Q9ES28 · ARHG7_MOUSE
- ProteinRho guanine nucleotide exchange factor 7
- GeneArhgef7
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids862 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Acts as a RAC1 guanine nucleotide exchange factor (GEF) and can induce membrane ruffling. May function as a positive regulator of apoptosis. Functions in cell migration, attachment and cell spreading. Promotes targeting of RAC1 to focal adhesions. Downstream of NMDA receptors and CaMKK-CaMK1 signaling cascade, promotes the formation of spines and synapses in hippocampal neurons (By similarity).
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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Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRho guanine nucleotide exchange factor 7
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9ES28
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Detected at cell adhesions. A small proportion is detected at focal adhesions.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000080922 | 1-862 | Rho guanine nucleotide exchange factor 7 | |||
Sequence: MNSAEQTVTWLITLGVLESPKKTISDPEVFLQASLKDGVVLCRLLERLLPGTIEKVYPEPRNESECLSNIREFLRACGASLRLETFDANDLYQGQNFNKVLSSLVTLNKVTADIGLGSDSVCARPSSHRIKSFDSLGSQSSHSRTSKLLQSQYRSLDMTDNTNSQLVVRAKFNFQQTNEDELSFSKGDVIHVTRVEEGGWWEGTHNGRTGWFPSNYVREIKPSEKPVSPKSGTLKSPPKGFDTTAINKSYYNVVLQNILETEHEYSKELQSVLSTYLRPLQTSDKLSSANTSYLMGNLEEISSFQQVLVQSLEECTKSPEAQQRVGGCFLSLMPQMRTLYLAYCANHPSAVSVLTEHSEDLGEFMETKGASSPGILVLTTGLSKPFMRLDKYPTLLKELERHMEDYHPDRQDIQKSMTAFKNLSAQCQEVRKRKELELQILTEPIRSWEGDDIKTLGSVTYMSQVTIQCAGSEEKNERYLLLFPNLLLMLSASPRMSGFIYQGKLPTTGMTITKLEDSENHRNAFEISGSMIERILVSCTSQQDLHEWVEHLQKQTKVTSVSNPTIKPHSVPSHTLPSHPLTPSSKHADSKPVALTPAYHTLPHPSHHGTPHTTISWGPLEPPKTPKPWSLSCLRPAPPLRPSAALCYKEDLSKSPKTMKKLLPKRKPERKPSDEEFAVRKSTAALEEDAQILKVIEAYCTSAKTRQTLNSTWQGTDLMHNHVLADDDQSSLDSLGRRSSLSRLEPSDLSEDSEYDSIWTAHSYRMGSASRSRKESAPQVLLPEEEKIIVEETKSNGQTVIEEKSLVDTVYALKDEVQELRQDNKKMKKSLEEEQRARKDLEKLVRKVLKNMNDPAWDETNL | ||||||
Modified residue | 132 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 155 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 164 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 228 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 236 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 497 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 673 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 776 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated on Ser-673 by CaMK1; enhancement of GEF activity and downstream activation of RAC1 (By similarity).
Phosphorylated by PTK2/FAK1; this promotes interaction with RAC1
Phosphorylated by PTK2/FAK1; this promotes interaction with RAC1
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with PAK kinases through the SH3 domain. Interacts with unphosphorylated PAK1. Interacts with ITCH. Interacts with SCRIB; interaction is direct and may play a role in regulation of apoptosis (By similarity).
Interacts with GIT1 and TGFB1I1. Interacts with FRMPD4 (via N-terminus). Interacts with CaMK1. Interacts with BIN2 (By similarity).
Interacts with PTK2/FAK1 and RAC1. Interacts with PARVB. Interacts with YWHAZ (PubMed:16959763).
Interacts (via PH domain) with NOX1 (via FAD-binding FR-type domain) (By similarity).
Interacts with GIT1 and TGFB1I1. Interacts with FRMPD4 (via N-terminus). Interacts with CaMK1. Interacts with BIN2 (By similarity).
Interacts with PTK2/FAK1 and RAC1. Interacts with PARVB. Interacts with YWHAZ (PubMed:16959763).
Interacts (via PH domain) with NOX1 (via FAD-binding FR-type domain) (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9ES28 | Git1 Q68FF6 | 2 | EBI-642580, EBI-645933 | |
XENO | Q9ES28 | Git1 Q9Z272 | 2 | EBI-642580, EBI-3842379 | |
BINARY | Q9ES28 | Git2 Q9JLQ2 | 6 | EBI-642580, EBI-642860 | |
XENO | Q9ES28 | GIT2 Q14161 | 2 | EBI-642580, EBI-1046878 | |
BINARY | Q9ES28 | Parvb Q9ES46 | 2 | EBI-642580, EBI-6914996 | |
XENO | Q9ES28 | PARVB Q9HBI1 | 10 | EBI-642580, EBI-1047679 | |
XENO | Q9ES28 | Shank2 Q9QX74-4 | 3 | EBI-642580, EBI-36481413 | |
XENO | Q9ES28-2 | Shank1 Q9WV48 | 6 | EBI-8620514, EBI-80909 | |
XENO | Q9ES28-2 | Shank2 Q9QX74 | 4 | EBI-8620514, EBI-397902 | |
XENO | Q9ES28-2 | Shank3 Q9JLU4 | 2 | EBI-8620514, EBI-6271152 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-112 | Calponin-homology (CH) | ||||
Sequence: MNSAEQTVTWLITLGVLESPKKTISDPEVFLQASLKDGVVLCRLLERLLPGTIEKVYPEPRNESECLSNIREFLRACGASLRLETFDANDLYQGQNFNKVLSSLVTLNKVTA | ||||||
Domain | 163-222 | SH3 | ||||
Sequence: NSQLVVRAKFNFQQTNEDELSFSKGDVIHVTRVEEGGWWEGTHNGRTGWFPSNYVREIKP | ||||||
Domain | 250-430 | DH | ||||
Sequence: YYNVVLQNILETEHEYSKELQSVLSTYLRPLQTSDKLSSANTSYLMGNLEEISSFQQVLVQSLEECTKSPEAQQRVGGCFLSLMPQMRTLYLAYCANHPSAVSVLTEHSEDLGEFMETKGASSPGILVLTTGLSKPFMRLDKYPTLLKELERHMEDYHPDRQDIQKSMTAFKNLSAQCQEV | ||||||
Domain | 452-557 | PH | ||||
Sequence: DIKTLGSVTYMSQVTIQCAGSEEKNERYLLLFPNLLLMLSASPRMSGFIYQGKLPTTGMTITKLEDSENHRNAFEISGSMIERILVSCTSQQDLHEWVEHLQKQTK | ||||||
Compositional bias | 559-585 | Polar residues | ||||
Sequence: TSVSNPTIKPHSVPSHTLPSHPLTPSS | ||||||
Region | 559-591 | Disordered | ||||
Sequence: TSVSNPTIKPHSVPSHTLPSHPLTPSSKHADSK | ||||||
Region | 657-679 | Disordered | ||||
Sequence: KTMKKLLPKRKPERKPSDEEFAV | ||||||
Region | 728-748 | Disordered | ||||
Sequence: DQSSLDSLGRRSSLSRLEPSD | ||||||
Coiled coil | 804-854 | |||||
Sequence: KSLVDTVYALKDEVQELRQDNKKMKKSLEEEQRARKDLEKLVRKVLKNMND |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 8 isoforms produced by Alternative splicing & Alternative initiation.
Q9ES28-1
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.
- NameB
- Length862
- Mass (Da)97,056
- Last updated2007-02-06 v2
- Checksum46D61B606B8391B4
Q9ES28-2
- NameA
- Differences from canonical
- 712-771: TWQGTDLMHNHVLADDDQSSLDSLGRRSSLSRLEPSDLSEDSEYDSIWTAHSYRMGSASR → S
Q9ES28-3
- NameC
- Differences from canonical
- 576-650: Missing
Q9ES28-4
- NameD
Q9ES28-5
- NameE
- Synonymsd
Q9ES28-6
- NameF
- NoteProduced by alternative initiation at Met-158 of isoform G.
Q9ES28-7
- NameG
- Synonymsb(L)
Q9ES28-8
- NameH
- Synonymsb
- NoteProduced by alternative initiation at Met-158 of isoform G.
- Differences from canonical
- 1-157: Missing
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0R4J0X8 | A0A0R4J0X8_MOUSE | Arhgef7 | 646 | ||
A0A6I8MX11 | A0A6I8MX11_MOUSE | Arhgef7 | 25 | ||
D3Z0V2 | D3Z0V2_MOUSE | Arhgef7 | 636 | ||
A0A1B0GSX2 | A0A1B0GSX2_MOUSE | Arhgef7 | 131 | ||
A0A1B0GSX4 | A0A1B0GSX4_MOUSE | Arhgef7 | 68 | ||
A0A1B0GRS3 | A0A1B0GRS3_MOUSE | Arhgef7 | 200 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_023052 | 1-52 | in isoform D, isoform F and isoform G | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_023051 | 1-157 | in isoform H | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_023053 | 53-55 | in isoform D, isoform F and isoform G | |||
Sequence: IEK → MLQ | ||||||
Sequence conflict | 485-488 | in Ref. 2; AAO65479, 5; AAG18017/AAG18018 and 7; AAB57691 | ||||
Sequence: NLLL → KPSV | ||||||
Sequence conflict | 492 | in Ref. 2; AAO65479, 5; AAG18017/AAG18018 and 7; AAB57691 | ||||
Sequence: A → P | ||||||
Compositional bias | 559-585 | Polar residues | ||||
Sequence: TSVSNPTIKPHSVPSHTLPSHPLTPSS | ||||||
Alternative sequence | VSP_001816 | 576-650 | in isoform C | |||
Sequence: Missing | ||||||
Sequence conflict | 616 | in Ref. 2; AAO65479, 5; AAG18017 and 7; AAB57691 | ||||
Sequence: S → R | ||||||
Sequence conflict | 624-625 | in Ref. 7; AAB57691 | ||||
Sequence: KT → PH | ||||||
Sequence conflict | 628 | in Ref. 2; AAO65479 and 7; AAB57691 | ||||
Sequence: P → A | ||||||
Sequence conflict | 630 | in Ref. 7; AAB57691 | ||||
Sequence: S → G | ||||||
Sequence conflict | 633 | in Ref. 2; AAO65479, 5; AAG18017 and 7; AAB57691 | ||||
Sequence: C → W | ||||||
Sequence conflict | 635-636 | in Ref. 7; AAB57691 | ||||
Sequence: RP → WT | ||||||
Alternative sequence | VSP_001817 | 712-771 | in isoform A and isoform D | |||
Sequence: TWQGTDLMHNHVLADDDQSSLDSLGRRSSLSRLEPSDLSEDSEYDSIWTAHSYRMGSASR → S | ||||||
Alternative sequence | VSP_023054 | 712-820 | in isoform F | |||
Sequence: TWQGTDLMHNHVLADDDQSSLDSLGRRSSLSRLEPSDLSEDSEYDSIWTAHSYRMGSASRSRKESAPQVLLPEEEKIIVEETKSNGQTVIEEKSLVDTVYALKDEVQEL → SECRSSPRVGTDYKQLLHGLAALEREVSGA | ||||||
Alternative sequence | VSP_023055 | 772-824 | in isoform E | |||
Sequence: SRKESAPQVLLPEEEKIIVEETKSNGQTVIEEKSLVDTVYALKDEVQELRQDN → KSCCSYISHQN | ||||||
Alternative sequence | VSP_023056 | 821-862 | in isoform F | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_023057 | 825-862 | in isoform E | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK129064 EMBL· GenBank· DDBJ | BAC97874.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AY220301 EMBL· GenBank· DDBJ | AAO65479.1 EMBL· GenBank· DDBJ | mRNA | ||
AK052545 EMBL· GenBank· DDBJ | BAC35033.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK139156 EMBL· GenBank· DDBJ | BAE23905.1 EMBL· GenBank· DDBJ | mRNA | ||
BC044838 EMBL· GenBank· DDBJ | AAH44838.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AF247654 EMBL· GenBank· DDBJ | AAG18017.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AF247655 EMBL· GenBank· DDBJ | AAG18018.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AF343877 EMBL· GenBank· DDBJ | AAK97363.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
U96634 EMBL· GenBank· DDBJ | AAB57691.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |