Q14008 · CKAP5_HUMAN
- ProteinCytoskeleton-associated protein 5
- GeneCKAP5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2032 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. Acts as a processive microtubule polymerase. Promotes cytoplasmic microtubule nucleation and elongation. Plays a major role in organizing spindle poles. In spindle formation protects kinetochore microtubules from depolymerization by KIF2C and has an essential role in centrosomal microtubule assembly independently of KIF2C activity. Contributes to centrosome integrity. Acts as a component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge. The TACC3/ch-TOG/clathrin complex is required for the maintenance of kinetochore fiber tension (PubMed:23532825).
Enhances the strength of NDC80 complex-mediated kinetochore-tip microtubule attachments (PubMed:27156448).
Enhances the strength of NDC80 complex-mediated kinetochore-tip microtubule attachments (PubMed:27156448).
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 | centrosome | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | kinetochore | |
Cellular Component | membrane | |
Cellular Component | nucleolus | |
Cellular Component | plasma membrane | |
Cellular Component | protein-containing complex | |
Cellular Component | spindle pole | |
Molecular Function | cadherin binding | |
Molecular Function | microtubule binding | |
Molecular Function | microtubule plus end polymerase | |
Molecular Function | microtubule plus-end binding | |
Molecular Function | ribonucleoprotein complex binding | |
Biological Process | cell division | |
Biological Process | centrosome cycle | |
Biological Process | centrosome duplication | |
Biological Process | establishment or maintenance of microtubule cytoskeleton polarity | |
Biological Process | microtubule depolymerization | |
Biological Process | microtubule polymerization | |
Biological Process | mitotic spindle organization | |
Biological Process | positive regulation of microtubule nucleation | |
Biological Process | RNA transport | |
Biological Process | spindle organization |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCytoskeleton-associated protein 5
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ14008
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Detected on centrosomes and kinetochores during interphase and mitosis independently from TACC3 and clathrin. Located to spindle poles and microtubules during mitosis. In complex with TACC3 localized to microtubule plus-ends in mitosis and interphase. In complex with TACC3 and clathrin localized to inter-microtubule bridges in mitotic spindles. Accumulation sites at microtubule plus ends protruded approximately 100 nm from MAPRE1/EB1 sites in interphase cells.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_045627 | 785 | in dbSNP:rs11038988 | |||
Sequence: Y → C | ||||||
Mutagenesis | 1939 | Disrupts interaction with TACC3. | ||||
Sequence: L → A or R | ||||||
Mutagenesis | 1939 | Abolishes localization to spindle microtubules, no effect on localization to centrosomes and kinetochores; when associated with A-1942. | ||||
Sequence: L → A | ||||||
Mutagenesis | 1942 | Disrupts interaction with TACC3. | ||||
Sequence: L → A or R | ||||||
Mutagenesis | 1942 | Abolishes localization to spindle microtubules, no effect on localization to centrosomes and kinetochores; when associated with A-1939. | ||||
Sequence: L → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,599 variants from UniProt as well as other sources including ClinVar and dbSNP.
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_0000089663 | 1-2032 | UniProt | Cytoskeleton-associated protein 5 | |||
Sequence: MGDDSEWLKLPVDQKCEHKLWKARLSGYEEALKIFQKIKDEKSPEWSKFLGLIKKFVTDSNAVVQLKGLEAALVYVENAHVAGKTTGEVVSGVVSKVFNQPKAKAKELGIEICLMYIEIEKGEAVQEELLKGLDNKNPKIIVACIETLRKALSEFGSKIILLKPIIKVLPKLFESREKAVRDEAKLIAVEIYRWIRDALRPPLQNINSVQLKELEEEWVKLPTSAPRPTRFLRSQQELEAKLEQQQSAGGDAEGGGDDGDEVPQIDAYELLEAVEILSKLPKDFYDKIEAKKWQERKEALESVEVLIKNPKLEAGDYADLVKALKKVVGKDTNVMLVALAAKCLTGLAVGLRKKFGQYAGHVVPTILEKFKEKKPQVVQALQEAIDAIFLTTTLQNISEDVLAVMDNKNPTIKQQTSLFIARSFRHCTASTLPKSLLKPFCAALLKHINDSAPEVRDAAFEALGTALKVVGEKAVNPFLADVDKLKLDKIKECSEKVELIHGKKAGLAADKKEFKPLPGRTAASGAAGDKDTKDISAPKPGPLKKAPAAKAGGPPKKGKPAAPGGAGNTGTKNKKGLETKEIVEPELSIEVCEEKASAVLPPTCIQLLDSSNWKERLACMEEFQKAVELMDRTEMPCQALVRMLAKKPGWKETNFQVMQMKLHIVALIAQKGNFSKTSAQVVLDGLVDKIGDVKCGNNAKEAMTAIAEACMLPWTAEQVVSMAFSQKNPKNQSETLNWLSNAIKEFGFSGLNVKAFISNVKTALAATNPAVRTAAITLLGVMYLYVGPSLRMFFEDEKPALLSQIDAEFEKMQGQSPPAPTRGISKHSTSGTDEGEDGDEPDDGSNDVVDLLPRTEISDKITSELVSKIGDKNWKIRKEGLDEVAGIINDAKFIQPNIGELPTALKGRLNDSNKILVQQTLNILQQLAVAMGPNIKQHVKNLGIPIITVLGDSKNNVRAAALATVNAWAEQTGMKEWLEGEDLSEELKKENPFLRQELLGWLAEKLPTLRSTPTDLILCVPHLYSCLEDRNGDVRKKAQDALPFFMMHLGYEKMAKATGKLKPTSKDQVLAMLEKAKVNMPAKPAPPTKATSKPMGGSAPAKFQPASAPAEDCISSSTEPKPDPKKAKAPGLSSKAKSAQGKKMPSKTSLKEDEDKSGPIFIVVPNGKEQRMKDEKGLKVLKWNFTTPRDEYIEQLKTQMSSCVAKWLQDEMFHSDFQHHNKALAVMVDHLESEKEGVIGCLDLILKWLTLRFFDTNTSVLMKALEYLKLLFTLLSEEEYHLTENEASSFIPYLVVKVGEPKDVIRKDVRAILNRMCLVYPASKMFPFIMEGTKSKNSKQRAECLEELGCLVESYGMNVCQPTPGKALKEIAVHIGDRDNAVRNAALNTIVTVYNVHGDQVFKLIGNLSEKDMSMLEERIKRSAKRPSAAPIKQVEEKPQRAQNISSNANMLRKGPAEDMSSKLNQARSMSGHPEAAQMVRREFQLDLDEIENDNGTVRCEMPELVQHKLDDIFEPVLIPEPKIRAVSPHFDDMHSNTASTINFIISQVASGDINTSIQALTQIDEVLRQEDKAEAMSGHIDQFLIATFMQLRLIYNTHMADEKLEKDEIIKLYSCIIGNMISLFQIESLAREASTGVLKDLMHGLITLMLDSRIEDLEEGQQVIRSVNLLVVKVLEKSDQTNILSALLVLLQDSLLATASSPKFSELVMKCLWRMVRLLPDTINSINLDRILLDIHIFMKVFPKEKLKQCKSEFPIRTLKTLLHTLCKLKGPKILDHLTMIDNKNESELEAHLCRMMKHSMDQTGSKSDKETEKGASRIDEKSSKAKVNDFLAEIFKKIGSKENTKEGLAELYEYKKKYSDADIEPFLKNSSQFFQSYVERGLRVIEMEREGKGRISTSTGISPQMEVTCVPTPTSTVSSIGNTNGEEVGPSVYLERLKILRQRCGLDNTKQDDRPPLTSLLSKPAVPTVASSTDMLHSKLSQLRESREQHQHSDLDSNQTHSSGTVTSSSSTANIDDLKKRLERIKSSRK | |||||||
Modified residue | 48 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 247 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 569 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 816 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 816 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 832 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 845 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 845 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1107 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1149 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1469 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1469 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1861 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1861 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1964 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1983 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1995 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Overexpressed in hepatomas and colonic tumors. Also expressed in skeletal muscle, brain, heart, placenta, lung, liver, kidney and pancreas. Expression is elevated in the brain; highly expressed in the Purkinje cell bodies of the cerebellum.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with TACC1 (PubMed:11903063).
Interacts with SLAIN2 and SLAIN1 (PubMed:21646404).
Interacts with HNRNPA2B1 (PubMed:15703215).
Interacts with TACC3 independently of clathrin (PubMed:25596274).
Interacts with TACC3 and clathrin forming the TACC3/ch-TOG/clathrin complex located at spindle inter-microtubules bridges (PubMed:21297582, PubMed:23532825).
Interacts with NDC80; indicative for an association with the NDC80 complex (PubMed:27156448).
Interacts with SLAIN2 and SLAIN1 (PubMed:21646404).
Interacts with HNRNPA2B1 (PubMed:15703215).
Interacts with TACC3 independently of clathrin (PubMed:25596274).
Interacts with TACC3 and clathrin forming the TACC3/ch-TOG/clathrin complex located at spindle inter-microtubules bridges (PubMed:21297582, PubMed:23532825).
Interacts with NDC80; indicative for an association with the NDC80 complex (PubMed:27156448).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q14008 | NCK1 P16333 | 3 | EBI-310585, EBI-389883 | |
BINARY | Q14008 | SLAIN2 Q9P270 | 7 | EBI-310585, EBI-3959887 | |
BINARY | Q14008 | TACC1 O75410 | 6 | EBI-310585, EBI-624237 | |
BINARY | Q14008 | TACC1 O75410-1 | 3 | EBI-310585, EBI-624252 | |
BINARY | Q14008 | TACC1 O75410-6 | 2 | EBI-310585, EBI-624278 | |
BINARY | Q14008 | TACC3 Q9Y6A5 | 10 | EBI-310585, EBI-2554984 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, repeat, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-223 | TOG 1 | ||||
Sequence: MGDDSEWLKLPVDQKCEHKLWKARLSGYEEALKIFQKIKDEKSPEWSKFLGLIKKFVTDSNAVVQLKGLEAALVYVENAHVAGKTTGEVVSGVVSKVFNQPKAKAKELGIEICLMYIEIEKGEAVQEELLKGLDNKNPKIIVACIETLRKALSEFGSKIILLKPIIKVLPKLFESREKAVRDEAKLIAVEIYRWIRDALRPPLQNINSVQLKELEEEWVKLPT | ||||||
Repeat | 159-197 | HEAT 1 | ||||
Sequence: IILLKPIIKVLPKLFESREKAVRDEAKLIAVEIYRWIRD | ||||||
Region | 268-502 | TOG 2 | ||||
Sequence: YELLEAVEILSKLPKDFYDKIEAKKWQERKEALESVEVLIKNPKLEAGDYADLVKALKKVVGKDTNVMLVALAAKCLTGLAVGLRKKFGQYAGHVVPTILEKFKEKKPQVVQALQEAIDAIFLTTTLQNISEDVLAVMDNKNPTIKQQTSLFIARSFRHCTASTLPKSLLKPFCAALLKHINDSAPEVRDAAFEALGTALKVVGEKAVNPFLADVDKLKLDKIKECSEKVELIHG | ||||||
Repeat | 356-394 | HEAT 2 | ||||
Sequence: GQYAGHVVPTILEKFKEKKPQVVQALQEAIDAIFLTTTL | ||||||
Repeat | 434-472 | HEAT 3 | ||||
Sequence: KSLLKPFCAALLKHINDSAPEVRDAAFEALGTALKVVGE | ||||||
Region | 516-579 | Disordered | ||||
Sequence: PLPGRTAASGAAGDKDTKDISAPKPGPLKKAPAAKAGGPPKKGKPAAPGGAGNTGTKNKKGLET | ||||||
Region | 588-817 | TOG 3 | ||||
Sequence: SIEVCEEKASAVLPPTCIQLLDSSNWKERLACMEEFQKAVELMDRTEMPCQALVRMLAKKPGWKETNFQVMQMKLHIVALIAQKGNFSKTSAQVVLDGLVDKIGDVKCGNNAKEAMTAIAEACMLPWTAEQVVSMAFSQKNPKNQSETLNWLSNAIKEFGFSGLNVKAFISNVKTALAATNPAVRTAAITLLGVMYLYVGPSLRMFFEDEKPALLSQIDAEFEKMQGQSP | ||||||
Repeat | 750-788 | HEAT 4 | ||||
Sequence: GLNVKAFISNVKTALAATNPAVRTAAITLLGVMYLYVGP | ||||||
Region | 811-851 | Disordered | ||||
Sequence: KMQGQSPPAPTRGISKHSTSGTDEGEDGDEPDDGSNDVVDL | ||||||
Region | 853-1081 | TOG 4 | ||||
Sequence: PRTEISDKITSELVSKIGDKNWKIRKEGLDEVAGIINDAKFIQPNIGELPTALKGRLNDSNKILVQQTLNILQQLAVAMGPNIKQHVKNLGIPIITVLGDSKNNVRAAALATVNAWAEQTGMKEWLEGEDLSEELKKENPFLRQELLGWLAEKLPTLRSTPTDLILCVPHLYSCLEDRNGDVRKKAQDALPFFMMHLGYEKMAKATGKLKPTSKDQVLAMLEKAKVNMP | ||||||
Repeat | 855-893 | HEAT 5 | ||||
Sequence: TEISDKITSELVSKIGDKNWKIRKEGLDEVAGIINDAKF | ||||||
Repeat | 936-974 | HEAT 6 | ||||
Sequence: KQHVKNLGIPIITVLGDSKNNVRAAALATVNAWAEQTGM | ||||||
Repeat | 1013-1051 | HEAT 7 | ||||
Sequence: PTDLILCVPHLYSCLEDRNGDVRKKAQDALPFFMMHLGY | ||||||
Region | 1077-1160 | Disordered | ||||
Sequence: KVNMPAKPAPPTKATSKPMGGSAPAKFQPASAPAEDCISSSTEPKPDPKKAKAPGLSSKAKSAQGKKMPSKTSLKEDEDKSGPI | ||||||
Region | 1193-1428 | TOG 5 | ||||
Sequence: IEQLKTQMSSCVAKWLQDEMFHSDFQHHNKALAVMVDHLESEKEGVIGCLDLILKWLTLRFFDTNTSVLMKALEYLKLLFTLLSEEEYHLTENEASSFIPYLVVKVGEPKDVIRKDVRAILNRMCLVYPASKMFPFIMEGTKSKNSKQRAECLEELGCLVESYGMNVCQPTPGKALKEIAVHIGDRDNAVRNAALNTIVTVYNVHGDQVFKLIGNLSEKDMSMLEERIKRSAKRPS | ||||||
Repeat | 1284-1322 | HEAT 8 | ||||
Sequence: ENEASSFIPYLVVKVGEPKDVIRKDVRAILNRMCLVYPA | ||||||
Repeat | 1324-1357 | HEAT 9 | ||||
Sequence: KMFPFIMEGTKSKNSKQRAECLEELGCLVESYGM | ||||||
Repeat | 1361-1399 | HEAT 10 | ||||
Sequence: QPTPGKALKEIAVHIGDRDNAVRNAALNTIVTVYNVHGD | ||||||
Region | 1422-1443 | Disordered | ||||
Sequence: RSAKRPSAAPIKQVEEKPQRAQ | ||||||
Region | 1801-1822 | Disordered | ||||
Sequence: SMDQTGSKSDKETEKGASRIDE | ||||||
Region | 1932-1957 | Interaction with TACC3 | ||||
Sequence: PSVYLERLKILRQRCGLDNTKQDDRP | ||||||
Region | 1949-2032 | Disordered | ||||
Sequence: DNTKQDDRPPLTSLLSKPAVPTVASSTDMLHSKLSQLRESREQHQHSDLDSNQTHSSGTVTSSSSTANIDDLKKRLERIKSSRK | ||||||
Compositional bias | 1966-1981 | Polar residues | ||||
Sequence: PAVPTVASSTDMLHSK | ||||||
Compositional bias | 1982-1997 | Basic and acidic residues | ||||
Sequence: LSQLRESREQHQHSDL | ||||||
Compositional bias | 1998-2017 | Polar residues | ||||
Sequence: DSNQTHSSGTVTSSSSTANI |
Domain
The TOG (tumor overexpressed gene) domains are arranged in a N-terminal pentameric array with each domain composed of six (for the most part non-canonical) HEAT repeats forming a oblong paddle-like structure. Intra-HEAT loops are positioned along a face of the TOG domain and bind to a single alpha/beta-tubulin heterodimer. The TOG domains in the array seem to be structurally and functionally polarized. Differential functions may range from microtubule (MT) lattice binding and/or free tubulin heterodimer binding to potentiating stable incorporation of tubulin into the MT lattice.
Sequence similarities
Belongs to the TOG/XMAP215 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q14008-1
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
- Length2,032
- Mass (Da)225,495
- Last updated2008-11-04 v3
- ChecksumB2BBFB1CF2ED688B
Q14008-2
- Name2
- Differences from canonical
- 1564-1623: Missing
Q14008-3
- Name3
- Differences from canonical
- 1774-1774: K → KSCMCLPQ
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for sequence conflict, alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 476 | in Ref. 1; CAA63212 and 2; BAA07892 | ||||
Sequence: N → K | ||||||
Alternative sequence | VSP_035668 | 1564-1623 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_036400 | 1774 | in isoform 3 | |||
Sequence: K → KSCMCLPQ | ||||||
Sequence conflict | 1814 | in Ref. 1; CAA63212 | ||||
Sequence: E → A | ||||||
Sequence conflict | 1822 | in Ref. 1; CAA63212 | ||||
Sequence: E → A | ||||||
Compositional bias | 1966-1981 | Polar residues | ||||
Sequence: PAVPTVASSTDMLHSK | ||||||
Compositional bias | 1982-1997 | Basic and acidic residues | ||||
Sequence: LSQLRESREQHQHSDL | ||||||
Compositional bias | 1998-2017 | Polar residues | ||||
Sequence: DSNQTHSSGTVTSSSSTANI |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X92474 EMBL· GenBank· DDBJ | CAA63212.1 EMBL· GenBank· DDBJ | mRNA | ||
D43948 EMBL· GenBank· DDBJ | BAA07892.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC115088 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC017856 EMBL· GenBank· DDBJ | AAH17856.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BC070136 EMBL· GenBank· DDBJ | AAH70136.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BC111043 EMBL· GenBank· DDBJ | AAI11044.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BC120869 EMBL· GenBank· DDBJ | AAI20870.1 EMBL· GenBank· DDBJ | mRNA | ||
BC120870 EMBL· GenBank· DDBJ | AAI20871.1 EMBL· GenBank· DDBJ | mRNA | Frameshift |