Q96N67 · DOCK7_HUMAN
- ProteinDedicator of cytokinesis protein 7
- GeneDOCK7
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2140 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Functions as a guanine nucleotide exchange factor (GEF), which activates Rac1 and Rac3 Rho small GTPases by exchanging bound GDP for free GTP. Does not have a GEF activity for CDC42. Required for STMN1 'Ser-15' phosphorylation during axon formation and consequently for neuronal polarization (PubMed:16982419).
As part of the DISP complex, may regulate the association of septins with actin and thereby regulate the actin cytoskeleton (PubMed:29467281).
Has a role in pigmentation (By similarity).
Involved in the regulation of cortical neurogenesis through the control of radial glial cells (RGCs) proliferation versus differentiation; negatively regulates the basal-to-apical interkinetic nuclear migration of RGCs by antagonizing the microtubule growth-promoting function of TACC3 (By similarity).
As part of the DISP complex, may regulate the association of septins with actin and thereby regulate the actin cytoskeleton (PubMed:29467281).
Has a role in pigmentation (By similarity).
Involved in the regulation of cortical neurogenesis through the control of radial glial cells (RGCs) proliferation versus differentiation; negatively regulates the basal-to-apical interkinetic nuclear migration of RGCs by antagonizing the microtubule growth-promoting function of TACC3 (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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Aspect | Term | |
---|---|---|
Cellular Component | axon | |
Cellular Component | basal part of cell | |
Cellular Component | focal adhesion | |
Cellular Component | growth cone | |
Cellular Component | neuron projection | |
Molecular Function | guanyl-nucleotide exchange factor activity | |
Molecular Function | small GTPase binding | |
Biological Process | activation of GTPase activity | |
Biological Process | axonogenesis | |
Biological Process | establishment of neuroblast polarity | |
Biological Process | interkinetic nuclear migration | |
Biological Process | microtubule cytoskeleton organization | |
Biological Process | negative regulation of cold-induced thermogenesis | |
Biological Process | neuron projection development | |
Biological Process | positive regulation of peptidyl-serine phosphorylation | |
Biological Process | positive regulation of vascular associated smooth muscle cell migration | |
Biological Process | regulation of neurogenesis | |
Biological Process | small GTPase-mediated signal transduction |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDedicator of cytokinesis protein 7
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ96N67
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Enriched in the developing axons of hippocampal neurons.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Developmental and epileptic encephalopathy 23 (DEE23)
- Note
- DescriptionA severe disease characterized by early-onset intractable epilepsy, dysmorphic features, intellectual disability, and cortical blindness. Brain imaging shows an abnormally marked pontobulbar sulcus with mild pontine hypoplasia, white matter abnormalities, and atrophy in the occipital lobe.
- See alsoMIM:615859
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_057524 | 824 | in dbSNP:rs35400360 | |||
Sequence: I → T |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2,364 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000189995 | 1-2140 | UniProt | Dedicator of cytokinesis protein 7 | |||
Sequence: MAERRAFAQKISRTVAAEVRKQISGQYSGSPQLLKNLNIVGNISHHTTVPLTEAVDPVDLEDYLITHPLAVDSGPLRDLIEFPPDDIEVVYSPRDCRTLVSAVPEESEMDPHVRDCIRSYTEDWAIVIRKYHKLGTGFNPNTLDKQKERQKGLPKQVFESDEAPDGNSYQDDQDDLKRRSMSIDDTPRGSWACSIFDLKNSLPDALLPNLLDRTPNEEIDRQNDDQRKSNRHKELFALHPSPDEEEPIERLSVPDIPKEHFGQRLLVKCLSLKFEIEIEPIFASLALYDVKEKKKISENFYFDLNSEQMKGLLRPHVPPAAITTLARSAIFSITYPSQDVFLVIKLEKVLQQGDIGECAEPYMIFKEADATKNKEKLEKLKSQADQFCQRLGKYRMPFAWTAIHLMNIVSSAGSLERDSTEVEISTGERKGSWSERRNSSIVGRRSLERTTSGDDACNLTSFRPATLTVTNFFKQEGDRLSDEDLYKFLADMRRPSSVLRRLRPITAQLKIDISPAPENPHYCLTPELLQVKLYPDSRVRPTREILEFPARDVYVPNTTYRNLLYIYPQSLNFANRQGSARNITVKVQFMYGEDPSNAMPVIFGKSSCSEFSKEAYTAVVYHNRSPDFHEEIKVKLPATLTDHHHLLFTFYHVSCQQKQNTPLETPVGYTWIPMLQNGRLKTGQFCLPVSLEKPPQAYSVLSPEVPLPGMKWVDNHKGVFNVEVVAVSSIHTQDPYLDKFFALVNALDEHLFPVRIGDMRIMENNLENELKSSISALNSSQLEPVVRFLHLLLDKLILLVIRPPVIAGQIVNLGQASFEAMASIINRLHKNLEGNHDQHGRNSLLASYIHYVFRLPNTYPNSSSPGPGGLGGSVHYATMARSAVRPASLNLNRSRSLSNSNPDISGTPTSPDDEVRSIIGSKGLDRSNSWVNTGGPKAAPWGSNPSPSAESTQAMDRSCNRMSSHTETSSFLQTLTGRLPTKKLFHEELALQWVVCSGSVRESALQQAWFFFELMVKSMVHHLYFNDKLEAPRKSRFPERFMDDIAALVSTIASDIVSRFQKDTEMVERLNTSLAFFLNDLLSVMDRGFVFSLIKSCYKQVSSKLYSLPNPSVLVSLRLDFLRIICSHEHYVTLNLPCSLLTPPASPSPSVSSATSQSSGFSTNVQDQKIANMFELSVPFRQQHYLAGLVLTELAVILDPDAEGLFGLHKKVINMVHNLLSSHDSDPRYSDPQIKARVAMLYLPLIGIIMETVPQLYDFTETHNQRGRPICIATDDYESESGSMISQTVAMAIAGTSVPQLTRPGSFLLTSTSGRQHTTFSAESSRSLLICLLWVLKNADETVLQKWFTDLSVLQLNRLLDLLYLCVSCFEYKGKKVFERMNSLTFKKSKDMRAKLEEAILGSIGARQEMVRRSRGQLGTYTIASPPERSPSGSAFGSQENLRWRKDMTHWRQNTEKLDKSRAEIEHEALIDGNLATEANLIILDTLEIVVQTVSVTESKESILGGVLKVLLHSMACNQSAVYLQHCFATQRALVSKFPELLFEEETEQCADLCLRLLRHCSSSIGTIRSHASASLYLLMRQNFEIGNNFARVKMQVTMSLSSLVGTSQNFNEEFLRRSLKTILTYAEEDLELRETTFPDQVQDLVFNLHMILSDTVKMKEHQEDPEMLIDLMYRIAKGYQTSPDLRLTWLQNMAGKHSERSNHAEAAQCLVHSAALVAEYLSMLEDRKYLPVGCVTFQNISSNVLEESAVSDDVVSPDEEGICSGKYFTESGLVGLLEQAAASFSMAGMYEAVNEVYKVLIPIHEANRDAKKLSTIHGKLQEAFSKIVHQSTGWERMFGTYFRVGFYGTKFGDLDEQEFVYKEPAITKLAEISHRLEGFYGERFGEDVVEVIKDSNPVDKCKLDPNKAYIQITYVEPYFDTYEMKDRITYFDKNYNLRRFMYCTPFTLDGRAHGELHEQFKRKTILTTSHAFPYIKTRVNVTHKEEIILTPIEVAIEDMQKKTQELAFATHQDPADPKMLQMVLQGSVGTTVNQGPLEVAQVFLSEIPSDPKLFRHHNKLRLCFKDFTKRCEDALRKNKSLIGPDQKEYQRELERNYHRLKEALQPLINRKIPQLYKAVLPVTCHRDSFSRMSLRKMDL | |||||||
Modified residue (large scale data) | 27 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 28 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 30 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 30 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 136 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 142 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 180 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 180 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 182 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 182 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 190 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 214 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 381 | UniProt | N6-methyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 414 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 439 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 440 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 446 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 450 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 451 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 452 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 452 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 862 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 862 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 863 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 864 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 864 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 873 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 878 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 882 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 882 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 888 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 888 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 894 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 896 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 896 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 898 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 900 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 900 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 905 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 905 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 907 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 907 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 909 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 909 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 910 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 910 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 917 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 929 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 929 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 946 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 948 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 963 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 964 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 964 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 966 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1306 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1383 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1383 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1390 | UniProt | In isoform Q96N67-3; Phosphoserine | ||||
Sequence: K | |||||||
Modified residue | 1390 | UniProt | In isoform Q96N67-4; Phosphoserine | ||||
Sequence: K | |||||||
Modified residue | 1394 | UniProt | In isoform Q96N67-3; Phosphoserine | ||||
Sequence: A | |||||||
Modified residue | 1394 | UniProt | In isoform Q96N67-4; Phosphoserine | ||||
Sequence: A | |||||||
Modified residue | 1398 | UniProt | In isoform Q96N67-3; Phosphoserine | ||||
Sequence: E | |||||||
Modified residue | 1398 | UniProt | In isoform Q96N67-4; Phosphoserine | ||||
Sequence: E | |||||||
Modified residue (large scale data) | 1403 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1421 | UniProt | In isoform Q96N67-2; Phosphoserine | ||||
Sequence: Y | |||||||
Modified residue | 1421 | UniProt | In isoform Q96N67-6; Phosphoserine | ||||
Sequence: Y | |||||||
Modified residue | 1425 | UniProt | In isoform Q96N67-2; Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1425 | UniProt | In isoform Q96N67-6; Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1425 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1429 | UniProt | In isoform Q96N67-2; Phosphoserine | ||||
Sequence: R | |||||||
Modified residue | 1429 | UniProt | In isoform Q96N67-6; Phosphoserine | ||||
Sequence: R | |||||||
Modified residue | 1430 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1430 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1432 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1432 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1434 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1434 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1438 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1438 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1962 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 2124 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 2129 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2129 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2131 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2134 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Component of the DOCK7-induced septin displacement/DISP complex, at least composed of DOCK7, LRCH3 and MYO6 (PubMed:29467281).
Interacts with TSC1. Interacts with nucleotide-free RAC1 and RAC3. Interacts with TACC3 and CRY1 (By similarity).
Interacts with NOD2 (PubMed:27812135).
Interacts with TSC1. Interacts with nucleotide-free RAC1 and RAC3. Interacts with TACC3 and CRY1 (By similarity).
Interacts with NOD2 (PubMed:27812135).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q96N67 | LRCH1 Q9Y2L9 | 6 | EBI-2433703, EBI-2797324 | |
BINARY | Q96N67 | LRCH3 Q96II8 | 13 | EBI-2433703, EBI-8795942 | |
BINARY | Q96N67 | LRCH4 O75427 | 2 | EBI-2433703, EBI-718707 | |
BINARY | Q96N67 | NBEAL2 Q6ZNJ1 | 8 | EBI-2433703, EBI-2862306 | |
BINARY | Q96N67 | SEC16A O15027 | 3 | EBI-2433703, EBI-357515 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, coiled coil, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 138-183 | Disordered | ||||
Sequence: FNPNTLDKQKERQKGLPKQVFESDEAPDGNSYQDDQDDLKRRSMSI | ||||||
Compositional bias | 144-158 | Basic and acidic residues | ||||
Sequence: DKQKERQKGLPKQVF | ||||||
Coiled coil | 365-395 | |||||
Sequence: FKEADATKNKEKLEKLKSQADQFCQRLGKYR | ||||||
Domain | 561-727 | C2 DOCK-type | ||||
Sequence: RNLLYIYPQSLNFANRQGSARNITVKVQFMYGEDPSNAMPVIFGKSSCSEFSKEAYTAVVYHNRSPDFHEEIKVKLPATLTDHHHLLFTFYHVSCQQKQNTPLETPVGYTWIPMLQNGRLKTGQFCLPVSLEKPPQAYSVLSPEVPLPGMKWVDNHKGVFNVEVVAV | ||||||
Compositional bias | 888-914 | Polar residues | ||||
Sequence: SLNLNRSRSLSNSNPDISGTPTSPDDE | ||||||
Region | 888-971 | Disordered | ||||
Sequence: SLNLNRSRSLSNSNPDISGTPTSPDDEVRSIIGSKGLDRSNSWVNTGGPKAAPWGSNPSPSAESTQAMDRSCNRMSSHTETSSF | ||||||
Compositional bias | 944-971 | Polar residues | ||||
Sequence: NPSPSAESTQAMDRSCNRMSSHTETSSF | ||||||
Domain | 1678-2114 | DOCKER | ||||
Sequence: KGYQTSPDLRLTWLQNMAGKHSERSNHAEAAQCLVHSAALVAEYLSMLEDRKYLPVGCVTFQNISSNVLEESAVSDDVVSPDEEGICSGKYFTESGLVGLLEQAAASFSMAGMYEAVNEVYKVLIPIHEANRDAKKLSTIHGKLQEAFSKIVHQSTGWERMFGTYFRVGFYGTKFGDLDEQEFVYKEPAITKLAEISHRLEGFYGERFGEDVVEVIKDSNPVDKCKLDPNKAYIQITYVEPYFDTYEMKDRITYFDKNYNLRRFMYCTPFTLDGRAHGELHEQFKRKTILTTSHAFPYIKTRVNVTHKEEIILTPIEVAIEDMQKKTQELAFATHQDPADPKMLQMVLQGSVGTTVNQGPLEVAQVFLSEIPSDPKLFRHHNKLRLCFKDFTKRCEDALRKNKSLIGPDQKEYQRELERNYHRLKEALQPLINRKIP | ||||||
Coiled coil | 2086-2112 | |||||
Sequence: DQKEYQRELERNYHRLKEALQPLINRK |
Domain
The DOCKER domain mediates GEF activity.
Sequence similarities
Belongs to the DOCK family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 7 isoforms produced by Alternative splicing.
Q96N67-1
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
- Length2,140
- Mass (Da)242,561
- Last updated2007-01-09 v4
- ChecksumA14857DCB9C3AE6E
Q96N67-2
- Name2
- Differences from canonical
- 1419-1427: Missing
- 1832-1836: STGWE → DGK
Q96N67-3
- Name3
- Differences from canonical
- 923-953: Missing
- 1419-1427: Missing
Q96N67-4
- Name4
- Differences from canonical
- 923-953: Missing
- 1419-1427: Missing
- 1832-1836: STGWE → DGK
Q96N67-5
- Name5
- Differences from canonical
- 923-953: Missing
Q96N67-6
- Name6
- Differences from canonical
- 1419-1427: Missing
Q96N67-7
- Name7
Computationally mapped potential isoform sequences
There are 9 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0U1RQJ5 | A0A0U1RQJ5_HUMAN | DOCK7 | 255 | ||
A0A0U1RR97 | A0A0U1RR97_HUMAN | DOCK7 | 101 | ||
A0A0U1RQT6 | A0A0U1RQT6_HUMAN | DOCK7 | 173 | ||
A0A0U1RQG7 | A0A0U1RQG7_HUMAN | DOCK7 | 46 | ||
A0A0U1RRC1 | A0A0U1RRC1_HUMAN | DOCK7 | 248 | ||
A0A1B0GUE9 | A0A1B0GUE9_HUMAN | DOCK7 | 602 | ||
A0A1B0GWE0 | A0A1B0GWE0_HUMAN | DOCK7 | 1229 | ||
A0A1B0GVW2 | A0A1B0GVW2_HUMAN | DOCK7 | 443 | ||
A0A0C4DGY6 | A0A0C4DGY6_HUMAN | DOCK7 | 245 |
Sequence caution
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 144-158 | Basic and acidic residues | ||||
Sequence: DKQKERQKGLPKQVF | ||||||
Alternative sequence | VSP_054534 | 601-632 | in isoform 7 | |||
Sequence: VIFGKSSCSEFSKEAYTAVVYHNRSPDFHEEI → SPSCTHPIPTVRPLPLWCYHSIFSLLSWDFIT | ||||||
Alternative sequence | VSP_054535 | 633-2140 | in isoform 7 | |||
Sequence: Missing | ||||||
Sequence conflict | 750 | in Ref. 2; BAC86032 | ||||
Sequence: H → R | ||||||
Compositional bias | 888-914 | Polar residues | ||||
Sequence: SLNLNRSRSLSNSNPDISGTPTSPDDE | ||||||
Alternative sequence | VSP_012440 | 923-953 | in isoform 3, isoform 4 and isoform 5 | |||
Sequence: Missing | ||||||
Compositional bias | 944-971 | Polar residues | ||||
Sequence: NPSPSAESTQAMDRSCNRMSSHTETSSF | ||||||
Alternative sequence | VSP_022240 | 1419-1427 | in isoform 2, isoform 3, isoform 4 and isoform 6 | |||
Sequence: Missing | ||||||
Sequence conflict | 1440 | in Ref. 2; BAC86032 | ||||
Sequence: E → G | ||||||
Sequence conflict | 1520 | in Ref. 2; BAB70933 | ||||
Sequence: S → N | ||||||
Sequence conflict | 1521 | in Ref. 2; BAC86032 | ||||
Sequence: A → V | ||||||
Sequence conflict | 1639 | in Ref. 2; BAC86032 | ||||
Sequence: P → L | ||||||
Alternative sequence | VSP_007707 | 1832-1836 | in isoform 2 and isoform 4 | |||
Sequence: STGWE → DGK | ||||||
Sequence conflict | 1859 | in Ref. 2; BAB70933 | ||||
Sequence: E → K | ||||||
Sequence conflict | 1908 | in Ref. 2; BAB71042 | ||||
Sequence: K → T |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DQ341187 EMBL· GenBank· DDBJ | ABC68221.1 EMBL· GenBank· DDBJ | mRNA | ||
AK055401 EMBL· GenBank· DDBJ | BAB70917.1 EMBL· GenBank· DDBJ | mRNA | ||
AK055493 EMBL· GenBank· DDBJ | BAB70933.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK055905 EMBL· GenBank· DDBJ | BAB71042.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AK125049 EMBL· GenBank· DDBJ | BAC86032.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK292640 EMBL· GenBank· DDBJ | BAF85329.1 EMBL· GenBank· DDBJ | mRNA | ||
AC096946 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC103923 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL138847 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL451044 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471059 EMBL· GenBank· DDBJ | EAX06582.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DQ309763 EMBL· GenBank· DDBJ | ABC33725.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
DQ118679 EMBL· GenBank· DDBJ | AAZ38451.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ118680 EMBL· GenBank· DDBJ | AAZ38452.1 EMBL· GenBank· DDBJ | mRNA | ||
AB051558 EMBL· GenBank· DDBJ | BAB21862.1 EMBL· GenBank· DDBJ | mRNA | ||
BC016392 EMBL· GenBank· DDBJ | AAH16392.2 EMBL· GenBank· DDBJ | mRNA | Frameshift |