHKLAANHHYALDLICQRCNELRYLSDILVNEIKAKRIQLS | ||||||
Domain | 495-675 | DH | ||||
Sequence: LKNHVLNELIQTERVYVRELYTVLLGYRAEMDNPEMFDLMPPLLRNKKDILFGNMAEIYEFHNDIFLSSLENCAHAPERVGPCFLERKDDFQMYAKYCQNKPRSETIWRKYSECAFFQECQRKLKHRLRLDSYLLKPVQRITKYQLLLKELLKYSKDCEGSALLKKALDAMLDLLKSVNDS | ||||||
Domain | 687-809 | PH | ||||
Sequence: NLNELGKMIMQGGFSVWIGHKKGATKMKDLARFKPMQRHLFLYEKAIVFCKRRVESGEGSDRYPSYSFKHCWKMDEVGITEYVKGDNRKFEIWYGEKEEVYIVQASNVDVKMTWLKEIRNILL |
Domain
The CRAL-TRIO domain is involved in interaction with inositol phospholipids.
The DH domain is essential for transforming activity and directly catalyzes GDP-GTP exchange activity. It may interact with CCPG1.
Sequence similarities
Belongs to the MCF2 family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 6 isoforms produced by Alternative splicing.
P10911-1
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.
- Name1
- SynonymsVar.1
- Length925
- Mass (Da)107,673
- Last updated2006-03-07 v3
- Checksum96233C7AFC85D637
P10911-2
- Name2
- SynonymsVar.2
P10911-3
- Name3
- SynonymsVar.3
- Differences from canonical
- 1-17: MAEANPRRGKMRFRRNA → MQDIAFLSGGRGKDNAWIITFPENCNFRCIPEEVIAKVLTYLTSIARQNGSDSRFTIILDRRLDTWSSLKISLQKIS
P10911-4
- Name4
- SynonymsVar.4
- Differences from canonical
- 454-454: Q → QVGVGYSFFQACKLFSK
P10911-5
- Name5
P10911-6
- Name6
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2U3TZL4 | A0A2U3TZL4_HUMAN | MCF2 | 1028 | ||
H0Y662 | H0Y662_HUMAN | MCF2 | 429 | ||
Q5JYJ5 | Q5JYJ5_HUMAN | MCF2 | 528 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_008150 | 1-17 | in isoform 3 and isoform 5 | |||
Sequence: MAEANPRRGKMRFRRNA → MQDIAFLSGGRGKDNAWIITFPENCNFRCIPEEVIAKVLTYLTSIARQNGSDSRFTIILDRRLDTWSSLKISLQKIS | ||||||
Sequence conflict | 54 | in Ref. 1 and 3 | ||||
Sequence: L → P | ||||||
Alternative sequence | VSP_046118 | 58-96 | in isoform 6 | |||
Sequence: Missing | ||||||
Sequence conflict | 178 | in Ref. 5; BAH12371 | ||||
Sequence: C → S | ||||||
Sequence conflict | 330 | in Ref. 5; BAH14787 | ||||
Sequence: L → F | ||||||
Sequence conflict | 358 | in Ref. 5; BAH12371 | ||||
Sequence: D → Y | ||||||
Alternative sequence | VSP_008153 | 454 | in isoform 4 and isoform 5 | |||
Sequence: Q → QVGVGYSFFQACKLFSK | ||||||
Sequence conflict | 634 | in Ref. 8 | ||||
Sequence: R → Q | ||||||
Sequence conflict | 687 | in Ref. 5; BAH14787 | ||||
Sequence: N → I | ||||||
Alternative sequence | VSP_008151 | 842-860 | in isoform 2 and isoform 6 | |||
Sequence: KQQGAFISTEETELEHTST → DLCRRWLSYIDEATMSNGK | ||||||
Alternative sequence | VSP_008152 | 861-925 | in isoform 2 and isoform 6 | |||
Sequence: Missing | ||||||
Sequence conflict | 886 | in Ref. 9 | ||||
Sequence: A → V | ||||||
Sequence conflict | 900 | in Ref. 5; BAH13855 | ||||
Sequence: F → S |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X12556 EMBL· GenBank· DDBJ | CAA31069.1 EMBL· GenBank· DDBJ | mRNA | ||
AB085901 EMBL· GenBank· DDBJ | BAC41200.1 EMBL· GenBank· DDBJ | mRNA | ||
AB085902 EMBL· GenBank· DDBJ | BAC41201.1 EMBL· GenBank· DDBJ | mRNA | ||
AL117234 EMBL· GenBank· DDBJ | CAB55301.1 EMBL· GenBank· DDBJ | mRNA | ||
AK296488 EMBL· GenBank· DDBJ | BAH12371.1 EMBL· GenBank· DDBJ | mRNA | ||
AK302957 EMBL· GenBank· DDBJ | BAH13855.1 EMBL· GenBank· DDBJ | mRNA | ||
AK316416 EMBL· GenBank· DDBJ | BAH14787.1 EMBL· GenBank· DDBJ | mRNA | ||
AL033403 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL161777 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471150 EMBL· GenBank· DDBJ | EAW88427.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471150 EMBL· GenBank· DDBJ | EAW88430.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
J03639 EMBL· GenBank· DDBJ | AAA52172.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
X13230 EMBL· GenBank· DDBJ | CAA31617.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. |