Q9UPN4 · CP131_HUMAN
- ProteinCentrosomal protein of 131 kDa
- GeneCEP131
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1083 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of centriolar satellites contributing to the building of a complex and dynamic network required to regulate cilia/flagellum formation (PubMed:17954613, PubMed:24185901).
In proliferating cells, MIB1-mediated ubiquitination induces its sequestration within centriolar satellites, precluding untimely cilia formation initiation (PubMed:24121310).
In contrast, during normal and ultraviolet or heat shock cellular stress-induced ciliogenesis, its non-ubiquitinated form is rapidly displaced from centriolar satellites and recruited to centrosome/basal bodies in a microtubule- and p38 MAPK-dependent manner (PubMed:24121310, PubMed:26616734).
Acts also as a negative regulator of BBSome ciliary trafficking (PubMed:24550735).
Plays a role in sperm flagellar formation; may be involved in the regulation of intraflagellar transport (IFT) and/or intramanchette (IMT) trafficking, which are important for axoneme extension and/or cargo delivery to the nascent sperm tail (By similarity).
Required for optimal cell proliferation and cell cycle progression; may play a role in the regulation of genome stability in non-ciliogenic cells (PubMed:22797915, PubMed:26297806).
Involved in centriole duplication (By similarity).
Required for CEP152, WDR62 and CEP63 centrosomal localization and promotes the centrosomal localization of CDK2 (PubMed:26297806).
Essential for maintaining proper centriolar satellite integrity (PubMed:30804208).
In proliferating cells, MIB1-mediated ubiquitination induces its sequestration within centriolar satellites, precluding untimely cilia formation initiation (PubMed:24121310).
In contrast, during normal and ultraviolet or heat shock cellular stress-induced ciliogenesis, its non-ubiquitinated form is rapidly displaced from centriolar satellites and recruited to centrosome/basal bodies in a microtubule- and p38 MAPK-dependent manner (PubMed:24121310, PubMed:26616734).
Acts also as a negative regulator of BBSome ciliary trafficking (PubMed:24550735).
Plays a role in sperm flagellar formation; may be involved in the regulation of intraflagellar transport (IFT) and/or intramanchette (IMT) trafficking, which are important for axoneme extension and/or cargo delivery to the nascent sperm tail (By similarity).
Required for optimal cell proliferation and cell cycle progression; may play a role in the regulation of genome stability in non-ciliogenic cells (PubMed:22797915, PubMed:26297806).
Involved in centriole duplication (By similarity).
Required for CEP152, WDR62 and CEP63 centrosomal localization and promotes the centrosomal localization of CDK2 (PubMed:26297806).
Essential for maintaining proper centriolar satellite integrity (PubMed:30804208).
Miscellaneous
Transient cell cultured-based knock-down (by RNAi) of CEP131 leads to a reduction in ciliogenesis (PubMed:17954613, PubMed:24121310).
However, analysis of mice with chronic absence of CEP131 following genetic deletion (knockout) shows that cilia develop and function normally in vivo. This suggests that CEP131 is not essential for ciliogenesis, except for the modified cilia of the developing sperm flagella, and that there is an alternative mechanism to compensate for the lack of CEP131
However, analysis of mice with chronic absence of CEP131 following genetic deletion (knockout) shows that cilia develop and function normally in vivo. This suggests that CEP131 is not essential for ciliogenesis, except for the modified cilia of the developing sperm flagella, and that there is an alternative mechanism to compensate for the lack of CEP131
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | acrosomal vesicle | |
Cellular Component | centriolar satellite | |
Cellular Component | centriole | |
Cellular Component | centrosome | |
Cellular Component | ciliary basal body | |
Cellular Component | ciliary transition zone | |
Cellular Component | cytosol | |
Cellular Component | manchette | |
Cellular Component | nuclear membrane | |
Cellular Component | nucleoplasm | |
Cellular Component | sperm head-tail coupling apparatus | |
Molecular Function | protein homodimerization activity | |
Molecular Function | protein-containing complex binding | |
Biological Process | cilium assembly | |
Biological Process | intraciliary transport involved in cilium assembly | |
Biological Process | intramanchette transport | |
Biological Process | manchette assembly | |
Biological Process | non-motile cilium assembly | |
Biological Process | positive regulation of cell population proliferation | |
Biological Process | positive regulation of intracellular protein transport | |
Biological Process | protein localization to centrosome | |
Biological Process | regulation of centrosome duplication | |
Biological Process | sperm axoneme assembly |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCentrosomal protein of 131 kDa
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9UPN4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Colocalized with pericentriolar material protein PCM1 at centriolar satellites. During spermiogenesis, becomes enriched with nephrocystin NPHP1 at the transition zone, a structure at the base of the ciliary axoneme important for regulating traffic into the ciliary compartment. Traffics towards and away from the centrosome/basal body and the transition zone of the ciliary axoneme in a microtubule-dependent manner. Localized at the Golgi-derived acrosome and the centrosome-containing head-tail coupling apparatus (HTCA) (By similarity).
Ubiquitinated form is sequestered and colocalized with BBS4, CEP290, PCM1 and PCNT at centriolar satellites in proliferating cells. Colocalized with the pericentriolar material protein PCM1 at centrosome. Traffics towards and away from centriolar satellites and centrosome in a microtubule- and dynein-dependent manner in interphase cells. Displaced from centriolar satellites but still remains associated with the centrosome in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock, in a process that requires p38 MAPK signaling (PubMed:26616734).
Ubiquitinated form is sequestered and colocalized with BBS4, CEP290, PCM1 and PCNT at centriolar satellites in proliferating cells. Colocalized with the pericentriolar material protein PCM1 at centrosome. Traffics towards and away from centriolar satellites and centrosome in a microtubule- and dynein-dependent manner in interphase cells. Displaced from centriolar satellites but still remains associated with the centrosome in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock, in a process that requires p38 MAPK signaling (PubMed:26616734).
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_056740 | 43 | in dbSNP:rs8067409 | |||
Sequence: V → I | ||||||
Mutagenesis | 47 | Partially reduces in vitro phosphorylation by MAPKAPK2 and decreases binding to 14-3-3. Abolishes in vitro phosphorylation by MAPKAPK2, interaction with 14-3-3 and stress-induced centriolar satellite remodeling; when associated with A-78. | ||||
Sequence: S → A | ||||||
Natural variant | VAR_060226 | 70 | in dbSNP:rs752612451 | |||
Sequence: I → V | ||||||
Mutagenesis | 78 | Partially reduces in vitro phosphorylation by MAPKAPK2 and decreases binding to 14-3-3. Abolishes in vitro phosphorylation by MAPKAPK2, interaction with 14-3-3 and stress-induced centriolar satellite remodeling; when associated with A-47. Loss of PLK4-mediated phosphorylation. No effect on its localization to centriole and centriolar satellite or on its function in ciliogenesis. Cannot rescue centriolar satellite dispersion defect mediated by deletion of CEP131. | ||||
Sequence: S → A | ||||||
Mutagenesis | 78 | Phosphomimetic mutant. No effect on its localization to centriole and centriolar satellite or on its function in ciliogenesis. Can rescue centriolar satellite dispersion defect mediated by deletion of CEP131. | ||||
Sequence: S → D | ||||||
Natural variant | VAR_060227 | 272 | in dbSNP:rs2466773 | |||
Sequence: T → A | ||||||
Natural variant | VAR_060228 | 397 | in dbSNP:rs2659015 | |||
Sequence: T → A | ||||||
Natural variant | VAR_060229 | 473 | in dbSNP:rs2659016 | |||
Sequence: V → A | ||||||
Mutagenesis | 731 | No effect on interaction with 14-3-3. | ||||
Sequence: S → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,382 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_0000064781 | 1-1083 | UniProt | Centrosomal protein of 131 kDa | |||
Sequence: MKGTRAIGSVPERSPAGVDLSLTGLPPPVSRRPGSAATTKPIVRSVSVVTGSEQKRKVLEATGPGGSQAINNLRRSNSTTQVSQPRSGSPRPTEPTDFLMLFEGSPSGKKRPASLSTAPSEKGATWNVLDDQPRGFTLPSNARSSSALDSPAGPRRKECTVALAPNFTANNRSNKGAVGNCVTTMVHNRYTPSERAPPLKSSNQTAPSLNNIIKAATCEGSESSGFGKLPKNVSSATHSARNNTGGSTGLPRRKEVTEEEAERFIHQVNQATVTIQRWYRHQVQRRGAGAARLEHLLQAKREEQRQRSGEGTLLDLHQQKEAARRKAREEKARQARRAAIQELQQKRALRAQKASTAERGPPENPRETRVPGMRQPAQELSPTPGGTAHQALKANNTGGGLPAAGPGDRCLPTSDSSPEPQQPPEDRTQDVLAQDAAGDNLEMMAPSRGSAKSRGPLEELLHTLQLLEKEPDVLPRPRTHHRGRYAWASEVTTEDDASSLTADNLEKFGKLSAFPEPPEDGTLLSEAKLQSIMSFLDEMEKSGQDQLDSQQEGWVPEAGPGPLELGSEVSTSVMRLKLEVEEKKQAMLLLQRALAQQRDLTARRVKETEKALSRQLQRQREHYEATIQRHLAFIDQLIEDKKVLSEKCEAVVAELKQEDQRCTERVAQAQAQHELEIKKLKELMSATEKARREKWISEKTKKIKEVTVRGLEPEIQKLIARHKQEVRRLKSLHEAELLQSDERASQRCLRQAEELREQLEREKEALGQQERERARQRFQQHLEQEQWALQQQRQRLYSEVAEERERLGQQAARQRAELEELRQQLEESSSALTRALRAEFEKGREEQERRHQMELNTLKQQLELERQAWEAGRTRKEEAWLLNREQELREEIRKGRDKEIELVIHRLEADMALAKEESEKAAESRIKRLRDKYEAELSELEQSERKLQERCSELKGQLGEAEGENLRLQGLVRQKERALEDAQAVNEQLSSERSNLAQVIRQEFEDRLAASEEETRQAKAELATLQARQQLELEEVHRRVKTALARKEEAVSSLRTQHEAAVKRADHLEELLEQHRRPTPSTK | |||||||
Modified residue | 14 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 14 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 21 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 35 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 35 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 47 | UniProt | Phosphoserine; by MAPKAPK2 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 47 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 52 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 76 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 78 | UniProt | Phosphoserine; by MAPKAPK2 and PLK4 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 78 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 87 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 89 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 89 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 93 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 96 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 105 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 105 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 107 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 114 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 114 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 120 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 137 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 145 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 146 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 146 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 150 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 150 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 208 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 221 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 224 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 247 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 308 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 381 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 381 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 383 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 383 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 414 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 417 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 447 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 450 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 453 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 453 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 489 | UniProt | In isoform Q9UPN4-2; Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 489 | UniProt | In isoform Q9UPN4-3; Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 496 | UniProt | In isoform Q9UPN4-2; Phosphoserine | ||||
Sequence: D | |||||||
Modified residue | 496 | UniProt | In isoform Q9UPN4-3; Phosphoserine | ||||
Sequence: D | |||||||
Modified residue | 499 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 499 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 512 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 522 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 525 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 534 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 731 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 731 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 745 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 798 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 798 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Ubiquitinated. Undergoes monoubiquitination catalyzed by the E3 ubiquitin-protein ligase MIB1 in proliferating cells, preventing cilia formation. Monoubiquitination by MIB1 is inhibited in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock, resulting in cilia formation initiation.
MAPKAPK2-dependent phosphorylation at Ser-47 and Ser-78 occurs in response to cellular stress such as exposure to ultraviolet irradiation and promotes binding to 14-3-3 proteins which leads to cytoplasmic sequestration of CEP131 and blocks formation of new centriolar satellites (PubMed:26616734).
Phosphorylation at Ser-78 mediated by PLK4 is essential for proper organization and integrity of centriolar satellites but is dispensable for its localization to centrioles and its function in ciliogenesis (PubMed:30804208).
Phosphorylation at Ser-78 mediated by PLK4 is essential for proper organization and integrity of centriolar satellites but is dispensable for its localization to centrioles and its function in ciliogenesis (PubMed:30804208).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
Up-regulated by the transcription factor SP1.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Self-associates. Associates with the centriolar satellite BBSome protein complex. Interacts with BBS4; the interaction limits BBS4 availability for association with the BBSome complex, and hence negatively regulates ciliary localization of the BBSome complex (PubMed:24550735).
Interacts with MIB1 (PubMed:24121310).
Interacts with PCM1; the interaction increases in response to ultraviolet light (UV) radiation (PubMed:22797915, PubMed:24121310).
Associates with microtubules; association with microtubules is reduced in response to cellular stress, such as UV stimulation, in a process that requires p38 MAP kinase signaling (PubMed:24121310).
Interacts with CEP290, DCTN1, PCNT, PCM1 and CEP152. Interacts with 14-3-3 proteins following UV-induced phosphorylation by MAPKAPK2; this inhibits formation of novel centriolar satellites (PubMed:26616734).
Interacts with SDCCAG8 (PubMed:27224062).
Interacts with CCDC61 (PubMed:31789463).
Interacts with PLK4 (PubMed:30804208).
Interacts with MIB1 (PubMed:24121310).
Interacts with PCM1; the interaction increases in response to ultraviolet light (UV) radiation (PubMed:22797915, PubMed:24121310).
Associates with microtubules; association with microtubules is reduced in response to cellular stress, such as UV stimulation, in a process that requires p38 MAP kinase signaling (PubMed:24121310).
Interacts with CEP290, DCTN1, PCNT, PCM1 and CEP152. Interacts with 14-3-3 proteins following UV-induced phosphorylation by MAPKAPK2; this inhibits formation of novel centriolar satellites (PubMed:26616734).
Interacts with SDCCAG8 (PubMed:27224062).
Interacts with CCDC61 (PubMed:31789463).
Interacts with PLK4 (PubMed:30804208).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9UPN4 | CEP152 O94986 | 3 | EBI-2558372, EBI-311012 | |
BINARY | Q9UPN4 | CEP290 O15078 | 9 | EBI-2558372, EBI-1811944 | |
BINARY | Q9UPN4 | PCM1 Q15154 | 6 | EBI-2558372, EBI-741421 | |
BINARY | Q9UPN4 | SDCCAG8 Q86SQ7 | 3 | EBI-2558372, EBI-1047850 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-155 | Disordered | ||||
Sequence: MKGTRAIGSVPERSPAGVDLSLTGLPPPVSRRPGSAATTKPIVRSVSVVTGSEQKRKVLEATGPGGSQAINNLRRSNSTTQVSQPRSGSPRPTEPTDFLMLFEGSPSGKKRPASLSTAPSEKGATWNVLDDQPRGFTLPSNARSSSALDSPAGPR | ||||||
Region | 1-250 | Interaction with PLK4 | ||||
Sequence: MKGTRAIGSVPERSPAGVDLSLTGLPPPVSRRPGSAATTKPIVRSVSVVTGSEQKRKVLEATGPGGSQAINNLRRSNSTTQVSQPRSGSPRPTEPTDFLMLFEGSPSGKKRPASLSTAPSEKGATWNVLDDQPRGFTLPSNARSSSALDSPAGPRRKECTVALAPNFTANNRSNKGAVGNCVTTMVHNRYTPSERAPPLKSSNQTAPSLNNIIKAATCEGSESSGFGKLPKNVSSATHSARNNTGGSTGL | ||||||
Compositional bias | 65-91 | Polar residues | ||||
Sequence: GGSQAINNLRRSNSTTQVSQPRSGSPR | ||||||
Region | 220-258 | Disordered | ||||
Sequence: GSESSGFGKLPKNVSSATHSARNNTGGSTGLPRRKEVTE | ||||||
Compositional bias | 227-250 | Polar residues | ||||
Sequence: GKLPKNVSSATHSARNNTGGSTGL | ||||||
Domain | 269-289 | IQ | ||||
Sequence: NQATVTIQRWYRHQVQRRGAG | ||||||
Region | 301-429 | Disordered | ||||
Sequence: REEQRQRSGEGTLLDLHQQKEAARRKAREEKARQARRAAIQELQQKRALRAQKASTAERGPPENPRETRVPGMRQPAQELSPTPGGTAHQALKANNTGGGLPAAGPGDRCLPTSDSSPEPQQPPEDRTQ | ||||||
Compositional bias | 317-337 | Basic and acidic residues | ||||
Sequence: HQQKEAARRKAREEKARQARR | ||||||
Compositional bias | 380-394 | Polar residues | ||||
Sequence: LSPTPGGTAHQALKA | ||||||
Compositional bias | 414-428 | Polar residues | ||||
Sequence: SDSSPEPQQPPEDRT | ||||||
Compositional bias | 1047-1077 | Basic and acidic residues | ||||
Sequence: KEEAVSSLRTQHEAAVKRADHLEELLEQHRR | ||||||
Region | 1047-1083 | Disordered | ||||
Sequence: KEEAVSSLRTQHEAAVKRADHLEELLEQHRRPTPSTK |
Sequence similarities
Belongs to the CEP131 family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q9UPN4-1
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
- Length1,083
- Mass (Da)122,149
- Last updated2010-11-30 v3
- Checksum31C8CA426569CCAC
Q9UPN4-2
- Name2
- Differences from canonical
- 491-493: Missing
Q9UPN4-3
- Name3
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 65-91 | Polar residues | ||||
Sequence: GGSQAINNLRRSNSTTQVSQPRSGSPR | ||||||
Compositional bias | 227-250 | Polar residues | ||||
Sequence: GKLPKNVSSATHSARNNTGGSTGL | ||||||
Compositional bias | 317-337 | Basic and acidic residues | ||||
Sequence: HQQKEAARRKAREEKARQARR | ||||||
Compositional bias | 380-394 | Polar residues | ||||
Sequence: LSPTPGGTAHQALKA | ||||||
Compositional bias | 414-428 | Polar residues | ||||
Sequence: SDSSPEPQQPPEDRT | ||||||
Alternative sequence | VSP_015823 | 491-493 | in isoform 2 and isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_040204 | 777-812 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 1047-1077 | Basic and acidic residues | ||||
Sequence: KEEAVSSLRTQHEAAVKRADHLEELLEQHRR |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB029041 EMBL· GenBank· DDBJ | BAA83070.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC027601 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC011615 EMBL· GenBank· DDBJ | AAH11615.2 EMBL· GenBank· DDBJ | mRNA | ||
BC136580 EMBL· GenBank· DDBJ | AAI36581.1 EMBL· GenBank· DDBJ | mRNA |