Q8TDJ6 · DMXL2_HUMAN
- ProteinDmX-like protein 2
- GeneDMXL2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids3036 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May serve as a scaffold protein for MADD and RAB3GA on synaptic vesicles (PubMed:11809763).
Plays a role in the brain as a key controller of neuronal and endocrine homeostatic processes (By similarity).
Plays a role in the brain as a key controller of neuronal and endocrine homeostatic processes (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 | extracellular space | |
Cellular Component | neuronal dense core vesicle | |
Cellular Component | RAVE complex | |
Cellular Component | synaptic vesicle | |
Cellular Component | synaptic vesicle membrane | |
Molecular Function | small GTPase binding | |
Biological Process | vacuolar acidification |
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameDmX-like protein 2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8TDJ6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane ; Peripheral membrane protein
Note: The external layer of the inferior boundary for the hypothalamus part of the human brain (the so called median eminence (ME)) displayed a punctate pattern of expression; expression also observed in the cell bodies lining the third ventricle, in the long processes extending from these cell bodies toward the external layer of the ME, in small clear vesicles, and in large dense core vesicles.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Polyendocrine-polyneuropathy syndrome (PEPNS)
- Note
- DescriptionA progressive endocrine and neurodevelopmental disorder manifesting early in childhood with growth retardation and recurrent episodes of profound asymptomatic hypoglycemia. PEPNS is characterized by central hypothyroidism, hypogonadotropic hypogonadism, incomplete puberty, progressive non-autoimmune insulin-dependent diabetes mellitus, peripheral demyelinating sensorimotor polyneuropathy, and cerebellar and pyramidal signs.
- See alsoMIM:616113
Natural variants in PEPNS
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_072642 | 1942-1946 | missing | in PEPNS |
Deafness, autosomal dominant, 71 (DFNA71)
- Note
- DescriptionA form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. DFNA71 is characterized by bilateral mild to moderate hearing loss before age 20 years, which gradually progresses to severe to profound hearing loss.
- See alsoMIM:617605
Natural variants in DFNA71
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_079484 | 2417 | R>H | in DFNA71 |
Developmental and epileptic encephalopathy 81 (DEE81)
- Note
- DescriptionA form of epileptic encephalopathy, a heterogeneous group of severe early-onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. DEE81 is an autosomal recessive form characterized by onset soon after birth, little developmental progress with no eye contact and no motor or cognitive development. Other features may include facial dysmorphism, such as hypotonic facies and epicanthal folds, as well as sensorineural hearing loss and peripheral neuropathy.
- See alsoMIM:618663
Natural variants in DEE81
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_083446 | 1493-3036 | missing | in DEE81 | |
VAR_083447 | 1712 | A>V | in DEE81; dbSNP:rs372749193 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_062094 | 144 | in dbSNP:rs35097381 | |||
Sequence: E → Q | ||||||
Natural variant | VAR_057593 | 497 | in dbSNP:rs17524906 | |||
Sequence: T → M | ||||||
Natural variant | VAR_057594 | 903 | in dbSNP:rs16953073 | |||
Sequence: N → D | ||||||
Natural variant | VAR_057595 | 1288 | in dbSNP:rs12102203 | |||
Sequence: S → P | ||||||
Natural variant | VAR_057596 | 1481 | in dbSNP:rs35349640 | |||
Sequence: D → G | ||||||
Natural variant | VAR_083446 | 1493-3036 | in DEE81 | |||
Sequence: Missing | ||||||
Natural variant | VAR_069028 | 1698 | in dbSNP:rs149028181 | |||
Sequence: N → S | ||||||
Natural variant | VAR_083447 | 1712 | in DEE81; dbSNP:rs372749193 | |||
Sequence: A → V | ||||||
Natural variant | VAR_072642 | 1942-1946 | in PEPNS | |||
Sequence: Missing | ||||||
Natural variant | VAR_079484 | 2417 | in DFNA71 | |||
Sequence: R → H |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 3,373 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, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000223324 | 1-3036 | UniProt | DmX-like protein 2 | |||
Sequence: MHLHQVLTGAVNPGDNCYSVGSVGDVPFTAYGSGCDIVILANDFECVQIIPGAKHGNIQVSCVECSNQQGRIAASYGNAVCIFEPLGINSHKRNCQLKCQWLKTGQFFLSSVTYNLAWDPQDNRLLTATDSIQLWAPPGDDILEEEEEIDNTVPPVLNDWKCVWQCKTSVSVHLMEWSPDGEYFATAGKDDCLLKVWYPMTGWKSSIIPQDHHEVKRRQSSTQFSFVYLAHPRAVTGFSWRKTSKYMPRGSVCNVLLTSCHDGVCRLWAETLLPEDCLLGEQICETTTSSIASSLSHAGRHKDRIQHALETIHHLKNLRKGQRRSSVLVTHAELMPDQTAMHEVQRHISHHANALCHFHIAASINPATDIPNVLVGTAFNVDDGNGGFVVHWLNNKEFHFTSSTEVFMHQLRKLSDKQVDHENDDADREDEEHSQEDRERGLHMKLDHDLSLDRESEAGTGSSEHEDGEREGSPRTYSRLSVPMPLPTVLLDRKIETLLTEWNKNPDMLFTIHPVDGTFLVWHVKYLDEYNPGIFRQVQVSFSSRIPVAFPSGDASSLSKNIMMYACINATKDSHHTLLHQEGMSVGSPHGSQPHSRSHSTHMNILAPTVMMISKHIDGSLNQWAVTFADKSAFTTVLTVSHKFRYCGHRFHLNDLACHSVLPLLLTSSHHNALLTPELDCQWDSDNKLSRLMDPVKHIKGSSKQPLRNAATRTFHDPNAIYSELILWRVDPIGPLSYTGGVSELARINSLHTSAFSNVAWLPTLIPSYCLGTYCNSASACFVASDGKNLRLYQAVVDARKLLDELSDPESSKLIGEVFNIVSQQSTARPGCIIELDAITNQCGSNTQLLHVFQEDFIIGYKPHKEDMEKKETEIFFQPSQGYRPPPFSEKFFLVVIEKDSNNNSILHMWHLHLKSVQACLAKASEGASSESLLSVPGQKNVDSSPETSPSVSPMPHSSSIANLQTASKLILSSRLVYSQPLDLPESVEVIRATPSAGHLSSSSIYPVCLAPYLVVTTCSDNKVRFWKCCMEANPECNKSDEKEIYHWKRWPLMNDEGEDNSSTVSIVGRPVAVSCSYTGRLAVAYKQPIHHNGFVSKEFSMHVCIFECESTGGSEWVLEQTIHLDDLVKVGSVLDSRVSVDSNLFVYSKSDALLSKDRYLIPNIKHLVHLDWVSKEDGSHILTVGVGANIFMYGRLSGIVTEQTNSKDGVAVITLPLGGSIKQGVKSRWVLLRSIDLVSSVDGTPSLPVSLSWVRDGILVVGMDCEMHVYAQWKHAVKFGDTEADSSNAEEAAMQDHSTFKSNMLARKSVVEGTAISDDVFCSPTVIQDGGLFEAAHVLSPTLPQYHPTQLLELMDLGKVRRAKAILSHLVKCIAGEVAIVRDPDAGEGTKRHLSRTISVSGSTAKETVTVGKDGTRDYTEIDSIPPLPLYALLAADQDTSYRISEESTKIPQSYEDQTVSQPEDQYSELFQIQDIPTDDIDLEPEKRENKSKVINLSQYGPAYFGQEHARVLSSHLMHSSLPGLTRLEQMFLVALADTVATTSTELDESRDKSCSGRDTLDECGLRYLLAMRLHTCLLTSLPPLYRVQLLHQGVSTCHFAWAFHSEAEEELINMIPAIQRGDPQWSELRAMGIGWWVRNINTLRRCIEKVAKASFQRNNDALDAALFYLSMKKKAVVWGLFRSQHDEKMTTFFSHNFNEDRWRKAALKNAFSLLGKQRFEQSAAFFLLAGSLKDAIEVCLEKMEDIQLAMVIARLYESEFETSSTYISILNQKILGCQKDGSGFSCKRLHPDPFLRSLAYWVMKDYTRALDTLLEQTPKEDDEHQVIIKSCNPVAFSFYNYLRTHPLLIRRNLASPEGTLATLGLKTEKNFVDKINLIERKLFFTTANAHFKVGCPVLALEVLSKIPKVTKTSALSAKKDQPDFISHRMDDVPSHSKALSDGNGSSGIEWSNVTSSQYDWSQPIVKVDEEPLNLDWGEDHDSALDEEEDDAVGLVMKSTDAREKDKQSDQKASDPNMLLTPQEEDDPEGDTEVDVIAEQLKFRACLKILMTELRTLATGYEVDGGKLRFQLYNWLEKEIAALHEICNHESVIKEYSSKTYSKVESDLLDQEEMVDKPDIGSYERHQIERRRLQAKREHAERRKSWLQKNQDLLRVFLSYCSLHGAQGGGLASVRMELKFLLQESQQETTVKQLQSPLPLPTTLPLLSASIASTKTVIANPVLYLNNHIHDILYTIVQMKTPPHPSIEDVKVHTLHSLAASLSASIYQALCDSHSYSQTEGNQFTGMAYQGLLLSDRRRLRTESIEEHATPNSSPAQWPGVSSLINLLSSAQDEDQPKLNILLCEAVVAVYLSLLIHALATNSSSELFRLAAHPLNNRMWAAVFGGGVKLVVKPRRQSENISAPPVLSEDIDKHRRRFNMRMLVPGRPVKDATPPPVPAERPSYKEKFIPPELSMWDYFVAKPFLPLSDSGVIYDSDESIHSDEEDDAFFSDTQIQEHQDPNSYSWALLHLTMVKLALHNVKNFFPIAGLEFSELPVTSPLGIAVIKNLENWEQILQEKMDQFEGPPPNYINTYPTDLSVGAGPAILRNKAMLEPENTPFKSRDSSAFPVKRLWHFLVKQEVLQETFIRYIFTKKRKQSEVEADLGYPGGKAKVIHKESDMIMAFSVNKANCNEIVLASTHDVQELDVTSLLACQSYIWIGEEYDRESKSSDDVDYRGSTTTLYQPSATSYSASQVHPPSSLPWLGTGQTSTGASVLMKRNLHNVKRMTSHPVHQYYLTGAQDGSVRMFEWTRPQQLVCFRQAGNARVTRLYFNSQGNKCGVADGEGFLSIWQVNQTASNPKPYMSWQCHSKATSDFAFITSSSLVATSGHSNDNRNVCLWDTLISPGNSLIHGFTCHDHGATVLQYAPKQQLLISGGRKGHVCIFDIRQRQLIHTFQAHDSAIKALALDPYEEYFTTGSAEGNIKVWRLTGHGLIHSFKSEHAKQSIFRNIGAGVMQIDIIQGNRLFSCGADGTLKTRVLPNAFNIPNRILDIL | |||||||
Modified residue | 326 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 326 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 330 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 451 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 463 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 473 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 473 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 588 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 588 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 925 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 929 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 930 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 932 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 944 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 944 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 945 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 945 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 949 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 953 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 960 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1140 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1140 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1143 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1143 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1151 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1151 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1287 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1288 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1400 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1400 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1404 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1405 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1417 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1857 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1857 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1861 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1984 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1984 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2022 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2123 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2197 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2399 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2399 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2434 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 2640 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2640 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Structure
Family & Domains
Features
Showing features for repeat, region, compositional bias, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 108-145 | WD 1 | ||||
Sequence: FLSSVTYNLAWDPQDNRLLTATDSIQLWAPPGDDILEE | ||||||
Repeat | 167-207 | WD 2 | ||||
Sequence: KTSVSVHLMEWSPDGEYFATAGKDDCLLKVWYPMTGWKSSI | ||||||
Repeat | 230-278 | WD 3 | ||||
Sequence: AHPRAVTGFSWRKTSKYMPRGSVCNVLLTSCHDGVCRLWAETLLPEDCL | ||||||
Region | 417-480 | Disordered | ||||
Sequence: KQVDHENDDADREDEEHSQEDRERGLHMKLDHDLSLDRESEAGTGSSEHEDGEREGSPRTYSRL | ||||||
Compositional bias | 433-474 | Basic and acidic residues | ||||
Sequence: HSQEDRERGLHMKLDHDLSLDRESEAGTGSSEHEDGEREGSP | ||||||
Repeat | 492-532 | WD 4 | ||||
Sequence: DRKIETLLTEWNKNPDMLFTIHPVDGTFLVWHVKYLDEYNP | ||||||
Repeat | 595-634 | WD 5 | ||||
Sequence: HSRSHSTHMNILAPTVMMISKHIDGSLNQWAVTFADKSAF | ||||||
Repeat | 751-803 | WD 6 | ||||
Sequence: LHTSAFSNVAWLPTLIPSYCLGTYCNSASACFVASDGKNLRLYQAVVDARKLL | ||||||
Repeat | 878-920 | WD 7 | ||||
Sequence: QPSQGYRPPPFSEKFFLVVIEKDSNNNSILHMWHLHLKSVQAC | ||||||
Region | 932-959 | Disordered | ||||
Sequence: SLLSVPGQKNVDSSPETSPSVSPMPHSS | ||||||
Repeat | 1000-1037 | WD 8 | ||||
Sequence: LSSSSIYPVCLAPYLVVTTCSDNKVRFWKCCMEANPEC | ||||||
Repeat | 1163-1204 | WD 9 | ||||
Sequence: PNIKHLVHLDWVSKEDGSHILTVGVGANIFMYGRLSGIVTEQ | ||||||
Repeat | 1244-1281 | WD 10 | ||||
Sequence: GTPSLPVSLSWVRDGILVVGMDCEMHVYAQWKHAVKFG | ||||||
Region | 1927-1952 | Disordered | ||||
Sequence: ISHRMDDVPSHSKALSDGNGSSGIEW | ||||||
Compositional bias | 1999-2013 | Basic and acidic residues | ||||
Sequence: KSTDAREKDKQSDQK | ||||||
Region | 1999-2033 | Disordered | ||||
Sequence: KSTDAREKDKQSDQKASDPNMLLTPQEEDDPEGDT | ||||||
Coiled coil | 2122-2153 | |||||
Sequence: GSYERHQIERRRLQAKREHAERRKSWLQKNQD | ||||||
Repeat | 2761-2800 | WD 11 | ||||
Sequence: RNLHNVKRMTSHPVHQYYLTGAQDGSVRMFEWTRPQQLVC | ||||||
Repeat | 2804-2843 | WD 12 | ||||
Sequence: AGNARVTRLYFNSQGNKCGVADGEGFLSIWQVNQTASNPK | ||||||
Repeat | 2850-2892 | WD 13 | ||||
Sequence: CHSKATSDFAFITSSSLVATSGHSNDNRNVCLWDTLISPGNSL | ||||||
Repeat | 2898-2937 | WD 14 | ||||
Sequence: CHDHGATVLQYAPKQQLLISGGRKGHVCIFDIRQRQLIHT | ||||||
Repeat | 2940-2979 | WD 15 | ||||
Sequence: AHDSAIKALALDPYEEYFTTGSAEGNIKVWRLTGHGLIHS | ||||||
Repeat | 2992-3030 | WD 16 | ||||
Sequence: NIGAGVMQIDIIQGNRLFSCGADGTLKTRVLPNAFNIPN |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q8TDJ6-1
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
- Length3,036
- Mass (Da)339,641
- Last updated2010-05-18 v2
- Checksum25E9B1D05C69882C
Q8TDJ6-2
- Name2
- Differences from canonical
- 922-1557: Missing
Q8TDJ6-3
- Name3
- Differences from canonical
- 2278-2278: S → SS
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 128 | in Ref. 1; AAL93215 | ||||
Sequence: A → T | ||||||
Compositional bias | 433-474 | Basic and acidic residues | ||||
Sequence: HSQEDRERGLHMKLDHDLSLDRESEAGTGSSEHEDGEREGSP | ||||||
Alternative sequence | VSP_043015 | 922-1557 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 974 | in Ref. 1; AAL93215 | ||||
Sequence: S → F | ||||||
Compositional bias | 1999-2013 | Basic and acidic residues | ||||
Sequence: KSTDAREKDKQSDQK | ||||||
Alternative sequence | VSP_044977 | 2278 | in isoform 3 | |||
Sequence: S → SS | ||||||
Sequence conflict | 2984 | in Ref. 1; AAL93215 | ||||
Sequence: H → Y |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF389880 EMBL· GenBank· DDBJ | AAL93215.1 EMBL· GenBank· DDBJ | mRNA | ||
AB020663 EMBL· GenBank· DDBJ | BAA74879.2 EMBL· GenBank· DDBJ | mRNA | ||
AC020892 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC066613 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC140781 EMBL· GenBank· DDBJ | AAI40782.1 EMBL· GenBank· DDBJ | mRNA | ||
BC144539 EMBL· GenBank· DDBJ | AAI44540.1 EMBL· GenBank· DDBJ | mRNA |