B2RY04 · DOCK5_MOUSE
- ProteinDedicator of cytokinesis protein 5
- GeneDock5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1868 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Guanine nucleotide exchange factor (GEF) for Rho and Rac. GEF proteins activate small GTPases by exchanging bound GDP for free GTP (PubMed:18396277).
Along with DOCK1, mediates CRK/CRKL regulation of epithelial and endothelial cell spreading and migration on type IV collagen (By similarity).
Along with DOCK1, mediates CRK/CRKL regulation of epithelial and endothelial cell spreading and migration on type IV collagen (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 | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | anchoring junction | |
Cellular Component | cell projection | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | plasma membrane | |
Cellular Component | podosome | |
Molecular Function | GTPase activator activity | |
Molecular Function | guanyl-nucleotide exchange factor activity | |
Molecular Function | small GTPase binding | |
Biological Process | bone remodeling | |
Biological Process | cell migration | |
Biological Process | myoblast fusion | |
Biological Process | negative regulation of vascular associated smooth muscle contraction | |
Biological Process | podosome assembly | |
Biological Process | positive regulation of epithelial cell migration | |
Biological Process | positive regulation of substrate adhesion-dependent cell spreading | |
Biological Process | positive regulation of vascular associated smooth muscle cell migration | |
Biological Process | Rac protein signal transduction |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDedicator of cytokinesis protein 5
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionB2RY04
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Associated with the edge of the plasma membrane in intestinal epithelial cells spreading on type IV collagen.
Keywords
- Cellular component
Phenotypes & Variants
Involvement in disease
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 94 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000358858 | 1-1868 | Dedicator of cytokinesis protein 5 | |||
Sequence: MARWIPTKRQKYGVAIYNYNASQDVELSLQIGDTVHILEMYEGWYRGYALQNRSKKGIFPETYIHLKEATVEDGGQHETVIPGELPLVQELTNTLREWAVIWRKLYVNNKVTLFRQLQQMTYSLIEWRSQILSGTLPKDELAELKKKVTAKIDHGNRMLGLDLVVRDDNGNILDPDETSTVALFRAHEVASKRIEEKIQEEKSILQNLDLRGQAIFSTVHTYGLYVNFKNFVCNIGEDAELFIALYDPDQSTFISENYLIRWGSNGMPKEIEKLNNLQAVFTDLSSTDLIRPRISLVCQIVRVGRMELKEGKKHTCGLRRPFGVAVMDISDIVHGKVDDEEKQHFIPFQQIAMETYIRQRQLIMSPLITSHVIGENEPLTSVLNKVIAAKEVNHKGQGLWVSLKLLPGDLTQVQKNFSHLVDRSTAIARKMGFPEIILPGDVRNDIYVTLIHGEFDKGKKKTPKNVEVTMSVFDEEGNLLEKAIHPGAGYEGVSEYKSVVYYQVKQPCWYETVKVFIAIEEVTRCHIRFTFRHRSSQESRDKSERAFGVAFVKLMNADGTTLQDGRHDLVVYKGDNKKMEDAKYYLTLPGTKAELEEKELQASKNPSVFTPSKDSTKDSFQIATLICSTKLTQNVDLLGLLNWRSNSQNIKHNLKKLMEVDGGEIVKFLQDTLDALFNIMMEMSDNETYDFLVFDALVFIISLIGDIKFQHFNPVLETYIYKHFSATLAHVKLSKVLNFYVANAEDPSKTELLFAALKALKYLFRFIIQSRVLYLRFYGQSEDGDEFNDSIRQLFLAFNTLMDRPLEEAVKIKGAALKYLPSIINDVKLVFDPMELSVLFCKFIQSIPDNQLVRQKLNCMTKIVESSLFQQAECREVLLPLLTDQLSGQLDDHSTKPDHEASSQLLSNILEVLDRTDVGPTSAHVQLIMERLLRRINRTVIGMSRQSPHIGSFVACMIAVLRQMEDSHYSHYISTFKTRQDIIDFLMETFIMFKDLIGKNVYAKDWMVMNMTQNRVFLRAINQFAEVLTKSFMDQASFELQLWNNYFHLAVAFLTHESLQLETFSEAKRNKIVKKYGDMRKEIGFRIRDMWYNLGPHKIKFIPSMVGPILEVTLTPEVELRKATIPIFFDMMQCEFNLSGNGNFHMFENELITKLDQEVEGGRGDEQYKVLLEKLLLEHCRKHKYLANSGEAFAFLVSSLLENLLDYRTIIIHDESKENRMSCTVNVLNFYKDKKREDIYIRYLYKLRDLHRDCENYTEAAYTLLLHAELLQWSDKPCVPHLLQRDSYYVYTQQELKEKLYQEIISYFDKGKMWEKAIKLSKELAETYESKVFDYEGLGSLLKKRALFYENIIKAMRPQPEYFAVGYYGQGFPSFLRNKIFIYRGKEYERREDFSLRLLTQFPNAEKMTSTTPPGEDIKSSPKQYLQCFTVKPVMSLPPSYKDKPVPEQILNYYRANEVQQFSYSRPFRKGEKDPENEFATMWIERTTYRTAYTFPGILKWFEAKEISVEEISPLENAIETMELTNERVSNCVQQHAWDHSLSVHPLSMLLSGIVDPAVMGGFSNYEKAFFTEKYLQEHPEDQEKVELLKRLIALQIPLLTEGIRIHGEKLTEQLKPLHARLSSCFRELKEKVEKLYGVITLPPSMTERKPSRAGSMVLPYILSSTLRRLSVTSVASSVISTSSNSSDNASSRPGSDGSILEPLFERRASSGARVEDLPPKEDSENRISKFKRKDWNLSKSQVIAEKAPEPDVMSPGKKTQRPKSLQLVDSRLTPFHSPSPLQSTALSPPPLTPKATRTLSSPSLQTDGLTASVPPPPPPKSKPYESSQRNSAEIAPPLPVRRDSKAPPPPPPKARKSGILSSEPGSQ | ||||||
Modified residue | 365 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 818 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 1755 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1765 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1771 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1784 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1788 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1793 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1832 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1867 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in lens, where it predominantly localizes to anterior epithelial cells, and is weakly expressed in lens fiber (at protein level). Expressed in brain, eye, lung, spleen and kidney, but not in thymus or peripheral blood leukocytes.
Developmental stage
In the lens, expressed from 15.5 dpc to maturity (PubMed:18396277).
Expression increases during osteoclast differentiation (PubMed:27505886).
Expression increases during osteoclast differentiation (PubMed:27505886).
Gene expression databases
Interaction
Subunit
Interacts with CRK and CRKL (By similarity).
Interacts (via N-terminus) with tensin TNS3 (via N-terminus); the interaction increases DOCK5 guanine nucleotide exchange activity towards Rac (PubMed:27505886).
Interacts with ELMO1 (PubMed:27505886).
Interacts (via N-terminus) with tensin TNS3 (via N-terminus); the interaction increases DOCK5 guanine nucleotide exchange activity towards Rac (PubMed:27505886).
Interacts with ELMO1 (PubMed:27505886).
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 8-69 | SH3 | ||||
Sequence: KRQKYGVAIYNYNASQDVELSLQIGDTVHILEMYEGWYRGYALQNRSKKGIFPETYIHLKEA | ||||||
Domain | 443-627 | C2 DOCK-type | ||||
Sequence: RNDIYVTLIHGEFDKGKKKTPKNVEVTMSVFDEEGNLLEKAIHPGAGYEGVSEYKSVVYYQVKQPCWYETVKVFIAIEEVTRCHIRFTFRHRSSQESRDKSERAFGVAFVKLMNADGTTLQDGRHDLVVYKGDNKKMEDAKYYLTLPGTKAELEEKELQASKNPSVFTPSKDSTKDSFQIATLIC | ||||||
Domain | 1231-1642 | DOCKER | ||||
Sequence: YKDKKREDIYIRYLYKLRDLHRDCENYTEAAYTLLLHAELLQWSDKPCVPHLLQRDSYYVYTQQELKEKLYQEIISYFDKGKMWEKAIKLSKELAETYESKVFDYEGLGSLLKKRALFYENIIKAMRPQPEYFAVGYYGQGFPSFLRNKIFIYRGKEYERREDFSLRLLTQFPNAEKMTSTTPPGEDIKSSPKQYLQCFTVKPVMSLPPSYKDKPVPEQILNYYRANEVQQFSYSRPFRKGEKDPENEFATMWIERTTYRTAYTFPGILKWFEAKEISVEEISPLENAIETMELTNERVSNCVQQHAWDHSLSVHPLSMLLSGIVDPAVMGGFSNYEKAFFTEKYLQEHPEDQEKVELLKRLIALQIPLLTEGIRIHGEKLTEQLKPLHARLSSCFRELKEKVEKLYGVITL | ||||||
Compositional bias | 1681-1696 | Polar residues | ||||
Sequence: STSSNSSDNASSRPGS | ||||||
Region | 1681-1730 | Disordered | ||||
Sequence: STSSNSSDNASSRPGSDGSILEPLFERRASSGARVEDLPPKEDSENRISK | ||||||
Compositional bias | 1709-1730 | Basic and acidic residues | ||||
Sequence: ASSGARVEDLPPKEDSENRISK | ||||||
Region | 1742-1868 | Disordered | ||||
Sequence: QVIAEKAPEPDVMSPGKKTQRPKSLQLVDSRLTPFHSPSPLQSTALSPPPLTPKATRTLSSPSLQTDGLTASVPPPPPPKSKPYESSQRNSAEIAPPLPVRRDSKAPPPPPPKARKSGILSSEPGSQ | ||||||
Compositional bias | 1760-1811 | Polar residues | ||||
Sequence: TQRPKSLQLVDSRLTPFHSPSPLQSTALSPPPLTPKATRTLSSPSLQTDGLT | ||||||
Compositional bias | 1842-1856 | Pro residues | ||||
Sequence: RRDSKAPPPPPPKAR |
Domain
The DOCKER domain may mediate some GEF activity.
Sequence similarities
Belongs to the DOCK family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,868
- Mass (Da)214,429
- Last updated2011-07-27 v2
- ChecksumD4AB0D8CD588F73D
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 49 | in Ref. 2; AAI58047/AAI58136/AAI58139 | ||||
Sequence: A → R | ||||||
Compositional bias | 1681-1696 | Polar residues | ||||
Sequence: STSSNSSDNASSRPGS | ||||||
Compositional bias | 1709-1730 | Basic and acidic residues | ||||
Sequence: ASSGARVEDLPPKEDSENRISK | ||||||
Compositional bias | 1760-1811 | Polar residues | ||||
Sequence: TQRPKSLQLVDSRLTPFHSPSPLQSTALSPPPLTPKATRTLSSPSLQTDGLT | ||||||
Compositional bias | 1842-1856 | Pro residues | ||||
Sequence: RRDSKAPPPPPPKAR |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC090431 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC093020 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC158046 EMBL· GenBank· DDBJ | AAI58047.1 EMBL· GenBank· DDBJ | mRNA | ||
BC158135 EMBL· GenBank· DDBJ | AAI58136.1 EMBL· GenBank· DDBJ | mRNA | ||
BC158138 EMBL· GenBank· DDBJ | AAI58139.1 EMBL· GenBank· DDBJ | mRNA |