Q8TAA9 · VANG1_HUMAN
- ProteinVang-like protein 1
- GeneVANGL1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids524 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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 | lateral plasma membrane | |
Cellular Component | plasma membrane | |
Biological Process | pigmentation | |
Biological Process | Wnt signaling pathway, planar cell polarity pathway |
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameVang-like protein 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8TAA9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-117 | Cytoplasmic | ||||
Sequence: MDTESTYSGYSYYSSHSKKSHRQGERTRERHKSPRNKDGRGSEKSVTIQPPTGEPLLGNDSTRTEEVQDDNWGETTTAITGTSEHSISQEDIARISKDMEDSVGLDCKRYLGLTVAS | ||||||
Transmembrane | 118-138 | Helical; Name=1 | ||||
Sequence: FLGLLVFLTPIAFILLPPILW | ||||||
Topological domain | 139-151 | Extracellular | ||||
Sequence: RDELEPCGTICEG | ||||||
Transmembrane | 152-172 | Helical; Name=2 | ||||
Sequence: LFISMAFKLLILLIGTWALFF | ||||||
Topological domain | 173-182 | Cytoplasmic | ||||
Sequence: RKRRADMPRV | ||||||
Transmembrane | 183-203 | Helical; Name=3 | ||||
Sequence: FVFRALLLVLIFLFVVSYWLF | ||||||
Topological domain | 204-222 | Extracellular | ||||
Sequence: YGVRILDSRDRNYQGIVQY | ||||||
Transmembrane | 223-243 | Helical; Name=4 | ||||
Sequence: AVSLVDALLFIHYLAIVLLEL | ||||||
Topological domain | 244-524 | Cytoplasmic | ||||
Sequence: RQLQPMFTLQVVRSTDGESRFYSLGHLSIQRAALVVLENYYKDFTIYNPNLLTASKFRAAKHMAGLKVYNVDGPSNNATGQSRAMIAAAARRRDSSHNELYYEEAEHERRVKKRKARLVVAVEEAFIHIQRLQAEEQQKAPGEVMDPREAAQAIFPSMARALQKYLRITRQQNYHSMESILQHLAFCITNGMTPKAFLERYLSAGPTLQYDKDRWLSTQWRLVSDEAVTNGLRDGIVFVLKCLDFSLVVNVKKIPFIILSEEFIDPKSHKFVLRLQSETSV |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Neural tube defects (NTD)
- Note
- DescriptionCongenital malformations of the central nervous system and adjacent structures related to defective neural tube closure during the first trimester of pregnancy. Failure of neural tube closure can occur at any level of the embryonic axis. Common NTD forms include anencephaly, myelomeningocele and spina bifida, which result from the failure of fusion in the cranial and spinal region of the neural tube. NTDs have a multifactorial etiology encompassing both genetic and environmental components.
- See alsoMIM:182940
Natural variants in NTD
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_062322 | 83 | S>L | in NTD; uncertain significance; dbSNP:rs146695372 | |
VAR_062323 | 153 | F>S | in NTD; uncertain significance | |
VAR_062325 | 181 | R>Q | in NTD; uncertain significance; dbSNP:rs761123443 | |
VAR_062326 | 202 | L>F | in NTD; uncertain significance | |
VAR_035210 | 274 | R>Q | in NTD; does not abolish ability to interact with DVL1, DVL2 and DVL3; dbSNP:rs121918219 | |
VAR_035211 | 328 | M>T | in NTD; does not abolish ability to interact with DVL1, DVL2 and DVL3; dbSNP:rs121918220 | |
VAR_062329 | 404 | A>S | in NTD; uncertain significance; dbSNP:rs775571796 |
Sacral defect with anterior meningocele (SDAM)
- Note
- DescriptionForm of caudal dysgenesis. It is present at birth and becomes symptomatic later in life, usually because of obstructive labor in females, chronic constipation, or meningitis. Inheritance is autosomal dominant.
- See alsoMIM:600145
Natural variants in SDAM
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_035209 | 239 | V>I | in SDAM; abolishes ability to interact with DVL1, DVL2 and DVL3; dbSNP:rs121918218 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_062321 | 25 | in dbSNP:rs61734296 | |||
Sequence: E → K | ||||||
Natural variant | VAR_062322 | 83 | in NTD; uncertain significance; dbSNP:rs146695372 | |||
Sequence: S → L | ||||||
Natural variant | VAR_027143 | 116 | in dbSNP:rs4839469 | |||
Sequence: A → T | ||||||
Natural variant | VAR_062323 | 153 | in NTD; uncertain significance | |||
Sequence: F → S | ||||||
Natural variant | VAR_062324 | 175 | in dbSNP:rs201441696 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_062325 | 181 | in NTD; uncertain significance; dbSNP:rs761123443 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_062326 | 202 | in NTD; uncertain significance | |||
Sequence: L → F | ||||||
Natural variant | VAR_035209 | 239 | in SDAM; abolishes ability to interact with DVL1, DVL2 and DVL3; dbSNP:rs121918218 | |||
Sequence: V → I | ||||||
Natural variant | VAR_062327 | 251 | in dbSNP:rs201630629 | |||
Sequence: T → M | ||||||
Natural variant | VAR_035210 | 274 | in NTD; does not abolish ability to interact with DVL1, DVL2 and DVL3; dbSNP:rs121918219 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_062328 | 290 | in dbSNP:rs145309218 | |||
Sequence: Y → H | ||||||
Natural variant | VAR_035211 | 328 | in NTD; does not abolish ability to interact with DVL1, DVL2 and DVL3; dbSNP:rs121918220 | |||
Sequence: M → T | ||||||
Natural variant | VAR_035435 | 347 | in dbSNP:rs34059106 | |||
Sequence: E → A | ||||||
Natural variant | VAR_062329 | 404 | in NTD; uncertain significance; dbSNP:rs775571796 | |||
Sequence: A → S | ||||||
Natural variant | VAR_062330 | 468 | ||||
Sequence: D → E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 703 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_0000186193 | 1-524 | UniProt | Vang-like protein 1 | |||
Sequence: MDTESTYSGYSYYSSHSKKSHRQGERTRERHKSPRNKDGRGSEKSVTIQPPTGEPLLGNDSTRTEEVQDDNWGETTTAITGTSEHSISQEDIARISKDMEDSVGLDCKRYLGLTVASFLGLLVFLTPIAFILLPPILWRDELEPCGTICEGLFISMAFKLLILLIGTWALFFRKRRADMPRVFVFRALLLVLIFLFVVSYWLFYGVRILDSRDRNYQGIVQYAVSLVDALLFIHYLAIVLLELRQLQPMFTLQVVRSTDGESRFYSLGHLSIQRAALVVLENYYKDFTIYNPNLLTASKFRAAKHMAGLKVYNVDGPSNNATGQSRAMIAAAARRRDSSHNELYYEEAEHERRVKKRKARLVVAVEEAFIHIQRLQAEEQQKAPGEVMDPREAAQAIFPSMARALQKYLRITRQQNYHSMESILQHLAFCITNGMTPKAFLERYLSAGPTLQYDKDRWLSTQWRLVSDEAVTNGLRDGIVFVLKCLDFSLVVNVKKIPFIILSEEFIDPKSHKFVLRLQSETSV | |||||||
Modified residue (large scale data) | 7 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 8 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 10 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 12 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 14 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 15 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 17 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 45 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 47 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 86 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 86 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 88 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 88 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 96 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 296 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 312 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 322 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 325 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 338 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 520 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 523 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Heterodimer with VANGL2. Interacts through its C-terminal region with the N-terminal half of DVL1, DVL2 and DVL3. The PDZ domain of DVL1, DVL2 and DVL3 is required for the interaction (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8TAA9 | CD82 P27701 | 6 | EBI-682393, EBI-682379 | |
BINARY | Q8TAA9 | CREB3 O43889-2 | 3 | EBI-682393, EBI-625022 | |
BINARY | Q8TAA9 | PTPN3 P26045 | 4 | EBI-682393, EBI-1047946 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-17 | Polar residues | ||||
Sequence: MDTESTYSGYSYYSSHS | ||||||
Region | 1-85 | Disordered | ||||
Sequence: MDTESTYSGYSYYSSHSKKSHRQGERTRERHKSPRNKDGRGSEKSVTIQPPTGEPLLGNDSTRTEEVQDDNWGETTTAITGTSEH | ||||||
Compositional bias | 18-42 | Basic and acidic residues | ||||
Sequence: KKSHRQGERTRERHKSPRNKDGRGS | ||||||
Compositional bias | 43-62 | Polar residues | ||||
Sequence: EKSVTIQPPTGEPLLGNDST | ||||||
Compositional bias | 71-85 | Polar residues | ||||
Sequence: NWGETTTAITGTSEH |
Sequence similarities
Belongs to the Vang family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q8TAA9-1
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
- Length524
- Mass (Da)59,975
- Last updated2002-06-01 v1
- Checksum65CB263D26274585
Q8TAA9-2
- Name2
- Differences from canonical
- 67-68: Missing
Sequence caution
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-17 | Polar residues | ||||
Sequence: MDTESTYSGYSYYSSHS | ||||||
Compositional bias | 18-42 | Basic and acidic residues | ||||
Sequence: KKSHRQGERTRERHKSPRNKDGRGS | ||||||
Compositional bias | 43-62 | Polar residues | ||||
Sequence: EKSVTIQPPTGEPLLGNDST | ||||||
Alternative sequence | VSP_008742 | 67-68 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 71-85 | Polar residues | ||||
Sequence: NWGETTTAITGTSEH |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB075805 EMBL· GenBank· DDBJ | BAB86362.1 EMBL· GenBank· DDBJ | mRNA | ||
AB057596 EMBL· GenBank· DDBJ | BAB86334.1 EMBL· GenBank· DDBJ | mRNA | ||
AF481859 EMBL· GenBank· DDBJ | AAO61751.1 EMBL· GenBank· DDBJ | mRNA | ||
AL450389 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471122 EMBL· GenBank· DDBJ | EAW56630.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471122 EMBL· GenBank· DDBJ | EAW56631.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC032773 EMBL· GenBank· DDBJ | AAH32773.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC065272 EMBL· GenBank· DDBJ | AAH65272.1 EMBL· GenBank· DDBJ | mRNA |